data_7I6H
# 
_entry.id   7I6H 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I6H         pdb_00007i6h 10.2210/pdb7i6h/pdb 
WWPDB D_1001408376 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I6H 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                    15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S,4aR,8aR)-1-[(4-methoxypyridin-3-yl)acetyl]decahydroquinoline-3-carboxamide' 331.409   3   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                       65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                             78.133    4   ?         ? ? ? 
5 water       nat water                                                                            18.015    256 ?         ? ? ? 
# 
_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,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S,4aR,8aR)-1-[(4-methoxypyridin-3-yl)acetyl]decahydroquinoline-3-carboxamide' A1B4W 
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 
A1B4W non-polymer         . '(3S,4aR,8aR)-1-[(4-methoxypyridin-3-yl)acetyl]decahydroquinoline-3-carboxamide' ? 'C18 H25 N3 O3'  
331.409 
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 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 ?   ?   ?   C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B4W 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4W 
_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 
C 2 A1B4W 1   201 201 A1B4W LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 2   DMS   DMS A . 
F 4 DMS   1   204 6   DMS   DMS A . 
G 2 A1B4W 1   201 201 A1B4W LIG C . 
H 2 A1B4W 1   202 202 A1B4W LIG C . 
I 3 ZN    1   203 1   ZN    ZN  C . 
J 4 DMS   1   204 2   DMS   DMS C . 
K 4 DMS   1   205 6   DMS   DMS C . 
L 5 HOH   1   301 184 HOH   HOH A . 
L 5 HOH   2   302 95  HOH   HOH A . 
L 5 HOH   3   303 236 HOH   HOH A . 
L 5 HOH   4   304 103 HOH   HOH A . 
L 5 HOH   5   305 259 HOH   HOH A . 
L 5 HOH   6   306 58  HOH   HOH A . 
L 5 HOH   7   307 109 HOH   HOH A . 
L 5 HOH   8   308 283 HOH   HOH A . 
L 5 HOH   9   309 225 HOH   HOH A . 
L 5 HOH   10  310 23  HOH   HOH A . 
L 5 HOH   11  311 93  HOH   HOH A . 
L 5 HOH   12  312 157 HOH   HOH A . 
L 5 HOH   13  313 14  HOH   HOH A . 
L 5 HOH   14  314 59  HOH   HOH A . 
L 5 HOH   15  315 70  HOH   HOH A . 
L 5 HOH   16  316 116 HOH   HOH A . 
L 5 HOH   17  317 5   HOH   HOH A . 
L 5 HOH   18  318 22  HOH   HOH A . 
L 5 HOH   19  319 66  HOH   HOH A . 
L 5 HOH   20  320 63  HOH   HOH A . 
L 5 HOH   21  321 247 HOH   HOH A . 
L 5 HOH   22  322 278 HOH   HOH A . 
L 5 HOH   23  323 190 HOH   HOH A . 
L 5 HOH   24  324 7   HOH   HOH A . 
L 5 HOH   25  325 48  HOH   HOH A . 
L 5 HOH   26  326 152 HOH   HOH A . 
L 5 HOH   27  327 28  HOH   HOH A . 
L 5 HOH   28  328 60  HOH   HOH A . 
L 5 HOH   29  329 284 HOH   HOH A . 
L 5 HOH   30  330 63  HOH   HOH A . 
L 5 HOH   31  331 289 HOH   HOH A . 
L 5 HOH   32  332 17  HOH   HOH A . 
L 5 HOH   33  333 56  HOH   HOH A . 
L 5 HOH   34  334 19  HOH   HOH A . 
L 5 HOH   35  335 49  HOH   HOH A . 
L 5 HOH   36  336 125 HOH   HOH A . 
L 5 HOH   37  337 61  HOH   HOH A . 
L 5 HOH   38  338 88  HOH   HOH A . 
L 5 HOH   39  339 73  HOH   HOH A . 
L 5 HOH   40  340 171 HOH   HOH A . 
L 5 HOH   41  341 10  HOH   HOH A . 
L 5 HOH   42  342 252 HOH   HOH A . 
L 5 HOH   43  343 100 HOH   HOH A . 
L 5 HOH   44  344 72  HOH   HOH A . 
L 5 HOH   45  345 13  HOH   HOH A . 
L 5 HOH   46  346 71  HOH   HOH A . 
L 5 HOH   47  347 27  HOH   HOH A . 
L 5 HOH   48  348 66  HOH   HOH A . 
L 5 HOH   49  349 38  HOH   HOH A . 
L 5 HOH   50  350 243 HOH   HOH A . 
L 5 HOH   51  351 226 HOH   HOH A . 
L 5 HOH   52  352 114 HOH   HOH A . 
L 5 HOH   53  353 115 HOH   HOH A . 
L 5 HOH   54  354 85  HOH   HOH A . 
L 5 HOH   55  355 30  HOH   HOH A . 
L 5 HOH   56  356 176 HOH   HOH A . 
L 5 HOH   57  357 33  HOH   HOH A . 
L 5 HOH   58  358 133 HOH   HOH A . 
L 5 HOH   59  359 113 HOH   HOH A . 
L 5 HOH   60  360 149 HOH   HOH A . 
L 5 HOH   61  361 229 HOH   HOH A . 
L 5 HOH   62  362 115 HOH   HOH A . 
L 5 HOH   63  363 26  HOH   HOH A . 
L 5 HOH   64  364 99  HOH   HOH A . 
L 5 HOH   65  365 224 HOH   HOH A . 
L 5 HOH   66  366 235 HOH   HOH A . 
L 5 HOH   67  367 53  HOH   HOH A . 
L 5 HOH   68  368 233 HOH   HOH A . 
L 5 HOH   69  369 234 HOH   HOH A . 
L 5 HOH   70  370 19  HOH   HOH A . 
L 5 HOH   71  371 242 HOH   HOH A . 
L 5 HOH   72  372 272 HOH   HOH A . 
L 5 HOH   73  373 42  HOH   HOH A . 
L 5 HOH   74  374 197 HOH   HOH A . 
L 5 HOH   75  375 49  HOH   HOH A . 
L 5 HOH   76  376 12  HOH   HOH A . 
L 5 HOH   77  377 60  HOH   HOH A . 
L 5 HOH   78  378 250 HOH   HOH A . 
L 5 HOH   79  379 119 HOH   HOH A . 
L 5 HOH   80  380 276 HOH   HOH A . 
L 5 HOH   81  381 47  HOH   HOH A . 
L 5 HOH   82  382 128 HOH   HOH A . 
L 5 HOH   83  383 85  HOH   HOH A . 
L 5 HOH   84  384 202 HOH   HOH A . 
L 5 HOH   85  385 112 HOH   HOH A . 
L 5 HOH   86  386 35  HOH   HOH A . 
L 5 HOH   87  387 16  HOH   HOH A . 
L 5 HOH   88  388 96  HOH   HOH A . 
L 5 HOH   89  389 237 HOH   HOH A . 
L 5 HOH   90  390 106 HOH   HOH A . 
L 5 HOH   91  391 12  HOH   HOH A . 
L 5 HOH   92  392 92  HOH   HOH A . 
L 5 HOH   93  393 21  HOH   HOH A . 
L 5 HOH   94  394 40  HOH   HOH A . 
L 5 HOH   95  395 26  HOH   HOH A . 
L 5 HOH   96  396 270 HOH   HOH A . 
L 5 HOH   97  397 77  HOH   HOH A . 
L 5 HOH   98  398 102 HOH   HOH A . 
L 5 HOH   99  399 269 HOH   HOH A . 
L 5 HOH   100 400 228 HOH   HOH A . 
L 5 HOH   101 401 52  HOH   HOH A . 
L 5 HOH   102 402 62  HOH   HOH A . 
L 5 HOH   103 403 258 HOH   HOH A . 
L 5 HOH   104 404 104 HOH   HOH A . 
L 5 HOH   105 405 264 HOH   HOH A . 
L 5 HOH   106 406 15  HOH   HOH A . 
L 5 HOH   107 407 177 HOH   HOH A . 
L 5 HOH   108 408 279 HOH   HOH A . 
L 5 HOH   109 409 154 HOH   HOH A . 
L 5 HOH   110 410 53  HOH   HOH A . 
L 5 HOH   111 411 126 HOH   HOH A . 
L 5 HOH   112 412 136 HOH   HOH A . 
L 5 HOH   113 413 257 HOH   HOH A . 
L 5 HOH   114 414 201 HOH   HOH A . 
L 5 HOH   115 415 239 HOH   HOH A . 
L 5 HOH   116 416 135 HOH   HOH A . 
L 5 HOH   117 417 129 HOH   HOH A . 
L 5 HOH   118 418 146 HOH   HOH A . 
L 5 HOH   119 419 138 HOH   HOH A . 
L 5 HOH   120 420 104 HOH   HOH A . 
L 5 HOH   121 421 281 HOH   HOH A . 
L 5 HOH   122 422 268 HOH   HOH A . 
L 5 HOH   123 423 222 HOH   HOH A . 
L 5 HOH   124 424 187 HOH   HOH A . 
M 5 HOH   1   301 137 HOH   HOH C . 
M 5 HOH   2   302 84  HOH   HOH C . 
M 5 HOH   3   303 8   HOH   HOH C . 
M 5 HOH   4   304 2   HOH   HOH C . 
M 5 HOH   5   305 240 HOH   HOH C . 
M 5 HOH   6   306 103 HOH   HOH C . 
M 5 HOH   7   307 51  HOH   HOH C . 
M 5 HOH   8   308 32  HOH   HOH C . 
M 5 HOH   9   309 78  HOH   HOH C . 
M 5 HOH   10  310 275 HOH   HOH C . 
M 5 HOH   11  311 33  HOH   HOH C . 
M 5 HOH   12  312 69  HOH   HOH C . 
M 5 HOH   13  313 111 HOH   HOH C . 
M 5 HOH   14  314 124 HOH   HOH C . 
M 5 HOH   15  315 64  HOH   HOH C . 
M 5 HOH   16  316 43  HOH   HOH C . 
M 5 HOH   17  317 253 HOH   HOH C . 
M 5 HOH   18  318 50  HOH   HOH C . 
M 5 HOH   19  319 65  HOH   HOH C . 
M 5 HOH   20  320 231 HOH   HOH C . 
M 5 HOH   21  321 155 HOH   HOH C . 
M 5 HOH   22  322 43  HOH   HOH C . 
M 5 HOH   23  323 97  HOH   HOH C . 
M 5 HOH   24  324 248 HOH   HOH C . 
M 5 HOH   25  325 130 HOH   HOH C . 
M 5 HOH   26  326 238 HOH   HOH C . 
M 5 HOH   27  327 98  HOH   HOH C . 
M 5 HOH   28  328 210 HOH   HOH C . 
M 5 HOH   29  329 30  HOH   HOH C . 
M 5 HOH   30  330 38  HOH   HOH C . 
M 5 HOH   31  331 6   HOH   HOH C . 
M 5 HOH   32  332 107 HOH   HOH C . 
M 5 HOH   33  333 1   HOH   HOH C . 
M 5 HOH   34  334 11  HOH   HOH C . 
M 5 HOH   35  335 122 HOH   HOH C . 
M 5 HOH   36  336 246 HOH   HOH C . 
M 5 HOH   37  337 271 HOH   HOH C . 
M 5 HOH   38  338 80  HOH   HOH C . 
M 5 HOH   39  339 117 HOH   HOH C . 
M 5 HOH   40  340 285 HOH   HOH C . 
M 5 HOH   41  341 20  HOH   HOH C . 
M 5 HOH   42  342 39  HOH   HOH C . 
M 5 HOH   43  343 223 HOH   HOH C . 
M 5 HOH   44  344 67  HOH   HOH C . 
M 5 HOH   45  345 123 HOH   HOH C . 
M 5 HOH   46  346 274 HOH   HOH C . 
M 5 HOH   47  347 46  HOH   HOH C . 
M 5 HOH   48  348 261 HOH   HOH C . 
M 5 HOH   49  349 73  HOH   HOH C . 
M 5 HOH   50  350 29  HOH   HOH C . 
M 5 HOH   51  351 31  HOH   HOH C . 
M 5 HOH   52  352 54  HOH   HOH C . 
M 5 HOH   53  353 126 HOH   HOH C . 
M 5 HOH   54  354 245 HOH   HOH C . 
M 5 HOH   55  355 71  HOH   HOH C . 
M 5 HOH   56  356 79  HOH   HOH C . 
M 5 HOH   57  357 277 HOH   HOH C . 
M 5 HOH   58  358 4   HOH   HOH C . 
M 5 HOH   59  359 110 HOH   HOH C . 
