data_7HUX
# 
_entry.id   7HUX 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HUX         pdb_00007hux 10.2210/pdb7hux/pdb 
WWPDB D_1001407962 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HUX 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2-methyl-1H-1,3-benzimidazol-1-yl)acetyl]piperidine-3-carboxamide' 300.356   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                   65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    3  ?         ? ? ? 
5 water       nat water                                                                        18.015    66 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2-methyl-1H-1,3-benzimidazol-1-yl)acetyl]piperidine-3-carboxamide' A1BRL 
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 
A1BRL non-polymer         . '(3S)-1-[(2-methyl-1H-1,3-benzimidazol-1-yl)acetyl]piperidine-3-carboxamide' ? 'C16 H20 N4 O2'  
300.356 
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        A1BRL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BRL 
_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 A1BRL 1  201 201 A1BRL LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 2   DMS   DMS A . 
E 4 DMS   1  204 6   DMS   DMS A . 
F 4 DMS   1  205 7   DMS   DMS A . 
G 5 HOH   1  301 1   HOH   HOH A . 
G 5 HOH   2  302 15  HOH   HOH A . 
G 5 HOH   3  303 24  HOH   HOH A . 
G 5 HOH   4  304 12  HOH   HOH A . 
G 5 HOH   5  305 61  HOH   HOH A . 
G 5 HOH   6  306 9   HOH   HOH A . 
G 5 HOH   7  307 16  HOH   HOH A . 
G 5 HOH   8  308 11  HOH   HOH A . 
G 5 HOH   9  309 38  HOH   HOH A . 
G 5 HOH   10 310 4   HOH   HOH A . 
G 5 HOH   11 311 3   HOH   HOH A . 
G 5 HOH   12 312 65  HOH   HOH A . 
G 5 HOH   13 313 57  HOH   HOH A . 
G 5 HOH   14 314 43  HOH   HOH A . 
G 5 HOH   15 315 35  HOH   HOH A . 
G 5 HOH   16 316 56  HOH   HOH A . 
G 5 HOH   17 317 54  HOH   HOH A . 
G 5 HOH   18 318 10  HOH   HOH A . 
G 5 HOH   19 319 64  HOH   HOH A . 
G 5 HOH   20 320 5   HOH   HOH A . 
G 5 HOH   21 321 27  HOH   HOH A . 
G 5 HOH   22 322 25  HOH   HOH A . 
G 5 HOH   23 323 18  HOH   HOH A . 
G 5 HOH   24 324 70  HOH   HOH A . 
G 5 HOH   25 325 41  HOH   HOH A . 
G 5 HOH   26 326 59  HOH   HOH A . 
G 5 HOH   27 327 13  HOH   HOH A . 
G 5 HOH   28 328 26  HOH   HOH A . 
G 5 HOH   29 329 45  HOH   HOH A . 
G 5 HOH   30 330 60  HOH   HOH A . 
G 5 HOH   31 331 37  HOH   HOH A . 
G 5 HOH   32 332 6   HOH   HOH A . 
G 5 HOH   33 333 31  HOH   HOH A . 
G 5 HOH   34 334 28  HOH   HOH A . 
G 5 HOH   35 335 42  HOH   HOH A . 
G 5 HOH   36 336 19  HOH   HOH A . 
G 5 HOH   37 337 29  HOH   HOH A . 
G 5 HOH   38 338 55  HOH   HOH A . 
G 5 HOH   39 339 14  HOH   HOH A . 
G 5 HOH   40 340 33  HOH   HOH A . 
G 5 HOH   41 341 22  HOH   HOH A . 
G 5 HOH   42 342 17  HOH   HOH A . 
G 5 HOH   43 343 62  HOH   HOH A . 
G 5 HOH   44 344 58  HOH   HOH A . 
G 5 HOH   45 345 50  HOH   HOH A . 
G 5 HOH   46 346 66  HOH   HOH A . 
G 5 HOH   47 347 63  HOH   HOH A . 
G 5 HOH   48 348 52  HOH   HOH A . 
G 5 HOH   49 349 40  HOH   HOH A . 
G 5 HOH   50 350 53  HOH   HOH A . 
G 5 HOH   51 351 8   HOH   HOH A . 
G 5 HOH   52 352 72  HOH   HOH A . 
G 5 HOH   53 353 34  HOH   HOH A . 
G 5 HOH   54 354 48  HOH   HOH A . 
G 5 HOH   55 355 32  HOH   HOH A . 
G 5 HOH   56 356 67  HOH   HOH A . 
G 5 HOH   57 357 44  HOH   HOH A . 
G 5 HOH   58 358 39  HOH   HOH A . 
G 5 HOH   59 359 30  HOH   HOH A . 
G 5 HOH   60 360 7   HOH   HOH A . 
G 5 HOH   61 361 20  HOH   HOH A . 
G 5 HOH   62 362 51  HOH   HOH A . 
G 5 HOH   63 363 21  HOH   HOH A . 
G 5 HOH   64 364 23  HOH   HOH A . 
G 5 HOH   65 365 68  HOH   HOH A . 
G 5 HOH   66 366 2   HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HUX 
_cell.length_a           73.146 
_cell.length_b           61.404 
_cell.length_c           32.665 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.58 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HUX 
_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          7HUX 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.31 
_exptl_crystal.density_percent_sol   46.65 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-10-10 
_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   0.92209 
_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        0.92209 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.00 
_reflns.d_resolution_high            1.89 
_reflns.number_obs                   11618 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.254 
_reflns.pdbx_netI_over_sigmaI        4.0 
_reflns.pdbx_redundancy              6.9 
_reflns.pdbx_Rrim_I_all              0.275 
_reflns.pdbx_Rpim_I_all              0.104 
_reflns.pdbx_CC_half                 0.989 
_reflns.pdbx_number_measured_all     80584 
_reflns.pdbx_chi_squared             0.32 
_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                  1.89 
_reflns_shell.d_res_low                   1.93 
_reflns_shell.number_measured_all         5260 
_reflns_shell.number_unique_obs           740 
_reflns_shell.Rmerge_I_obs                2.221 
_reflns_shell.pdbx_chi_squared            0.20 
_reflns_shell.pdbx_redundancy             7.1 
_reflns_shell.percent_possible_obs        99.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             2.399 
_reflns_shell.pdbx_Rpim_I_all             0.899 
_reflns_shell.pdbx_CC_half                0.323 
_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                                 7HUX 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     11535 
_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                             47.01 
_refine.ls_d_res_high                            1.891 
_refine.ls_percent_reflns_obs                    99.3 
_refine.ls_R_factor_obs                          0.2402 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2378 
_refine.ls_R_factor_R_free                       0.2950 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.510 
_refine.ls_number_reflns_R_free                  520 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.933 
_refine.correlation_coeff_Fo_to_Fc_free          0.891 
_refine.B_iso_mean                               33.56 
_refine.aniso_B[1][1]                            -0.24830 
_refine.aniso_B[2][2]                            4.63120 
_refine.aniso_B[3][3]                            -4.38290 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            5.11970 
_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             0.186 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.178 
_refine.pdbx_overall_SU_R_Blow_DPI               0.188 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.178 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HUX 
_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         31 
_refine_hist.number_atoms_solvent             66 
_refine_hist.number_atoms_total               1171 
_refine_hist.d_res_high                       1.891 
_refine_hist.d_res_low                        47.01 
# 
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                  0.008 ? 2.00  1137 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.90  ? 2.00  1546 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  376  '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  210  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1134 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.59  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.41 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  868  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   27 
_refine_ls_shell.d_res_high                       1.89 
_refine_ls_shell.d_res_low                        1.92 
_refine_ls_shell.number_reflns_R_work             423 
_refine_ls_shell.R_factor_R_work                  0.3943 
_refine_ls_shell.percent_reflns_obs               92.40 
_refine_ls_shell.R_factor_R_free                  0.3133 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.73 
_refine_ls_shell.number_reflns_R_free             21 
_refine_ls_shell.number_reflns_all                444 
_refine_ls_shell.R_factor_all                     0.3907 
# 
_struct.entry_id                  7HUX 
_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-0031970-001 (A71EV2A-x3225)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUX 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G 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              7HUX 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 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 ? ? ? ? ? ? ? 2.354 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.453 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
# 
_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_555 108.4 ? 
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_555 104.6 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.8 ? 
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_555 112.0 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.5 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 29  ? N ASP A 35  O LEU A 34  ? O LEU A 40  
AA1 2 3 N SER A 37  ? N SER A 43  O ARG A 10  ? O ARG A 16  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O GLY A 116 ? O GLY A 122 
AA2 4 5 N ILE A 117 ? N ILE A 123 O ALA A 129 ? O ALA A 135 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HUX 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -136.00 
_pdbx_validate_torsion.psi             -34.19 
# 
_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         15.2997 
_pdbx_refine_tls.origin_y         7.1415 
_pdbx_refine_tls.origin_z         14.2870 
_pdbx_refine_tls.T[1][1]          0.0375 
_pdbx_refine_tls.T[2][2]          0.0046 
_pdbx_refine_tls.T[3][3]          -0.2220 
_pdbx_refine_tls.T[1][2]          -0.0100 
_pdbx_refine_tls.T[1][3]          0.0788 
_pdbx_refine_tls.T[2][3]          -0.0115 
_pdbx_refine_tls.L[1][1]          0.7857 
_pdbx_refine_tls.L[2][2]          3.8485 
_pdbx_refine_tls.L[3][3]          1.4626 
_pdbx_refine_tls.L[1][2]          1.2942 
_pdbx_refine_tls.L[1][3]          -0.3304 
_pdbx_refine_tls.L[2][3]          -1.3063 
_pdbx_refine_tls.S[1][1]          -0.0536 
_pdbx_refine_tls.S[1][2]          0.0286 
_pdbx_refine_tls.S[1][3]          0.0105 
_pdbx_refine_tls.S[2][1]          0.0576 
_pdbx_refine_tls.S[2][2]          0.0591 
_pdbx_refine_tls.S[2][3]          -0.0940 
_pdbx_refine_tls.S[3][1]          -0.0377 
_pdbx_refine_tls.S[3][2]          -0.0767 
_pdbx_refine_tls.S[3][3]          -0.0056 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
6 1 N 0 A DMS 203 ? D DMS ?   
# 
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 
A1BRL N1   N  Y N 1   
A1BRL N3   N  N N 2   
A1BRL C4   C  Y N 3   
A1BRL C5   C  Y N 4   
A1BRL C6   C  Y N 5   
A1BRL C7   C  Y N 6   
A1BRL C8   C  N N 7   
A1BRL C10  C  N N 8   
A1BRL C13  C  N S 9   
A1BRL C15  C  N N 10  
A1BRL O1   O  N N 11  
A1BRL C14  C  N N 12  
A1BRL C12  C  N N 13  
A1BRL C11  C  N N 14  
A1BRL N2   N  N N 15  
A1BRL C9   C  N N 16  
A1BRL O    O  N N 17  
A1BRL C1   C  Y N 18  
A1BRL C    C  N N 19  
A1BRL C2   C  Y N 20  
A1BRL N    N  Y N 21  
A1BRL C3   C  Y N 22  
A1BRL H17  H  N N 23  
A1BRL H16  H  N N 24  
A1BRL H5   H  N N 25  
A1BRL H6   H  N N 26  
A1BRL H7   H  N N 27  
A1BRL H8   H  N N 28  
A1BRL H9   H  N N 29  
A1BRL H10  H  N N 30  
A1BRL H11  H  N N 31  
A1BRL H    H  N N 32  
A1BRL H18  H  N N 33  
A1BRL H19  H  N N 34  
A1BRL H14  H  N N 35  
A1BRL H15  H  N N 36  
A1BRL H12  H  N N 37  
A1BRL H13  H  N N 38  
A1BRL H2   H  N N 39  
A1BRL H3   H  N N 40  
A1BRL H1   H  N N 41  
A1BRL H4   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
DMS   S    S  N N 130 
DMS   O    O  N N 131 
DMS   C1   C  N N 132 
DMS   C2   C  N N 133 
DMS   H11  H  N N 134 
DMS   H12  H  N N 135 
DMS   H13  H  N N 136 
DMS   H21  H  N N 137 
DMS   H22  H  N N 138 
DMS   H23  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
THR   N    N  N N 356 
THR   CA   C  N S 357 
THR   C    C  N N 358 
THR   O    O  N N 359 
THR   CB   C  N R 360 
THR   OG1  O  N N 361 
THR   CG2  C  N N 362 
THR   OXT  O  N N 363 
THR   H    H  N N 364 
THR   H2   H  N N 365 
THR   HA   H  N N 366 
THR   HB   H  N N 367 
THR   HG1  H  N N 368 
THR   HG21 H  N N 369 
THR   HG22 H  N N 370 
THR   HG23 H  N N 371 
THR   HXT  H  N N 372 
TRP   N    N  N N 373 
TRP   CA   C  N S 374 
TRP   C    C  N N 375 
TRP   O    O  N N 376 
TRP   CB   C  N N 377 
TRP   CG   C  Y N 378 
TRP   CD1  C  Y N 379 
TRP   CD2  C  Y N 380 
TRP   NE1  N  Y N 381 
TRP   CE2  C  Y N 382 
TRP   CE3  C  Y N 383 
TRP   CZ2  C  Y N 384 
TRP   CZ3  C  Y N 385 
TRP   CH2  C  Y N 386 
TRP   OXT  O  N N 387 
TRP   H    H  N N 388 
TRP   H2   H  N N 389 
TRP   HA   H  N N 390 
TRP   HB2  H  N N 391 
TRP   HB3  H  N N 392 
TRP   HD1  H  N N 393 
TRP   HE1  H  N N 394 
TRP   HE3  H  N N 395 
TRP   HZ2  H  N N 396 
TRP   HZ3  H  N N 397 
TRP   HH2  H  N N 398 
TRP   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
ZN    ZN   ZN N N 443 
# 
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 
A1BRL C   C1   sing N N 1   
A1BRL C1  N    doub Y N 2   
A1BRL N   C2   sing Y N 3   
A1BRL C2  C3   doub Y N 4   
A1BRL C3  C4   sing Y N 5   
A1BRL C4  C5   doub Y N 6   
A1BRL C5  C6   sing Y N 7   
A1BRL C6  C7   doub Y N 8   
A1BRL C2  C7   sing Y N 9   
A1BRL C7  N1   sing Y N 10  
A1BRL C1  N1   sing Y N 11  
A1BRL N1  C8   sing N N 12  
A1BRL C8  C9   sing N N 13  
A1BRL O   C9   doub N N 14  
A1BRL C9  N2   sing N N 15  
A1BRL N2  C10  sing N N 16  
A1BRL C10 C11  sing N N 17  
A1BRL C11 C12  sing N N 18  
A1BRL C12 C13  sing N N 19  
A1BRL C13 C14  sing N N 20  
A1BRL N3  C14  sing N N 21  
A1BRL C14 O1   doub N N 22  
A1BRL C15 C13  sing N N 23  
A1BRL N2  C15  sing N N 24  
A1BRL N3  H17  sing N N 25  
A1BRL N3  H16  sing N N 26  
A1BRL C4  H5   sing N N 27  
A1BRL C5  H6   sing N N 28  
A1BRL C6  H7   sing N N 29  
A1BRL C8  H8   sing N N 30  
A1BRL C8  H9   sing N N 31  
A1BRL C10 H10  sing N N 32  
A1BRL C10 H11  sing N N 33  
A1BRL C13 H    sing N N 34  
A1BRL C15 H18  sing N N 35  
A1BRL C15 H19  sing N N 36  
A1BRL C12 H14  sing N N 37  
A1BRL C12 H15  sing N N 38  
A1BRL C11 H12  sing N N 39  
A1BRL C11 H13  sing N N 40  
A1BRL C   H2   sing N N 41  
A1BRL C   H3   sing N N 42  
A1BRL C   H1   sing N N 43  
A1BRL C3  H4   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
DMS   S   O    doub N N 127 
DMS   S   C1   sing N N 128 
DMS   S   C2   sing N N 129 
DMS   C1  H11  sing N N 130 
DMS   C1  H12  sing N N 131 
DMS   C1  H13  sing N N 132 
DMS   C2  H21  sing N N 133 
DMS   C2  H22  sing N N 134 
DMS   C2  H23  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HUX 
_atom_sites.fract_transf_matrix[1][1]   0.013671 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000616 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016286 
_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]   0.030645 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.232 6.626   24.390 1.00 38.40 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.354 6.725   23.451 1.00 38.89 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.355 5.576   22.402 1.00 38.10 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.577 4.613   22.519 1.00 38.26 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.677 6.805   24.216 1.00 40.80 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.761 5.788   25.201 1.00 43.59 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.192 5.708   21.375 1.00 36.78 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.294 4.708   20.321 1.00 36.28 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.674 5.255   18.954 1.00 35.01 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.395 6.418   18.632 1.00 34.42 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.317 4.411   18.136 1.00 33.95 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.759 4.820   16.805 1.00 33.81 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.798 3.646   15.812 1.00 33.05 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.877 2.482   16.217 1.00 32.95 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.138 5.462   16.895 1.00 33.96 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.740 3.964   14.510 1.00 32.18 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.842 3.000   13.420 1.00 31.66 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.224 3.179   12.813 1.00 31.87 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.638 4.303   12.500 1.00 31.68 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.753 3.229   12.344 1.00 31.77 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.338 3.155   12.920 1.00 31.79 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.929 2.241   11.169 1.00 32.64 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.309 3.722   11.962 1.00 32.73 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.958 2.081   12.680 1.00 32.18 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.291 2.128   12.120 1.00 33.05 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.307 1.392   10.802 1.00 34.42 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.376 0.168   10.810 1.00 35.44 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.280 1.515   13.113 1.00 33.03 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.481 2.391   14.323 1.00 33.55 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.347 3.471   14.284 1.00 34.74 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.746 2.190   15.481 1.00 34.38 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.522 4.298   15.386 1.00 35.10 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.888 3.029   16.580 1.00 35.22 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.785 4.078   16.528 1.00 35.81 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.962 4.899   17.604 1.00 37.52 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.232 2.127   9.671  1.00 34.37 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.249 1.564   8.311  1.00 34.52 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.408 2.154   7.507  1.00 35.05 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.514 3.382   7.371  1.00 35.90 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.882 1.713   7.589  1.00 34.66 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.455 3.172   7.475  1.00 35.09 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.898 1.047   6.230  1.00 35.33 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.305 1.289   7.031  1.00 34.46 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.479 1.700   6.269  1.00 35.13 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.336 2.703   7.015  1.00 35.82 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.763 2.423   8.133  1.00 36.61 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.562 3.889   6.436  1.00 35.47 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.314 4.926   7.142  1.00 35.82 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.416 6.019   7.716  1.00 34.96 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.854 7.155   7.889  1.00 34.08 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.421 5.491   6.290  1.00 37.91 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.580 4.533   6.239  1.00 43.71 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.302 4.349   7.229  1.00 46.08 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.757 3.873   5.106  1.00 44.43 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.169 5.657   8.066  1.00 34.37 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.229 6.616   8.627  1.00 33.60 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.690 6.163   9.966  1.00 32.48 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.546 4.963   10.229 1.00 32.73 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.041 6.837   7.668  1.00 33.64 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.421 7.326   6.289  1.00 34.23 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.070 8.541   6.113  1.00 35.10 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.094 6.592   5.155  1.00 35.18 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.401 9.002   4.844  1.00 36.02 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.419 7.042   3.884  1.00 36.20 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.073 8.249   3.730  1.00 37.19 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.381 8.694   2.468  1.00 38.84 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.366 7.143   10.809 1.00 30.58 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.701 6.945   12.080 1.00 29.23 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.402 7.774   11.993 1.00 28.33 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.444 8.937   11.601 1.00 28.19 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.607 7.401   13.247 1.00 30.32 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.894 7.749   14.564 1.00 32.04 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.884 7.828   15.711 1.00 35.22 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.591 8.927   16.635 1.00 38.29 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.054 8.772   17.844 1.00 38.76 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.750 7.558   18.292 1.00 37.14 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.816 9.832   18.615 1.00 37.32 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.258 7.171   12.290 1.00 27.94 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.976 7.877   12.248 1.00 27.72 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.468 7.980   13.676 1.00 28.25 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.262 6.948   14.325 1.00 29.64 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.943 7.125   11.368 1.00 27.42 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.637 7.917   11.262 1.00 27.14 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.516 6.822   9.981  1.00 27.31 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.250 9.192   14.161 1.00 26.90 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.739 9.439   15.511 1.00 27.26 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.537 10.388  15.450 1.00 26.78 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.339 11.087  14.443 1.00 26.69 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.826 10.059  16.445 1.00 28.16 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.953 9.091   16.720 1.00 29.17 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.351 11.387  15.902 1.00 28.25 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.766 10.495  16.563 1.00 25.80 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.712 11.510  16.670 1.00 25.65 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.452 12.858  16.671 1.00 26.42 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.473 12.989  17.345 1.00 27.14 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.938 11.373  17.996 1.00 25.80 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.036 10.163  18.064 1.00 29.00 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.450 9.064   18.474 1.00 30.00 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.785 10.332  17.678 1.00 28.87 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.014 13.807  15.865 1.00 26.16 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.675 15.110  15.781 1.00 25.97 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.761 15.809  17.157 1.00 26.84 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.803 16.386  17.488 1.00 27.29 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.989 15.984  14.720 1.00 24.90 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.748 17.232  14.304 1.00 24.48 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.749 18.170  13.689 1.00 25.02 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.350 19.389  13.129 1.00 26.69 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.481 20.534  13.785 1.00 27.96 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.102 20.627  15.054 1.00 27.09 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.011 21.594  13.184 1.00 27.26 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.701 15.702  17.988 1.00 27.19 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.710 16.346  19.310 1.00 28.29 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.725 15.742  20.303 1.00 29.04 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.049 16.383  21.286 1.00 28.56 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.298 16.420  19.937 1.00 29.30 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.779 15.129  20.487 1.00 29.96 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.058 14.241  19.690 1.00 31.37 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.860 14.626  21.743 1.00 30.54 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.753 13.218  20.481 1.00 32.09 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.206 13.404  21.727 1.00 31.62 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.285 14.569  19.991 1.00 29.55 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.278 13.927  20.842 1.00 30.38 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.707 13.912  20.224 1.00 32.10 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.619 13.363  20.835 1.00 32.55 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.817 12.502  21.175 1.00 29.66 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.475 12.397  21.896 1.00 30.15 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.065 10.959  22.078 1.00 30.98 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.519 13.080  23.259 1.00 30.02 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.909 14.520  19.041 1.00 32.60 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.223 14.526  18.399 1.00 33.38 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.302 15.212  19.226 1.00 34.57 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.078 16.274  19.804 1.00 34.93 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.142 15.139  17.000 1.00 33.27 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.476 14.598  19.264 1.00 34.82 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.619 15.061  20.041 1.00 35.91 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.468 16.133  19.297 1.00 36.64 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.182 16.444  18.142 1.00 37.00 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.477 13.828  20.453 1.00 37.35 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.234 13.397  19.324 1.00 39.14 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.653 12.676  21.036 1.00 37.71 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.534 16.661  19.935 1.00 37.07 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.443 17.588  19.282 1.00 38.01 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.145 16.890  18.111 1.00 37.66 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.279 17.489  17.050 1.00 37.84 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.468 18.148  20.270 1.00 40.04 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.864 19.097  21.258 1.00 44.97 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.260 20.278  20.850 1.00 47.40 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.778 19.005  22.609 1.00 46.60 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.824 20.856  21.959 1.00 48.12 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.113 20.128  23.041 1.00 48.05 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.540 15.611  18.287 1.00 36.85 