M 5 HOH   60  360 37  HOH   HOH C . 
M 5 HOH   61  361 11  HOH   HOH C . 
M 5 HOH   62  362 227 HOH   HOH C . 
M 5 HOH   63  363 148 HOH   HOH C . 
M 5 HOH   64  364 204 HOH   HOH C . 
M 5 HOH   65  365 91  HOH   HOH C . 
M 5 HOH   66  366 254 HOH   HOH C . 
M 5 HOH   67  367 89  HOH   HOH C . 
M 5 HOH   68  368 7   HOH   HOH C . 
M 5 HOH   69  369 262 HOH   HOH C . 
M 5 HOH   70  370 37  HOH   HOH C . 
M 5 HOH   71  371 45  HOH   HOH C . 
M 5 HOH   72  372 256 HOH   HOH C . 
M 5 HOH   73  373 62  HOH   HOH C . 
M 5 HOH   74  374 241 HOH   HOH C . 
M 5 HOH   75  375 52  HOH   HOH C . 
M 5 HOH   76  376 83  HOH   HOH C . 
M 5 HOH   77  377 50  HOH   HOH C . 
M 5 HOH   78  378 83  HOH   HOH C . 
M 5 HOH   79  379 31  HOH   HOH C . 
M 5 HOH   80  380 280 HOH   HOH C . 
M 5 HOH   81  381 124 HOH   HOH C . 
M 5 HOH   82  382 260 HOH   HOH C . 
M 5 HOH   83  383 13  HOH   HOH C . 
M 5 HOH   84  384 251 HOH   HOH C . 
M 5 HOH   85  385 232 HOH   HOH C . 
M 5 HOH   86  386 54  HOH   HOH C . 
M 5 HOH   87  387 244 HOH   HOH C . 
M 5 HOH   88  388 144 HOH   HOH C . 
M 5 HOH   89  389 132 HOH   HOH C . 
M 5 HOH   90  390 41  HOH   HOH C . 
M 5 HOH   91  391 87  HOH   HOH C . 
M 5 HOH   92  392 255 HOH   HOH C . 
M 5 HOH   93  393 44  HOH   HOH C . 
M 5 HOH   94  394 230 HOH   HOH C . 
M 5 HOH   95  395 3   HOH   HOH C . 
M 5 HOH   96  396 273 HOH   HOH C . 
M 5 HOH   97  397 249 HOH   HOH C . 
M 5 HOH   98  398 68  HOH   HOH C . 
M 5 HOH   99  399 267 HOH   HOH C . 
M 5 HOH   100 400 16  HOH   HOH C . 
M 5 HOH   101 401 127 HOH   HOH C . 
M 5 HOH   102 402 194 HOH   HOH C . 
M 5 HOH   103 403 90  HOH   HOH C . 
M 5 HOH   104 404 292 HOH   HOH C . 
M 5 HOH   105 405 294 HOH   HOH C . 
M 5 HOH   106 406 291 HOH   HOH C . 
M 5 HOH   107 407 47  HOH   HOH C . 
M 5 HOH   108 408 282 HOH   HOH C . 
M 5 HOH   109 409 116 HOH   HOH C . 
M 5 HOH   110 410 286 HOH   HOH C . 
M 5 HOH   111 411 17  HOH   HOH C . 
M 5 HOH   112 412 293 HOH   HOH C . 
M 5 HOH   113 413 185 HOH   HOH C . 
M 5 HOH   114 414 9   HOH   HOH C . 
M 5 HOH   115 415 90  HOH   HOH C . 
M 5 HOH   116 416 139 HOH   HOH C . 
M 5 HOH   117 417 141 HOH   HOH C . 
M 5 HOH   118 418 266 HOH   HOH C . 
M 5 HOH   119 419 93  HOH   HOH C . 
M 5 HOH   120 420 198 HOH   HOH C . 
M 5 HOH   121 421 290 HOH   HOH C . 
M 5 HOH   122 422 82  HOH   HOH C . 
M 5 HOH   123 423 132 HOH   HOH C . 
M 5 HOH   124 424 123 HOH   HOH C . 
M 5 HOH   125 425 199 HOH   HOH C . 
M 5 HOH   126 426 25  HOH   HOH C . 
M 5 HOH   127 427 140 HOH   HOH C . 
M 5 HOH   128 428 182 HOH   HOH C . 
M 5 HOH   129 429 141 HOH   HOH C . 
M 5 HOH   130 430 218 HOH   HOH C . 
M 5 HOH   131 431 295 HOH   HOH C . 
M 5 HOH   132 432 207 HOH   HOH C . 
# 
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           7I6H 
_cell.length_a           72.450 
_cell.length_b           61.710 
_cell.length_c           65.150 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.05 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I6H 
_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          7I6H 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.23 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-30 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92204 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I6H 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.46 
_reflns.d_resolution_high            1.39 
_reflns.number_obs                   57175 
_reflns.percent_possible_obs         99.2 
_reflns.pdbx_Rmerge_I_obs            0.120 
_reflns.pdbx_netI_over_sigmaI        11.2 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.131 
_reflns.pdbx_Rpim_I_all              0.051 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     354356 
_reflns.pdbx_chi_squared             0.94 
_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                  1.39 
_reflns_shell.d_res_low                   1.43 
_reflns_shell.number_measured_all         17582 
_reflns_shell.number_unique_obs           4016 
_reflns_shell.Rmerge_I_obs                1.885 
_reflns_shell.pdbx_chi_squared            0.94 
_reflns_shell.pdbx_redundancy             4.4 
_reflns_shell.percent_possible_obs        95.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.142 
_reflns_shell.pdbx_Rpim_I_all             1.003 
_reflns_shell.pdbx_CC_half                0.379 
_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                                 7I6H 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     57169 
_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                             37.46 
_refine.ls_d_res_high                            1.390 
_refine.ls_percent_reflns_obs                    99.1 
_refine.ls_R_factor_obs                          0.2099 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2089 
_refine.ls_R_factor_R_free                       0.2298 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.900 
_refine.ls_number_reflns_R_free                  2801 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.951 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_refine.B_iso_mean                               21.30 
_refine.aniso_B[1][1]                            -1.13940 
_refine.aniso_B[2][2]                            0.90520 
_refine.aniso_B[3][3]                            0.23420 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.61840 
_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             0.067 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.067 
_refine.pdbx_overall_SU_R_Blow_DPI               0.069 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.068 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I6H 
_refine_analyze.Luzzati_coordinate_error_obs    0.21 
_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        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         74 
_refine_hist.number_atoms_solvent             256 
_refine_hist.number_atoms_total               2478 
_refine_hist.d_res_high                       1.390 
_refine_hist.d_res_low                        37.46 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  2298 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3126 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  780  '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  417  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2286 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.66  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.43 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  283  '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  2016 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.39 
_refine_ls_shell.d_res_low                        1.40 
_refine_ls_shell.number_reflns_R_work             1091 
_refine_ls_shell.R_factor_R_work                  0.3499 
_refine_ls_shell.percent_reflns_obs               94.56 
_refine_ls_shell.R_factor_R_free                  0.3798 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.63 
_refine_ls_shell.number_reflns_R_free             53 
_refine_ls_shell.number_reflns_all                1144 
_refine_ls_shell.R_factor_all                     0.3513 
# 
_struct.entry_id                  7I6H 
_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-0037745-001 (A71EV2A-x4967)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I6H 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M 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 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I6H A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I6H C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,L   
2 1 B,G,H,I,J,K,M 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 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 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 I ZN . ZN ? ? C CYS 56  C ZN 203 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 I ZN . ZN ? ? C CYS 58  C ZN 203 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 I ZN . ZN ? ? C CYS 116 C ZN 203 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 I ZN . ZN ? ? C HIS 118 C ZN 203 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
# 
_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 ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.0 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.1 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.5 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.2 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.5 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.2 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.1 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.6 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.3 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.9 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.4 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? I ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 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 
AA1 3 4 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N THR B 120 ? N THR C 126 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O GLN B 89  ? O GLN C 95  N ILE B 76  ? N ILE C 82  
# 
_pdbx_entry_details.entry_id                   7I6H 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14 ? ? -99.58 35.42 
2 1 ASN C 14 ? ? -99.56 35.83 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 19.5231 6.8045   18.1464 -0.0019 -0.0428 -0.0045 0.0002  0.0053  0.0009  0.8863 1.3343 0.3284 
-0.5338 -0.0221 0.0624  -0.0064 -0.0101 0.1083 0.0086 0.0512 0.0412  0.0073 0.0439 -0.0448 
'X-RAY DIFFRACTION' 2 ? refined 14.9617 -23.7757 14.3795 0.0028  -0.0368 -0.0128 -0.0033 -0.0060 -0.0034 0.7494 0.9733 0.5623 
0.4407  -0.0517 -0.0156 -0.0108 0.0195  0.0746 0.0061 0.0373 -0.0084 0.0035 0.0018 -0.0265 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
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 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
11 1 N 0 A DMS 203 ? E DMS ?   
12 1 N 0 A DMS 204 ? F DMS ?   
13 1 N 0 C DMS 204 ? J DMS ?   