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.195 14.829  17.238 1.00 36.37 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.267 14.646  16.032 1.00 33.89 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.723 14.755  14.900 1.00 32.79 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.705 13.479  17.791 1.00 39.45 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.279 12.520  16.747 1.00 45.05 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.487 12.517  16.463 1.00 46.80 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.428 11.664  16.168 1.00 45.92 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.967 14.406  16.271 1.00 32.86 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.984 14.264  15.199 1.00 31.86 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.878 15.552  14.345 1.00 31.76 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.881 15.467  13.123 1.00 31.48 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.612 13.888  15.775 1.00 32.73 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.496 12.457  16.286 1.00 35.88 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.139 11.562  15.702 1.00 35.82 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.758 12.238  17.265 1.00 37.46 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.808 16.735  14.974 1.00 31.77 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.732 18.010  14.243 1.00 32.05 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.042 18.361  13.559 1.00 33.13 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.024 18.922  12.472 1.00 33.59 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.267 19.170  15.145 1.00 31.31 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.786 19.206  15.366 1.00 31.06 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.107 18.704  16.434 1.00 31.57 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.796 19.735  14.471 1.00 30.71 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.757 18.899  16.270 1.00 31.71 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.538 19.534  15.074 1.00 31.30 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.852 20.366  13.225 1.00 31.12 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.347 19.911  14.457 1.00 31.38 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.670 20.759  12.628 1.00 31.69 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.436 20.524  13.241 1.00 31.60 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.181 18.027  14.186 1.00 33.40 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.493 18.272  13.593 1.00 33.99 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.762 17.361  12.386 1.00 34.31 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.706 17.626  11.653 1.00 34.86 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.598 18.082  14.639 1.00 34.11 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.982 16.261  12.202 1.00 34.01 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.137 15.340  11.067 1.00 34.18 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.775 15.129  10.360 1.00 33.59 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.445 14.017  9.961  1.00 32.79 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.692 14.002  11.550 1.00 35.74 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.103 14.087  12.079 1.00 39.49 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.075 14.234  11.323 1.00 40.87 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.244 13.978  13.390 1.00 40.09 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.984 16.217  10.253 1.00 33.39 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.652 16.265  9.684  1.00 32.78 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.654 15.876  8.239  1.00 33.02 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.432 16.429  7.463  1.00 34.16 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.095 17.701  9.802  1.00 32.51 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.682 17.931  9.248  1.00 32.82 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.661 17.112  10.020 1.00 33.14 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.304 19.407  9.294  1.00 32.84 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.755 14.954  7.865  1.00 31.94 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.530 14.533  6.493  1.00 31.31 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.195 15.167  6.054  1.00 31.39 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.126 15.821  5.025  1.00 31.65 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.489 12.989  6.374  1.00 31.37 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.027 12.558  4.983  1.00 32.00 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.827 12.360  6.737  1.00 31.21 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.147 15.001  6.874  1.00 31.01 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.809 15.494  6.597  1.00 30.24 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.995 15.578  7.907  1.00 28.26 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.165 14.765  8.808  1.00 27.52 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.130 14.537  5.598  1.00 30.92 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.661 14.777  5.381  1.00 32.14 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.092 15.711  4.567  1.00 33.25 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.580 14.063  5.989  1.00 32.17 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.725 15.632  4.643  1.00 33.49 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.383 14.614  5.492  1.00 33.05 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.507 12.993  6.888  1.00 32.38 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.132 14.107  5.835  1.00 33.54 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.266 12.515  7.246  1.00 33.19 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.096 13.078  6.732  1.00 33.37 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.153 16.593  8.024  1.00 27.15 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.265 16.726  9.169  1.00 26.86 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.935 17.275  8.691  1.00 27.08 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.905 18.063  7.742  1.00 26.29 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.882 17.565  10.326 1.00 27.35 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.395 18.954  9.939  1.00 28.77 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.354 20.058  9.825  1.00 27.98 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.536 20.974  8.991  1.00 33.46 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.323 19.973  10.522 1.00 23.85 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.835 16.888  9.369  1.00 27.49 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.503 17.396  9.049  1.00 27.44 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.670 17.572  10.328 1.00 26.44 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.155 16.593  10.849 1.00 26.68 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.803 16.475  8.051  1.00 29.30 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.650 17.096  7.295  1.00 33.52 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.008 18.021  7.838  1.00 33.33 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.384 16.651  6.166  1.00 37.06 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.527 18.820  10.805 1.00 25.33 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.759 19.168  12.000 0.50 25.81 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.764 19.118  12.020 0.50 25.89 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.304 18.681  11.904 1.00 25.92 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.747 18.173  12.883 1.00 25.73 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.786 20.679  12.210 0.50 26.30 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.859 20.596  12.389 0.50 26.60 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.666 21.016  13.578 0.50 27.91 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.205 21.406  11.428 0.50 28.70 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.700 18.813  10.706 1.00 24.94 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.321 18.372  10.517 1.00 25.04 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.172 16.852  10.644 1.00 24.08 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.086 16.396  10.948 1.00 24.03 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.735 18.893  9.207  1.00 26.88 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.193 18.142  8.095  1.00 29.93 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.259 16.072  10.499 1.00 23.13 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.192 14.616  10.676 1.00 23.17 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.815 14.131  12.006 1.00 23.99 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.746 12.933  12.294 1.00 24.99 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.906 13.898  9.511  1.00 23.20 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.187 14.024  8.175  1.00 22.19 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.962 13.426  7.037  1.00 23.83 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.023 11.966  7.128  1.00 25.45 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.256 11.159  6.101  1.00 27.35 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.436 11.657  4.880  1.00 27.70 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.295 9.843   6.280  1.00 27.24 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.467 15.038  12.781 1.00 23.71 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.210 14.732  14.000 1.00 23.05 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.322 13.724  13.655 1.00 23.52 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.560 12.789  14.422 1.00 23.72 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.298 14.220  15.152 1.00 23.18 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.027 13.962  16.464 1.00 23.38 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.861 14.811  16.859 1.00 22.39 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.803 12.879  17.069 1.00 24.97 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.005 13.898  12.499 1.00 23.93 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.105 12.992  12.116 1.00 25.02 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.387 13.747  11.869 1.00 25.48 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.375 14.851  11.354 1.00 26.02 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.821 12.209  10.821 1.00 24.78 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.818 11.060  10.841 1.00 25.76 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.807 10.373  9.491  1.00 25.91 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.087 10.088  11.984 1.00 25.18 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.494 13.101  12.165 1.00 25.27 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.829 13.602  11.891 1.00 25.34 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.667 12.377  11.460 1.00 25.82 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.446 11.255  11.917 1.00 26.21 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.461 14.358  13.108 1.00 25.20 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.837 15.014  12.836 1.00 26.09 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.956 16.376  13.486 1.00 27.21 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.986 14.120  13.289 1.00 26.65 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.546 12.575  10.499 1.00 26.05 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.447 11.548  10.023 1.00 26.92 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.860 12.141  10.091 1.00 27.99 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.083 13.261  9.640  1.00 28.03 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.085 11.064  8.584  1.00 27.16 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.142 10.105  8.024  1.00 27.30 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.699 10.429  8.539  1.00 27.21 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.796 11.408  10.677 1.00 29.10 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.188 11.838  10.738 1.00 30.51 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.095 10.725  10.184 1.00 32.53 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.667 9.573   10.068 1.00 32.17 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.589 12.244  12.157 1.00 30.76 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.362 11.215  13.105 1.00 33.80 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.345 11.070  9.842  1.00 34.22 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.265 10.094  9.287  1.00 36.61 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.082 9.389   10.362 1.00 39.00 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.377 9.968   11.413 1.00 39.43 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.184 10.749  8.262  1.00 37.73 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.855 11.839  8.861  1.00 40.39 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.463 8.136   10.082 1.00 40.18 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.270 7.316   10.984 1.00 42.10 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.504 6.786   10.266 1.00 44.93 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.502 6.630   9.043  1.00 45.28 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.449 6.138   11.562 1.00 42.72 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.312 5.114   10.577 1.00 44.11 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.076 6.559   12.072 1.00 41.99 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.547 6.482   11.026 1.00 46.81 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.762 5.890   10.465 1.00 48.73 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.604 4.345   10.435 1.00 50.33 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.051 3.697   9.489  1.00 50.56 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.019 6.375   11.221 1.00 50.18 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.788 6.314   12.633 1.00 51.15 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.419 7.796   10.838 1.00 50.74 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.944 3.766   11.449 1.00 51.11 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.706 2.323   11.483 1.00 52.31 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.483 1.958   10.629 1.00 53.39 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.612 2.799   10.415 1.00 53.35 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.520 1.853   12.918 1.00 52.33 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.417 0.707   10.138 1.00 54.35 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.312 0.255   9.284  1.00 55.45 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.103 -0.265  10.073 1.00 55.40 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.267 -1.037  11.012 1.00 56.27 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.795 -0.829  8.312  1.00 58.13 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.075 -0.792  6.970  1.00 64.08 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.619 0.296   6.068  1.00 70.72 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.783 0.705   6.180  1.00 73.03 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.793 0.790   5.143  1.00 71.44 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.904 0.131   9.647  1.00 54.18 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.634 -0.273  10.240 1.00 53.22 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.001 -1.437  9.502  1.00 51.84 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.043 -1.500  8.274  1.00 51.71 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.381 -2.348  10.240 1.00 50.90 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.807 -3.551  9.658  1.00 50.32 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.276 -3.658  9.763  1.00 48.54 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.742 -4.744  9.507  1.00 49.19 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.487 -4.780  10.249 1.00 51.95 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.294 -4.761  10.114 1.00 58.01 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.567 -2.564  10.104 1.00 45.96 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.102 -2.604  10.152 1.00 44.48 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.548 -2.632  8.727  1.00 42.33 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.079 -1.970  7.839  1.00 42.66 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.520 -1.375  10.889 1.00 46.58 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.474 -1.508  12.391 1.00 51.06 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.207 -2.621  12.874 1.00 53.15 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.690 -0.491  13.083 1.00 51.47 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.469 -3.376  8.511  1.00 40.42 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.840 -3.464  7.195  1.00 38.67 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.582 -2.622  7.209  1.00 35.98 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.729 -2.829  8.068  1.00 35.59 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.487 -4.921  6.862  1.00 39.77 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.706 -5.654  6.695  1.00 40.66 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.613 -5.036  5.606  1.00 40.00 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.456 -1.695  6.264  1.00 33.77 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.275 -0.847  6.179  1.00 32.16 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.209 -1.561  5.343  1.00 31.00 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.529 -2.147  4.318  1.00 30.54 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.627 0.577   5.639  1.00 32.06 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.831 1.171   6.400  1.00 33.03 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.419 1.523   5.695  1.00 31.43 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.626 1.293   7.920  1.00 33.98 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.970 -1.602  5.834  1.00 30.23 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.886 -2.222  5.087  1.00 30.03 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.535 -1.283  3.917  1.00 29.81 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.570 -0.062  4.049  1.00 29.40 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.669 -2.421  5.984  1.00 28.83 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.205 -1.858  2.782  1.00 30.22 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.790 -1.116  1.603  1.00 29.92 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.484 -1.787  1.265  1.00 30.52 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.494 -2.805  0.576  1.00 31.78 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.831 -1.249  0.492  1.00 30.29 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.205 -0.628  0.830  1.00 31.50 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.202 0.819   1.319  1.00 32.00 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.578 1.263   1.565  1.00 31.44 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.913 2.373   2.205  1.00 30.68 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.977 3.179   2.683  1.00 29.35 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.192 2.690   2.371  1.00 28.07 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.373 -1.287  1.839  1.00 30.03 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.068 -1.947  1.780  1.00 31.02 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.923  -0.980  2.198  1.00 32.16 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.171 0.157   2.614  1.00 31.63 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.112 -3.148  2.734  1.00 32.52 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.178 -2.697  4.511  1.00 37.67 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.675  -1.493  2.217  1.00 33.39 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.530  -0.754  2.747  1.00 34.74 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.813  -1.576  3.820  1.00 35.17 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.584  -1.561  3.885  1.00 35.99 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.562  -0.278  1.647  1.00 37.54 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.762  -1.356  0.950  1.00 44.06 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.097  -2.556  1.120  1.00 46.24 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.793  -1.007  0.239  1.00 46.85 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.590  -2.305  4.659  1.00 34.34 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.111  -3.127  5.775  1.00 32.99 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.317  -2.256  6.746  1.00 32.39 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.712  -1.122  7.009  1.00 32.55 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.296  -3.766  6.499  1.00 32.20 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.888  -5.318  5.783  1.00 31.04 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.228  -2.780  7.298  1.00 31.66 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.476  -2.057  8.332  1.00 31.41 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.413  -2.824  9.665  1.00 29.72 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.554  -2.537  10.480 1.00 29.51 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.079  -1.623  7.853  1.00 33.97 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.101  -0.423  6.898  1.00 38.06 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.714  0.145   6.698  1.00 42.09 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.156  0.104   5.599  1.00 45.04 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.117  0.675   7.760  1.00 40.79 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.271  -3.845  9.842  1.00 28.59 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.444  -4.644  11.053 1.00 28.55 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.958  -4.786  11.298 1.00 27.07 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.760  -4.794  10.361 1.00 27.00 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.752  -6.043  11.016 1.00 30.81 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.514  -6.948  10.204 1.00 32.14 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.281  -5.990  10.573 1.00 31.14 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.327  -4.909  12.555 1.00 25.75 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.725  -5.046  12.949 1.00 24.57 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.896  -5.124  14.455 1.00 23.58 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.922  -5.239  15.176 1.00 23.30 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.132 -5.040  14.947 1.00 23.24 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.455 -5.139  16.367 1.00 22.99 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.373 -3.987  16.766 1.00 23.59 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.386 -3.749  16.107 1.00 24.16 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.136 -6.506  16.636 1.00 22.55 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.535 -6.651  18.096 1.00 22.56 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.233 -7.662  16.199 1.00 22.78 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.045 -3.303  17.846 1.00 23.90 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.877 -2.212  18.335 1.00 23.69 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.450 -2.483  19.746 1.00 23.33 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.875 -3.247  20.509 1.00 23.36 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.137 -0.879  18.268 1.00 23.30 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.185 -0.624  19.420 1.00 23.39 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.898  -1.151  19.416 1.00 23.83 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.529 0.238   20.451 1.00 24.15 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.010  -0.898  20.458 1.00 24.75 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.651  0.498   21.504 1.00 24.86 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.389  -0.065  21.499 1.00 25.28 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.520  0.204   22.519 1.00 25.91 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.573 -1.848  20.078 1.00 23.07 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.166 -2.011  21.388 1.00 24.19 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.742 -0.851  22.288 1.00 24.28 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.833 0.306   21.877 1.00 24.52 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.688 -2.141  21.292 1.00 24.56 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.323 -2.244  22.657 1.00 25.39 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.147 -3.376  23.443 1.00 25.94 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.011 -1.174  23.204 1.00 26.21 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.723 -3.476  24.702 1.00 27.18 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.583 -1.256  24.465 1.00 27.18 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.419 -2.401  25.223 1.00 28.25 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.967 -2.467  26.477 1.00 29.62 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.258 -1.164  23.511 1.00 24.74 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.773 -0.176  24.469 1.00 25.03 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.682 -0.240  25.695 1.00 26.50 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.523 -1.138  26.517 1.00 26.36 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.317 -0.472  24.822 1.00 25.53 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.607 0.601   26.101 1.00 27.25 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.671 0.670   25.789 1.00 26.83 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.646 0.635   26.870 1.00 27.73 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.038 0.767   28.225 1.00 27.41 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.499 0.106   29.137 1.00 26.93 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.764 1.663   26.680 1.00 30.44 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.289 2.987   26.515 1.00 34.37 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.965 1.555   28.348 1.00 27.88 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.249 1.729   29.599 1.00 28.79 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.588 0.438   30.116 1.00 28.66 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.128 0.399   31.270 1.00 28.85 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.248 2.871   29.501 1.00 30.30 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.158 2.548   28.655 1.00 32.30 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.577 -0.620  29.304 1.00 27.46 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.078 -1.905  29.750 1.00 28.05 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.090 -3.042  29.519 1.00 29.47 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.753 -4.201  29.791 1.00 29.76 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.774 -2.227  29.025 1.00 28.94 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.635  -1.273  29.332 1.00 30.81 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.968  -1.608  30.661 1.00 31.50 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.745  -0.834  30.854 1.00 32.60 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.709  0.407   31.338 1.00 33.91 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.834  1.028   31.686 1.00 32.52 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.551  1.046   31.459 1.00 33.38 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.307 -2.730  28.974 1.00 30.03 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.332 -3.693  28.557 1.00 30.80 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.696 -4.854  27.735 1.00 30.76 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.988 -6.031  27.969 1.00 30.67 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.108 -4.227  29.750 1.00 32.08 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.095 -3.249  30.353 1.00 36.81 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.738 -3.917  31.547 1.00 41.42 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.299 -2.951  32.483 1.00 45.90 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.229 -3.059  33.811 1.00 47.88 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.581 -4.080  34.371 1.00 47.97 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.768 -2.127  34.587 1.00 45.73 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.778 -4.501  26.815 1.00 30.27 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.999 -5.478  26.049 1.00 30.43 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.704 -5.011  24.633 1.00 29.00 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.509 -3.820  24.376 1.00 27.79 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.634 -5.726  26.740 1.00 33.45 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.635 -6.762  27.845 1.00 39.11 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 10.295 -6.734  28.592 1.00 45.75 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 10.282 -7.630  29.819 1.00 50.74 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 11.151 -7.109  30.923 1.00 53.71 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.609 -5.986  23.738 1.00 28.43 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.242 -5.814  22.347 1.00 28.21 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.743 -6.096  22.264 1.00 29.03 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.251 -7.032  22.910 1.00 30.10 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.013 -6.805  21.473 1.00 28.05 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.495 -6.591  21.480 1.00 28.22 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.138 -5.912  20.445 1.00 29.58 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.416 -6.974  22.385 1.00 28.56 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.421 -5.912  20.760 1.00 29.60 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.637 -6.525  21.924 1.00 29.62 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.011 -5.267  21.511 1.00 28.46 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.562  -5.409  21.348 1.00 28.69 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.156  -5.454  19.875 1.00 28.11 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.574  -4.600  19.093 1.00 28.21 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.815  -4.232  22.023 1.00 28.60 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.889  -4.200  23.535 1.00 29.44 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.089  -5.033  24.312 1.00 30.37 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.732  -3.314  24.191 1.00 30.74 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.144  -4.996  25.710 1.00 31.36 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.784  -3.256  25.585 1.00 31.78 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.983  -4.093  26.341 1.00 32.53 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 8.054  -4.028  27.715 1.00 35.64 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.331  -6.437  19.474 1.00 27.85 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.851  -6.447  18.072 1.00 27.70 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.766  -5.372  17.924 1.00 28.46 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.939  -5.184  18.840 1.00 30.16 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.289  -7.856  17.881 1.00 27.97 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.934  -8.323  19.294 1.00 28.74 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.743  -7.527  20.290 1.00 26.87 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.810  -4.623  16.851 1.00 26.95 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.871  -3.535  16.622 1.00 26.93 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.347  -3.534  15.206 1.00 27.98 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.001  -3.980  14.259 1.00 28.72 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.492  -2.136  16.957 1.00 26.78 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.442  -1.843  18.447 1.00 27.35 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.909  -1.990  16.402 1.00 26.27 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.175  -2.964  15.051 1.00 28.16 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.596  -2.683  13.754 1.00 28.72 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.719  -1.141  13.668 1.00 28.74 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.420  -0.467  14.650 1.00 29.49 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.147  -3.140  13.727 1.00 30.20 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.540  -2.629  12.562 1.00 34.64 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.289  -0.596  12.591 1.00 28.27 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.513  0.841   12.508 1.00 28.33 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.979  1.460   11.224 1.00 29.55 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.765  0.763   10.232 1.00 30.31 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.997  1.193   12.744 1.00 28.13 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.978  0.502   11.820 1.00 28.56 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.448  -0.772  12.106 1.00 29.31 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.428  1.125   10.669 1.00 28.90 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.369  -1.393  11.268 1.00 29.52 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.358  0.506   9.843  1.00 29.57 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.811  -0.754  10.140 1.00 29.30 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.750  2.783   11.245 1.00 29.19 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.223  3.469   10.081 1.00 29.54 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.331  3.846   9.068  1.00 29.11 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.521  3.758   9.390  1.00 29.01 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.433  4.696   10.520 1.00 31.41 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.290  5.645   11.125 1.00 33.71 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.926  4.217   7.830  1.00 28.66 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.826  4.648   6.767  1.00 28.82 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.432  6.016   7.141  1.00 28.39 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.733  6.851   7.701  1.00 28.58 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.063  4.722   5.419  1.00 30.89 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.640  3.335   4.897  1.00 35.58 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.502  3.238   3.359  1.00 40.94 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.522  1.781   2.922  1.00 45.17 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.728  1.531   1.681  1.00 47.57 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.725  6.260   6.870  1.00 28.12 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.331  7.551   7.270  1.00 28.31 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.563  8.779   6.768  1.00 28.88 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.227  8.862   5.577  1.00 28.92 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.774  7.467   6.745  1.00 29.09 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.787  6.320   5.780  1.00 29.81 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.710  5.369   6.229  1.00 28.00 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.257  9.718   7.686  1.00 28.86 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.446  10.877  7.343  1.00 30.36 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.733  12.138  8.207  1.00 31.18 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.640  12.127  9.029  1.00 32.12 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.965  10.488  7.380  1.00 32.67 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.534  10.289  8.714  1.00 36.80 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.992  13.237  7.970  1.00 31.14 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.112  14.489  8.699  1.00 32.05 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.194  14.363  9.886  1.00 33.66 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.992  14.168  9.707  1.00 33.83 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.588  15.648  7.839  1.00 32.10 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.568  16.603  7.189  1.00 33.06 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.812  17.802  6.625  1.00 34.06 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.630  17.071  8.142  1.00 32.76 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.742  14.453  11.096 1.00 34.51 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.954  14.311  12.308 1.00 35.84 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.294  15.448  13.266 1.00 37.60 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.464  15.800  13.409 1.00 37.38 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.234  12.908  12.927 1.00 36.04 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.666  11.784  12.046 1.00 36.86 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.714  12.785  14.352 1.00 36.26 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.298  10.505  12.261 1.00 38.27 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.278  16.021  13.927 1.00 38.96 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.510  17.089  14.890 1.00 40.69 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.138  16.542  16.196 1.00 41.14 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.621  15.603  16.797 1.00 41.33 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.213  17.856  15.169 1.00 41.36 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.454  19.149  15.898 1.00 42.50 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 2.028  20.227  15.253 1.00 43.83 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.149  19.271  17.239 1.00 43.52 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.265  21.416  15.931 1.00 44.87 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.370  20.465  17.910 1.00 44.70 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.928  21.529  17.254 1.00 44.70 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.278  17.109  16.596 1.00 40.78 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.018  16.687  17.773 1.00 41.01 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.065  17.853  18.755 1.00 41.93 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.507  18.952  18.398 1.00 42.35 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.453  16.220  17.379 1.00 41.19 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.308  15.935  18.610 1.00 41.25 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.419  15.008  16.450 1.00 41.17 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.599  17.610  19.995 1.00 42.13 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.555  18.579  21.086 1.00 42.16 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.910  19.208  21.385 1.00 41.48 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.941  18.552  21.253 1.00 40.79 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.003  17.907  22.348 1.00 46.09 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.529  17.568  22.255 1.00 53.89 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.658  18.788  22.038 1.00 65.04 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.547  19.611  22.976 1.00 68.07 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.108  18.937  20.921 1.00 68.20 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.906  20.475  21.806 1.00 41.72 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.116  21.234  22.137 1.00 42.32 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.013  20.534  23.155 1.00 42.91 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.514  19.779  23.986 1.00 43.78 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.729  22.601  22.676 1.00 42.19 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.319  20.822  23.123 1.00 42.40 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.299 20.275  24.057 1.00 42.78 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.511 21.237  24.194 1.00 44.19 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.543 22.301  23.563 1.00 44.37 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.735 18.871  23.621 1.00 43.54 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.806 18.862  22.690 1.00 44.47 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.502 20.874  25.031 1.00 44.91 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.725 21.678  25.223 1.00 45.58 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.627 21.692  23.973 1.00 44.10 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.532 22.511  23.866 1.00 44.19 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.551 21.143  26.417 1.00 49.74 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.736 20.509  27.531 1.00 58.46 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.724 18.990  27.543 1.00 68.06 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 14.627 18.399  28.182 1.00 71.04 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 12.801 18.392  26.940 1.00 69.51 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.413 20.759  23.054 1.00 42.78 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.216 20.623  21.849 1.00 41.45 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.570 21.281  20.635 1.00 40.23 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.266 21.696  19.707 1.00 40.32 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.411 19.129  21.562 1.00 41.38 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.986 18.368  22.736 1.00 42.55 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.325 18.495  23.082 1.00 43.66 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.187 17.548  23.519 1.00 42.94 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.865 17.783  24.143 1.00 44.28 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.713 16.843  24.590 1.00 43.79 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 17.056 16.958  24.896 1.00 45.10 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.598 16.254  25.943 1.00 47.16 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.245 21.284  20.587 1.00 38.77 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.512 21.799  19.444 1.00 38.00 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.270 22.503  19.902 1.00 38.85 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.589 22.008  20.806 1.00 39.08 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 12.003 20.624  18.565 1.00 36.54 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 13.073 19.748  17.969 1.00 35.04 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.867 20.203  16.926 1.00 34.81 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.255 18.444  18.407 1.00 34.46 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.855 19.401  16.373 1.00 34.89 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.231 17.627  17.853 1.00 34.68 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 15.028 18.108  16.831 1.00 34.73 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 16.010 17.328  16.279 1.00 33.68 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.846 23.551  19.175 1.00 38.94 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.511  24.118  19.450 1.00 39.24 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.431  23.160  18.879 1.00 39.30 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.771  22.199  18.167 1.00 39.09 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.539  25.433  18.674 1.00 39.84 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.439 25.122  17.484 1.00 39.86 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.497 24.191  18.009 1.00 38.24 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 7.141  23.407  19.172 1.00 39.09 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 6.076  22.552  18.625 1.00 39.24 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 6.039  22.706  17.079 1.00 39.18 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.899  23.811  16.534 1.00 39.63 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.729  22.891  19.248 1.00 39.30 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 6.216  21.584  16.386 1.00 37.91 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.312  21.581  14.945 1.00 36.52 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.767  20.256  14.360 1.00 36.48 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.364  19.354  15.100 1.00 36.72 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.810  21.750  14.602 1.00 35.68 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.601  20.475  14.917 1.00 35.31 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 10.086 20.658  15.123 1.00 34.99 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.876 19.498  14.689 1.00 34.90 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.897 18.320  15.304 1.00 34.49 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.676 17.343  14.855 1.00 31.77 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.146 18.112  16.380 1.00 34.56 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.814  20.121  13.023 1.00 36.14 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.448  18.887  12.352 1.00 35.62 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.742  18.180  12.014 1.00 33.68 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.541  18.731  11.267 1.00 34.64 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.750  19.183  11.024 1.00 36.57 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.299  19.585  11.152 1.00 38.48 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.289  18.633  11.138 1.00 39.85 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.935  20.921  11.235 1.00 39.77 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.950  19.001  11.217 1.00 41.37 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.602  21.301  11.313 1.00 41.16 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.613  20.339  11.302 1.00 42.67 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.697 20.739  11.347 1.00 45.29 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.965  16.982  12.550 1.00 31.03 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.127  16.194  12.180 1.00 28.83 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.759  15.392  10.919 1.00 28.01 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.666  14.815  10.838 1.00 28.67 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.533  15.260  13.327 1.00 28.72 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.761  14.400  13.049 1.00 28.77 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.424 13.953  14.335 1.00 30.00 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.570 14.712  15.302 1.00 28.43 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.842 12.703  14.363 1.00 31.82 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.653  15.348  9.938  1.00 26.25 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.422  14.575  8.709  1.00 25.58 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.062  13.169  8.821  1.00 24.92 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.865  12.908  9.748  1.00 23.73 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.972  15.324  7.496  1.00 26.83 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.373 15.525  7.608  1.00 29.21 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.671  12.264  7.891  1.00 24.52 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.170  10.896  7.810  1.00 24.78 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.059  10.144  9.165  1.00 24.95 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.991  9.439   9.550  1.00 25.06 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.608 10.893  7.263  1.00 25.25 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.726 11.531  5.915  1.00 29.03 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.723 10.772  4.753  1.00 31.24 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.796 12.839  5.575  1.00 29.98 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.833 11.636  3.758  1.00 31.45 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.856 12.888  4.199  1.00 31.02 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.927  10.348  9.901  1.00 24.75 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.668  9.754   11.214 1.00 25.03 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.623  8.645   11.109 1.00 24.67 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.669  8.768   10.347 1.00 24.37 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.184  10.826  12.212 1.00 25.30 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.209  10.445  13.694 1.00 26.82 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.620  10.152  14.164 1.00 27.17 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.537  11.519  14.562 1.00 27.22 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.831  7.560   11.849 1.00 24.17 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.961  6.378   11.857 1.00 24.91 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.468  6.083   13.276 1.00 25.49 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.297  5.919   14.179 1.00 25.71 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.762  5.171   11.320 1.00 25.25 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.360  5.447   9.922  1.00 26.50 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.363  4.122   9.237  1.00 28.89 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.604  3.993   10.427 1.00 18.55 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.134  6.032   13.493 1.00 25.07 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.639  5.733   14.836 1.00 24.86 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.251  4.271   15.015 1.00 24.77 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.771  3.616   14.076 1.00 24.04 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.496  6.669   15.279 1.00 24.56 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.803  8.188   15.289 1.00 26.24 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.634  8.993   15.887 1.00 26.21 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 4.061  8.503   16.023 1.00 26.49 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.461  3.776   16.241 1.00 25.11 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.085  2.445   16.691 1.00 26.05 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.465  2.557   18.096 1.00 27.31 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.774  3.484   18.846 1.00 27.81 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.313  1.540   16.739 1.00 25.70 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.584  1.618   18.451 1.00 27.30 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.012  1.572   19.785 1.00 27.70 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.041  0.801   20.587 1.00 28.45 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.358  -0.340  20.235 1.00 28.82 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.367 0.867   19.841 1.00 27.36 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.847 0.745   21.288 1.00 26.82 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.392 1.619   18.989 1.00 27.13 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.627  1.452   21.580 1.00 27.56 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.652  0.806   22.378 1.00 27.93 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.285  1.734   23.381 1.00 28.23 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.139  2.958   23.287 1.00 29.42 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.010  1.154   24.331 1.00 27.09 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.693  1.916   25.334 1.00 27.09 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.964  2.634   24.881 1.00 27.15 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.837  2.056   24.241 1.00 26.60 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.019  1.037   26.561 1.00 27.82 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.698  1.805   27.655 1.00 30.17 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 6.042  2.823   28.328 1.00 32.63 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.990  1.782   28.052 1.00 31.36 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.938  3.352   29.148 1.00 33.07 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.127  2.762   29.012 1.00 33.10 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.119  3.849   25.380 1.00 28.07 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.323  4.649   25.266 1.00 29.30 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.301  5.760   26.344 1.00 30.13 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.239  6.135   26.825 1.00 29.88 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.471  5.228   23.866 1.00 30.04 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 8.006  6.560   23.740 1.00 32.74 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.462  6.293   26.693 1.00 30.68 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.557  7.413   27.616 1.00 31.79 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.812 8.229   27.337 1.00 32.73 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.716 7.707   26.681 1.00 32.57 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.471  6.958   29.083 1.00 33.95 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.464 5.890   29.494 1.00 36.16 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 10.171 5.394   30.903 1.00 39.49 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.788 5.919   31.854 1.00 39.32 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.309  4.498   31.061 1.00 39.66 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.931 9.511   27.807 1.00 33.77 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.171 10.280  27.539 1.00 34.27 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.389 9.451   27.949 1.00 34.37 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.408 8.942   29.074 1.00 35.46 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.024 11.511  28.443 1.00 34.98 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.556 11.694  28.606 1.00 35.32 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.963  10.306  28.597 1.00 33.49 