14 1 N 0 C DMS 205 ? K 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 
A1B4W N1   N  N N 1   
A1B4W C4   C  Y N 2   
A1B4W C5   C  Y N 3   
A1B4W C6   C  N N 4   
A1B4W C7   C  N N 5   
A1B4W C8   C  N N 6   
A1B4W C10  C  N N 7   
A1B4W C13  C  N N 8   
A1B4W C15  C  N N 9   
A1B4W C17  C  N R 10  
A1B4W O2   O  N N 11  
A1B4W N2   N  N N 12  
A1B4W C9   C  N S 13  
A1B4W C11  C  N N 14  
A1B4W C12  C  N S 15  
A1B4W C16  C  N N 16  
A1B4W C14  C  N N 17  
A1B4W O1   O  N N 18  
A1B4W C1   C  Y N 19  
A1B4W O    O  N N 20  
A1B4W C    C  N N 21  
A1B4W N    N  Y N 22  
A1B4W C3   C  Y N 23  
A1B4W C2   C  Y N 24  
A1B4W H8   H  N N 25  
A1B4W H9   H  N N 26  
A1B4W H10  H  N N 27  
A1B4W H11  H  N N 28  
A1B4W H12  H  N N 29  
A1B4W H18  H  N N 30  
A1B4W H17  H  N N 31  
A1B4W H22  H  N N 32  
A1B4W H21  H  N N 33  
A1B4W H2   H  N N 34  
A1B4W H13  H  N N 35  
A1B4W H14  H  N N 36  
A1B4W H    H  N N 37  
A1B4W H16  H  N N 38  
A1B4W H15  H  N N 39  
A1B4W H1   H  N N 40  
A1B4W H24  H  N N 41  
A1B4W H23  H  N N 42  
A1B4W H20  H  N N 43  
A1B4W H19  H  N N 44  
A1B4W H4   H  N N 45  
A1B4W H5   H  N N 46  
A1B4W H3   H  N N 47  
A1B4W H7   H  N N 48  
A1B4W H6   H  N N 49  
ALA   N    N  N N 50  
ALA   CA   C  N S 51  
ALA   C    C  N N 52  
ALA   O    O  N N 53  
ALA   CB   C  N N 54  
ALA   OXT  O  N N 55  
ALA   H    H  N N 56  
ALA   H2   H  N N 57  
ALA   HA   H  N N 58  
ALA   HB1  H  N N 59  
ALA   HB2  H  N N 60  
ALA   HB3  H  N N 61  
ALA   HXT  H  N N 62  
ARG   N    N  N N 63  
ARG   CA   C  N S 64  
ARG   C    C  N N 65  
ARG   O    O  N N 66  
ARG   CB   C  N N 67  
ARG   CG   C  N N 68  
ARG   CD   C  N N 69  
ARG   NE   N  N N 70  
ARG   CZ   C  N N 71  
ARG   NH1  N  N N 72  
ARG   NH2  N  N N 73  
ARG   OXT  O  N N 74  
ARG   H    H  N N 75  
ARG   H2   H  N N 76  
ARG   HA   H  N N 77  
ARG   HB2  H  N N 78  
ARG   HB3  H  N N 79  
ARG   HG2  H  N N 80  
ARG   HG3  H  N N 81  
ARG   HD2  H  N N 82  
ARG   HD3  H  N N 83  
ARG   HE   H  N N 84  
ARG   HH11 H  N N 85  
ARG   HH12 H  N N 86  
ARG   HH21 H  N N 87  
ARG   HH22 H  N N 88  
ARG   HXT  H  N N 89  
ASN   N    N  N N 90  
ASN   CA   C  N S 91  
ASN   C    C  N N 92  
ASN   O    O  N N 93  
ASN   CB   C  N N 94  
ASN   CG   C  N N 95  
ASN   OD1  O  N N 96  
ASN   ND2  N  N N 97  
ASN   OXT  O  N N 98  
ASN   H    H  N N 99  
ASN   H2   H  N N 100 
ASN   HA   H  N N 101 
ASN   HB2  H  N N 102 
ASN   HB3  H  N N 103 
ASN   HD21 H  N N 104 
ASN   HD22 H  N N 105 
ASN   HXT  H  N N 106 
ASP   N    N  N N 107 
ASP   CA   C  N S 108 
ASP   C    C  N N 109 
ASP   O    O  N N 110 
ASP   CB   C  N N 111 
ASP   CG   C  N N 112 
ASP   OD1  O  N N 113 
ASP   OD2  O  N N 114 
ASP   OXT  O  N N 115 
ASP   H    H  N N 116 
ASP   H2   H  N N 117 
ASP   HA   H  N N 118 
ASP   HB2  H  N N 119 
ASP   HB3  H  N N 120 
ASP   HD2  H  N N 121 
ASP   HXT  H  N N 122 
CYS   N    N  N N 123 
CYS   CA   C  N R 124 
CYS   C    C  N N 125 
CYS   O    O  N N 126 
CYS   CB   C  N N 127 
CYS   SG   S  N N 128 
CYS   OXT  O  N N 129 
CYS   H    H  N N 130 
CYS   H2   H  N N 131 
CYS   HA   H  N N 132 
CYS   HB2  H  N N 133 
CYS   HB3  H  N N 134 
CYS   HG   H  N N 135 
CYS   HXT  H  N N 136 
DMS   S    S  N N 137 
DMS   O    O  N N 138 
DMS   C1   C  N N 139 
DMS   C2   C  N N 140 
DMS   H11  H  N N 141 
DMS   H12  H  N N 142 
DMS   H13  H  N N 143 
DMS   H21  H  N N 144 
DMS   H22  H  N N 145 
DMS   H23  H  N N 146 
GLN   N    N  N N 147 
GLN   CA   C  N S 148 
GLN   C    C  N N 149 
GLN   O    O  N N 150 
GLN   CB   C  N N 151 
GLN   CG   C  N N 152 
GLN   CD   C  N N 153 
GLN   OE1  O  N N 154 
GLN   NE2  N  N N 155 
GLN   OXT  O  N N 156 
GLN   H    H  N N 157 
GLN   H2   H  N N 158 
GLN   HA   H  N N 159 
GLN   HB2  H  N N 160 
GLN   HB3  H  N N 161 
GLN   HG2  H  N N 162 
GLN   HG3  H  N N 163 
GLN   HE21 H  N N 164 
GLN   HE22 H  N N 165 
GLN   HXT  H  N N 166 
GLU   N    N  N N 167 
GLU   CA   C  N S 168 
GLU   C    C  N N 169 
GLU   O    O  N N 170 
GLU   CB   C  N N 171 
GLU   CG   C  N N 172 
GLU   CD   C  N N 173 
GLU   OE1  O  N N 174 
GLU   OE2  O  N N 175 
GLU   OXT  O  N N 176 
GLU   H    H  N N 177 
GLU   H2   H  N N 178 
GLU   HA   H  N N 179 
GLU   HB2  H  N N 180 
GLU   HB3  H  N N 181 
GLU   HG2  H  N N 182 
GLU   HG3  H  N N 183 
GLU   HE2  H  N N 184 
GLU   HXT  H  N N 185 
GLY   N    N  N N 186 
GLY   CA   C  N N 187 
GLY   C    C  N N 188 
GLY   O    O  N N 189 
GLY   OXT  O  N N 190 
GLY   H    H  N N 191 
GLY   H2   H  N N 192 
GLY   HA2  H  N N 193 
GLY   HA3  H  N N 194 
GLY   HXT  H  N N 195 
HIS   N    N  N N 196 
HIS   CA   C  N S 197 
HIS   C    C  N N 198 
HIS   O    O  N N 199 
HIS   CB   C  N N 200 
HIS   CG   C  Y N 201 
HIS   ND1  N  Y N 202 
HIS   CD2  C  Y N 203 
HIS   CE1  C  Y N 204 
HIS   NE2  N  Y N 205 
HIS   OXT  O  N N 206 
HIS   H    H  N N 207 
HIS   H2   H  N N 208 
HIS   HA   H  N N 209 
HIS   HB2  H  N N 210 
HIS   HB3  H  N N 211 
HIS   HD1  H  N N 212 
HIS   HD2  H  N N 213 
HIS   HE1  H  N N 214 
HIS   HE2  H  N N 215 
HIS   HXT  H  N N 216 
HOH   O    O  N N 217 
HOH   H1   H  N N 218 
HOH   H2   H  N N 219 
ILE   N    N  N N 220 
ILE   CA   C  N S 221 
ILE   C    C  N N 222 
ILE   O    O  N N 223 
ILE   CB   C  N S 224 
ILE   CG1  C  N N 225 
ILE   CG2  C  N N 226 
ILE   CD1  C  N N 227 
ILE   OXT  O  N N 228 
ILE   H    H  N N 229 
ILE   H2   H  N N 230 
ILE   HA   H  N N 231 
ILE   HB   H  N N 232 
ILE   HG12 H  N N 233 
ILE   HG13 H  N N 234 
ILE   HG21 H  N N 235 
ILE   HG22 H  N N 236 
ILE   HG23 H  N N 237 
ILE   HD11 H  N N 238 
ILE   HD12 H  N N 239 
ILE   HD13 H  N N 240 
ILE   HXT  H  N N 241 
LEU   N    N  N N 242 
LEU   CA   C  N S 243 
LEU   C    C  N N 244 
LEU   O    O  N N 245 
LEU   CB   C  N N 246 
LEU   CG   C  N N 247 
LEU   CD1  C  N N 248 
LEU   CD2  C  N N 249 
LEU   OXT  O  N N 250 
LEU   H    H  N N 251 
LEU   H2   H  N N 252 
LEU   HA   H  N N 253 
LEU   HB2  H  N N 254 
LEU   HB3  H  N N 255 
LEU   HG   H  N N 256 
LEU   HD11 H  N N 257 
LEU   HD12 H  N N 258 
LEU   HD13 H  N N 259 
LEU   HD21 H  N N 260 
LEU   HD22 H  N N 261 
LEU   HD23 H  N N 262 
LEU   HXT  H  N N 263 
LYS   N    N  N N 264 
LYS   CA   C  N S 265 
LYS   C    C  N N 266 
LYS   O    O  N N 267 
LYS   CB   C  N N 268 
LYS   CG   C  N N 269 
LYS   CD   C  N N 270 
LYS   CE   C  N N 271 
LYS   NZ   N  N N 272 
LYS   OXT  O  N N 273 
LYS   H    H  N N 274 
LYS   H2   H  N N 275 
LYS   HA   H  N N 276 
LYS   HB2  H  N N 277 
LYS   HB3  H  N N 278 
LYS   HG2  H  N N 279 
LYS   HG3  H  N N 280 
LYS   HD2  H  N N 281 
LYS   HD3  H  N N 282 
LYS   HE2  H  N N 283 
LYS   HE3  H  N N 284 
LYS   HZ1  H  N N 285 
LYS   HZ2  H  N N 286 
LYS   HZ3  H  N N 287 
LYS   HXT  H  N N 288 
MET   N    N  N N 289 
MET   CA   C  N S 290 
MET   C    C  N N 291 
MET   O    O  N N 292 
MET   CB   C  N N 293 
MET   CG   C  N N 294 
MET   SD   S  N N 295 
MET   CE   C  N N 296 
MET   OXT  O  N N 297 
MET   H    H  N N 298 
MET   H2   H  N N 299 
MET   HA   H  N N 300 
MET   HB2  H  N N 301 
MET   HB3  H  N N 302 
MET   HG2  H  N N 303 
MET   HG3  H  N N 304 
MET   HE1  H  N N 305 
MET   HE2  H  N N 306 
MET   HE3  H  N N 307 
MET   HXT  H  N N 308 
PHE   N    N  N N 309 
PHE   CA   C  N S 310 
PHE   C    C  N N 311 
PHE   O    O  N N 312 
PHE   CB   C  N N 313 
PHE   CG   C  Y N 314 
PHE   CD1  C  Y N 315 
PHE   CD2  C  Y N 316 
PHE   CE1  C  Y N 317 
PHE   CE2  C  Y N 318 
PHE   CZ   C  Y N 319 
PHE   OXT  O  N N 320 
PHE   H    H  N N 321 
PHE   H2   H  N N 322 
PHE   HA   H  N N 323 
PHE   HB2  H  N N 324 
PHE   HB3  H  N N 325 
PHE   HD1  H  N N 326 
PHE   HD2  H  N N 327 
PHE   HE1  H  N N 328 
PHE   HE2  H  N N 329 
PHE   HZ   H  N N 330 
PHE   HXT  H  N N 331 
PRO   N    N  N N 332 
PRO   CA   C  N S 333 
PRO   C    C  N N 334 
PRO   O    O  N N 335 
PRO   CB   C  N N 336 
PRO   CG   C  N N 337 
PRO   CD   C  N N 338 
PRO   OXT  O  N N 339 
PRO   H    H  N N 340 
PRO   HA   H  N N 341 
PRO   HB2  H  N N 342 
PRO   HB3  H  N N 343 
PRO   HG2  H  N N 344 
PRO   HG3  H  N N 345 
PRO   HD2  H  N N 346 
PRO   HD3  H  N N 347 
PRO   HXT  H  N N 348 
SER   N    N  N N 349 
SER   CA   C  N S 350 
SER   C    C  N N 351 
SER   O    O  N N 352 
SER   CB   C  N N 353 
SER   OG   O  N N 354 
SER   OXT  O  N N 355 
SER   H    H  N N 356 
SER   H2   H  N N 357 
SER   HA   H  N N 358 
SER   HB2  H  N N 359 
SER   HB3  H  N N 360 
SER   HG   H  N N 361 
SER   HXT  H  N N 362 
THR   N    N  N N 363 
THR   CA   C  N S 364 
THR   C    C  N N 365 
THR   O    O  N N 366 
THR   CB   C  N R 367 
THR   OG1  O  N N 368 
THR   CG2  C  N N 369 
THR   OXT  O  N N 370 
THR   H    H  N N 371 
THR   H2   H  N N 372 
THR   HA   H  N N 373 
THR   HB   H  N N 374 
THR   HG1  H  N N 375 
THR   HG21 H  N N 376 
THR   HG22 H  N N 377 
THR   HG23 H  N N 378 
THR   HXT  H  N N 379 
TRP   N    N  N N 380 
TRP   CA   C  N S 381 
TRP   C    C  N N 382 
TRP   O    O  N N 383 
TRP   CB   C  N N 384 
TRP   CG   C  Y N 385 
TRP   CD1  C  Y N 386 
TRP   CD2  C  Y N 387 
TRP   NE1  N  Y N 388 
TRP   CE2  C  Y N 389 
TRP   CE3  C  Y N 390 
TRP   CZ2  C  Y N 391 
TRP   CZ3  C  Y N 392 
TRP   CH2  C  Y N 393 
TRP   OXT  O  N N 394 
TRP   H    H  N N 395 
TRP   H2   H  N N 396 
TRP   HA   H  N N 397 
TRP   HB2  H  N N 398 
TRP   HB3  H  N N 399 
TRP   HD1  H  N N 400 
TRP   HE1  H  N N 401 
TRP   HE3  H  N N 402 
TRP   HZ2  H  N N 403 
TRP   HZ3  H  N N 404 
TRP   HH2  H  N N 405 
TRP   HXT  H  N N 406 
TYR   N    N  N N 407 
TYR   CA   C  N S 408 
TYR   C    C  N N 409 
TYR   O    O  N N 410 
TYR   CB   C  N N 411 
TYR   CG   C  Y N 412 
TYR   CD1  C  Y N 413 
TYR   CD2  C  Y N 414 
TYR   CE1  C  Y N 415 
TYR   CE2  C  Y N 416 
TYR   CZ   C  Y N 417 
TYR   OH   O  N N 418 
TYR   OXT  O  N N 419 
TYR   H    H  N N 420 
TYR   H2   H  N N 421 
TYR   HA   H  N N 422 
TYR   HB2  H  N N 423 
TYR   HB3  H  N N 424 
TYR   HD1  H  N N 425 
TYR   HD2  H  N N 426 
TYR   HE1  H  N N 427 
TYR   HE2  H  N N 428 
TYR   HH   H  N N 429 
TYR   HXT  H  N N 430 
VAL   N    N  N N 431 
VAL   CA   C  N S 432 
VAL   C    C  N N 433 
VAL   O    O  N N 434 
VAL   CB   C  N N 435 
VAL   CG1  C  N N 436 
VAL   CG2  C  N N 437 
VAL   OXT  O  N N 438 
VAL   H    H  N N 439 
VAL   H2   H  N N 440 
VAL   HA   H  N N 441 
VAL   HB   H  N N 442 
VAL   HG11 H  N N 443 
VAL   HG12 H  N N 444 
VAL   HG13 H  N N 445 
VAL   HG21 H  N N 446 
VAL   HG22 H  N N 447 
VAL   HG23 H  N N 448 
VAL   HXT  H  N N 449 
ZN    ZN   ZN N N 450 
# 
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 
A1B4W C   O    sing N N 1   
A1B4W O   C1   sing N N 2   
A1B4W C1  C2   doub Y N 3   
A1B4W C2  C3   sing Y N 4   
A1B4W C3  N    doub Y N 5   
A1B4W N   C4   sing Y N 6   
A1B4W C4  C5   doub Y N 7   
A1B4W C1  C5   sing Y N 8   
A1B4W C5  C6   sing N N 9   
A1B4W C6  C7   sing N N 10  
A1B4W O1  C7   doub N N 11  
A1B4W C7  N1   sing N N 12  
A1B4W N1  C8   sing N N 13  
A1B4W C8  C9   sing N N 14  
A1B4W C9  C10  sing N N 15  
A1B4W N2  C10  sing N N 16  
A1B4W C10 O2   doub N N 17  
A1B4W C11 C9   sing N N 18  
A1B4W C12 C11  sing N N 19  
A1B4W C12 C13  sing N N 20  
A1B4W C13 C14  sing N N 21  
A1B4W C14 C15  sing N N 22  
A1B4W C15 C16  sing N N 23  
A1B4W C16 C17  sing N N 24  
A1B4W C17 C12  sing N N 25  
A1B4W N1  C17  sing N N 26  
A1B4W C4  H8   sing N N 27  
A1B4W C6  H9   sing N N 28  
A1B4W C6  H10  sing N N 29  
A1B4W C8  H11  sing N N 30  
A1B4W C8  H12  sing N N 31  
A1B4W C13 H18  sing N N 32  
A1B4W C13 H17  sing N N 33  
A1B4W C15 H22  sing N N 34  
A1B4W C15 H21  sing N N 35  
A1B4W C17 H2   sing N N 36  
A1B4W N2  H13  sing N N 37  
A1B4W N2  H14  sing N N 38  
A1B4W C9  H    sing N N 39  
A1B4W C11 H16  sing N N 40  
A1B4W C11 H15  sing N N 41  
A1B4W C12 H1   sing N N 42  
A1B4W C16 H24  sing N N 43  
A1B4W C16 H23  sing N N 44  
A1B4W C14 H20  sing N N 45  
A1B4W C14 H19  sing N N 46  
A1B4W C   H4   sing N N 47  
A1B4W C   H5   sing N N 48  
A1B4W C   H3   sing N N 49  
A1B4W C3  H7   sing N N 50  
A1B4W C2  H6   sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
DMS   S   O    doub N N 134 
DMS   S   C1   sing N N 135 
DMS   S   C2   sing N N 136 
DMS   C1  H11  sing N N 137 
DMS   C1  H12  sing N N 138 
DMS   C1  H13  sing N N 139 
DMS   C2  H21  sing N N 140 
DMS   C2  H22  sing N N 141 
DMS   C2  H23  sing N N 142 
GLN   N   CA   sing N N 143 
GLN   N   H    sing N N 144 
GLN   N   H2   sing N N 145 
GLN   CA  C    sing N N 146 
GLN   CA  CB   sing N N 147 
GLN   CA  HA   sing N N 148 
GLN   C   O    doub N N 149 
GLN   C   OXT  sing N N 150 
GLN   CB  CG   sing N N 151 
GLN   CB  HB2  sing N N 152 
GLN   CB  HB3  sing N N 153 
GLN   CG  CD   sing N N 154 
GLN   CG  HG2  sing N N 155 
GLN   CG  HG3  sing N N 156 
GLN   CD  OE1  doub N N 157 
GLN   CD  NE2  sing N N 158 
GLN   NE2 HE21 sing N N 159 
GLN   NE2 HE22 sing N N 160 
GLN   OXT HXT  sing N N 161 
GLU   N   CA   sing N N 162 
GLU   N   H    sing N N 163 
GLU   N   H2   sing N N 164 
GLU   CA  C    sing N N 165 
GLU   CA  CB   sing N N 166 
GLU   CA  HA   sing N N 167 
GLU   C   O    doub N N 168 
GLU   C   OXT  sing N N 169 
GLU   CB  CG   sing N N 170 
GLU   CB  HB2  sing N N 171 
GLU   CB  HB3  sing N N 172 
GLU   CG  CD   sing N N 173 
GLU   CG  HG2  sing N N 174 
GLU   CG  HG3  sing N N 175 
GLU   CD  OE1  doub N N 176 
GLU   CD  OE2  sing N N 177 
GLU   OE2 HE2  sing N N 178 
GLU   OXT HXT  sing N N 179 
GLY   N   CA   sing N N 180 
GLY   N   H    sing N N 181 
GLY   N   H2   sing N N 182 
GLY   CA  C    sing N N 183 
GLY   CA  HA2  sing N N 184 
GLY   CA  HA3  sing N N 185 
GLY   C   O    doub N N 186 
GLY   C   OXT  sing N N 187 
GLY   OXT HXT  sing N N 188 
HIS   N   CA   sing N N 189 
HIS   N   H    sing N N 190 
HIS   N   H2   sing N N 191 
HIS   CA  C    sing N N 192 
HIS   CA  CB   sing N N 193 
HIS   CA  HA   sing N N 194 
HIS   C   O    doub N N 195 
HIS   C   OXT  sing N N 196 
HIS   CB  CG   sing N N 197 
HIS   CB  HB2  sing N N 198 
HIS   CB  HB3  sing N N 199 
HIS   CG  ND1  sing Y N 200 
HIS   CG  CD2  doub Y N 201 
HIS   ND1 CE1  doub Y N 202 
HIS   ND1 HD1  sing N N 203 
HIS   CD2 NE2  sing Y N 204 
HIS   CD2 HD2  sing N N 205 
HIS   CE1 NE2  sing Y N 206 
HIS   CE1 HE1  sing N N 207 
HIS   NE2 HE2  sing N N 208 
HIS   OXT HXT  sing N N 209 
HOH   O   H1   sing N N 210 
HOH   O   H2   sing N N 211 
ILE   N   CA   sing N N 212 
ILE   N   H    sing N N 213 
ILE   N   H2   sing N N 214 
ILE   CA  C    sing N N 215 
ILE   CA  CB   sing N N 216 
ILE   CA  HA   sing N N 217 
ILE   C   O    doub N N 218 
ILE   C   OXT  sing N N 219 
ILE   CB  CG1  sing N N 220 
ILE   CB  CG2  sing N N 221 
ILE   CB  HB   sing N N 222 
ILE   CG1 CD1  sing N N 223 
ILE   CG1 HG12 sing N N 224 
ILE   CG1 HG13 sing N N 225 
ILE   CG2 HG21 sing N N 226 
ILE   CG2 HG22 sing N N 227 
ILE   CG2 HG23 sing N N 228 
ILE   CD1 HD11 sing N N 229 
ILE   CD1 HD12 sing N N 230 
ILE   CD1 HD13 sing N N 231 
ILE   OXT HXT  sing N N 232 
LEU   N   CA   sing N N 233 
LEU   N   H    sing N N 234 
LEU   N   H2   sing N N 235 
LEU   CA  C    sing N N 236 
LEU   CA  CB   sing N N 237 
LEU   CA  HA   sing N N 238 
LEU   C   O    doub N N 239 
LEU   C   OXT  sing N N 240 
LEU   CB  CG   sing N N 241 
LEU   CB  HB2  sing N N 242 
LEU   CB  HB3  sing N N 243 
LEU   CG  CD1  sing N N 244 
LEU   CG  CD2  sing N N 245 
LEU   CG  HG   sing N N 246 
LEU   CD1 HD11 sing N N 247 
LEU   CD1 HD12 sing N N 248 
LEU   CD1 HD13 sing N N 249 
LEU   CD2 HD21 sing N N 250 
LEU   CD2 HD22 sing N N 251 
LEU   CD2 HD23 sing N N 252 
LEU   OXT HXT  sing N N 253 
LYS   N   CA   sing N N 254 
LYS   N   H    sing N N 255 
LYS   N   H2   sing N N 256 
LYS   CA  C    sing N N 257 
LYS   CA  CB   sing N N 258 
LYS   CA  HA   sing N N 259 
LYS   C   O    doub N N 260 
LYS   C   OXT  sing N N 261 
LYS   CB  CG   sing N N 262 
LYS   CB  HB2  sing N N 263 
LYS   CB  HB3  sing N N 264 
LYS   CG  CD   sing N N 265 
LYS   CG  HG2  sing N N 266 
LYS   CG  HG3  sing N N 267 
LYS   CD  CE   sing N N 268 
LYS   CD  HD2  sing N N 269 
LYS   CD  HD3  sing N N 270 
LYS   CE  NZ   sing N N 271 
LYS   CE  HE2  sing N N 272 
LYS   CE  HE3  sing N N 273 
LYS   NZ  HZ1  sing N N 274 
LYS   NZ  HZ2  sing N N 275 
LYS   NZ  HZ3  sing N N 276 
LYS   OXT HXT  sing N N 277 
MET   N   CA   sing N N 278 
MET   N   H    sing N N 279 
MET   N   H2   sing N N 280 
MET   CA  C    sing N N 281 
MET   CA  CB   sing N N 282 
MET   CA  HA   sing N N 283 
MET   C   O    doub N N 284 