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.283 9.189   27.005 1.00 33.04 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.426 8.305   27.236 1.00 31.93 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.455 7.122   26.280 1.00 31.20 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.504 6.508   26.063 1.00 31.13 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.306 6.819   25.651 1.00 30.14 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.179 5.727   24.699 1.00 28.55 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.552 6.059   23.272 1.00 27.31 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.643 5.130   22.468 1.00 26.36 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.779 5.131   24.733 1.00 28.94 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.599 4.224   25.926 1.00 28.24 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.563 3.524   26.277 1.00 26.84 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.486 4.214   26.503 1.00 28.40 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.812 7.353   22.945 1.00 26.75 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.242 7.759   21.596 1.00 26.96 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.549 7.036   21.268 1.00 27.18 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.405 6.930   22.146 1.00 27.92 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.421 9.273   21.500 1.00 27.01 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.897 10.224  21.738 1.00 29.95 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.668 6.499   20.060 1.00 26.07 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.884 5.804   19.656 1.00 25.63 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.714 4.308   19.484 1.00 25.59 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.464 3.690   18.723 1.00 27.07 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.696 3.729   20.130 1.00 23.61 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.370 2.310   19.985 1.00 22.61 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.970 2.029   18.547 1.00 21.92 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.210 2.787   17.938 1.00 20.56 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.530 0.964   17.987 1.00 21.27 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.345 0.600   16.622 1.00 21.83 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.038 -0.148  16.418 1.00 22.56 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.631 -0.940  17.268 1.00 22.52 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.607 -0.209  16.179 1.00 22.36 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.808 0.718   15.892 1.00 22.56 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.341 -1.108  14.986 1.00 23.35 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.152 -0.060  15.630 1.00 23.06 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.372 0.151   15.300 1.00 22.70 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.203 -0.540  14.800 1.00 23.45 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.703 -1.396  13.605 1.00 24.19 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.431 -0.910  12.751 1.00 23.55 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.129 0.445   14.348 1.00 23.90 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.924 -0.197  13.619 1.00 24.67 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.167 -1.135  14.549 1.00 25.38 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.962  0.879   13.128 1.00 24.98 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.401 -2.686  13.610 1.00 25.15 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.884 -3.608  12.601 1.00 26.58 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.773 -4.456  12.081 1.00 28.45 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.940 -4.910  12.851 1.00 27.99 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.899 -4.587  13.197 1.00 28.46 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.242 -4.026  13.567 1.00 33.42 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.167 -5.169  13.951 1.00 37.75 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.616 -5.860  12.744 1.00 42.35 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.805 -5.680  12.171 1.00 44.78 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.718 -4.910  12.749 1.00 45.65 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.104 -6.308  11.041 1.00 44.24 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.822 -4.766  10.791 1.00 30.13 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.896 -5.706  10.168 1.00 31.52 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.752 -6.902  9.652  1.00 33.33 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.968 -6.929  9.899  1.00 33.30 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.160 -5.012  9.033  1.00 31.59 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.251 -4.485  7.692  1.00 32.66 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.150 -7.871  8.927  1.00 34.58 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.933 -8.992  8.373  1.00 36.62 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.047 -8.521  7.391  1.00 36.93 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.014 -9.249  7.166  1.00 37.18 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.013 -10.008 7.669  1.00 39.48 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.436 -9.481  6.361  1.00 45.06 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.451 -10.423 5.746  1.00 51.63 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.239  -10.181 5.768  1.00 54.74 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.952 -11.509 5.168  1.00 51.98 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.915 -7.307  6.829  1.00 36.34 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.885 -6.764  5.870  1.00 35.88 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.029 -5.952  6.486  1.00 34.54 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.960 -5.556  5.772  1.00 35.36 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.174 -5.920  4.801  1.00 37.12 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.045 -6.628  4.118  1.00 40.97 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.727 -6.319  4.397  1.00 43.26 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.073 -7.601  3.178  1.00 42.36 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.001 -7.077  3.588  1.00 43.33 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.767 -7.886  2.860  1.00 43.39 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.937 -5.672  7.780  1.00 32.53 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.955 -4.911  8.484  1.00 30.90 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.413 -3.714  9.227  1.00 28.43 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.261 -3.702  9.657  1.00 28.01 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.251 -2.690  9.358  1.00 27.19 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.968 -1.472  10.092 1.00 26.80 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.005 -0.553  9.362  1.00 26.10 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.286 -0.125  8.241  1.00 26.20 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.284 -0.761  10.476 1.00 27.53 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.000 0.588   11.115 1.00 28.20 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.117 -1.644  11.412 1.00 27.41 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.845 -0.294  9.984  1.00 24.41 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.801 0.570   9.433  1.00 23.90 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.990 2.040   9.904  1.00 24.01 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.756 2.990   9.146  1.00 23.99 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.425 0.039   9.895  1.00 23.22 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.308 0.962   9.440  1.00 22.48 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.198 -1.391  9.402  1.00 23.35 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.348 2.202   11.175 1.00 23.36 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.566 3.525   11.734 1.00 23.43 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.848 3.509   13.223 1.00 23.18 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.099 2.450   13.798 1.00 23.36 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.817 4.691   13.873 1.00 22.25 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.087 4.768   15.317 1.00 21.59 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 14.002 5.532   16.086 1.00 20.87 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.391 6.467   15.547 1.00 19.86 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.474 5.399   15.597 1.00 22.81 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.651 6.711   14.838 1.00 24.68 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.632 4.429   15.355 1.00 23.26 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.747 7.545   15.382 1.00 26.42 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.826 5.220   17.402 1.00 20.90 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.839 5.920   18.253 1.00 21.20 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.162 7.407   18.255 1.00 22.02 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.336 7.774   18.333 1.00 21.49 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.777 5.387   19.726 1.00 21.49 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.834 6.227   20.561 1.00 22.03 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.372 3.914   19.798 1.00 22.17 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.136 8.249   18.099 1.00 22.64 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.321 9.676   18.056 1.00 23.64 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.273 10.394  18.897 1.00 25.34 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.583 11.422  19.478 1.00 24.84 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.264 10.160  16.613 1.00 25.27 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.406 11.566  16.527 1.00 27.28 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.022 9.872   18.968 1.00 26.58 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.962  10.519  19.767 1.00 27.96 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.178  9.475   20.598 1.00 30.20 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.340  8.264   20.403 1.00 30.12 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.994  11.349  18.864 1.00 29.17 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.192  10.453  18.108 1.00 30.01 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.698  12.343  17.938 1.00 29.94 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.308  9.947   21.487 1.00 31.52 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.441  9.089   22.266 1.00 33.35 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.456  9.873   23.098 1.00 34.75 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.562  11.093  23.232 1.00 35.61 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.516  9.163   23.681 1.00 35.30 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.511  9.756   24.558 1.00 36.54 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.134  9.210   24.289 1.00 36.86 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.854  8.805   23.172 1.00 36.95 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.279  9.183   25.291 1.00 37.60 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.101 8.703   25.127 1.00 39.08 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.175 7.198   24.758 1.00 37.99 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.173 6.769   24.184 1.00 39.01 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.845 9.544   24.046 1.00 42.43 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.803 11.058  24.223 1.00 49.07 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.394 11.585  25.266 1.00 51.93 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.259 11.804  23.211 1.00 49.78 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.861  6.424   25.081 1.00 35.76 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.912  5.008   24.729 1.00 34.55 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.218  4.793   23.248 1.00 33.25 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.798  3.800   22.649 1.00 33.29 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.944  5.732   22.640 1.00 31.60 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.295  5.706   21.232 1.00 31.07 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.779  5.986   21.127 1.00 31.50 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.280  6.858   21.845 1.00 32.81 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.540  6.820   20.478 1.00 30.50 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.027  6.781   20.540 1.00 31.79 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.537 8.166   20.527 1.00 32.58 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.545 5.972   19.398 1.00 32.69 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.486  5.256   20.241 1.00 29.56 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.902  5.441   20.006 1.00 27.50 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.126  5.830   18.541 1.00 26.61 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.563  5.217   17.629 1.00 26.21 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.764  4.227   20.470 1.00 26.87 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.219  2.902   19.944 1.00 26.73 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.239  4.415   20.105 1.00 26.54 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.906  6.885   18.336 1.00 25.32 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.252  7.367   17.015 1.00 25.24 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.666  7.006   16.611 1.00 24.86 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.601  7.085   17.413 1.00 24.52 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.818  6.581   15.361 1.00 24.88 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.104 6.173   14.789 1.00 24.34 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.412 7.015   13.577 1.00 23.88 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.578  7.181   12.687 1.00 24.02 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.081 4.692   14.355 1.00 23.63 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.634  3.710   15.420 1.00 23.47 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.528 3.226   16.361 1.00 23.94 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.340  3.206   15.424 1.00 23.51 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 10.123 2.304   17.319 1.00 24.05 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.945  2.267   16.370 1.00 23.41 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.832  1.831   17.317 1.00 23.12 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.643 7.491   13.521 1.00 23.39 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.171 8.247   12.399 1.00 23.26 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.626 7.233   11.366 1.00 23.42 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.528 6.453   11.643 1.00 23.67 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.357 9.074   12.860 1.00 22.57 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.990 7.219   10.187 1.00 23.80 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.319 6.295   9.125  1.00 23.98 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.682 6.639   8.522  1.00 24.22 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.034 7.818   8.444  1.00 24.70 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.237 6.391   8.037  1.00 26.79 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.440 5.425   6.880  1.00 30.28 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.455 4.217   7.124  1.00 30.21 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.619 5.894   5.736  1.00 33.42 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.472 5.624   8.149  1.00 23.99 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.749 5.825   7.454  1.00 24.92 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.808 5.102   6.062  1.00 25.42 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.768 5.300   5.312  1.00 25.50 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.972 5.473   8.329  1.00 25.48 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.961 6.263   9.636  1.00 26.82 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.056 3.968   8.588  1.00 25.18 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.798 4.272   5.725  1.00 25.34 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.774 3.456   4.505  1.00 26.46 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.922 4.224   3.185  1.00 27.74 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.435 3.664   2.215  1.00 28.00 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.523 2.565   4.461  1.00 26.26 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.365 1.660   5.690  1.00 25.74 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.063 0.890   5.630  1.00 24.84 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.945 1.740   6.046  1.00 26.28 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.695  1.314   6.201  1.00 27.34 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.372  0.058   5.901  1.00 27.00 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.749  2.150   6.620  1.00 23.93 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.520 5.502   3.151  1.00 28.26 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.651 6.335   1.964  1.00 28.63 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.058 6.946   1.789  1.00 28.98 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.322 7.567   0.753  1.00 28.97 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.603 7.448   1.993  1.00 30.24 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.822 8.444   3.106  1.00 34.36 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.111 8.010   4.242  1.00 36.51 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.711 9.656   2.846  1.00 35.00 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.955 6.801   2.784  1.00 28.44 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.308 7.364   2.674  1.00 28.10 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.171 6.359   1.932  1.00 28.45 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.012 5.692   2.532  1.00 28.26 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.880 7.715   4.070  1.00 27.43 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 18.005 8.663   4.902  1.00 27.77 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.584 8.899   6.321  1.00 28.27 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.778 9.982   4.195  1.00 27.76 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.936 6.228   0.615  1.00 28.63 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.622 5.248   -0.235 1.00 29.48 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.147 5.413   -0.265 1.00 30.75 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.876 4.430   -0.472 1.00 30.77 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.070 5.306   -1.680 1.00 30.07 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.544 5.212   -1.868 1.00 31.17 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.200 5.060   -3.347 1.00 30.94 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.945 4.044   -1.077 1.00 32.32 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.620 6.654   -0.060 1.00 31.02 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.036 7.004   -0.086 1.00 31.96 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.849 6.423   1.067  1.00 33.84 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.070 6.337   0.950  1.00 34.23 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.218 8.517   -0.171 1.00 31.08 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.448 9.290   0.848  1.00 31.16 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.193 9.810   0.714  1.00 31.51 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.884 9.624   2.172  1.00 31.20 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.834 10.476  1.861  1.00 31.62 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.864 10.397  2.765  1.00 31.76 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.076 9.418   2.884  1.00 31.79 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.981 10.924  4.052  1.00 32.53 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.192 9.949   4.156  1.00 32.82 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.157 10.696  4.726  1.00 32.71 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.192 5.998   2.157  1.00 34.89 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.863 5.385   3.300  1.00 37.26 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.608 4.087   2.910  1.00 40.67 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.526 3.692   3.621  1.00 40.89 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.839 5.031   4.396  1.00 36.98 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.207 6.163   5.212  1.00 37.68 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.128 5.597   6.180  1.00 37.78 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.255 6.913   6.021  1.00 37.82 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.190 3.407   1.823  1.00 43.08 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.823 2.165   1.366  1.00 46.58 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.791 2.341   0.206  1.00 49.50 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.218 1.329   -0.350 1.00 50.33 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.756 1.185   0.859  1.00 49.14 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.815 0.694   1.907  1.00 54.50 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.257 0.515   3.057  1.00 56.08 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.631 0.487   1.582  1.00 56.78 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.066 3.574   -0.236 1.00 51.19 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.915 3.786   -1.412 1.00 53.25 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.971 4.880   -1.222 1.00 54.24 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.745 5.166   -2.147 1.00 54.66 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.036 4.111   -2.630 1.00 56.85 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.136 5.316   -2.404 1.00 63.43 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.357 5.789   -3.618 1.00 71.57 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.155 7.020   -3.754 1.00 72.35 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.951 4.929   -4.434 1.00 74.52 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BRL B 2 .   ? 9.536  11.085  24.570 1.00 35.49 ? 201 A1BRL A N1  1 
HETATM 1079 N  N3  . A1BRL B 2 .   ? 11.719 14.141  18.029 1.00 30.71 ? 201 A1BRL A N3  1 
HETATM 1080 C  C4  . A1BRL B 2 .   ? 6.181  10.442  26.841 1.00 35.55 ? 201 A1BRL A C4  1 
HETATM 1081 C  C5  . A1BRL B 2 .   ? 6.650  11.752  26.825 1.00 35.52 ? 201 A1BRL A C5  1 
HETATM 1082 C  C6  . A1BRL B 2 .   ? 7.797  12.089  26.125 1.00 35.66 ? 201 A1BRL A C6  1 
HETATM 1083 C  C7  . A1BRL B 2 .   ? 8.438  11.083  25.420 1.00 35.64 ? 201 A1BRL A C7  1 
HETATM 1084 C  C8  . A1BRL B 2 .   ? 10.357 12.251  24.273 1.00 35.69 ? 201 A1BRL A C8  1 
HETATM 1085 C  C10 . A1BRL B 2 .   ? 11.650 14.680  23.359 1.00 33.38 ? 201 A1BRL A C10 1 
HETATM 1086 C  C13 . A1BRL B 2 .   ? 11.589 14.489  20.416 1.00 32.69 ? 201 A1BRL A C13 1 
HETATM 1087 C  C15 . A1BRL B 2 .   ? 10.324 14.597  21.271 1.00 33.17 ? 201 A1BRL A C15 1 
HETATM 1088 O  O1  . A1BRL B 2 .   ? 10.863 16.083  18.773 1.00 30.72 ? 201 A1BRL A O1  1 
HETATM 1089 C  C14 . A1BRL B 2 .   ? 11.361 14.976  18.995 1.00 31.53 ? 201 A1BRL A C14 1 
HETATM 1090 C  C12 . A1BRL B 2 .   ? 12.665 15.313  21.139 1.00 32.89 ? 201 A1BRL A C12 1 
HETATM 1091 C  C11 . A1BRL B 2 .   ? 12.938 14.765  22.541 1.00 32.97 ? 201 A1BRL A C11 1 
HETATM 1092 N  N2  . A1BRL B 2 .   ? 10.574 14.026  22.596 1.00 34.05 ? 201 A1BRL A N2  1 
HETATM 1093 C  C9  . A1BRL B 2 .   ? 9.835  12.990  23.042 1.00 35.16 ? 201 A1BRL A C9  1 
HETATM 1094 O  O   . A1BRL B 2 .   ? 8.793  12.645  22.496 1.00 35.35 ? 201 A1BRL A O   1 
HETATM 1095 C  C1  . A1BRL B 2 .   ? 9.677  9.809   24.091 1.00 34.70 ? 201 A1BRL A C1  1 
HETATM 1096 C  C   . A1BRL B 2 .   ? 10.760 9.410   23.160 1.00 33.91 ? 201 A1BRL A C   1 
HETATM 1097 C  C2  . A1BRL B 2 .   ? 7.973  9.774   25.410 1.00 35.48 ? 201 A1BRL A C2  1 
HETATM 1098 N  N   . A1BRL B 2 .   ? 8.762  8.998   24.563 1.00 35.20 ? 201 A1BRL A N   1 
HETATM 1099 C  C3  . A1BRL B 2 .   ? 6.841  9.439   26.149 1.00 35.27 ? 201 A1BRL A C3  1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 11.028 -4.785  5.587  1.00 29.95 2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 19.429 20.805  5.476  0.00 33.20 ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 18.747 22.107  5.774  0.00 25.03 ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 18.222 19.734  4.649  0.00 29.73 ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 20.477 21.059  4.019  0.00 29.67 ? 203 DMS   A C2  1 
HETATM 1105 S  S   . DMS   E 4 .   ? 19.919 -0.362  19.878 1.00 79.66 ? 204 DMS   A S   1 
HETATM 1106 O  O   . DMS   E 4 .   ? 18.460 -0.404  19.563 1.00 79.24 ? 204 DMS   A O   1 
HETATM 1107 C  C1  . DMS   E 4 .   ? 20.107 0.180   21.608 1.00 79.69 ? 204 DMS   A C1  1 
HETATM 1108 C  C2  . DMS   E 4 .   ? 20.679 1.123   19.144 1.00 79.58 ? 204 DMS   A C2  1 
HETATM 1109 S  S   . DMS   F 4 .   ? 7.446  16.172  25.111 1.00 82.93 ? 205 DMS   A S   1 
HETATM 1110 O  O   . DMS   F 4 .   ? 8.586  15.438  25.786 1.00 82.86 ? 205 DMS   A O   1 
HETATM 1111 C  C1  . DMS   F 4 .   ? 6.056  15.018  24.849 1.00 82.81 ? 205 DMS   A C1  1 
HETATM 1112 C  C2  . DMS   F 4 .   ? 7.873  16.336  23.367 1.00 82.81 ? 205 DMS   A C2  1 
HETATM 1113 O  O   . HOH   G 5 .   ? 20.267 8.504   19.045 1.00 23.76 ? 301 HOH   A O   1 
HETATM 1114 O  O   . HOH   G 5 .   ? 3.046  7.895   9.820  1.00 66.68 ? 302 HOH   A O   1 
HETATM 1115 O  O   . HOH   G 5 .   ? 9.048  2.409   2.937  1.00 23.24 ? 303 HOH   A O   1 
HETATM 1116 O  O   . HOH   G 5 .   ? 11.320 11.541  11.329 1.00 28.01 ? 304 HOH   A O   1 
HETATM 1117 O  O   . HOH   G 5 .   ? 23.804 21.619  8.003  1.00 42.62 ? 305 HOH   A O   1 
HETATM 1118 O  O   . HOH   G 5 .   ? 23.711 0.071   16.023 1.00 39.69 ? 306 HOH   A O   1 
HETATM 1119 O  O   . HOH   G 5 .   ? 18.090 20.944  9.714  1.00 35.41 ? 307 HOH   A O   1 
HETATM 1120 O  O   . HOH   G 5 .   ? 10.700 8.097   4.792  1.00 32.85 ? 308 HOH   A O   1 
HETATM 1121 O  O   . HOH   G 5 .   ? 3.517  -4.967  21.058 1.00 41.06 ? 309 HOH   A O   1 
HETATM 1122 O  O   . HOH   G 5 .   ? 0.527  -0.237  16.505 1.00 20.18 ? 310 HOH   A O   1 
HETATM 1123 O  O   . HOH   G 5 .   ? 15.194 2.656   23.311 1.00 24.08 ? 311 HOH   A O   1 
HETATM 1124 O  O   . HOH   G 5 .   ? 10.146 18.070  20.432 1.00 33.06 ? 312 HOH   A O   1 
HETATM 1125 O  O   . HOH   G 5 .   ? 6.260  7.427   28.998 1.00 43.34 ? 313 HOH   A O   1 
HETATM 1126 O  O   . HOH   G 5 .   ? 23.283 18.297  19.502 1.00 35.31 ? 314 HOH   A O   1 
HETATM 1127 O  O   . HOH   G 5 .   ? 0.021  -3.196  9.946  1.00 57.51 ? 315 HOH   A O   1 
HETATM 1128 O  O   . HOH   G 5 .   ? 0.139  15.996  8.868  1.00 55.83 ? 316 HOH   A O   1 
HETATM 1129 O  O   . HOH   G 5 .   ? 12.734 24.596  22.552 1.00 32.86 ? 317 HOH   A O   1 