MET   C   OXT  sing N N 285 
MET   CB  CG   sing N N 286 
MET   CB  HB2  sing N N 287 
MET   CB  HB3  sing N N 288 
MET   CG  SD   sing N N 289 
MET   CG  HG2  sing N N 290 
MET   CG  HG3  sing N N 291 
MET   SD  CE   sing N N 292 
MET   CE  HE1  sing N N 293 
MET   CE  HE2  sing N N 294 
MET   CE  HE3  sing N N 295 
MET   OXT HXT  sing N N 296 
PHE   N   CA   sing N N 297 
PHE   N   H    sing N N 298 
PHE   N   H2   sing N N 299 
PHE   CA  C    sing N N 300 
PHE   CA  CB   sing N N 301 
PHE   CA  HA   sing N N 302 
PHE   C   O    doub N N 303 
PHE   C   OXT  sing N N 304 
PHE   CB  CG   sing N N 305 
PHE   CB  HB2  sing N N 306 
PHE   CB  HB3  sing N N 307 
PHE   CG  CD1  doub Y N 308 
PHE   CG  CD2  sing Y N 309 
PHE   CD1 CE1  sing Y N 310 
PHE   CD1 HD1  sing N N 311 
PHE   CD2 CE2  doub Y N 312 
PHE   CD2 HD2  sing N N 313 
PHE   CE1 CZ   doub Y N 314 
PHE   CE1 HE1  sing N N 315 
PHE   CE2 CZ   sing Y N 316 
PHE   CE2 HE2  sing N N 317 
PHE   CZ  HZ   sing N N 318 
PHE   OXT HXT  sing N N 319 
PRO   N   CA   sing N N 320 
PRO   N   CD   sing N N 321 
PRO   N   H    sing N N 322 
PRO   CA  C    sing N N 323 
PRO   CA  CB   sing N N 324 
PRO   CA  HA   sing N N 325 
PRO   C   O    doub N N 326 
PRO   C   OXT  sing N N 327 
PRO   CB  CG   sing N N 328 
PRO   CB  HB2  sing N N 329 
PRO   CB  HB3  sing N N 330 
PRO   CG  CD   sing N N 331 
PRO   CG  HG2  sing N N 332 
PRO   CG  HG3  sing N N 333 
PRO   CD  HD2  sing N N 334 
PRO   CD  HD3  sing N N 335 
PRO   OXT HXT  sing N N 336 
SER   N   CA   sing N N 337 
SER   N   H    sing N N 338 
SER   N   H2   sing N N 339 
SER   CA  C    sing N N 340 
SER   CA  CB   sing N N 341 
SER   CA  HA   sing N N 342 
SER   C   O    doub N N 343 
SER   C   OXT  sing N N 344 
SER   CB  OG   sing N N 345 
SER   CB  HB2  sing N N 346 
SER   CB  HB3  sing N N 347 
SER   OG  HG   sing N N 348 
SER   OXT HXT  sing N N 349 
THR   N   CA   sing N N 350 
THR   N   H    sing N N 351 
THR   N   H2   sing N N 352 
THR   CA  C    sing N N 353 
THR   CA  CB   sing N N 354 
THR   CA  HA   sing N N 355 
THR   C   O    doub N N 356 
THR   C   OXT  sing N N 357 
THR   CB  OG1  sing N N 358 
THR   CB  CG2  sing N N 359 
THR   CB  HB   sing N N 360 
THR   OG1 HG1  sing N N 361 
THR   CG2 HG21 sing N N 362 
THR   CG2 HG22 sing N N 363 
THR   CG2 HG23 sing N N 364 
THR   OXT HXT  sing N N 365 
TRP   N   CA   sing N N 366 
TRP   N   H    sing N N 367 
TRP   N   H2   sing N N 368 
TRP   CA  C    sing N N 369 
TRP   CA  CB   sing N N 370 
TRP   CA  HA   sing N N 371 
TRP   C   O    doub N N 372 
TRP   C   OXT  sing N N 373 
TRP   CB  CG   sing N N 374 
TRP   CB  HB2  sing N N 375 
TRP   CB  HB3  sing N N 376 
TRP   CG  CD1  doub Y N 377 
TRP   CG  CD2  sing Y N 378 
TRP   CD1 NE1  sing Y N 379 
TRP   CD1 HD1  sing N N 380 
TRP   CD2 CE2  doub Y N 381 
TRP   CD2 CE3  sing Y N 382 
TRP   NE1 CE2  sing Y N 383 
TRP   NE1 HE1  sing N N 384 
TRP   CE2 CZ2  sing Y N 385 
TRP   CE3 CZ3  doub Y N 386 
TRP   CE3 HE3  sing N N 387 
TRP   CZ2 CH2  doub Y N 388 
TRP   CZ2 HZ2  sing N N 389 
TRP   CZ3 CH2  sing Y N 390 
TRP   CZ3 HZ3  sing N N 391 
TRP   CH2 HH2  sing N N 392 
TRP   OXT HXT  sing N N 393 
TYR   N   CA   sing N N 394 
TYR   N   H    sing N N 395 
TYR   N   H2   sing N N 396 
TYR   CA  C    sing N N 397 
TYR   CA  CB   sing N N 398 
TYR   CA  HA   sing N N 399 
TYR   C   O    doub N N 400 
TYR   C   OXT  sing N N 401 
TYR   CB  CG   sing N N 402 
TYR   CB  HB2  sing N N 403 
TYR   CB  HB3  sing N N 404 
TYR   CG  CD1  doub Y N 405 
TYR   CG  CD2  sing Y N 406 
TYR   CD1 CE1  sing Y N 407 
TYR   CD1 HD1  sing N N 408 
TYR   CD2 CE2  doub Y N 409 
TYR   CD2 HD2  sing N N 410 
TYR   CE1 CZ   doub Y N 411 
TYR   CE1 HE1  sing N N 412 
TYR   CE2 CZ   sing Y N 413 
TYR   CE2 HE2  sing N N 414 
TYR   CZ  OH   sing N N 415 
TYR   OH  HH   sing N N 416 
TYR   OXT HXT  sing N N 417 
VAL   N   CA   sing N N 418 
VAL   N   H    sing N N 419 
VAL   N   H2   sing N N 420 
VAL   CA  C    sing N N 421 
VAL   CA  CB   sing N N 422 
VAL   CA  HA   sing N N 423 
VAL   C   O    doub N N 424 
VAL   C   OXT  sing N N 425 
VAL   CB  CG1  sing N N 426 
VAL   CB  CG2  sing N N 427 
VAL   CB  HB   sing N N 428 
VAL   CG1 HG11 sing N N 429 
VAL   CG1 HG12 sing N N 430 
VAL   CG1 HG13 sing N N 431 
VAL   CG2 HG21 sing N N 432 
VAL   CG2 HG22 sing N N 433 
VAL   CG2 HG23 sing N N 434 
VAL   OXT HXT  sing N N 435 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I6H 
_atom_sites.fract_transf_matrix[1][1]   0.013803 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000735 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016205 
_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]   0.015371 
_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   ? 16.232 6.382   8.074  1.00 20.74 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.007 6.484   8.871  1.00 20.10 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 14.877 5.335   9.851  1.00 19.35 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.522 4.306   9.695  1.00 19.76 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.793 6.494   7.936  1.00 22.55 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.651 5.217   7.330  1.00 24.74 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.042 5.516   10.870 1.00 17.60 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.736 4.461   11.819 1.00 16.82 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.294 5.029   13.151 1.00 16.61 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.662 6.159   13.501 1.00 17.79 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.592 4.209   13.953 1.00 15.25 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.175 4.678   15.266 1.00 15.96 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.100 3.497   16.223 1.00 15.76 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.042 2.334   15.786 1.00 15.72 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.784 5.288   15.140 1.00 16.59 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.085 3.797   17.545 1.00 13.86 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 11.856 2.806   18.586 1.00 13.71 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.438 3.050   19.093 1.00 13.89 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.080 4.198   19.355 1.00 15.03 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 12.817 3.016   19.767 1.00 13.84 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.283 2.965   19.264 1.00 14.19 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.576 1.919   20.853 1.00 14.19 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.258 3.511   20.290 1.00 16.28 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.639  1.979   19.259 1.00 15.19 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.263  2.111   19.756 1.00 16.90 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.175  1.361   21.054 1.00 17.21 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.256  0.146   21.036 1.00 19.53 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.272  1.537   18.730 1.00 17.20 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.217  2.349   17.460 1.00 18.37 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.417  3.477   17.371 1.00 18.60 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.008  2.026   16.373 1.00 19.11 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.376  4.245   16.213 1.00 19.66 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 7.984  2.787   15.213 1.00 20.95 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.176  3.902   15.142 1.00 21.88 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.143  4.670   14.000 1.00 25.41 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.148  2.056   22.189 1.00 17.45 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.137  1.420   23.500 1.00 19.57 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 6.991  2.030   24.293 1.00 20.91 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 6.886  3.265   24.364 1.00 20.55 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.501  1.572   24.239 1.00 21.43 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 9.987  3.026   24.252 1.00 22.19 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.391  1.054   25.670 1.00 22.04 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.061  1.194   24.777 1.00 21.14 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 4.912  1.709   25.511 1.00 20.82 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.112  2.682   24.656 1.00 21.41 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 3.884  2.387   23.483 1.00 21.64 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.767  3.855   25.192 1.00 21.79 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.093  4.872   24.393 1.00 22.42 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.068  5.946   23.901 1.00 20.40 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.686  7.118   23.741 1.00 20.98 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 1.910  5.499   25.134 1.00 25.98 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.780  4.508   25.285 1.00 32.86 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.038  4.228   24.327 1.00 37.15 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.661  3.936   26.470 1.00 33.02 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.311  5.533   23.583 1.00 18.28 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.312  6.500   23.114 1.00 17.40 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 6.920  6.046   21.801 1.00 16.21 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.074  4.840   21.566 1.00 16.83 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.478  6.555   24.109 1.00 18.30 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.100  7.113   25.457 1.00 19.93 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.517  8.367   25.575 1.00 20.91 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.324  6.390   26.614 1.00 21.64 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.160  8.884   26.809 1.00 22.15 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 6.997  6.911   27.859 1.00 22.52 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.380  8.145   27.949 1.00 23.31 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.061  8.686   29.169 1.00 25.96 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.339  7.030   20.991 1.00 15.50 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.034  6.847   19.736 1.00 15.40 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.350  7.645   19.866 1.00 15.16 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.301  8.840   20.158 1.00 15.27 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.187  7.353   18.536 1.00 16.27 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 7.958  7.584   17.241 1.00 18.05 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.060  7.897   16.035 1.00 18.28 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.651  8.880   15.126 1.00 19.34 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.132  8.615   13.921 1.00 22.70 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.126  7.367   13.455 1.00 24.18 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.607  9.598   13.156 1.00 21.66 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.513 6.965   19.739 1.00 14.34 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.822 7.611   19.849 1.00 13.54 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.409 7.727   18.472 1.00 13.13 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.532 6.710   17.786 1.00 14.27 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.799 6.792   20.755 1.00 14.41 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.099 7.593   21.027 1.00 15.05 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.127 6.330   22.052 1.00 15.73 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.786 8.942   18.042 1.00 12.74 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.345 9.172   16.715 1.00 14.07 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.555 10.085  16.814 1.00 13.37 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.740 10.786  17.828 1.00 13.87 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.301 9.823   15.765 1.00 15.11 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.196 8.840   15.422 1.00 18.84 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.763 11.123  16.357 1.00 16.05 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.350 10.186  15.717 1.00 13.04 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.387 11.203  15.665 1.00 12.67 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.703 12.560  15.631 1.00 13.60 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.729 12.741  14.861 1.00 14.33 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.192 11.084  14.386 1.00 12.24 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.970 9.797   14.292 1.00 14.07 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.474 8.774   13.780 1.00 15.91 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.208 9.832   14.788 1.00 14.86 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.173 13.520  16.455 1.00 13.21 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.483 14.809  16.514 1.00 13.25 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.458 15.480  15.116 1.00 14.51 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.438 16.074  14.733 1.00 15.80 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.176 15.677  17.552 1.00 13.58 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.443 17.005  17.864 1.00 13.04 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.350 17.825  18.774 1.00 14.55 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.730 19.072  19.276 1.00 14.72 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.702 20.225  18.610 1.00 15.47 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.138 20.286  17.360 1.00 17.27 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.216 21.328  19.191 1.00 16.11 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.559 15.302  14.346 1.00 14.49 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.614 15.942  13.019 1.00 14.85 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.658 15.303  12.002 1.00 16.19 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.439 15.906  10.926 1.00 18.61 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.077 16.038  12.459 1.00 15.61 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.675 14.735  12.010 1.00 16.92 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.272 13.854  12.906 1.00 16.71 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.783 14.231  10.758 1.00 19.02 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.718 12.829  12.169 1.00 17.55 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.441 13.017  10.867 1.00 18.70 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.136 14.112  12.284 1.00 16.09 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.199 13.461  11.364 1.00 15.94 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.756 13.509  11.884 1.00 17.37 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.870 12.918  11.266 1.00 18.46 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.599 11.989  11.077 1.00 16.02 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 15.984 11.828  10.443 1.00 17.93 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.287 10.344  10.213 1.00 18.17 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.081 12.625  9.098  1.00 18.25 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.516 14.150  13.050 1.00 15.99 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.157 14.191  13.622 1.00 16.15 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.202 14.875  12.658 1.00 16.78 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.566 15.857  12.044 1.00 17.88 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.171 14.950  14.943 1.00 15.74 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.007  14.319  12.528 1.00 17.70 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.021  14.877  11.585 1.00 18.84 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.210  15.993  12.241 1.00 20.13 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.292  16.187  13.454 1.00 20.49 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.085  13.736  11.136 1.00 21.05 