HETATM 1130 O  O   . HOH   G 5 .   ? 17.856 2.510   23.107 1.00 27.23 ? 318 HOH   A O   1 
HETATM 1131 O  O   . HOH   G 5 .   ? 8.441  19.423  18.480 1.00 29.41 ? 319 HOH   A O   1 
HETATM 1132 O  O   . HOH   G 5 .   ? 13.252 10.304  9.509  1.00 14.85 ? 320 HOH   A O   1 
HETATM 1133 O  O   . HOH   G 5 .   ? 11.822 1.774   33.710 1.00 30.68 ? 321 HOH   A O   1 
HETATM 1134 O  O   . HOH   G 5 .   ? 7.037  3.411   32.930 1.00 33.44 ? 322 HOH   A O   1 
HETATM 1135 O  O   . HOH   G 5 .   ? 18.395 18.695  17.001 1.00 23.48 ? 323 HOH   A O   1 
HETATM 1136 O  O   . HOH   G 5 .   ? 5.380  -7.467  7.422  1.00 33.25 ? 324 HOH   A O   1 
HETATM 1137 O  O   . HOH   G 5 .   ? 15.749 12.138  24.222 1.00 26.83 ? 325 HOH   A O   1 
HETATM 1138 O  O   . HOH   G 5 .   ? 14.681 14.224  3.688  1.00 30.52 ? 326 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 5 .   ? 5.379  -1.668  24.167 1.00 30.33 ? 327 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 5 .   ? 10.428 4.494   3.548  1.00 24.44 ? 328 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 5 .   ? 0.872  1.613   24.490 1.00 38.72 ? 329 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 5 .   ? 28.723 -2.213  13.077 1.00 39.27 ? 330 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 5 .   ? 1.572  -3.082  19.952 1.00 49.06 ? 331 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 5 .   ? 19.962 23.345  15.477 1.00 32.41 ? 332 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 5 .   ? 30.245 10.687  19.133 1.00 30.79 ? 333 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 5 .   ? 10.324 3.887   33.883 1.00 40.19 ? 334 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 5 .   ? 19.112 9.229   25.686 1.00 29.42 ? 335 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 5 .   ? 1.811  -1.892  17.405 1.00 30.18 ? 336 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 5 .   ? 5.861  1.647   6.589  1.00 29.36 ? 337 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 5 .   ? 28.480 21.455  18.796 1.00 33.47 ? 338 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 5 .   ? 3.279  3.844   27.909 1.00 36.63 ? 339 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 5 .   ? 24.019 2.603   19.780 1.00 38.36 ? 340 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 5 .   ? 22.500 18.736  5.939  1.00 32.72 ? 341 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 5 .   ? 4.299  -5.578  6.670  1.00 28.92 ? 342 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 5 .   ? 18.453 0.386   29.840 1.00 31.07 ? 343 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 5 .   ? 14.334 21.005  8.060  1.00 39.08 ? 344 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 5 .   ? 18.738 12.711  2.001  1.00 34.04 ? 345 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 5 .   ? 16.712 13.341  26.321 1.00 29.62 ? 346 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 5 .   ? 6.239  13.968  21.392 1.00 40.14 ? 347 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 5 .   ? 6.041  22.775  11.289 1.00 38.52 ? 348 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 5 .   ? 4.604  5.750   24.827 1.00 40.89 ? 349 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 5 .   ? 14.460 -4.816  34.264 1.00 33.93 ? 350 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 5 .   ? 8.589  -7.677  9.214  1.00 46.28 ? 351 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 5 .   ? 3.065  22.432  22.394 1.00 50.45 ? 352 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 5 .   ? 7.332  10.967  4.209  1.00 44.77 ? 353 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 5 .   ? 4.155  10.727  19.356 1.00 42.70 ? 354 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 5 .   ? 22.216 8.897   21.169 1.00 25.65 ? 355 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 5 .   ? 19.875 8.623   -2.153 1.00 29.39 ? 356 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 5 .   ? 0.705  -3.823  17.170 0.50 12.68 ? 357 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 5 .   ? 4.089  -2.794  21.851 1.00 49.84 ? 358 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 5 .   ? 28.852 16.356  23.290 1.00 40.90 ? 359 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 5 .   ? 21.082 21.610  17.951 1.00 41.77 ? 360 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 5 .   ? 2.427  1.403   26.898 1.00 36.85 ? 361 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 5 .   ? 8.156  20.219  7.547  1.00 65.36 ? 362 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 5 .   ? 1.121  -1.830  23.912 1.00 41.74 ? 363 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 5 .   ? 8.537  23.123  26.627 1.00 42.01 ? 364 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 5 .   ? 13.693 14.155  26.509 1.00 53.94 ? 365 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 5 .   ? 20.355 -3.894  22.396 1.00 53.83 ? 366 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   ? 0.6569 0.5075 0.2946 -0.0479 0.0112  0.0051  7   SER   A N   
2    C CA  . SER   A 1   ? 0.6435 0.5154 0.3187 -0.0460 0.0042  0.0104  7   SER   A CA  
3    C C   . SER   A 1   ? 0.6128 0.5112 0.3237 -0.0370 0.0121  0.0107  7   SER   A C   
4    O O   . SER   A 1   ? 0.6159 0.5158 0.3221 -0.0338 0.0186  0.0082  7   SER   A O   
5    C CB  . SER   A 1   ? 0.6702 0.5321 0.3480 -0.0579 -0.0182 0.0214  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.7134 0.5633 0.3797 -0.0646 -0.0292 0.0271  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.5795 0.4955 0.3226 -0.0335 0.0130  0.0135  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.5573 0.4918 0.3292 -0.0261 0.0230  0.0131  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.5303 0.4780 0.3220 -0.0217 0.0331  0.0108  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.5277 0.4728 0.3072 -0.0221 0.0358  0.0068  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.5035 0.4624 0.3242 -0.0177 0.0403  0.0133  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.4934 0.4609 0.3305 -0.0148 0.0522  0.0112  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.4780 0.4490 0.3288 -0.0099 0.0678  0.0088  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.4744 0.4440 0.3334 -0.0081 0.0675  0.0115  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.4844 0.4575 0.3485 -0.0178 0.0445  0.0200  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.4671 0.4388 0.3167 -0.0088 0.0818  0.0038  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.4600 0.4278 0.3151 -0.0064 0.0994  0.0005  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.4506 0.4225 0.3379 -0.0045 0.1091  0.0054  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.4457 0.4216 0.3366 -0.0068 0.1080  0.0063  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.4741 0.4345 0.2985 -0.0093 0.1080  -0.0080 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.4827 0.4425 0.2824 -0.0109 0.0989  -0.0107 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.4900 0.4386 0.3117 -0.0097 0.1268  -0.0118 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.5033 0.4601 0.2800 -0.0148 0.1017  -0.0149 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.4460 0.4169 0.3596 -0.0002 0.1194  0.0094  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.4429 0.4185 0.3945 0.0029  0.1322  0.0157  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.4678 0.4278 0.4120 0.0049  0.1597  0.0086  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.4812 0.4329 0.4325 0.0090  0.1694  0.0087  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.4242 0.4107 0.4201 0.0067  0.1227  0.0292  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.4258 0.4228 0.4261 0.0013  0.0953  0.0375  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.4307 0.4375 0.4520 -0.0022 0.0892  0.0445  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.4455 0.4384 0.4223 -0.0019 0.0763  0.0376  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.4350 0.4456 0.4531 -0.0096 0.0636  0.0517  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.4575 0.4523 0.4283 -0.0091 0.0527  0.0440  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.4559 0.4585 0.4462 -0.0133 0.0459  0.0510  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.4822 0.4816 0.4618 -0.0225 0.0222  0.0574  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.4761 0.4280 0.4017 0.0008  0.1723  0.0022  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.4915 0.4211 0.3992 -0.0006 0.1996  -0.0054 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.4900 0.4195 0.4223 0.0001  0.2180  -0.0024 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.4987 0.4368 0.4285 -0.0040 0.2099  -0.0013 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.5174 0.4303 0.3692 -0.0094 0.1979  -0.0160 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.5253 0.4467 0.3614 -0.0147 0.1838  -0.0165 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.5448 0.4278 0.3700 -0.0140 0.2244  -0.0236 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4768 0.3968 0.4359 0.0058  0.2437  -0.0001 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4757 0.3949 0.4644 0.0075  0.2664  0.0038  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.4590 0.4085 0.4936 0.0090  0.2487  0.0165  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.4494 0.4188 0.5229 0.0139  0.2313  0.0278  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.4565 0.4077 0.4836 0.0031  0.2505  0.0155  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.4395 0.4169 0.5045 0.0021  0.2315  0.0274  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.4387 0.4217 0.4679 -0.0050 0.2017  0.0239  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.4201 0.4145 0.4604 -0.0094 0.1904  0.0292  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4559 0.4347 0.5499 0.0013  0.2539  0.0321  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.5079 0.4917 0.6612 0.0107  0.2777  0.0423  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.5113 0.5194 0.7201 0.0155  0.2629  0.0579  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5292 0.4876 0.6712 0.0131  0.3150  0.0346  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.4476 0.4221 0.4364 -0.0060 0.1896  0.0157  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.4475 0.4251 0.4040 -0.0111 0.1653  0.0124  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.4314 0.4161 0.3867 -0.0090 0.1437  0.0151  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.4334 0.4153 0.3949 -0.0046 0.1479  0.0152  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.4716 0.4308 0.3758 -0.0161 0.1715  0.0005  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4873 0.4332 0.3802 -0.0210 0.1918  -0.0032 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4917 0.4449 0.3969 -0.0242 0.1892  0.0010  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.5167 0.4388 0.3812 -0.0241 0.2133  -0.0110 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.5127 0.4515 0.4044 -0.0297 0.2084  -0.0023 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.5414 0.4457 0.3881 -0.0307 0.2325  -0.0147 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.5461 0.4596 0.4073 -0.0331 0.2304  -0.0102 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5804 0.4742 0.4210 -0.0406 0.2500  -0.0138 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.4093 0.3997 0.3528 -0.0129 0.1216  0.0169  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3961 0.3875 0.3268 -0.0131 0.1017  0.0179  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.4020 0.3850 0.2893 -0.0159 0.0959  0.0091  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.4036 0.3854 0.2822 -0.0192 0.0944  0.0081  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3981 0.3991 0.3548 -0.0166 0.0816  0.0299  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.4311 0.4257 0.3605 -0.0207 0.0597  0.0298  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.4613 0.4610 0.4158 -0.0265 0.0392  0.0435  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.5141 0.5023 0.4386 -0.0350 0.0204  0.0436  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.5331 0.5085 0.4313 -0.0394 0.0055  0.0439  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.5118 0.4871 0.4121 -0.0361 0.0051  0.0448  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.5308 0.4899 0.3971 -0.0478 -0.0078 0.0429  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.4069 0.3845 0.2702 -0.0144 0.0939  0.0037  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.4171 0.3890 0.2472 -0.0159 0.0894  -0.0023 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.4277 0.3981 0.2475 -0.0158 0.0745  -0.0008 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.4448 0.4150 0.2662 -0.0143 0.0720  0.0001  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.4219 0.3877 0.2321 -0.0157 0.0998  -0.0085 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.4278 0.3912 0.2124 -0.0172 0.0942  -0.0114 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.4215 0.3812 0.2350 -0.0177 0.1168  -0.0106 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.4166 0.3824 0.2230 -0.0181 0.0660  -0.0008 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.4299 0.3871 0.2189 -0.0194 0.0549  -0.0003 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.4345 0.3842 0.1988 -0.0178 0.0575  -0.0053 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.4330 0.3849 0.1963 -0.0170 0.0631  -0.0069 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.4410 0.3930 0.2360 -0.0256 0.0408  0.0063  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.4408 0.4015 0.2662 -0.0271 0.0353  0.0146  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.4421 0.3927 0.2384 -0.0286 0.0402  0.0071  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.4323 0.3711 0.1769 -0.0176 0.0540  -0.0066 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.4397 0.3694 0.1655 -0.0149 0.0583  -0.0097 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.4542 0.3743 0.1753 -0.0186 0.0535  -0.0086 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.4660 0.3788 0.1866 -0.0249 0.0435  -0.0054 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.4535 0.3686 0.1583 -0.0147 0.0585  -0.0112 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.4903 0.4137 0.1980 -0.0115 0.0639  -0.0120 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.5006 0.4265 0.2127 -0.0138 0.0595  -0.0106 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.4871 0.4153 0.1946 -0.0064 0.0727  -0.0130 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.4513 0.3718 0.1709 -0.0159 0.0587  -0.0098 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.4540 0.3644 0.1682 -0.0196 0.0547  -0.0088 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.4816 0.3673 0.1709 -0.0238 0.0493  -0.0095 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.4915 0.3681 0.1774 -0.0317 0.0396  -0.0068 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.4396 0.3523 0.1540 -0.0155 0.0614  -0.0094 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.4375 0.3427 0.1498 -0.0195 0.0581  -0.0081 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.4478 0.3486 0.1542 -0.0144 0.0639  -0.0081 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.4724 0.3657 0.1760 -0.0180 0.0616  -0.0066 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.5010 0.3734 0.1881 -0.0195 0.0597  -0.0073 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.5021 0.3563 0.1710 -0.0185 0.0608  -0.0099 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.4948 0.3610 0.1800 -0.0232 0.0574  -0.0056 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.4965 0.3693 0.1671 -0.0201 0.0557  -0.0126 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.5318 0.3733 0.1700 -0.0254 0.0536  -0.0145 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.5474 0.3796 0.1765 -0.0365 0.0389  -0.0112 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5612 0.3640 0.1599 -0.0455 0.0326  -0.0113 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.5552 0.3823 0.1758 -0.0183 0.0685  -0.0185 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.5613 0.3946 0.1826 -0.0171 0.0710  -0.0188 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.5615 0.4219 0.2084 -0.0097 0.0766  -0.0176 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5836 0.3967 0.1801 -0.0236 0.0681  -0.0198 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.5739 0.4317 0.2135 -0.0112 0.0774  -0.0182 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5874 0.4172 0.1967 -0.0192 0.0727  -0.0195 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.5375 0.3926 0.1928 -0.0370 0.0325  -0.0072 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.5495 0.3999 0.2048 -0.0470 0.0166  -0.0011 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.5541 0.4227 0.2427 -0.0518 0.0051  0.0069  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5563 0.4256 0.2549 -0.0599 -0.0098 0.0150  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.5354 0.3948 0.1966 -0.0435 0.0188  -0.0011 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5575 0.3992 0.1888 -0.0401 0.0303  -0.0073 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5610 0.4146 0.2016 -0.0371 0.0323  -0.0067 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.5834 0.3864 0.1709 -0.0508 0.0248  -0.0081 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.5498 0.4323 0.2566 -0.0476 0.0119  0.0059  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.5427 0.4423 0.2832 -0.0515 0.0053  0.0135  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.5641 0.4498 0.2995 -0.0652 -0.0137 0.0219  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5886 0.4486 0.2899 -0.0716 -0.0181 0.0192  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.5333 0.4448 0.2861 -0.0459 0.0176  0.0102  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5501 0.4520 0.3208 -0.0703 -0.0248 0.0330  24  THR   A N   
135  C CA  . THR   A 18  ? 0.5655 0.4588 0.3403 -0.0854 -0.0470 0.0450  24  THR   A CA  
136  C C   . THR   A 18  ? 0.5663 0.4665 0.3593 -0.0901 -0.0484 0.0494  24  THR   A C   
137  O O   . THR   A 18  ? 0.5638 0.4756 0.3663 -0.0809 -0.0310 0.0428  24  THR   A O   
138  C CB  . THR   A 18  ? 0.5655 0.4756 0.3780 -0.0882 -0.0594 0.0581  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5600 0.5009 0.4263 -0.0808 -0.0492 0.0636  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5764 0.4820 0.3744 -0.0826 -0.0561 0.0537  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5723 0.4654 0.3709 -0.1057 -0.0703 0.0618  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5738 0.4756 0.3947 -0.1117 -0.0731 0.0682  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5369 0.4756 0.4183 -0.1022 -0.0595 0.0739  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.5327 0.4801 0.4251 -0.0983 -0.0457 0.0705  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.6053 0.4929 0.4233 -0.1325 -0.1022 0.0830  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.7047 0.5481 0.4558 -0.1440 -0.1121 0.0761  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7533 0.5774 0.4703 -0.1416 -0.0998 0.0643  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7491 0.5612 0.4603 -0.1582 -0.1313 0.0795  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.7960 0.5773 0.4549 -0.1530 -0.1093 0.0603  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.8015 0.5726 0.4518 -0.1642 -0.1282 0.0687  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.5085 0.4656 0.4262 -0.0983 -0.0613 0.0821  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4734 0.4608 0.4477 -0.0885 -0.0446 0.0874  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.4455 0.4356 0.4067 -0.0740 -0.0158 0.0712  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.4181 0.4219 0.4061 -0.0697 0.0012  0.0713  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4950 0.4967 0.5072 -0.0867 -0.0523 0.0996  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5380 0.5665 0.6073 -0.0746 -0.0303 0.1040  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5357 0.5835 0.6590 -0.0774 -0.0314 0.1191  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5526 0.5809 0.6112 -0.0614 -0.0089 0.0915  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.4515 0.4268 0.3704 -0.0681 -0.0108 0.0581  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.4439 0.4197 0.3469 -0.0571 0.0119  0.0445  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.4495 0.4194 0.3376 -0.0588 0.0190  0.0394  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.4400 0.4178 0.3383 -0.0537 0.0368  0.0356  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.4727 0.4344 0.3365 -0.0524 0.0123  0.0345  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.5066 0.4744 0.3823 -0.0483 0.0114  0.0368  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.4880 0.4722 0.4009 -0.0438 0.0202  0.0417  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.5407 0.4948 0.3877 -0.0495 0.0035  0.0337  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.4643 0.4170 0.3256 -0.0670 0.0055  0.0396  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.4755 0.4204 0.3221 -0.0691 0.0106  0.0357  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.4718 0.4314 0.3555 -0.0748 0.0122  0.0450  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.4774 0.4384 0.3604 -0.0730 0.0253  0.0413  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.4889 0.4067 0.2941 -0.0760 -0.0022 0.0329  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.5032 0.4054 0.2715 -0.0678 0.0055  0.0217  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.5213 0.4108 0.2676 -0.0666 0.0011  0.0188  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.5049 0.4039 0.2582 -0.0596 0.0194  0.0137  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.5342 0.4144 0.2562 -0.0575 0.0131  0.0095  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.5252 0.4117 0.2524 -0.0531 0.0231  0.0071  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.5063 0.4107 0.2656 -0.0581 0.0286  0.0127  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.5317 0.4147 0.2458 -0.0445 0.0345  0.0013  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.5216 0.4197 0.2626 -0.0507 0.0379  0.0065  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.5300 0.4192 0.2516 -0.0437 0.0403  0.0016  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.4602 0.4307 0.3780 -0.0823 -0.0014 0.0585  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.4468 0.4349 0.4097 -0.0876 0.0008  0.0701  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.4328 0.4400 0.4307 -0.0773 0.0267  0.0690  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.4245 0.4439 0.4563 -0.0799 0.0362  0.0762  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.4347 0.4311 0.4304 -0.0988 -0.0228 0.0878  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.4316 0.4393 0.4214 -0.0666 0.0389  0.0608  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.4228 0.4405 0.4356 -0.0578 0.0652  0.0580  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.4348 0.4383 0.4031 -0.0511 0.0790  0.0421  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.4235 0.4281 0.3943 -0.0440 0.0933  0.0377  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.4245 0.4562 0.4773 -0.0529 0.0655  0.0667  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.4477 0.4972 0.5556 -0.0592 0.0536  0.0858  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.4478 0.5098 0.5955 -0.0595 0.0682  0.0933  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.4535 0.5039 0.5657 -0.0652 0.0269  0.0953  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.4503 0.4396 0.3789 -0.0540 0.0732  0.0350  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.4600 0.4367 0.3490 -0.0496 0.0806  0.0233  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.4636 0.4387 0.3522 -0.0479 0.1030  0.0189  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.4740 0.4497 0.3744 -0.0523 0.1124  0.0219  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.4715 0.4345 0.3291 -0.0536 0.0705  0.0203  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.4912 0.4427 0.3132 -0.0493 0.0753  0.0115  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.4995 0.4502 0.3096 -0.0431 0.0712  0.0076  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.5038 0.4416 0.3023 -0.0523 0.0675  0.0105  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.4575 0.4276 0.3285 -0.0431 0.1116  0.0120  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.4574 0.4178 0.3143 -0.0440 0.1316  0.0065  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.4765 0.4242 0.2918 -0.0459 0.1254  0.0006  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.4892 0.4263 0.2869 -0.0514 0.1318  -0.0008 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.4554 0.4159 0.3207 -0.0392 0.1447  0.0042  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4790 0.4212 0.3157 -0.0428 0.1637  -0.0029 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.4330 0.4068 0.3461 -0.0361 0.1520  0.0122  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.4758 0.4246 0.2780 -0.0418 0.1125  -0.0013 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.4787 0.4192 0.2510 -0.0420 0.1060  -0.0043 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4534 0.3976 0.2226 -0.0363 0.0921  -0.0042 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.4378 0.3885 0.2192 -0.0329 0.0895  -0.0039 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4960 0.4286 0.2503 -0.0444 0.1159  -0.0079 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.5210 0.4486 0.2514 -0.0450 0.1069  -0.0081 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.5444 0.4630 0.2559 -0.0501 0.1027  -0.0059 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.5208 0.4534 0.2479 -0.0407 0.1003  -0.0086 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5506 0.4701 0.2516 -0.0488 0.0932  -0.0037 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.5391 0.4674 0.2493 -0.0432 0.0925  -0.0056 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.5174 0.4576 0.2554 -0.0356 0.1001  -0.0101 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.5447 0.4779 0.2519 -0.0406 0.0858  -0.0037 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.5292 0.4723 0.2596 -0.0333 0.0940  -0.0098 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.5368 0.4774 0.2538 -0.0357 0.0873  -0.0064 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.4467 0.3849 0.2001 -0.0355 0.0844  -0.0039 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.4454 0.3826 0.1927 -0.0299 0.0761  -0.0043 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.4545 0.3872 0.1873 -0.0277 0.0745  -0.0034 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4486 0.3759 0.1744 -0.0314 0.0749  -0.0014 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.4530 0.3844 0.2019 -0.0304 0.0678  -0.0030 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.4755 0.3983 0.2195 -0.0348 0.0655  -0.0010 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4752 0.3863 0.2016 -0.0316 0.0639  -0.0012 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.5480 0.4536 0.2698 -0.0349 0.0644  0.0007  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4267 0.3340 0.1457 -0.0254 0.0632  -0.0024 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.4597 0.3946 0.1901 -0.0221 0.0725  -0.0035 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.4612 0.3948 0.1866 -0.0189 0.0705  0.0001  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.4492 0.3803 0.1753 -0.0110 0.0705  0.0000  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.4490 0.3864 0.1784 -0.0085 0.0721  -0.0010 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4833 0.4232 0.2069 -0.0227 0.0709  0.0024  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.5376 0.4769 0.2591 -0.0233 0.0655  0.0099  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5336 0.4713 0.2614 -0.0164 0.0639  0.0134  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.5854 0.5239 0.2988 -0.0314 0.0630  0.0130  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.4409 0.3598 0.1619 -0.0074 0.0705  0.0009  36  SER   A N   
241  C CA  A SER   A 30  ? 0.4514 0.3607 0.1685 -0.0001 0.0748  0.0002  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.4523 0.3620 0.1695 -0.0001 0.0748  0.0001  36  SER   A CA  
243  C C   . SER   A 30  ? 0.4453 0.3652 0.1745 0.0061  0.0784  0.0050  36  SER   A C   
244  O O   . SER   A 30  ? 0.4433 0.3620 0.1724 0.0105  0.0838  0.0033  36  SER   A O   
245  C CB  A SER   A 30  ? 0.4668 0.3576 0.1749 0.0023  0.0763  0.0009  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.4713 0.3612 0.1781 0.0022  0.0765  0.0001  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.4982 0.3699 0.1924 0.0060  0.0821  -0.0029 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4948 0.3863 0.2094 0.0048  0.0761  0.0064  36  SER   A OG  
249  N N   . SER   A 31  ? 0.4261 0.3558 0.1655 0.0048  0.0744  0.0120  37  SER   A N   
250  C CA  . SER   A 31  ? 0.4179 0.3600 0.1735 0.0086  0.0747  0.0197  37  SER   A CA  
251  C C   . SER   A 31  ? 0.4014 0.3554 0.1583 0.0052  0.0741  0.0175  37  SER   A C   
252  O O   . SER   A 31  ? 0.3933 0.3563 0.1633 0.0090  0.0763  0.0224  37  SER   A O   
253  C CB  . SER   A 31  ? 0.4364 0.3841 0.2010 0.0053  0.0666  0.0301  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.4768 0.4288 0.2315 -0.0062 0.0593  0.0297  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.3931 0.3467 0.1390 -0.0014 0.0725  0.0106  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.3909 0.3526 0.1370 -0.0042 0.0729  0.0081  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.4047 0.3612 0.1456 -0.0014 0.0770  0.0012  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.4154 0.3773 0.1569 -0.0028 0.0775  -0.0006 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3936 0.3561 0.1319 -0.0137 0.0702  0.0064  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.3810 0.3451 0.1169 -0.0206 0.0641  0.0138  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.4096 0.3662 0.1296 -0.0312 0.0649  0.0107  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.4312 0.3888 0.1468 -0.0344 0.0683  0.0068  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.4641 0.4121 0.1628 -0.0447 0.0702  0.0054  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.4781 0.4140 0.1603 -0.0540 0.0687  0.0075  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.4645 0.4112 0.1592 -0.0466 0.0743  0.0017  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.4079 0.3515 0.1412 0.0008  0.0782  -0.0020 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.4058 0.3401 0.1298 0.0001  0.0782  -0.0069 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.4078 0.3494 0.1366 -0.0056 0.0741  -0.0087 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.4104 0.3522 0.1385 -0.0063 0.0731  -0.0103 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.4102 0.3406 0.1298 0.0044  0.0837  -0.0076 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.4231 0.3386 0.1267 0.0013  0.0818  -0.0117 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.4197 0.3200 0.1112 -0.0021 0.0779  -0.0132 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.4430 0.3608 0.1449 0.0006  0.0824  -0.0125 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.4097 0.3556 0.1438 -0.0096 0.0732  -0.0080 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.4191 0.3702 0.1615 -0.0138 0.0737  -0.0092 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.4242 0.3722 0.1719 -0.0174 0.0720  -0.0085 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.4341 0.3775 0.1770 -0.0185 0.0716  -0.0075 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.4140 0.3705 0.1570 -0.0169 0.0785  -0.0091 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.4258 0.3869 0.1662 -0.0164 0.0796  -0.0091 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.4304 0.3895 0.1645 -0.0229 0.0839  -0.0093 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.4163 0.3789 0.1616 -0.0139 0.0793  -0.0108 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.4158 0.3674 0.1768 -0.0196 0.0712  -0.0076 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.4119 0.3645 0.1864 -0.0237 0.0704  -0.0049 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.4081 0.3692 0.2036 -0.0240 0.0776  -0.0036 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.4108 0.3748 0.2102 -0.0215 0.0780  -0.0040 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.4129 0.3583 0.1863 -0.0268 0.0587  -0.0018 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.4177 0.3655 0.2082 -0.0327 0.0556  0.0032  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.4420 0.3756 0.2163 -0.0373 0.0457  0.0043  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.4119 0.3697 0.2308 -0.0350 0.0514  0.0097  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.4062 0.3693 0.2142 -0.0267 0.0858  -0.0022 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.4078 0.3762 0.2388 -0.0263 0.0971  -0.0004 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.4098 0.3847 0.2689 -0.0293 0.0960  0.0066  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.4132 0.3849 0.2667 -0.0332 0.0953  0.0070  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.4181 0.3786 0.2353 -0.0278 0.1138  -0.0055 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.4120 0.3728 0.2524 -0.0269 0.1309  -0.0042 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.4288 0.3842 0.2210 -0.0269 0.1119  -0.0100 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.4101 0.3942 0.3012 -0.0279 0.0943  0.0134  43  SER   A N   
298  C CA  . SER   A 37  ? 0.4129 0.4066 0.3396 -0.0313 0.0927  0.0230  43  SER   A CA  
299  C C   . SER   A 37  ? 0.4234 0.4249 0.3877 -0.0270 0.1107  0.0275  43  SER   A C   
300  O O   . SER   A 37  ? 0.4212 0.4193 0.3819 -0.0219 0.1199  0.0235  43  SER   A O   
301  C CB  . SER   A 37  ? 0.4121 0.4092 0.3474 -0.0358 0.0690  0.0315  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.4490 0.4474 0.3877 -0.0330 0.0609  0.0336  43  SER   A OG  
303  N N   . SER   A 38  ? 0.4292 0.4403 0.4308 -0.0292 0.1170  0.0364  44  SER   A N   
304  C CA  . SER   A 38  ? 0.4436 0.4613 0.4863 -0.0240 0.1382  0.0418  44  SER   A CA  
305  C C   . SER   A 38  ? 0.4527 0.4864 0.5426 -0.0216 0.1255  0.0559  44  SER   A C   
306  O O   . SER   A 38  ? 0.4525 0.4942 0.5516 -0.0276 0.0998  0.0652  44  SER   A O   
307  C CB  . SER   A 38  ? 0.4501 0.4699 0.5135 -0.0270 0.1561  0.0450  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.4731 0.5050 0.5564 -0.0339 0.1366  0.0554  44  SER   A OG  
309  N N   . THR   A 39  ? 0.4576 0.4932 0.5758 -0.0137 0.1434  0.0585  45  THR   A N   
310  C CA  . THR   A 39  ? 0.4600 0.5107 0.6289 -0.0102 0.1335  0.0738  45  THR   A CA  
311  C C   . THR   A 39  ? 0.4725 0.5332 0.7014 -0.0038 0.1596  0.0840  45  THR   A C   
312  O O   . THR   A 39  ? 0.4842 0.5325 0.7038 -0.0004 0.1908  0.0749  45  THR   A O   
313  C CB  . THR   A 39  ? 0.4772 0.5197 0.6264 -0.0050 0.1293  0.0686  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4992 0.5298 0.6471 0.0030  0.1602  0.0607  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4923 0.5224 0.5807 -0.0096 0.1121  0.0564  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.4691 0.5500 0.7594 -0.0027 0.1474  0.1038  46  THR   A N   
317  C CA  . THR   A 40  ? 0.4666 0.5596 0.8254 0.0052  0.1730  0.1167  46  THR   A CA  
318  C C   . THR   A 40  ? 0.4853 0.5702 0.8569 0.0170  0.1905  0.1154  46  THR   A C   
319  O O   . THR   A 40  ? 0.4834 0.5603 0.8772 0.0259  0.2272  0.1133  46  THR   A O   
320  C CB  . THR   A 40  ? 0.4528 0.5740 0.8799 -0.0003 0.1514  0.1419  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4648 0.5917 0.8869 -0.0071 0.1113  0.1513  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4590 0.5858 0.8829 -0.0104 0.1476  0.1432  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.5019 0.5849 0.8551 0.0166  0.1659  0.1158  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.5182 0.5915 0.8780 0.0268  0.1797  0.1140  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.5645 0.6089 0.8551 0.0284  0.2011  0.0897  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.5856 0.6209 0.8205 0.0207  0.1932  0.0764  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.5143 0.5951 0.8788 0.0240  0.1446  0.1244  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.5807 0.6092 0.8751 0.0376  0.2277  0.0851  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.6267 0.6248 0.8555 0.0369  0.2473  0.0639  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.6434 0.6340 0.8275 0.0343  0.2250  0.0564  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.6429 0.6415 0.8535 0.0385  0.2112  0.0664  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.6623 0.6392 0.9073 0.0460  0.2898  0.0608  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.7712 0.7137 0.9498 0.0405  0.3160  0.0403  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.8558 0.7970 1.0344 0.0357  0.3327  0.0384  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.8579 0.8202 1.0967 0.0396  0.3378  0.0525  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.8954 0.8114 1.0073 0.0260  0.3407  0.0223  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.6549 0.6298 0.7739 0.0271  0.2224  0.0401  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.6606 0.6276 0.7341 0.0237  0.2048  0.0320  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.6626 0.6024 0.7046 0.0255  0.2275  0.0207  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.6739 0.5931 0.6979 0.0242  0.2548  0.0123  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.6558 0.5919 0.6861 0.0267  0.2161  0.0201  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.6673 0.5762 0.6683 0.0274  0.2353  0.0107  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.6676 0.5663 0.6104 0.0189  0.2212  -0.0001 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.6911 0.5682 0.6097 0.0179  0.2318  -0.0062 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.6739 0.5829 0.7172 0.0372  0.2408  0.0206  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.7194 0.6421 0.8426 0.0485  0.2597  0.0368  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.6372 0.5499 0.5590 0.0125  0.1989  -0.0018 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.6369 0.5425 0.5106 0.0049  0.1871  -0.0100 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.6317 0.5128 0.4639 -0.0029 0.2046  -0.0205 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.6378 0.5133 0.4698 -0.0048 0.2178  -0.0224 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.6598 0.5847 0.5251 0.0014  0.1623  -0.0083 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.7063 0.6457 0.5879 0.0040  0.1411  -0.0008 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.7347 0.6684 0.6162 0.0058  0.1400  0.0004  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.7041 0.6572 0.5943 0.0030  0.1254  0.0039  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.6253 0.4901 0.4204 -0.0094 0.2036  -0.0266 52  THR   A N   
356  C CA  . THR   A 46  ? 0.6275 0.4651 0.3767 -0.0205 0.2158  -0.0351 52  THR   A CA  
357  C C   . THR   A 46  ? 0.5993 0.4470 0.3207 -0.0293 0.1946  -0.0360 52  THR   A C   
358  O O   . THR   A 46  ? 0.5906 0.4511 0.3104 -0.0293 0.1773  -0.0337 52  THR   A O   
359  C CB  . THR   A 46  ? 0.6589 0.4678 0.3843 -0.0239 0.2286  -0.0399 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.6654 0.4611 0.4182 -0.0148 0.2534  -0.0389 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6912 0.4691 0.3596 -0.0399 0.2343  -0.0476 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.5803 0.4215 0.2813 -0.0368 0.1966  -0.0383 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.5641 0.4147 0.2433 -0.0447 0.1771  -0.0372 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5724 0.3984 0.2073 -0.0589 0.1766  -0.0404 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5862 0.3803 0.1941 -0.0665 0.1944  -0.0456 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.5603 0.4170 0.2409 -0.0464 0.1760  -0.0361 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.5514 0.4283 0.2752 -0.0345 0.1778  -0.0323 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.5525 0.4221 0.2195 -0.0520 0.1549  -0.0327 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.5463 0.4487 0.2962 -0.0263 0.1595  -0.0271 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.5607 0.3994 0.1886 -0.0629 0.1573  -0.0368 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.5778 0.3962 0.1668 -0.0785 0.1522  -0.0371 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.5880 0.3951 0.1498 -0.0911 0.1477  -0.0356 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.5706 0.3973 0.1490 -0.0867 0.1396  -0.0320 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.5527 0.3925 0.1501 -0.0786 0.1328  -0.0313 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.6196 0.3918 0.1368 -0.1080 0.1526  -0.0381 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.6327 0.3879 0.1161 -0.1240 0.1460  -0.0355 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.6547 0.3976 0.1074 -0.1414 0.1293  -0.0303 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.6968 0.4016 0.1091 -0.1546 0.1392  -0.0353 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.6609 0.3768 0.1133 -0.1304 0.1711  -0.0438 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.6590 0.3894 0.1487 -0.1130 0.1887  -0.0472 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.6427 0.4086 0.1647 -0.1046 0.1736  -0.0411 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.6221 0.3968 0.1758 -0.0913 0.1909  -0.0439 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5909 0.3957 0.1791 -0.0809 0.1821  -0.0398 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5640 0.3917 0.1594 -0.0806 0.1588  -0.0337 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5462 0.3571 0.1631 -0.0712 0.1971  -0.0410 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.6303 0.4053 0.1053 -0.1409 0.1053  -0.0200 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.6482 0.4217 0.1086 -0.1552 0.0871  -0.0121 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.6401 0.4506 0.1313 -0.1539 0.0628  0.0019  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.6149 0.4501 0.1367 -0.1406 0.0617  0.0039  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.6613 0.4393 0.1351 -0.1466 0.0943  -0.0165 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.6894 0.5170 0.2250 -0.1212 0.0913  -0.0143 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.6549 0.4707 0.1432 -0.1662 0.0448  0.0121  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.6469 0.5000 0.1732 -0.1629 0.0250  0.0267  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.6369 0.5109 0.1884 -0.1572 0.0221  0.0299  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.6359 0.5278 0.2038 -0.1649 0.0044  0.0441  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.6904 0.5365 0.1996 -0.1843 0.0019  0.0419  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.7927 0.6148 0.2664 -0.2097 -0.0123 0.0488  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.8347 0.6362 0.2858 -0.2123 -0.0006 0.0388  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.8295 0.6525 0.2982 -0.2277 -0.0363 0.0653  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.6255 0.4973 0.1818 -0.1441 0.0393  0.0180  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.5962 0.4842 0.1730 -0.1376 0.0395  0.0190  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.5605 0.4876 0.1826 -0.1256 0.0319  0.0287  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.5516 0.4922 0.1930 -0.1132 0.0353  0.0279  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.5888 0.4682 0.1666 -0.1235 0.0588  0.0055  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.6041 0.4387 0.1366 -0.1357 0.0713  -0.0044 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.5405 0.4835 0.1790 -0.1290 0.0238  0.0376  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.5114 0.4884 0.1935 -0.1163 0.0222  0.0461  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.4830 0.4683 0.1779 -0.1066 0.0317  0.0417  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.4624 0.4710 0.1878 -0.1004 0.0314  0.0499  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.5308 0.5261 0.2340 -0.1272 0.0042  0.0652  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.5822 0.5776 0.2862 -0.1307 -0.0051 0.0720  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.6131 0.6338 0.3526 -0.1368 -0.0221 0.0936  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.6571 0.6702 0.3842 -0.1563 -0.0414 0.1060  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.5718 0.6214 0.3565 -0.1210 -0.0151 0.0998  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.4835 0.4480 0.1547 -0.1064 0.0407  0.0300  60  THR   A N   
416  C CA  . THR   A 54  ? 0.4803 0.4470 0.1575 -0.0980 0.0493  0.0249  60  THR   A CA  
417  C C   . THR   A 54  ? 0.4710 0.4211 0.1365 -0.0878 0.0616  0.0116  60  THR   A C   
418  O O   . THR   A 54  ? 0.4831 0.4139 0.1289 -0.0916 0.0650  0.0059  60  THR   A O   
419  C CB  . THR   A 54  ? 0.5166 0.4740 0.1799 -0.1114 0.0444  0.0281  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.5562 0.4814 0.1836 -0.1203 0.0479  0.0197  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.5114 0.4844 0.1873 -0.1254 0.0293  0.0439  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.4479 0.4046 0.1261 -0.0759 0.0681  0.0080  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.4378 0.3828 0.1128 -0.0662 0.0769  -0.0011 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.4186 0.3711 0.1062 -0.0563 0.0796  -0.0019 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.4093 0.3723 0.1035 -0.0574 0.0776  0.0030  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.4154 0.3615 0.1062 -0.0477 0.0838  -0.0069 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.4097 0.3571 0.1065 -0.0408 0.0838  -0.0070 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.4132 0.3639 0.1192 -0.0327 0.0836  -0.0085 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.4205 0.3668 0.1305 -0.0305 0.0856  -0.0111 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.4112 0.3434 0.1024 -0.0413 0.0855  -0.0090 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.4105 0.3412 0.1054 -0.0364 0.0825  -0.0075 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.4207 0.3460 0.0988 -0.0509 0.0856  -0.0078 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.4149 0.3706 0.1227 -0.0293 0.0824  -0.0069 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.4113 0.3660 0.1228 -0.0237 0.0808  -0.0080 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.4125 0.3567 0.1175 -0.0228 0.0767  -0.0071 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.4174 0.3568 0.1135 -0.0256 0.0770  -0.0058 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.4026 0.3658 0.1167 -0.0215 0.0832  -0.0068 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.4059 0.3682 0.1146 -0.0206 0.0873  -0.0049 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.4078 0.3778 0.1199 -0.0235 0.0913  -0.0011 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.4221 0.3739 0.1214 -0.0177 0.0886  -0.0063 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.4209 0.3892 0.1303 -0.0221 0.0991  0.0010  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.4366 0.3817 0.1263 -0.0172 0.0965  -0.0054 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.4367 0.3908 0.1332 -0.0186 0.1032  -0.0018 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.4493 0.3963 0.1387 -0.0175 0.1148  -0.0006 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.4094 0.3491 0.1179 -0.0205 0.0718  -0.0069 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.4307 0.3578 0.1306 -0.0223 0.0641  -0.0042 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.4403 0.3593 0.1229 -0.0233 0.0648  -0.0051 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.4411 0.3637 0.1268 -0.0208 0.0669  -0.0067 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.4305 0.3559 0.1466 -0.0212 0.0560  -0.0008 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4486 0.3603 0.1557 -0.0256 0.0436  0.0047  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4617 0.3639 0.1601 -0.0291 0.0394  0.0079  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4629 0.3679 0.1650 -0.0284 0.0350  0.0071  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4866 0.3730 0.1729 -0.0355 0.0256  0.0143  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4853 0.3737 0.1739 -0.0357 0.0208  0.0134  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5050 0.3836 0.1847 -0.0395 0.0158  0.0172  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5347 0.3938 0.1970 -0.0490 -0.0005 0.0247  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4579 0.3626 0.1196 -0.0275 0.0648  -0.0042 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4744 0.3637 0.1128 -0.0295 0.0696  -0.0058 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5084 0.3740 0.1246 -0.0372 0.0571  -0.0027 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5155 0.3690 0.1168 -0.0426 0.0540  -0.0004 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4836 0.3727 0.1135 -0.0294 0.0833  -0.0068 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5245 0.3880 0.1227 -0.0313 0.0963  -0.0093 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5155 0.3741 0.1298 -0.0392 0.0478  -0.0014 66  SER   A N   
464  C CA  . SER   A 60  ? 0.5406 0.3770 0.1359 -0.0491 0.0311  0.0041  66  SER   A CA  
465  C C   . SER   A 60  ? 0.5619 0.3668 0.1130 -0.0579 0.0343  0.0028  66  SER   A C   
466  O O   . SER   A 60  ? 0.5675 0.3546 0.1011 -0.0673 0.0210  0.0084  66  SER   A O   
467  C CB  . SER   A 60  ? 0.5731 0.4083 0.1754 -0.0512 0.0200  0.0068  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.6295 0.4584 0.2181 -0.0490 0.0307  0.0007  66  SER   A OG  
469  N N   . SER   A 61  ? 0.5762 0.3731 0.1099 -0.0548 0.0531  -0.0040 67  SER   A N   
470  C CA  . SER   A 61  ? 0.6137 0.3770 0.1031 -0.0623 0.0630  -0.0067 67  SER   A CA  
471  C C   . SER   A 61  ? 0.6154 0.3762 0.0972 -0.0652 0.0671  -0.0051 67  SER   A C   
472  O O   . SER   A 61  ? 0.6421 0.3709 0.0831 -0.0738 0.0741  -0.0064 67  SER   A O   
473  C CB  . SER   A 61  ? 0.6374 0.3950 0.1187 -0.0558 0.0861  -0.0133 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.6420 0.4293 0.1559 -0.0447 0.1016  -0.0145 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.5789 0.3688 0.0956 -0.0594 0.0632  -0.0025 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.5892 0.3767 0.1000 -0.0629 0.0643  -0.0002 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.5975 0.3943 0.1279 -0.0647 0.0444  0.0066  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.6022 0.3978 0.1306 -0.0672 0.0439  0.0091  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.5852 0.3964 0.1181 -0.0547 0.0828  -0.0031 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6155 0.4189 0.1363 -0.0518 0.1051  -0.0073 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.6471 0.4201 0.1295 -0.0601 0.1163  -0.0079 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.6634 0.4323 0.1431 -0.0551 0.1429  -0.0110 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.6960 0.4405 0.1521 -0.0549 0.1547  -0.0151 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.6944 0.4163 0.1248 -0.0612 0.1397  -0.0166 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.6885 0.4308 0.1491 -0.0484 0.1818  -0.0169 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.5937 0.4006 0.1468 -0.0626 0.0300  0.0103  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.5894 0.4087 0.1721 -0.0612 0.0151  0.0176  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5753 0.4136 0.1797 -0.0542 0.0251  0.0155  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5735 0.4085 0.1832 -0.0562 0.0176  0.0208  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.6199 0.4154 0.1837 -0.0727 -0.0049 0.0272  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.6899 0.4686 0.2401 -0.0816 -0.0218 0.0327  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.7635 0.5172 0.2931 -0.0954 -0.0439 0.0443  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.8416 0.5661 0.3364 -0.1099 -0.0595 0.0488  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.8963 0.5821 0.3409 -0.1269 -0.0709 0.0532  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.9078 0.5817 0.3333 -0.1303 -0.0671 0.0535  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.8911 0.5468 0.2998 -0.1420 -0.0857 0.0572  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5602 0.4155 0.1744 -0.0474 0.0411  0.0086  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.5530 0.4225 0.1806 -0.0440 0.0502  0.0067  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.5204 0.4113 0.1702 -0.0371 0.0589  0.0025  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.5032 0.3991 0.1536 -0.0344 0.0636  -0.0003 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.6010 0.4633 0.2067 -0.0482 0.0613  0.0048  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6860 0.5290 0.2708 -0.0559 0.0553  0.0089  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7815 0.6147 0.3423 -0.0603 0.0696  0.0068  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8625 0.6709 0.3944 -0.0700 0.0642  0.0106  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.9201 0.6996 0.4210 -0.0780 0.0529  0.0131  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.5054 0.4053 0.1696 -0.0356 0.0613  0.0023  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.4927 0.4077 0.1713 -0.0325 0.0684  -0.0010 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.5032 0.4245 0.1754 -0.0360 0.0761  -0.0012 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.5224 0.4367 0.1847 -0.0403 0.0762  0.0006  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.4867 0.4006 0.1785 -0.0310 0.0677  -0.0008 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.4845 0.3957 0.1920 -0.0268 0.0618  0.0017  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.4942 0.4130 0.2167 -0.0227 0.0657  -0.0003 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.4902 0.3924 0.2026 -0.0270 0.0519  0.0077  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.4897 0.4059 0.2291 -0.0199 0.0593  0.0045  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.4945 0.4014 0.2297 -0.0226 0.0495  0.0103  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.4890 0.4237 0.1688 -0.0346 0.0815  -0.0021 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.4876 0.4325 0.1699 -0.0380 0.0876  0.0006  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.4725 0.4294 0.1659 -0.0407 0.0866  0.0017  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.4700 0.4317 0.1701 -0.0376 0.0856  0.0002  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.4850 0.4338 0.1680 -0.0348 0.0956  0.0019  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.5081 0.4392 0.1713 -0.0355 0.0991  0.0010  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.5248 0.4504 0.1787 -0.0403 0.1044  0.0034  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.5334 0.4505 0.1839 -0.0332 0.0970  -0.0017 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5528 0.4569 0.1818 -0.0429 0.1084  0.0025  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5628 0.4574 0.1872 -0.0368 0.0994  -0.0022 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.5789 0.4661 0.1912 -0.0417 0.1057  -0.0004 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.6380 0.4979 0.2182 -0.0471 0.1085  -0.0011 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.4687 0.4282 0.1612 -0.0481 0.0859  0.0048  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.4627 0.4296 0.1601 -0.0541 0.0826  0.0072  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.4603 0.4461 0.1751 -0.0534 0.0839  0.0139  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.4763 0.4698 0.1997 -0.0516 0.0897  0.0181  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.4715 0.4319 0.1595 -0.0641 0.0801  0.0094  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.4825 0.4411 0.1683 -0.0627 0.0838  0.0108  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.4607 0.4149 0.1454 -0.0531 0.0871  0.0072  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.4371 0.4289 0.1579 -0.0541 0.0801  0.0152  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.4239 0.4336 0.1655 -0.0525 0.0803  0.0231  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.4343 0.4498 0.1791 -0.0628 0.0701  0.0299  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.4546 0.4561 0.1805 -0.0692 0.0652  0.0254  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.4202 0.4302 0.1669 -0.0412 0.0855  0.0194  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.4295 0.4350 0.1748 -0.0337 0.0957  0.0170  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.4227 0.4201 0.1556 -0.0395 0.0825  0.0112  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.4221 0.4566 0.1913 -0.0646 0.0674  0.0416  75  SER   A N   