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.369  13.258  12.284 1.00 22.14 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.832  12.593  10.472 1.00 22.10 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.292  16.654  11.460 1.00 20.38 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.388  17.631  12.054 1.00 21.63 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.534  16.945  13.163 1.00 20.06 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.324  17.517  14.226 1.00 21.88 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.428  18.181  10.966 1.00 25.35 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.099  18.900  9.844  1.00 31.90 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.889  20.014  10.068 1.00 34.72 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.995  18.692  8.508  1.00 34.60 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.276  20.430  8.868  1.00 36.23 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.750  19.670  7.893  1.00 36.25 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.091  15.699  12.924 1.00 20.40 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.282  14.985  13.919 1.00 20.01 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.069  14.686  15.206 1.00 19.21 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.512  14.736  16.315 1.00 19.79 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.710  13.694  13.335 1.00 24.84 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.759  12.959  14.231 1.00 35.57 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.633  13.397  14.453 1.00 39.01 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 2.178  11.799  14.739 1.00 39.97 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.385  14.362  15.074 1.00 16.80 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.198  14.131  16.282 1.00 16.45 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.245  15.405  17.135 1.00 17.25 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.087  15.318  18.352 1.00 17.54 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.644  13.751  15.919 1.00 15.70 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.770  12.347  15.402 1.00 19.13 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.121  11.438  15.991 1.00 18.70 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.501  12.155  14.383 1.00 18.44 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.478  16.571  16.503 1.00 17.24 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.555  17.820  17.238 1.00 17.06 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.179  18.207  17.827 1.00 19.24 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.120  18.768  18.928 1.00 20.17 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.102  18.936  16.327 1.00 16.30 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.600  18.882  16.199 1.00 16.47 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.330  18.423  15.138 1.00 17.19 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.546  19.342  17.168 1.00 16.01 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.683 18.590  15.386 1.00 17.02 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.837 19.145  16.630 1.00 16.63 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.426  19.911  18.437 1.00 16.49 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.002 19.493  17.339 1.00 17.14 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.574 20.270  19.119 1.00 16.71 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.835 20.062  18.564 1.00 16.60 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.080  17.848  17.144 1.00 19.52 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.725  18.137  17.673 1.00 20.71 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.350  17.213  18.856 1.00 21.74 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.348  17.458  19.559 1.00 23.27 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.690  17.970  16.564 1.00 21.33 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.080  16.079  19.035 1.00 20.10 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.825  15.181  20.144 1.00 20.16 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.117  15.044  21.000 1.00 19.03 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.410  13.991  21.532 1.00 18.61 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.407  13.815  19.588 1.00 21.82 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.044  13.840  18.951 1.00 24.90 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.046  13.820  19.665 1.00 25.95 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 0.973  13.909  17.618 1.00 25.56 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.892  16.134  21.129 1.00 18.27 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.171  16.139  21.823 1.00 17.66 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.083  15.777  23.294 1.00 18.87 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.320  16.383  24.050 1.00 19.88 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.758  17.549  21.688 1.00 17.95 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.131  17.763  22.356 1.00 19.19 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.201  16.873  21.709 1.00 19.95 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.588  19.235  22.225 1.00 19.12 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 6.941  14.831  23.728 1.00 18.75 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.086  14.494  25.136 1.00 19.50 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.391  15.096  25.668 1.00 19.27 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.421  15.713  26.754 1.00 20.82 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.091  12.948  25.319 1.00 20.67 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.507  12.543  26.740 1.00 22.24 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.728  12.358  24.993 1.00 21.61 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.499  14.924  24.902 1.00 17.34 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 10.818 15.385  25.350 1.00 17.46 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.757 15.447  24.129 1.00 15.52 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.652 14.612  23.227 1.00 16.69 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.403 14.368  26.375 1.00 18.78 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 12.874 14.521  26.718 1.00 19.43 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.428 15.357  27.650 1.00 21.08 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 13.964 13.761  26.167 1.00 18.13 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.813 15.211  27.660 1.00 21.05 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.155 14.193  26.805 1.00 19.44 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.045 12.744  25.217 1.00 18.07 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.413 13.633  26.512 1.00 19.20 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.282 12.197  24.923 1.00 19.10 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.452 12.645  25.560 1.00 18.55 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.676 16.388  24.117 1.00 16.74 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.683 16.458  23.066 1.00 16.40 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 14.985 16.997  23.632 1.00 15.62 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 14.974 17.792  24.575 1.00 16.22 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.216 17.253  21.839 1.00 17.49 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.653 18.641  22.135 1.00 18.14 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.673 19.734  22.385 1.00 19.87 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.349 20.649  23.176 1.00 23.44 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.788 19.673  21.823 1.00 18.37 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.116 16.627  23.010 1.00 15.61 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.406 17.129  23.442 1.00 14.89 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.293 17.269  22.211 1.00 15.48 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.688 16.260  21.616 1.00 15.60 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.990 16.216  24.528 1.00 15.95 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.299 16.674  25.142 1.00 23.35 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.031 17.431  24.481 1.00 26.10 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.605 16.247  26.287 1.00 23.90 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.532 18.499  21.786 1.00 16.36 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.328 18.771  20.609 0.50 17.29 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.332 18.759  20.602 0.50 17.10 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.762 18.245  20.780 1.00 17.60 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.346 17.746  19.817 1.00 19.07 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.333 20.271  20.323 0.50 19.94 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.340 20.251  20.267 0.50 19.20 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.216 20.576  19.260 0.50 23.77 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 19.725 21.029  21.388 0.50 22.08 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.299 18.326  22.016 1.00 17.44 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.670 17.835  22.225 1.00 17.81 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.782 16.325  22.043 1.00 17.38 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 23.894 15.861  21.853 1.00 19.41 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.246 18.236  23.578 1.00 21.59 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.720 17.486  24.658 1.00 26.61 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.678 15.576  22.126 1.00 14.72 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.741 14.113  21.957 1.00 13.78 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.146 13.678  20.593 1.00 14.12 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.173 12.483  20.283 1.00 14.10 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 20.897 13.443  23.071 1.00 14.24 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.443 13.665  24.475 1.00 16.19 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.553 13.036  25.525 1.00 17.40 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.555 11.571  25.402 1.00 15.93 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.368 10.739  26.423 1.00 17.17 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.180 11.215  27.655 1.00 18.13 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.420 9.423   26.235 1.00 16.90 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.583 14.602  19.816 1.00 13.48 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 19.885 14.274  18.577 1.00 12.90 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.726 13.311  18.830 1.00 12.76 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.417 12.480  17.968 1.00 13.83 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 20.805 13.734  17.458 1.00 13.59 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.105 13.469  16.128 1.00 15.14 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.277 14.328  15.697 1.00 15.28 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.423 12.422  15.488 1.00 14.07 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.021 13.488  19.966 1.00 12.80 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 16.869 12.631  20.254 1.00 11.84 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.578 13.447  20.422 1.00 12.14 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.598 14.549  20.958 1.00 13.26 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.040 11.832  21.542 1.00 13.30 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.042 10.693  21.480 1.00 14.09 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.108 9.989   22.861 1.00 15.21 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.704 9.689   20.371 1.00 14.12 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.471 12.821  20.032 1.00 12.40 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.149 13.367  20.274 1.00 12.57 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.216 12.199  20.560 1.00 13.27 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.334 11.135  19.915 1.00 13.22 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.652 14.203  19.087 1.00 12.68 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.270 14.874  19.289 1.00 13.98 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.189 16.200  18.524 1.00 15.83 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.116 13.969  18.797 1.00 15.73 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.323 12.373  21.560 1.00 13.76 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.338 11.355  21.920 1.00 15.54 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 8.944  11.987  21.794 1.00 16.56 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 8.710  13.077  22.324 1.00 17.01 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.562 10.847  23.359 1.00 16.48 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.463  9.845   23.754 1.00 17.22 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 11.944 10.179  23.476 1.00 15.90 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.051  11.311  21.085 1.00 17.15 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.668  11.775  20.910 1.00 16.70 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.705  10.699  21.476 1.00 17.99 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.090  9.540   21.696 1.00 17.18 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.352  12.064  19.442 1.00 18.30 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.530  10.914  18.618 1.00 18.95 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.443  11.097  21.721 1.00 19.40 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.478  10.125  22.261 1.00 20.97 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.690  9.437   21.159 1.00 22.07 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.466  10.001  20.096 1.00 22.55 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.560  10.780  23.281 1.00 24.15 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 1.928  11.864  22.651 1.00 25.36 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.283  8.191   21.409 1.00 22.54 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.538  7.378   20.441 1.00 25.09 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.223  6.898   21.078 1.00 28.32 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.105  6.846   22.307 1.00 29.03 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.353  6.110   20.037 1.00 26.19 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.457  5.234   21.156 1.00 27.28 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.754  6.422   19.542 1.00 25.92 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.746 6.532   20.238 1.00 30.18 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -2.017 5.988   20.723 1.00 31.97 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.939 4.449   20.838 1.00 33.29 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.629 3.856   21.672 1.00 34.92 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -3.161 6.435   19.808 1.00 34.11 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.821 6.099   18.454 1.00 35.73 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.436 7.929   19.908 1.00 34.66 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -1.112 3.800   20.006 1.00 31.97 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.979 2.342   20.043 1.00 31.96 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.224  1.925   20.895 1.00 31.73 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.196  2.667   21.011 1.00 31.44 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.819 1.807   18.630 1.00 32.20 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.173  0.727   21.457 1.00 30.64 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.255  0.205   22.292 1.00 31.68 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.414  -0.276  21.416 1.00 31.43 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.177  -0.927  20.393 1.00 32.25 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.737  -0.947  23.168 1.00 35.66 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.244  -0.895  24.607 1.00 43.23 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 0.661  0.284   25.356 1.00 52.35 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? -0.476 0.727   25.108 1.00 55.08 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 1.430  0.824   26.296 1.00 54.26 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.644  0.062   21.788 1.00 29.95 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.821  -0.262  20.982 1.00 28.52 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.291  -1.698  21.020 1.00 29.46 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 4.952  -2.423  21.946 1.00 31.36 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.126  -2.082  20.029 1.00 27.04 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.647  -3.435  19.838 1.00 25.90 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 7.990  -3.700  20.528 1.00 25.58 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.361  -4.859  20.657 1.00 26.01 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.748  -3.740  18.341 1.00 25.97 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 7.742  -2.541  17.389 1.00 27.87 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.746  -2.652  20.913 1.00 23.63 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.138 -2.770  21.419 1.00 21.88 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.302 -2.776  22.950 1.00 21.58 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.381  -2.317  23.618 1.00 24.39 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 10.960 -1.599  20.817 1.00 19.93 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.081 -1.671  19.298 1.00 23.26 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.484 -2.754  18.782 1.00 24.43 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 10.780 -0.638  18.603 1.00 20.80 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.479 -3.303  23.494 1.00 20.53 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 11.999 -3.440  24.897 1.00 21.66 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.344 -2.697  24.963 1.00 19.52 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.152 -2.876  24.076 1.00 19.11 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.295 -4.969  25.238 1.00 26.98 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.056 -5.594  25.525 1.00 32.34 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.259 -5.174  26.468 1.00 29.19 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.567 -1.830  25.988 1.00 17.81 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 14.842 -1.109  26.074 1.00 16.25 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 15.812 -1.877  26.949 1.00 15.36 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.444 -2.361  28.042 1.00 16.44 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.621 0.274   26.722 1.00 16.25 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.494 1.058   25.989 1.00 17.67 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 15.926 1.095   26.718 1.00 16.02 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 13.812 1.293   24.465 1.00 18.63 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.063 -2.016  26.500 1.00 14.36 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.117 -2.675  27.286 1.00 13.86 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.455 -1.792  28.522 1.00 14.80 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.497 -0.559  28.438 1.00 14.64 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.386 -2.798  26.419 1.00 14.41 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 18.733 -2.449  29.681 1.00 15.60 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.160 -1.710  30.869 1.00 15.87 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.442 -2.461  31.274 1.00 17.27 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.404 -3.479  31.987 1.00 18.67 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.090 -1.727  31.977 1.00 16.55 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.751 -1.122  31.561 1.00 16.80 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.798 0.375   31.187 1.00 20.04 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.467 0.853   30.798 1.00 20.04 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.235 2.002   30.164 1.00 20.83 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.240 2.804   29.830 1.00 19.88 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 13.994 2.359   29.861 1.00 19.84 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.571 -1.975  30.774 1.00 16.73 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 22.831 -2.715  30.847 1.00 17.95 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.026 -1.839  30.480 1.00 17.53 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 23.864 -0.698  30.042 1.00 18.36 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 22.748 -3.902  29.888 1.00 17.91 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 22.776 -3.408  28.124 1.00 15.54 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.255 -2.435  30.585 1.00 18.42 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.447 -1.730  30.127 1.00 19.67 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.128 -2.487  28.986 1.00 19.50 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.349 -2.396  28.826 1.00 20.02 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.448 -1.535  31.275 1.00 23.33 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 27.979 -2.803  31.883 1.00 33.50 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.458 -3.903  31.545 1.00 34.72 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 28.923 -2.714  32.696 1.00 40.59 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.347 -3.210  28.143 1.00 17.52 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 26.950 -3.911  26.987 1.00 15.91 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.708 -2.938  26.124 1.00 16.48 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.270 -1.784  25.927 1.00 15.71 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 25.885 -4.600  26.143 1.00 14.33 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.217 -6.101  26.877 1.00 17.04 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 28.831 -3.399  25.578 1.00 14.77 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.599 -2.628  24.604 1.00 14.54 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.725 -3.400  23.280 1.00 13.75 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.609 -3.109  22.456 1.00 13.86 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 30.994 -2.235  25.087 1.00 17.15 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 30.964 -1.073  26.058 1.00 21.36 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.380 -0.670  26.420 1.00 26.61 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 32.827 -0.888  27.553 1.00 27.67 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.101 -0.055  25.474 1.00 22.73 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 28.898 -4.480  23.088 1.00 12.83 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 28.791 -5.173  21.800 1.00 13.70 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.308 -5.340  21.483 1.00 13.40 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.464 -5.383  22.400 1.00 14.30 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.494 -6.540  21.792 1.00 16.43 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 28.801 -7.442  22.659 1.00 19.59 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 30.957 -6.454  22.195 1.00 16.45 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.014 -5.412  20.188 1.00 12.75 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.625 -5.593  19.764 1.00 12.63 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.570 -5.671  18.245 1.00 11.76 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.598 -5.919  17.600 1.00 12.37 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.363 -5.533  17.691 1.00 11.41 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.155 -5.648  16.243 1.00 11.00 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.273 -4.454  15.843 1.00 11.64 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.267 -4.183  16.502 1.00 12.30 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.438 -7.008  15.921 1.00 12.85 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.041 -7.092  14.442 1.00 14.67 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.322 -8.222  16.273 1.00 13.37 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.624 -3.791  14.720 1.00 11.36 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.779 -2.696  14.242 1.00 11.32 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.306 -2.952  12.801 1.00 11.72 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 22.906 -3.705  12.058 1.00 12.34 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.477 -1.299  14.284 1.00 11.41 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.507 -1.062  13.186 1.00 11.34 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.782 -1.617  13.269 1.00 12.21 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.256 -0.189  12.138 1.00 12.10 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.746 -1.394  12.280 1.00 12.67 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.233 0.081   11.170 1.00 12.73 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.481 -0.518  11.253 1.00 13.54 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.431 -0.284  10.272 1.00 15.09 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.173 -2.349  12.460 1.00 11.75 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.640 -2.439  11.116 1.00 12.38 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.153 -1.258  10.278 1.00 12.32 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.003 -0.083  10.666 1.00 12.49 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.088 -2.471  11.108 1.00 12.11 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.557 -2.598  9.704  1.00 13.53 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.763 -3.755  8.973  1.00 14.31 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.895 -1.537  9.094  1.00 14.98 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.352 -3.844  7.652  1.00 16.00 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.469 -1.617  7.787  1.00 15.95 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.686 -2.778  7.080  1.00 16.96 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.266 -2.891  5.773  1.00 20.75 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.709 -1.584  9.093  1.00 12.87 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.261 -0.600  8.163  1.00 12.43 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.411 -0.577  6.871  1.00 14.22 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.561 -1.465  6.008  1.00 14.57 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.703 -0.988  7.853  1.00 12.57 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.500 0.055   6.596  1.00 14.67 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.514 0.418   6.747  1.00 13.90 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.634 0.472   5.617  1.00 14.78 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.339 0.623   4.284  1.00 14.46 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.847 0.089   3.283  1.00 15.38 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.595 1.556   5.807  1.00 17.78 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.181 2.846   5.846  1.00 23.90 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.497 1.328   4.262  1.00 13.25 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.270 1.489   3.009  1.00 14.04 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.923 0.187   2.511  1.00 13.71 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.514 0.192   1.412  1.00 14.13 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.325 2.589   3.104  1.00 16.09 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.320 2.286   4.072  1.00 16.38 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.848 -0.908  3.288  1.00 13.26 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.354 -2.203  2.858  1.00 13.29 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.249 -3.289  3.020  1.00 14.52 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.530 -4.464  2.725  1.00 15.84 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.562 -2.604  3.738  1.00 14.58 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.809 -1.731  3.533  1.00 15.07 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.484 -2.051  2.207  1.00 15.81 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.657 -1.221  1.937  1.00 18.02 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.616 -0.044  1.308  1.00 17.78 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.452 0.473   0.926  1.00 17.48 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.741 0.645   1.094  1.00 17.15 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.026 -2.924  3.502  1.00 16.54 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 19.990 -3.922  3.798  1.00 17.85 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.521 -5.082  4.635  1.00 17.72 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.269 -6.272  4.335  1.00 19.18 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.340 -4.459  2.511  1.00 20.76 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.321 -3.522  1.980  1.00 25.48 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.445 -4.210  0.929  1.00 27.31 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.793 -3.183  0.144  1.00 28.76 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.034 -2.968  -1.145 1.00 29.73 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.876 -3.765  -1.819 1.00 29.62 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.452 -1.953  -1.770 1.00 28.53 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.367 -4.764  5.625  1.00 15.73 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.027 -5.826  6.405  1.00 15.37 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.209 -5.419  7.845  1.00 14.33 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.293 -4.239  8.133  1.00 14.51 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.473 -6.029  5.874  1.00 19.40 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.622 -7.022  4.724  1.00 28.19 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 25.111 -7.311  4.526  1.00 35.60 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.358 -8.475  3.577  1.00 41.03 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.295 -8.071  2.140  1.00 43.61 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.294 -6.404  8.724  1.00 14.54 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.685 -6.182  10.109 1.00 13.60 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.171 -6.496  10.264 1.00 14.51 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.687 -7.455  9.646  1.00 16.82 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 21.922 -7.105  11.053 1.00 13.38 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.445 -6.903  10.994 1.00 15.03 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.746 -6.145  11.940 1.00 17.99 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.560 -7.446  10.138 1.00 16.99 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.462 -6.240  11.589 1.00 16.88 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.314 -6.975  10.494 1.00 20.21 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 24.862 -5.698  11.085 1.00 12.49 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.283 -5.900  11.316 1.00 11.80 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.564 -5.965  12.812 1.00 12.63 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.040 -5.145  13.578 1.00 12.82 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.092 -4.689  10.786 1.00 12.66 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.147 -4.582  9.285  1.00 14.41 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 27.892 -5.482  8.527  1.00 16.15 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.498 -3.556  8.624  1.00 15.07 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 27.934 -5.391  7.134  1.00 17.80 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.536 -3.454  7.237  1.00 15.41 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.303 -4.337  6.497  1.00 17.72 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.375 -4.216  5.111  1.00 20.17 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.462 -6.853  13.238 1.00 12.06 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 27.870 -6.861  14.655 1.00 13.12 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 28.905 -5.728  14.925 1.00 15.63 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.735 -5.434  14.051 1.00 18.48 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.507 -8.251  14.818 1.00 14.49 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.068 -8.532  13.446 1.00 15.32 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.155 -7.898  12.432 1.00 12.72 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 28.871 -5.110  16.109 1.00 13.30 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.775 -4.003  16.415 1.00 13.12 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.247 -4.061  17.845 1.00 13.05 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.564 -4.568  18.729 1.00 13.24 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.082 -2.610  16.217 1.00 15.23 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.019 -2.223  14.730 1.00 15.34 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.683 -2.562  16.851 1.00 16.22 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.471 -3.532  18.067 1.00 13.47 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 31.998 -3.253  19.416 1.00 13.95 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 31.966 -1.707  19.476 1.00 14.25 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.436 -1.044  18.516 1.00 15.34 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.444 -3.685  19.516 1.00 15.59 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.458 -5.101  19.502 1.00 20.49 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.332 -1.115  20.516 1.00 12.37 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.181 0.341   20.539 1.00 12.73 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.671 0.943   21.841 1.00 13.67 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.721 0.270   22.895 1.00 14.28 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.710 0.772   20.248 1.00 12.50 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.676 0.004   21.040 1.00 12.65 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.124 -1.160  20.535 1.00 12.80 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.191 0.500   22.235 1.00 13.02 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.152 -1.876  21.252 1.00 12.56 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.222 -0.199  22.962 1.00 12.89 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.725 -1.406  22.462 1.00 12.46 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.046 2.235   21.774 1.00 13.28 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.511 2.908   22.981 1.00 14.55 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.327 3.246   23.910 1.00 15.13 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.162 3.306   23.481 1.00 15.81 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.284 4.165   22.601 1.00 15.01 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.458 5.058   21.855 1.00 16.73 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.634 3.478   25.196 1.00 14.91 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.599 3.872   26.148 1.00 16.17 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.052 5.255   25.765 1.00 16.78 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.779 6.091   25.224 1.00 16.84 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.206 3.916   27.562 1.00 18.48 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.560 2.522   28.051 1.00 21.36 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.045 2.593   29.530 1.00 26.46 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.398 1.217   30.019 1.00 32.80 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 32.879 1.245   31.431 1.00 37.57 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 28.815 5.586   26.189 1.00 16.63 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.240 6.880   25.818 1.00 17.15 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.107 8.030   26.295 1.00 17.13 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.487 8.059   27.459 1.00 17.61 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 26.887 6.886   26.548 1.00 18.30 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.568 5.435   26.786 1.00 19.95 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 27.856 4.710   26.891 1.00 17.15 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.399 8.982   25.387 1.00 15.86 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.266 10.095  25.763 1.00 17.48 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.009 11.313  24.891 1.00 18.55 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.167 11.278  23.982 1.00 17.91 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 31.719 9.639   25.658 1.00 21.55 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.124 9.562   24.305 1.00 25.87 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.742 12.410  25.185 1.00 19.13 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.621 13.669  24.432 1.00 21.35 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.600 13.588  23.280 1.00 23.18 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 32.815 13.499  23.537 1.00 25.30 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.098 14.813  25.337 1.00 23.22 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.088 15.554  26.126 1.00 26.90 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.789 16.576  27.029 1.00 28.91 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.126 16.285  25.226 1.00 27.42 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.111 13.654  22.029 1.00 22.71 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 31.950 13.536  20.833 1.00 23.94 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.710 14.687  19.884 1.00 24.24 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.562 15.049  19.662 1.00 22.63 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.689 12.168  20.158 1.00 26.40 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.274 11.043  21.019 1.00 28.96 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.270 12.108  18.743 1.00 27.25 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 31.743 9.811   20.764 1.00 31.07 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.783 15.300  19.341 1.00 24.52 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.620 16.400  18.393 1.00 25.65 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.023 15.938  17.056 1.00 26.72 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.454 14.938  16.478 1.00 27.46 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 33.975 17.116  18.147 1.00 26.58 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 33.909 18.254  17.156 1.00 28.18 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.187 18.047  15.813 1.00 30.00 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.551 19.515  17.558 1.00 29.52 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.141 19.096  14.899 1.00 30.90 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.506 20.568  16.641 1.00 30.53 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.786 20.344  15.315 1.00 30.13 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.015 16.695  16.574 1.00 27.06 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.339 16.494  15.298 1.00 27.62 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.359 17.816  14.517 1.00 28.27 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 29.925 18.859  15.040 1.00 27.83 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 28.873 16.060  15.532 1.00 27.79 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.156 15.864  14.195 1.00 29.33 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.803 14.797  16.374 1.00 27.54 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.783 17.773  13.251 1.00 29.57 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 30.878 18.970  12.420 1.00 30.80 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.523 19.607  12.151 1.00 30.73 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.490 18.945  12.291 1.00 29.68 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.556 18.621  11.088 1.00 35.77 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 33.009 18.254  11.266 1.00 45.87 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.813 18.383  9.992  1.00 58.31 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 33.686 19.422  9.298  1.00 60.37 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 34.567 17.432  9.678  1.00 61.75 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.510 20.906  11.753 1.00 30.79 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.248 21.560  11.430 1.00 31.41 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.554 20.874  10.263 1.00 32.45 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.206 20.301  9.384  1.00 32.96 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.480 23.015  11.071 1.00 31.84 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.229 20.899  10.282 1.00 32.13 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.439 20.318  9.219  1.00 32.68 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.267 21.262  8.969  1.00 33.64 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.141 22.332  9.615  1.00 34.32 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 24.923 18.937  9.641  1.00 33.67 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 23.948 19.059  10.670 1.00 33.45 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.396 20.863  8.040  1.00 34.03 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.211 21.630  7.734  1.00 35.21 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.263 21.747  8.932  1.00 34.60 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.499 22.705  8.988  1.00 34.75 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.493 21.016  6.514  1.00 39.94 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 21.200 19.535  6.662  1.00 47.28 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 21.192 18.742  5.369  1.00 57.70 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 20.187 18.828  4.626  1.00 61.10 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 22.189 18.029  5.101  1.00 60.30 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.315 20.799  9.906  1.00 33.54 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.427 20.801  11.076 1.00 32.44 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.054 21.306  12.379 1.00 29.89 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.328 21.797  13.248 1.00 29.08 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 19.869 19.392  11.338 1.00 33.04 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 18.883 18.893  10.314 1.00 35.74 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 19.214 17.860  9.451  1.00 37.76 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 17.595 19.409  10.249 1.00 38.01 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 18.293 17.351  8.545  1.00 39.36 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 16.665 18.914  9.342  1.00 39.93 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 17.023 17.891  8.484  1.00 41.49 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.121 17.426  7.559  1.00 44.77 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.382 21.221  12.519 1.00 28.64 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.031 21.624  13.768 1.00 27.30 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.294 22.406  13.536 1.00 27.92 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.045 22.096  12.613 1.00 27.53 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.462 20.366  14.557 1.00 25.59 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.338 19.438  14.979 1.00 22.63 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.464 19.798  15.988 1.00 23.37 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.207 18.175  14.423 1.00 22.52 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.468 18.939  16.422 1.00 21.73 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.210 17.293  14.856 1.00 21.34 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.343 17.687  15.855 1.00 21.61 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.329 16.873  16.299 1.00 19.71 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.620 23.330  14.455 1.00 29.24 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 25.944 23.964  14.376 1.00 29.64 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.002 22.939  14.795 1.00 29.79 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.687 21.888  15.392 1.00 30.29 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 25.847 25.089  15.419 1.00 30.71 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 24.882 24.514  16.466 1.00 31.51 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 23.871 23.738  15.663 1.00 29.67 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.292 23.258  14.587 1.00 29.47 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.389 22.404  15.058 1.00 29.14 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.276 22.339  16.597 1.00 28.08 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.008 23.373  17.225 1.00 29.43 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.731 23.020  14.660 1.00 30.06 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.292 21.115  17.166 1.00 26.89 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.044 20.985  18.594 1.00 25.13 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.516 19.636  19.118 1.00 25.18 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.902 18.763  18.338 1.00 25.65 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.506 21.118  18.807 1.00 25.09 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.748 19.813  18.374 1.00 26.11 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.322 20.037  17.932 1.00 25.86 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.422 18.910  18.248 1.00 24.07 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.371 17.757  17.586 1.00 24.78 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.460 16.838  17.906 1.00 21.79 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.273 17.479  16.649 1.00 23.85 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.451 19.460  20.433 1.00 24.21 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.694 18.164  21.021 1.00 25.06 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.341 17.504  21.163 1.00 23.39 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.434 18.084  21.766 1.00 24.73 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.286 18.322  22.416 1.00 27.43 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.681 18.888  22.367 1.00 30.37 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.777 18.063  22.202 1.00 32.62 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 31.900 20.256  22.442 1.00 32.50 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.066 18.582  22.132 1.00 34.32 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.181 20.787  22.351 1.00 34.35 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.264 19.939  22.196 1.00 35.83 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.556 20.421  22.148 1.00 39.08 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.197 16.310  20.599 1.00 19.93 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 26.951 15.569  20.776 1.00 17.71 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.202 14.671  21.988 1.00 17.55 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.250 13.997  22.071 1.00 18.75 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.608 14.755  19.532 1.00 16.92 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.333 13.916  19.775 1.00 17.35 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.697 13.436  18.487 1.00 18.85 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.564 14.201  17.516 1.00 22.05 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.250 12.180  18.465 1.00 15.92 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.281 14.671  22.932 1.00 15.78 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.423 13.883  24.153 1.00 