543  C CA  . SER   A 69  ? 0.4245 0.4662 0.2004 -0.0750 0.0547  0.0514  75  SER   A CA  
544  C C   . SER   A 69  ? 0.4160 0.4668 0.2094 -0.0643 0.0577  0.0532  75  SER   A C   
545  O O   . SER   A 69  ? 0.4161 0.4760 0.2285 -0.0526 0.0687  0.0543  75  SER   A O   
546  C CB  . SER   A 69  ? 0.4298 0.4892 0.2286 -0.0844 0.0481  0.0666  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.4789 0.5475 0.2897 -0.0940 0.0336  0.0792  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.4164 0.4597 0.1983 -0.0678 0.0504  0.0517  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.4107 0.4598 0.2060 -0.0580 0.0531  0.0526  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.4213 0.4766 0.2247 -0.0672 0.0390  0.0644  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.4389 0.4867 0.2261 -0.0832 0.0262  0.0689  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.4205 0.4531 0.1951 -0.0497 0.0608  0.0378  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.4422 0.4556 0.1876 -0.0584 0.0570  0.0299  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.4616 0.4623 0.1897 -0.0616 0.0605  0.0227  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.4525 0.4583 0.1874 -0.0633 0.0520  0.0298  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.4793 0.4597 0.1825 -0.0681 0.0612  0.0155  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.4775 0.4620 0.1843 -0.0707 0.0532  0.0219  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.4831 0.4548 0.1753 -0.0726 0.0588  0.0148  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.4058 0.4717 0.2319 -0.0581 0.0407  0.0702  77  SER   A N   
560  C CA  . SER   A 71  ? 0.4045 0.4767 0.2412 -0.0663 0.0258  0.0835  77  SER   A CA  
561  C C   . SER   A 71  ? 0.4168 0.4685 0.2208 -0.0717 0.0211  0.0750  77  SER   A C   
562  O O   . SER   A 71  ? 0.4277 0.4646 0.2099 -0.0655 0.0318  0.0594  77  SER   A O   
563  C CB  . SER   A 71  ? 0.4078 0.4994 0.2863 -0.0538 0.0306  0.0951  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.4420 0.5247 0.3143 -0.0389 0.0448  0.0831  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.4126 0.4627 0.2136 -0.0849 0.0044  0.0866  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.4322 0.4613 0.2016 -0.0920 0.0002  0.0807  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.4212 0.4538 0.2035 -0.0759 0.0097  0.0760  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.4057 0.4568 0.2235 -0.0651 0.0114  0.0852  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.4623 0.4872 0.2240 -0.1124 -0.0223 0.0970  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.5354 0.5464 0.2699 -0.1327 -0.0326 0.0992  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.6228 0.6108 0.3221 -0.1579 -0.0529 0.1082  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6985 0.6611 0.3565 -0.1772 -0.0566 0.1038  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7429 0.6889 0.3755 -0.2059 -0.0827 0.1200  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.4329 0.4472 0.1884 -0.0741 0.0173  0.0623  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.4311 0.4474 0.1973 -0.0601 0.0254  0.0581  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.4275 0.4538 0.2160 -0.0595 0.0154  0.0729  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.4333 0.4539 0.2115 -0.0740 0.0001  0.0827  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.4588 0.4536 0.1928 -0.0634 0.0318  0.0444  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4834 0.4617 0.1875 -0.0805 0.0264  0.0435  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.4526 0.4425 0.1689 -0.0841 0.0209  0.0505  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.4135 0.4519 0.2313 -0.0434 0.0241  0.0752  80  SER   A N   
582  C CA  . SER   A 74  ? 0.4194 0.4684 0.2656 -0.0400 0.0169  0.0907  80  SER   A CA  
583  C C   . SER   A 74  ? 0.4251 0.4733 0.2864 -0.0219 0.0315  0.0863  80  SER   A C   
584  O O   . SER   A 74  ? 0.4459 0.4837 0.2909 -0.0144 0.0448  0.0710  80  SER   A O   
585  C CB  . SER   A 74  ? 0.4300 0.5000 0.3113 -0.0432 0.0081  0.1092  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.4706 0.5520 0.3758 -0.0294 0.0245  0.1070  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.4120 0.4685 0.3026 -0.0164 0.0278  0.1006  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.4204 0.4723 0.3249 -0.0002 0.0418  0.0984  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.4268 0.4899 0.3622 0.0124  0.0574  0.1022  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.4103 0.4926 0.3823 0.0119  0.0522  0.1195  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.4125 0.4682 0.3391 -0.0001 0.0308  0.1148  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.4386 0.4767 0.3408 -0.0024 0.0269  0.1091  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.4392 0.4824 0.3725 0.0019  0.0193  0.1275  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.4475 0.4689 0.3282 0.0077  0.0445  0.0904  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.4469 0.4969 0.3674 0.0223  0.0762  0.0874  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.4554 0.5094 0.3968 0.0334  0.0947  0.0888  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.4873 0.5202 0.4212 0.0470  0.1146  0.0805  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.5024 0.5158 0.4020 0.0454  0.1147  0.0669  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.4649 0.5187 0.3859 0.0275  0.0972  0.0786  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.4661 0.5383 0.3961 0.0139  0.0794  0.0884  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.4660 0.5158 0.3960 0.0379  0.1192  0.0759  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.4957 0.5621 0.3965 0.0058  0.0775  0.0766  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.4930 0.5281 0.4590 0.0596  0.1323  0.0893  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.5278 0.5363 0.4821 0.0719  0.1543  0.0812  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.5543 0.5400 0.4689 0.0712  0.1686  0.0635  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.5527 0.5456 0.4722 0.0702  0.1756  0.0636  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.5185 0.5330 0.5202 0.0862  0.1725  0.0965  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.5480 0.5304 0.5363 0.0983  0.1944  0.0895  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.5710 0.5426 0.5516 0.0990  0.1858  0.0898  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.5724 0.5310 0.5501 0.1074  0.2242  0.0820  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.6006 0.5390 0.5654 0.1091  0.2060  0.0830  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.6056 0.5283 0.5646 0.1170  0.2456  0.0749  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.6109 0.5237 0.5639 0.1179  0.2360  0.0755  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.5724 0.5303 0.4467 0.0698  0.1704  0.0494  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5976 0.5305 0.4300 0.0662  0.1787  0.0341  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.6284 0.5248 0.4401 0.0742  0.2003  0.0278  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.6402 0.5234 0.4452 0.0762  0.1982  0.0270  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.6110 0.5418 0.4121 0.0541  0.1584  0.0242  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.6351 0.5380 0.3943 0.0494  0.1637  0.0109  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5965 0.5561 0.4117 0.0458  0.1410  0.0288  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6418 0.5186 0.4403 0.0777  0.2221  0.0233  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.6660 0.4998 0.4362 0.0836  0.2473  0.0161  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.6851 0.4860 0.4048 0.0748  0.2382  0.0036  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.6816 0.4880 0.3802 0.0631  0.2170  -0.0021 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.7271 0.5435 0.4808 0.0837  0.2688  0.0116  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.7995 0.6423 0.6059 0.0943  0.2852  0.0251  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.9297 0.7688 0.7726 0.1097  0.3061  0.0352  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.9907 0.7875 0.8081 0.1160  0.3346  0.0284  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.9402 0.8159 0.8354 0.1148  0.2937  0.0505  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.7060 0.4714 0.4076 0.0804  0.2550  0.0003  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.7418 0.4716 0.3948 0.0712  0.2473  -0.0101 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.7745 0.4797 0.3763 0.0564  0.2400  -0.0211 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.7912 0.4892 0.3832 0.0556  0.2522  -0.0231 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.7597 0.4470 0.3964 0.0797  0.2731  -0.0124 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.7830 0.4744 0.3535 0.0442  0.2200  -0.0268 87  SER   A N   
636  C CA  . SER   A 81  ? 0.8114 0.4787 0.3352 0.0283  0.2082  -0.0344 87  SER   A CA  
637  C C   . SER   A 81  ? 0.8520 0.4883 0.3386 0.0169  0.1951  -0.0391 87  SER   A C   
638  O O   . SER   A 81  ? 0.8520 0.4856 0.3483 0.0222  0.1972  -0.0374 87  SER   A O   
639  C CB  . SER   A 81  ? 0.8006 0.5079 0.3459 0.0225  0.1863  -0.0314 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.8002 0.5305 0.3591 0.0168  0.1620  -0.0293 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.8833 0.4954 0.3277 0.0001  0.1805  -0.0436 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.9126 0.4967 0.3226 -0.0140 0.1640  -0.0461 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.8679 0.4927 0.3151 -0.0151 0.1404  -0.0404 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.8796 0.4887 0.3107 -0.0238 0.1287  -0.0406 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.9924 0.5445 0.3531 -0.0337 0.1500  -0.0489 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.1210 0.6472 0.4528 -0.0344 0.1682  -0.0530 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.2227 0.7845 0.5787 -0.0352 0.1570  -0.0491 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.2707 0.8242 0.6042 -0.0513 0.1346  -0.0474 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.2158 0.8122 0.6131 -0.0205 0.1700  -0.0468 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.8194 0.4934 0.3129 -0.0079 0.1337  -0.0355 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7791 0.4898 0.3061 -0.0092 0.1150  -0.0306 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.7453 0.4774 0.3058 0.0034  0.1225  -0.0269 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.7366 0.4836 0.3117 0.0010  0.1108  -0.0241 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7579 0.5040 0.3104 -0.0104 0.1041  -0.0276 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.7881 0.5162 0.3125 -0.0223 0.0950  -0.0292 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.8113 0.5277 0.3198 -0.0368 0.0751  -0.0273 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.7987 0.5203 0.3127 -0.0202 0.1055  -0.0311 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.8328 0.5326 0.3171 -0.0492 0.0634  -0.0261 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.8250 0.5278 0.3108 -0.0324 0.0956  -0.0315 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.8502 0.5421 0.3212 -0.0471 0.0735  -0.0286 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.8912 0.5647 0.3360 -0.0606 0.0603  -0.0265 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.7199 0.4567 0.2964 0.0161  0.1410  -0.0251 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.6905 0.4501 0.3033 0.0274  0.1456  -0.0185 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.7069 0.4472 0.3221 0.0398  0.1698  -0.0171 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.7164 0.4453 0.3231 0.0428  0.1850  -0.0193 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.6449 0.4479 0.2957 0.0310  0.1393  -0.0125 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.6168 0.4421 0.2726 0.0213  0.1197  -0.0130 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.6074 0.4433 0.2718 0.0173  0.1078  -0.0109 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.6066 0.4419 0.2607 0.0167  0.1150  -0.0149 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.6000 0.4543 0.2712 0.0094  0.0942  -0.0111 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.6004 0.4546 0.2627 0.0093  0.1000  -0.0146 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.5948 0.4584 0.2665 0.0061  0.0909  -0.0128 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.5727 0.4527 0.2544 -0.0004 0.0802  -0.0124 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.7012 0.4427 0.3357 0.0483  0.1749  -0.0116 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.7026 0.4338 0.3547 0.0631  0.1996  -0.0068 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.6733 0.4466 0.3734 0.0709  0.2003  0.0034  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.6550 0.4610 0.3693 0.0641  0.1809  0.0057  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.7087 0.4335 0.3715 0.0683  0.1988  -0.0018 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.6953 0.4505 0.3688 0.0588  0.1715  0.0007  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.6839 0.4388 0.3302 0.0453  0.1588  -0.0078 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.6625 0.4342 0.3884 0.0843  0.2228  0.0102  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.6345 0.4469 0.4095 0.0902  0.2216  0.0223  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.6104 0.4573 0.4211 0.0894  0.1995  0.0344  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.6139 0.4546 0.4372 0.0951  0.2002  0.0406  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.6292 0.4333 0.4306 0.1051  0.2514  0.0293  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.5802 0.4587 0.4015 0.0806  0.1798  0.0370  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.5469 0.4515 0.3894 0.0755  0.1579  0.0465  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.5272 0.4657 0.3931 0.0697  0.1454  0.0542  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.5282 0.4714 0.3956 0.0704  0.1537  0.0519  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.5522 0.4451 0.3583 0.0643  0.1432  0.0356  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.5532 0.4515 0.3370 0.0540  0.1353  0.0257  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.5665 0.4475 0.3156 0.0449  0.1274  0.0146  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.5615 0.4592 0.3055 0.0347  0.1134  0.0110  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.5562 0.4593 0.2951 0.0320  0.1141  0.0071  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.5184 0.4342 0.2544 0.0237  0.1028  0.0044  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.5609 0.4547 0.2974 0.0376  0.1277  0.0059  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.5119 0.4704 0.3908 0.0621  0.1248  0.0629  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.4925 0.4768 0.3840 0.0530  0.1104  0.0692  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.4813 0.4613 0.3373 0.0406  0.0988  0.0566  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.5001 0.4739 0.3422 0.0349  0.0891  0.0549  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.4886 0.4913 0.4095 0.0492  0.0938  0.0873  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.4917 0.5087 0.4617 0.0599  0.1010  0.1055  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.4912 0.5321 0.4909 0.0575  0.0975  0.1170  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.5046 0.5116 0.4947 0.0721  0.1110  0.1128  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.4871 0.5446 0.5401 0.0673  0.1038  0.1366  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.4997 0.5215 0.5427 0.0832  0.1189  0.1319  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.4987 0.5472 0.5754 0.0808  0.1152  0.1444  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.5062 0.5721 0.6426 0.0917  0.1227  0.1657  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.4510 0.4339 0.2943 0.0365  0.1005  0.0487  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.4324 0.4134 0.2494 0.0257  0.0908  0.0390  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.4137 0.4117 0.2388 0.0153  0.0760  0.0473  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.4098 0.4231 0.2563 0.0149  0.0738  0.0571  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.4384 0.4134 0.2394 0.0257  0.0982  0.0285  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.4466 0.4199 0.2266 0.0164  0.0901  0.0197  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.4723 0.4329 0.2345 0.0172  0.0963  0.0100  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.4621 0.4051 0.2131 0.0219  0.1042  0.0062  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.4954 0.4616 0.2521 0.0117  0.0921  0.0065  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.3991 0.3925 0.2059 0.0057  0.0663  0.0439  96  SER   A N   
719  C CA  . SER   A 90  ? 0.3894 0.3901 0.1925 -0.0071 0.0533  0.0500  96  SER   A CA  
720  C C   . SER   A 90  ? 0.3879 0.3866 0.1722 -0.0139 0.0547  0.0402  96  SER   A C   
721  O O   . SER   A 90  ? 0.3779 0.3705 0.1534 -0.0090 0.0635  0.0293  96  SER   A O   
722  C CB  . SER   A 90  ? 0.4126 0.4042 0.2025 -0.0149 0.0445  0.0524  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.4542 0.4327 0.2230 -0.0154 0.0505  0.0398  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.3840 0.3857 0.1619 -0.0259 0.0453  0.0452  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.3951 0.3919 0.1545 -0.0333 0.0469  0.0373  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.3926 0.3953 0.1601 -0.0251 0.0558  0.0316  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.4008 0.3962 0.1551 -0.0251 0.0616  0.0214  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.4142 0.3952 0.1499 -0.0378 0.0513  0.0268  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.4701 0.4412 0.1918 -0.0478 0.0441  0.0316  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.5104 0.4687 0.2077 -0.0632 0.0390  0.0329  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.4815 0.4504 0.2071 -0.0456 0.0410  0.0359  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.5202 0.4687 0.2060 -0.0705 0.0330  0.0377  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.5061 0.4622 0.2102 -0.0599 0.0333  0.0401  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.3781 0.3932 0.1691 -0.0180 0.0578  0.0393  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.3785 0.3970 0.1756 -0.0109 0.0673  0.0353  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.3666 0.3969 0.1737 -0.0172 0.0627  0.0429  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.3542 0.3951 0.1768 -0.0229 0.0531  0.0559  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.3762 0.3952 0.1898 0.0018  0.0778  0.0376  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.3993 0.4119 0.2078 0.0086  0.0905  0.0304  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.4175 0.4151 0.2000 0.0068  0.0910  0.0177  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.4014 0.4095 0.2235 0.0199  0.1039  0.0336  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.3642 0.3920 0.1621 -0.0175 0.0678  0.0360  99  MET   A N   
743  C CA  . MET   A 93  ? 0.3688 0.4054 0.1724 -0.0244 0.0642  0.0416  99  MET   A CA  
744  C C   . MET   A 93  ? 0.3712 0.4118 0.1854 -0.0161 0.0759  0.0404  99  MET   A C   
745  O O   . MET   A 93  ? 0.3832 0.4119 0.1816 -0.0113 0.0837  0.0296  99  MET   A O   
746  C CB  . MET   A 93  ? 0.3861 0.4105 0.1629 -0.0345 0.0602  0.0336  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.4113 0.4251 0.1707 -0.0436 0.0526  0.0330  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.4591 0.4524 0.1860 -0.0542 0.0542  0.0229  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.3285 0.3174 0.0591 -0.0417 0.0657  0.0107  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.3517 0.4080 0.1929 -0.0152 0.0773  0.0524  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.3461 0.4034 0.1950 -0.0080 0.0916  0.0510  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.3450 0.4064 0.1896 -0.0165 0.0886  0.0519  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.3312 0.4015 0.1805 -0.0278 0.0755  0.0599  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.3269 0.3958 0.2105 0.0016  0.1027  0.0624  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.3493 0.4104 0.2371 0.0117  0.1091  0.0613  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.3341 0.4035 0.2581 0.0230  0.1251  0.0724  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.3719 0.4090 0.2254 0.0158  0.1163  0.0452  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.3566 0.4084 0.1891 -0.0123 0.1001  0.0441  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.3696 0.4228 0.1972 -0.0186 0.1005  0.0443  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.3840 0.4348 0.2188 -0.0110 0.1185  0.0447  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.3965 0.4350 0.2251 -0.0019 0.1306  0.0396  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.3816 0.4179 0.1771 -0.0231 0.0954  0.0322  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.3777 0.4371 0.2226 -0.0158 0.1211  0.0508  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.3838 0.4376 0.2310 -0.0104 0.1401  0.0506  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.4144 0.4448 0.2217 -0.0133 0.1398  0.0374  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.4231 0.4533 0.2187 -0.0219 0.1282  0.0356  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.3626 0.4367 0.2402 -0.0153 0.1434  0.0640  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3608 0.4239 0.2343 -0.0105 0.1663  0.0619  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.3356 0.4356 0.2596 -0.0135 0.1404  0.0808  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.4177 0.4263 0.2030 -0.0071 0.1508  0.0289  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4423 0.4279 0.1911 -0.0109 0.1475  0.0187  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4635 0.4228 0.1864 -0.0064 0.1567  0.0112  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.4766 0.4340 0.2073 0.0005  0.1648  0.0117  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.4675 0.4041 0.1578 -0.0115 0.1542  0.0049  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.4884 0.3946 0.1461 -0.0114 0.1591  -0.0016 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.4935 0.3943 0.1437 -0.0108 0.1453  -0.0058 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.4821 0.3918 0.1369 -0.0137 0.1288  -0.0063 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.5176 0.3987 0.1407 -0.0197 0.1582  -0.0047 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.5732 0.4174 0.1558 -0.0232 0.1612  -0.0103 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.6160 0.4394 0.1844 -0.0198 0.1832  -0.0124 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.6033 0.4283 0.1598 -0.0300 0.1442  -0.0131 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.6472 0.4354 0.1739 -0.0265 0.1784  -0.0175 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.6492 0.4390 0.1694 -0.0332 0.1534  -0.0171 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.5170 0.3980 0.1514 -0.0079 0.1540  -0.0090 105 SER   A N   
785  C CA  . SER   A 99  ? 0.5414 0.4102 0.1619 -0.0092 0.1426  -0.0129 105 SER   A CA  
786  C C   . SER   A 99  ? 0.5750 0.4080 0.1619 -0.0099 0.1560  -0.0172 105 SER   A C   
787  O O   . SER   A 99  ? 0.5753 0.3993 0.1608 -0.0055 0.1776  -0.0169 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5322 0.4259 0.1833 -0.0033 0.1363  -0.0107 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5649 0.4556 0.2233 0.0038  0.1493  -0.0100 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.5978 0.4093 0.1588 -0.0159 0.1440  -0.0205 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.6374 0.4098 0.1606 -0.0189 0.1545  -0.0251 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.6548 0.4195 0.1695 -0.0231 0.1374  -0.0262 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.6390 0.4254 0.1732 -0.0252 0.1174  -0.0233 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.6932 0.4272 0.1694 -0.0296 0.1602  -0.0276 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.7272 0.4577 0.1892 -0.0413 0.1361  -0.0251 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.7978 0.4900 0.2126 -0.0524 0.1428  -0.0266 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.8255 0.4760 0.1924 -0.0648 0.1364  -0.0285 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.7942 0.4956 0.2173 -0.0502 0.1541  -0.0254 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.6879 0.4210 0.1743 -0.0246 0.1455  -0.0301 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.6987 0.4254 0.1781 -0.0302 0.1273  -0.0301 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.7051 0.4282 0.1727 -0.0432 0.1016  -0.0266 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.7399 0.4352 0.1721 -0.0534 0.1000  -0.0267 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.7385 0.4178 0.1727 -0.0344 0.1414  -0.0355 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.7420 0.4178 0.1820 -0.0232 0.1721  -0.0376 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.7042 0.4041 0.1639 -0.0216 0.1730  -0.0344 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.6671 0.4202 0.1683 -0.0420 0.0838  -0.0223 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.6503 0.4078 0.1551 -0.0515 0.0604  -0.0163 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.6133 0.4103 0.1619 -0.0441 0.0566  -0.0130 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6021 0.4114 0.1694 -0.0477 0.0395  -0.0072 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.5872 0.4036 0.1542 -0.0338 0.0730  -0.0158 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.5449 0.3934 0.1466 -0.0281 0.0714  -0.0135 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.5098 0.3840 0.1437 -0.0219 0.0695  -0.0130 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.4832 0.3780 0.1403 -0.0194 0.0674  -0.0114 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.5466 0.4020 0.1509 -0.0233 0.0868  -0.0149 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.5522 0.3889 0.1319 -0.0303 0.0860  -0.0142 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.5373 0.3693 0.1132 -0.0370 0.0700  -0.0107 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.5621 0.3889 0.1282 -0.0291 0.1020  -0.0160 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.5048 0.3746 0.1370 -0.0204 0.0706  -0.0144 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.4916 0.3823 0.1504 -0.0161 0.0686  -0.0137 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4853 0.3858 0.1615 -0.0198 0.0557  -0.0099 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.5025 0.3896 0.1689 -0.0268 0.0441  -0.0066 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4988 0.3785 0.1489 -0.0156 0.0704  -0.0152 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.5434 0.4125 0.1821 -0.0084 0.0893  -0.0181 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.4563 0.3773 0.1571 -0.0160 0.0582  -0.0095 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.4410 0.3705 0.1626 -0.0176 0.0509  -0.0058 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.4347 0.3715 0.1660 -0.0163 0.0532  -0.0051 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.4436 0.3891 0.1959 -0.0150 0.0541  -0.0032 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.4164 0.3480 0.1325 -0.0166 0.0564  -0.0066 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.4003 0.3367 0.1220 -0.0161 0.0589  -0.0062 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.3837 0.3324 0.1166 -0.0135 0.0675  -0.0087 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.3658 0.3196 0.0957 -0.0123 0.0725  -0.0106 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.3707 0.3216 0.1158 -0.0133 0.0692  -0.0080 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.3752 0.3301 0.1243 -0.0134 0.0776  -0.0106 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.3883 0.3436 0.1253 -0.0163 0.0808  -0.0119 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.3906 0.3427 0.1222 -0.0172 0.0787  -0.0107 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.3772 0.3289 0.1437 -0.0119 0.0813  -0.0093 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.3727 0.3280 0.1564 -0.0100 0.0806  -0.0071 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.3931 0.3395 0.1547 -0.0138 0.0923  -0.0128 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.3705 0.3247 0.1809 -0.0070 0.0855  -0.0031 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.3904 0.3492 0.1227 -0.0190 0.0846  -0.0131 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.4028 0.3625 0.1259 -0.0244 0.0857  -0.0124 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.4180 0.3665 0.1348 -0.0290 0.0916  -0.0151 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.4109 0.3553 0.1286 -0.0291 0.0959  -0.0170 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.4055 0.3746 0.1281 -0.0261 0.0836  -0.0093 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.4166 0.3879 0.1327 -0.0344 0.0816  -0.0057 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.4248 0.3985 0.1409 -0.0353 0.0812  -0.0036 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.4146 0.3971 0.1375 -0.0358 0.0776  0.0004  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.4354 0.3757 0.1443 -0.0329 0.0935  -0.0156 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.4629 0.3859 0.1613 -0.0374 0.1019  -0.0190 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.4959 0.4108 0.1743 -0.0479 0.1001  -0.0183 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.4875 0.4094 0.1667 -0.0492 0.0943  -0.0153 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.4858 0.4003 0.1950 -0.0316 0.1073  -0.0200 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.5395 0.4587 0.2718 -0.0231 0.1092  -0.0188 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.5927 0.5024 0.3391 -0.0184 0.1146  -0.0172 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.6595 0.5503 0.3994 -0.0201 0.1310  -0.0214 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.6861 0.5720 0.4436 -0.0152 0.1433  -0.0214 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.6821 0.5835 0.4689 -0.0085 0.1380  -0.0162 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.6908 0.5539 0.4360 -0.0178 0.1618  -0.0263 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.5300 0.4267 0.1881 -0.0567 0.1058  -0.0210 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.5608 0.4428 0.1939 -0.0700 0.1034  -0.0202 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.5991 0.4512 0.2161 -0.0717 0.1182  -0.0267 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.5940 0.4434 0.2277 -0.0609 0.1291  -0.0298 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.5682 0.4478 0.1841 -0.0822 0.0964  -0.0169 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.5953 0.4521 0.1934 -0.0851 0.1087  -0.0230 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.6332 0.4614 0.2191 -0.0856 0.1192  -0.0278 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.6772 0.4708 0.2435 -0.0875 0.1366  -0.0347 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.6895 0.4645 0.2491 -0.0854 0.1538  -0.0404 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.7005 0.4526 0.2595 -0.0801 0.1732  -0.0455 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.7362 0.5019 0.2619 -0.1061 0.1338  -0.0350 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.8231 0.5738 0.3151 -0.1240 0.1274  -0.0337 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.9290 0.6525 0.3801 -0.1452 0.1200  -0.0319 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.9634 0.7030 0.4134 -0.1568 0.0994  -0.0226 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.9592 0.6393 0.3765 -0.1513 0.1371  -0.0399 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.6797 0.4642 0.2367 -0.0890 0.1479  -0.0387 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.6825 0.4496 0.2311 -0.0888 0.1638  -0.0435 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.6437 0.4342 0.2346 -0.0713 0.1697  -0.0429 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.6586 0.4364 0.2487 -0.0696 0.1853  -0.0463 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.7107 0.4706 0.2293 -0.1044 0.1539  -0.0413 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.7814 0.5176 0.2575 -0.1249 0.1442  -0.0395 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.8015 0.5603 0.2818 -0.1328 0.1200  -0.0300 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.8297 0.5204 0.2594 -0.1397 0.1560  -0.0451 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.8266 0.5554 0.2644 -0.1533 0.1147  -0.0288 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.8536 0.5388 0.2564 -0.1587 0.1358  -0.0385 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.5964 0.4183 0.2212 -0.0603 0.1572  -0.0380 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.5561 0.3993 0.2188 -0.0463 0.1583  -0.0358 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.5101 0.3828 0.1875 -0.0433 0.1401  -0.0309 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.5037 0.3866 0.1739 -0.0474 0.1269  -0.0280 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.4832 0.3681 0.1819 -0.0363 0.1410  -0.0296 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.4659 0.3739 0.1783 -0.0323 0.1269  -0.0257 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.4625 0.3729 0.1565 -0.0401 0.1198  -0.0249 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.4719 0.3707 0.1528 -0.0456 0.1263  -0.0269 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.4627 0.3800 0.2034 -0.0238 0.1296  -0.0239 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.4632 0.3977 0.2105 -0.0216 0.1164  -0.0209 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.4525 0.3715 0.2173 -0.0165 0.1310  -0.0208 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.4366 0.3606 0.1303 -0.0410 0.1071  -0.0210 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.4311 0.3613 0.1157 -0.0471 0.0983  -0.0170 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.4220 0.3671 0.1230 -0.0397 0.0937  -0.0148 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.4233 0.3687 0.1193 -0.0433 0.0906  -0.0126 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.4204 0.3587 0.1030 -0.0511 0.0894  -0.0122 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.4075 0.3562 0.0906 -0.0561 0.0792  -0.0049 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.4345 0.3554 0.0973 -0.0603 0.0926  -0.0142 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.4054 0.3597 0.1225 -0.0308 0.0922  -0.0149 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.3999 0.3627 0.1275 -0.0248 0.0885  -0.0135 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.3926 0.3591 0.1292 -0.0184 0.0857  -0.0134 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.3953 0.3587 0.1334 -0.0179 0.0864  -0.0141 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.3789 0.3482 0.1181 -0.0146 0.0823  -0.0123 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.3717 0.3378 0.1110 -0.0114 0.0790  -0.0121 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.3649 0.3306 0.0974 -0.0088 0.0795  -0.0109 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.3503 0.3197 0.0847 -0.0074 0.0812  -0.0093 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.3862 0.3482 0.1321 -0.0107 0.0753  -0.0120 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.4093 0.3724 0.1561 -0.0105 0.0761  -0.0122 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.3873 0.3494 0.1469 -0.0114 0.0763  -0.0112 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.4316 0.3900 0.1822 -0.0110 0.0708  -0.0110 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.3705 0.3288 0.0947 -0.0082 0.0790  -0.0111 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.3791 0.3317 0.0947 -0.0054 0.0843  -0.0106 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.3932 0.3385 0.1050 -0.0031 0.0848  -0.0114 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.3897 0.3284 0.0986 -0.0055 0.0784  -0.0125 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3929 0.3314 0.0922 -0.0072 0.0849  -0.0115 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.4073 0.3347 0.0949 -0.0042 0.0950  -0.0118 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3986 0.3430 0.1006 -0.0095 0.0846  -0.0104 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.3992 0.3464 0.1146 0.0012  0.0921  -0.0095 125 SER   A N   
922  C CA  . SER   A 119 ? 0.4161 0.3545 0.1277 0.0040  0.0941  -0.0099 125 SER   A CA  
923  C C   . SER   A 119 ? 0.4437 0.3703 0.1489 0.0094  0.1065  -0.0093 125 SER   A C   
924  O O   . SER   A 119 ? 0.4493 0.3561 0.1385 0.0102  0.1099  -0.0120 125 SER   A O   
925  C CB  . SER   A 119 ? 0.4268 0.3791 0.1543 0.0047  0.0912  -0.0068 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.4563 0.3996 0.1807 0.0075  0.0929  -0.0067 125 SER   A OG  
927  N N   . THR   A 120 ? 0.4517 0.3887 0.1696 0.0127  0.1146  -0.0053 126 THR   A N   
928  C CA  . THR   A 120 ? 0.4731 0.3991 0.1902 0.0191  0.1310  -0.0036 126 THR   A CA  
929  C C   . THR   A 120 ? 0.5019 0.4282 0.2173 0.0183  0.1393  -0.0028 126 THR   A C   
930  O O   . THR   A 120 ? 0.4961 0.4343 0.2142 0.0131  0.1306  -0.0025 126 THR   A O   
931  C CB  . THR   A 120 ? 0.4734 0.4150 0.2200 0.0262  0.1359  0.0046  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.4671 0.4345 0.2389 0.0245  0.1308  0.0122  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.4825 0.4242 0.2308 0.0262  0.1272  0.0046  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.5250 0.4368 0.2360 0.0235  0.1577  -0.0023 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5482 0.4596 0.2595 0.0232  0.1691  -0.0006 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.5718 0.4659 0.2828 0.0309  0.1945  0.0007  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.5908 0.4674 0.2949 0.0361  0.2035  -0.0011 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.5755 0.4724 0.2934 0.0315  0.2078  0.0038  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.5968 0.4756 0.3158 0.0389  0.2370  0.0054  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.5756 0.4841 0.3408 0.0440  0.2475  0.0174  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.5528 0.4968 0.3544 0.0434  0.2312  0.0264  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.5909 0.4838 0.3539 0.0477  0.2745  0.0183  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.5834 0.5054 0.3960 0.0526  0.2871  0.0318  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.5578 0.5064 0.3794 0.0424  0.2676  0.0356  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.5439 0.5255 0.4126 0.0437  0.2669  0.0492  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.5963 0.5489 0.4670 0.0630  0.2865  0.0462  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.6894 0.6181 0.5571 0.0742  0.3045  0.0439  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.7547 0.6403 0.5781 0.0752  0.3245  0.0322  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.6751 0.6283 0.5879 0.0818  0.2978  0.0559  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.5491 0.4823 0.3274 0.0320  0.2518  0.0249  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.5258 0.4789 0.3080 0.0225  0.2336  0.0273  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4912 0.4745 0.2978 0.0197  0.2074  0.0325  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4775 0.4840 0.3033 0.0134  0.1955  0.0394  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4726 0.4526 0.2753 0.0230  0.1986  0.0293  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4530 0.4550 0.2726 0.0198  0.1764  0.0334  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4756 0.4597 0.2617 0.0171  0.1642  0.0219  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5078 0.4676 0.2714 0.0210  0.1732  0.0150  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.4274 0.4459 0.2854 0.0277  0.1799  0.0444  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4222 0.4611 0.3248 0.0324  0.1935  0.0593  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.4231 0.4617 0.3530 0.0447  0.2084  0.0663  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.4130 0.4834 0.3457 0.0234  0.1736  0.0723  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.4488 0.4429 0.2314 0.0099  0.1447  0.0205  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.4345 0.4162 0.1940 0.0075  0.1334  0.0119  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.4130 0.4100 0.1881 0.0062  0.1210  0.0157  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.3968 0.4111 0.1880 0.0012  0.1132  0.0225  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.4377 0.4093 0.1739 0.0005  0.1254  0.0055  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.4271 0.4143 0.1742 -0.0055 0.1194  0.0099  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.4408 0.4042 0.1635 -0.0015 0.1137  -0.0005 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.4021 0.3900 0.1698 0.0093  0.1193  0.0118  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.3950 0.3922 0.1717 0.0074  0.1089  0.0144  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.3986 0.3884 0.1577 0.0024  0.0993  0.0070  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.4049 0.3797 0.1471 0.0030  0.1002  0.0003  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.3946 0.3931 0.1577 -0.0037 0.0905  0.0091  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.3939 0.3859 0.1449 -0.0082 0.0850  0.0031  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.3871 0.3803 0.1399 -0.0102 0.0807  0.0049  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.3837 0.3849 0.1442 -0.0138 0.0765  0.0120  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.3860 0.3795 0.1323 -0.0153 0.0819  0.0026  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.3847 0.3777 0.1291 -0.0149 0.0849  0.0022  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.3975 0.3800 0.1321 -0.0133 0.0860  -0.0032 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.3791 0.3820 0.1323 -0.0176 0.0854  0.0087  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.4015 0.3812 0.1313 -0.0142 0.0881  -0.0031 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.3793 0.3807 0.1295 -0.0182 0.0889  0.0084  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.3844 0.3732 0.1210 -0.0165 0.0906  0.0020  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.3859 0.3707 0.1319 -0.0094 0.0806  -0.0004 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.3854 0.3684 0.1299 -0.0122 0.0779  0.0000  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.3912 0.3712 0.1276 -0.0203 0.0770  -0.0018 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.3970 0.3719 0.1306 -0.0204 0.0802  -0.0067 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.3804 0.3553 0.1220 -0.0090 0.0790  -0.0044 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.3974 0.3779 0.1290 -0.0277 0.0728  0.0030  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.4084 0.3787 0.1240 -0.0375 0.0736  0.0008  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.4176 0.3767 0.1260 -0.0385 0.0801  -0.0048 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.4216 0.3822 0.1347 -0.0355 0.0791  -0.0039 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.4466 0.4166 0.1546 -0.0480 0.0646  0.0091  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.5056 0.4575 0.1873 -0.0616 0.0654  0.0069  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.5088 0.4553 0.1839 -0.0637 0.0694  0.0032  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.5551 0.4947 0.2199 -0.0706 0.0630  0.0086  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.4215 0.3691 0.1209 -0.0420 0.0883  -0.0102 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.4384 0.3747 0.1339 -0.0434 0.0981  -0.0145 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.4611 0.3754 0.1295 -0.0555 0.1057  -0.0170 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.4686 0.3699 0.1303 -0.0580 0.1169  -0.0204 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.4378 0.3776 0.1528 -0.0349 0.1051  -0.0179 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.4445 0.3983 0.1762 -0.0266 0.0966  -0.0156 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.4362 0.3701 0.1503 -0.0349 0.1111  -0.0204 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.4682 0.3755 0.1190 -0.0641 0.1006  -0.0150 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.5028 0.3827 0.1199 -0.0781 0.1073  -0.0176 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.5336 0.3951 0.1252 -0.0896 0.1082  -0.0166 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.5564 0.3888 0.1186 -0.0993 0.1214  -0.0218 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.5059 0.3831 0.1087 -0.0875 0.0967  -0.0134 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.4887 0.3788 0.1106 -0.0784 0.0975  -0.0148 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.4814 0.3709 0.0916 -0.0886 0.0860  -0.0092 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.4847 0.3989 0.1149 -0.0868 0.0704  0.0009  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.4940 0.4173 0.1276 -0.0932 0.0586  0.0092  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.5018 0.4097 0.1145 -0.1042 0.0580  0.0083  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.4345 0.3814 0.0935 -0.0891 0.0479  0.0192  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.5326 0.4078 0.1335 -0.0885 0.0961  -0.0102 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.5506 0.4092 0.1282 -0.0993 0.0948  -0.0080 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.5547 0.4080 0.1385 -0.0935 0.1110  -0.0142 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.5679 0.4035 0.1291 -0.1031 0.1135  -0.0136 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.5616 0.4371 0.1504 -0.1000 0.0748  0.0032  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.5927 0.4942 0.2185 -0.0828 0.0735  0.0039  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.6084 0.5232 0.2554 -0.0710 0.0789  -0.0004 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.5981 0.5033 0.2285 -0.0822 0.0668  0.0090  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.5326 0.4009 0.1472 -0.0790 0.1205  -0.0187 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.5244 0.3912 0.1519 -0.0739 0.1344  -0.0222 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.5424 0.3840 0.1545 -0.0787 0.1571  -0.0289 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.5299 0.3771 0.1667 -0.0692 0.1693  -0.0317 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.4939 0.3868 0.1617 -0.0587 0.1313  -0.0215 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.4878 0.4000 0.1673 -0.0534 0.1129  -0.0161 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.4782 0.4082 0.1877 -0.0414 0.1101  -0.0161 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.4921 0.4011 0.1617 -0.0582 0.1065  -0.0122 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.5691 0.3799 0.1387 -0.0943 0.1630  -0.0305 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.5997 0.3767 0.1438 -0.1013 0.1879  -0.0377 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.6073 0.3840 0.1770 -0.0925 0.2122  -0.0412 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.6132 0.3722 0.1838 -0.0903 0.2360  -0.0463 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.6392 0.3781 0.1250 -0.1228 0.1879  -0.0381 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.6620 0.3998 0.1224 -0.1355 0.1611  -0.0311 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.6953 0.3874 0.0927 -0.1599 0.1627  -0.0313 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.6698 0.4176 0.1406 -0.1311 0.1552  -0.0314 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.5968 0.3924 0.1893 -0.0876 0.2066  -0.0374 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.5976 0.3973 0.2193 -0.0806 0.2261  -0.0380 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5962 0.4201 0.2696 -0.0649 0.2309  -0.0362 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5919 0.4158 0.2928 -0.0597 0.2513  -0.0356 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.5799 0.3922 0.2089 -0.0817 0.2153  -0.0336 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.5652 0.4066 0.2120 -0.0753 0.1872  -0.0281 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.5770 0.4189 0.2013 -0.0812 0.1666  -0.0249 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.5413 0.4126 0.2316 -0.0623 0.1779  -0.0246 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.5602 0.4294 0.2118 -0.0712 0.1487  -0.0206 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.5446 0.4298 0.2324 -0.0607 0.1547  -0.0210 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.5302 0.4161 0.2616 -0.0530 0.1865  -0.0228 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.5371 0.4450 0.2540 -0.0509 0.1420  -0.0177 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.5252 0.4356 0.2861 -0.0450 0.1695  -0.0180 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.5249 0.4435 0.2746 -0.0444 0.1485  -0.0165 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.5980 0.4416 0.2859 -0.0580 0.2129  -0.0341 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.6066 0.4704 0.3389 -0.0451 0.2138  -0.0310 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.6538 0.4987 0.3926 -0.0425 0.2407  -0.0342 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.6368 0.4967 0.4201 -0.0320 0.2465  -0.0295 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.5971 0.4770 0.3311 -0.0412 0.1916  -0.0294 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.5968 0.4983 0.3367 -0.0392 0.1674  -0.0252 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.5960 0.5070 0.3325 -0.0364 0.1517  -0.0245 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.5794 0.5002 0.3573 -0.0319 0.1632  -0.0200 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.7109 0.5210 0.4051 -0.0527 0.2563  -0.0412 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.7643 0.5484 0.4571 -0.0510 0.2855  -0.0455 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.8129 0.5705 0.4975 -0.0551 0.3175  -0.0487 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.8373 0.5643 0.5107 -0.0555 0.3462  -0.0537 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.8246 0.5778 0.4648 -0.0621 0.2855  -0.0520 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.8834 0.6564 0.5307 -0.0582 0.2613  -0.0495 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.8786 0.6797 0.5725 -0.0448 0.2547  -0.0444 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.9306 0.6903 0.5367 -0.0699 0.2484  -0.0516 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.8325 0.5961 0.5165 -0.0595 0.3150  -0.0467 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.8726 0.6077 0.5430 -0.0654 0.3467  -0.0500 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.8608 0.6223 0.5779 -0.0590 0.3491  -0.0428 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.8743 0.6159 0.5868 -0.0632 0.3765  -0.0444 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.9556 0.6524 0.5521 -0.0855 0.3456  -0.0566 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.0360 0.7538 0.6202 -0.0914 0.3098  -0.0521 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.1730 0.8557 0.6906 -0.1120 0.3054  -0.0550 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.1799 0.8747 0.6945 -0.1163 0.2880  -0.0504 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.2413 0.8820 0.7080 -0.1248 0.3187  -0.0612 145 GLU   A OE2 
1078 N N1  . A1BRL B .   ? 0.6474 0.4588 0.2421 0.0072  0.1605  -0.0224 201 A1BRL A N1  
1079 N N3  . A1BRL B .   ? 0.5205 0.4239 0.2224 0.0173  0.1112  -0.0086 201 A1BRL A N3  
1080 C C4  . A1BRL B .   ? 0.6630 0.4413 0.2463 0.0177  0.2283  -0.0208 201 A1BRL A C4  
1081 C C5  . A1BRL B .   ? 0.6758 0.4314 0.2426 0.0196  0.2310  -0.0245 201 A1BRL A C5  
1082 C C6  . A1BRL B .   ? 0.6747 0.4387 0.2415 0.0155  0.2073  -0.0256 201 A1BRL A C6  
1083 C C7  . A1BRL B .   ? 0.6581 0.4530 0.2432 0.0108  0.1834  -0.0229 201 A1BRL A C7  
1084 C C8  . A1BRL B .   ? 0.6572 0.4564 0.2423 0.0061  0.1538  -0.0246 201 A1BRL A C8  
1085 C C10 . A1BRL B .   ? 0.6360 0.4184 0.2139 0.0064  0.1437  -0.0266 201 A1BRL A C10 
1086 C C13 . A1BRL B .   ? 0.5769 0.4325 0.2327 0.0161  0.1270  -0.0162 201 A1BRL A C13 
1087 C C15 . A1BRL B .   ? 0.5890 0.4309 0.2403 0.0228  0.1477  -0.0160 201 A1BRL A C15 
1088 O O1  . A1BRL B .   ? 0.5347 0.4069 0.2255 0.0273  0.1313  -0.0084 201 A1BRL A O1  
1089 C C14 . A1BRL B .   ? 0.5446 0.4235 0.2298 0.0209  0.1231  -0.0108 201 A1BRL A C14 
1090 C C12 . A1BRL B .   ? 0.6011 0.4254 0.2233 0.0087  0.1218  -0.0213 201 A1BRL A C12 
1091 C C11 . A1BRL B .   ? 0.6224 0.4201 0.2103 0.0005  0.1219  -0.0252 201 A1BRL A C11 
1092 N N2  . A1BRL B .   ? 0.6198 0.4365 0.2373 0.0158  0.1505  -0.0212 201 A1BRL A N2  
1093 C C9  . A1BRL B .   ? 0.6300 0.4539 0.2521 0.0165  0.1575  -0.0200 201 A1BRL A C9  
1094 O O   . A1BRL B .   ? 0.6136 0.4618 0.2677 0.0239  0.1651  -0.0143 201 A1BRL A O   
1095 C C1  . A1BRL B .   ? 0.6221 0.4606 0.2359 0.0046  0.1478  -0.0195 201 A1BRL A C1  
1096 C C   . A1BRL B .   ? 0.6003 0.4592 0.2289 0.0010  0.1267  -0.0183 201 A1BRL A C   
1097 C C2  . A1BRL B .   ? 0.6442 0.4596 0.2442 0.0095  0.1812  -0.0197 201 A1BRL A C2  
1098 N N   . A1BRL B .   ? 0.6264 0.4679 0.2431 0.0056  0.1584  -0.0179 201 A1BRL A N   
1099 C C3  . A1BRL B .   ? 0.6448 0.4521 0.2430 0.0123  0.2026  -0.0186 201 A1BRL A C3  
# 