15.61 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.750 12.504  24.006 1.00 16.75 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 24.937 12.303  23.079 1.00 15.97 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 25.823 14.645  25.343 1.00 17.47 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.440 14.904  25.153 1.00 19.41 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.081 11.572  24.935 1.00 15.38 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.479 10.235  24.996 1.00 15.92 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.664 9.494   23.668 1.00 15.43 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 24.818 8.672   23.299 1.00 15.46 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 23.991 10.337  25.400 1.00 17.03 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 23.791 10.976  26.757 1.00 18.74 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 23.703 10.200  27.903 1.00 20.92 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 23.741 12.280  27.112 1.00 19.51 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.583 11.065  28.921 1.00 22.05 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.577 12.321  28.490 1.00 20.92 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 26.813 9.734   22.997 1.00 14.08 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.076 9.089   21.707 1.00 13.71 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.060 7.954   21.875 1.00 14.00 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.032 8.070   22.626 1.00 14.70 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.667 10.128  20.727 1.00 15.13 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 27.827 9.735   19.267 1.00 17.79 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.424 9.483   18.600 1.00 17.72 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.520 10.889  18.492 1.00 21.12 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 27.807 6.865   21.119 1.00 13.90 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 28.661 5.651   21.136 1.00 13.11 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.231 5.416   19.755 1.00 13.65 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.455 5.389   18.819 1.00 14.50 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 27.802 4.447   21.556 1.00 14.01 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.224 4.665   22.974 1.00 14.73 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.097 3.345   23.467 1.00 17.84 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 24.768 3.653   22.256 1.00 19.78 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.564 5.265   19.593 1.00 13.63 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.099 5.058   18.235 1.00 14.34 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.515 3.626   18.028 1.00 14.35 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 31.997 2.969   18.960 1.00 14.22 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.333 5.967   17.917 1.00 15.96 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.145 7.444   18.051 1.00 20.15 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.432 8.207   17.631 1.00 21.63 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 30.994 7.931   17.203 1.00 21.03 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.425 3.184   16.773 1.00 13.25 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 31.927 1.867   16.378 1.00 13.71 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.436 1.953   14.945 1.00 13.64 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.121 2.883   14.210 1.00 14.47 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 30.779 0.833   16.417 1.00 15.40 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.281 0.978   14.564 1.00 12.83 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 33.726 0.863   13.189 1.00 13.08 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.621 0.068   12.455 1.00 14.69 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.275 -1.076  12.824 1.00 16.15 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.064 0.086   13.150 1.00 13.70 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.507 -0.163  11.699 1.00 14.89 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.091 0.892   13.912 1.00 13.74 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.082 0.704   11.434 1.00 14.22 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.019 0.118   10.628 1.00 15.27 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.559 1.124   9.591  1.00 15.42 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 30.867 2.324   9.645  1.00 15.71 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 29.862 0.620   8.568  1.00 15.38 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.385 1.447   7.502  1.00 14.71 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.152 2.238   7.897  1.00 15.13 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.224 1.698   8.495  1.00 15.02 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.054 0.572   6.280  1.00 14.93 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.579 1.412   5.123  1.00 15.40 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.440 2.296   4.474  1.00 17.38 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.322 1.597   4.629  1.00 16.49 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.689 2.940   3.577  1.00 17.48 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.405 2.548   3.643  1.00 17.17 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.097 3.499   7.517  1.00 15.01 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 26.882 4.297   7.680  1.00 15.30 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 26.959 5.466   6.711  1.00 16.98 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 28.072 5.911   6.360  1.00 19.04 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.674 4.798   9.107  1.00 15.88 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.746 5.655   9.479  1.00 18.62 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.782 5.852   6.215  1.00 14.67 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.482 6.998   5.369  1.00 16.15 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.368 7.820   6.064  1.00 17.40 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.708 7.339   6.980  1.00 16.46 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 24.982 6.490   4.012  1.00 18.88 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.081 5.750   3.301  1.00 19.22 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.731 5.135   1.956  1.00 19.45 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 24.983 5.779   1.181  1.00 22.96 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.245 4.037   1.660  1.00 19.40 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.176 9.105   5.699  1.00 18.59 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.177 9.939   6.429  1.00 18.30 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.779 9.323   6.608  1.00 18.88 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.193 9.357   7.700  1.00 19.76 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 23.137 11.236  5.596  1.00 19.21 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.501 11.329  4.966  1.00 20.40 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 24.910 9.875   4.667  1.00 18.91 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.280 8.680   5.553  1.00 16.69 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 19.972 8.030   5.555  1.00 16.18 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.887 6.818   6.462  1.00 16.36 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.800 6.258   6.675  1.00 17.15 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.059 6.343   6.980  1.00 14.79 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.029 5.226   7.922  1.00 13.19 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.588 5.627   9.327  1.00 13.30 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.316 4.753   10.157 1.00 13.57 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.422 4.573   8.037  1.00 13.22 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.726 3.775   6.783  1.00 13.92 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.795 3.148   6.255  1.00 15.41 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 23.917 3.758   6.356  1.00 14.58 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.445 6.930   9.580  1.00 13.30 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 19.986 7.410   10.889 1.00 13.34 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.647 6.785   11.225 1.00 14.43 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.779 6.701   10.350 1.00 15.90 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 19.900 8.937   10.922 1.00 14.31 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.517 9.724   11.080 1.00 16.97 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.518 6.314   12.445 1.00 12.70 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.288 5.661   12.879 1.00 13.88 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.371 4.155   12.935 1.00 14.25 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.546 3.499   13.582 1.00 14.41 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.414 3.571   12.319 1.00 12.64 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.624 2.122   12.427 1.00 12.16 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 18.861 1.740   13.886 1.00 12.10 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.621 2.411   14.581 1.00 12.98 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.257 0.627   14.325 1.00 11.15 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.389 0.252   15.709 1.00 11.42 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 19.656 -0.547  15.994 1.00 10.62 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.011 -1.436  15.205 1.00 12.20 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.102 -0.506  16.156 1.00 13.49 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 15.967 0.491   16.380 1.00 15.47 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.292 -1.369  17.423 1.00 15.23 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.562 -0.288  16.601 1.00 16.98 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.274 -0.266  17.161 1.00 11.06 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.394 -1.047  17.723 1.00 11.37 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 20.760 -1.859  18.884 1.00 11.88 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.104 -1.235  19.737 1.00 12.39 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.489 -0.096  18.272 1.00 12.07 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 23.626 -0.765  19.091 1.00 14.12 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.464 -1.702  18.238 1.00 14.15 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.533 0.328   19.696 1.00 14.32 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 20.932 -3.198  18.882 1.00 11.85 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.402 -4.076  19.920 1.00 11.95 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.525 -4.890  20.505 1.00 12.76 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.464 -5.309  19.813 1.00 14.75 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.404 -5.084  19.302 1.00 15.68 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.076 -4.468  18.985 1.00 20.58 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.156 -5.496  18.283 1.00 24.71 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 15.835 -5.418  18.918 1.00 32.77 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 14.814 -4.713  18.458 1.00 37.80 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 14.911 -4.065  17.299 1.00 42.07 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 13.664 -4.688  19.126 1.00 41.10 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.343 -5.244  21.791 1.00 12.95 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.203 -6.262  22.404 1.00 13.92 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.283 -7.397  22.884 1.00 14.29 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.063 -7.374  22.632 1.00 14.42 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 22.973 -5.654  23.574 1.00 14.91 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 21.885 -5.124  24.945 1.00 13.69 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 21.823 -8.354  23.654 1.00 15.16 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 20.963 -9.458  24.133 1.00 15.67 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 19.849 -8.988  25.079 1.00 16.53 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 18.926 -9.770  25.369 1.00 18.46 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 21.820 -10.556 24.817 1.00 17.91 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.411 -10.084 26.151 1.00 23.34 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.473 -11.023 26.697 1.00 33.18 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 24.693 -10.775 26.588 1.00 35.30 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.023 -12.092 27.313 1.00 31.80 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 19.942 -7.762  25.615 1.00 14.70 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 18.980 -7.261  26.599 1.00 14.59 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 17.859 -6.410  26.005 1.00 14.66 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.876 -6.138  26.699 1.00 16.12 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 19.660 -6.447  27.725 1.00 15.18 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 20.784 -7.190  28.372 1.00 16.74 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.127 -6.871  28.150 1.00 16.91 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 20.726 -8.235  29.240 1.00 19.72 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 22.839 -7.758  28.852 1.00 19.28 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.041 -8.624  29.495 1.00 20.03 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.016 -5.992  24.746 1.00 13.28 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.018 -5.145  24.135 1.00 13.35 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 17.644 -4.041  23.300 1.00 13.09 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 18.819 -4.102  22.901 1.00 14.04 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 16.841 -3.017  23.047 1.00 12.50 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.306 -1.887  22.252 1.00 12.48 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.292 -1.028  23.049 1.00 12.05 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.002 -0.603  24.187 1.00 12.98 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.100 -1.029  21.797 1.00 12.46 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 16.572 0.234   21.090 1.00 12.63 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.201 -1.844  20.866 1.00 13.12 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.449 -0.735  22.452 1.00 12.29 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.490 0.097   23.058 1.00 12.83 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.433 1.564   22.571 1.00 13.03 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 20.602 2.486   23.382 1.00 13.85 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 21.865 -0.485  22.683 1.00 13.16 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.046 0.415   23.138 1.00 14.86 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.017 -1.908  23.199 1.00 13.07 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.177 1.776   21.283 1.00 12.33 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.147 3.130   20.735 1.00 13.06 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 19.843 3.134   19.251 1.00 12.20 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.446 2.098   18.693 1.00 11.96 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 19.994 4.321   18.631 1.00 12.59 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 19.725 4.441   17.193 1.00 13.20 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 20.891 5.102   16.492 1.00 12.43 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.545 5.983   17.062 1.00 12.18 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.435 5.232   16.852 1.00 13.69 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.400 6.562   17.621 1.00 14.23 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.217 4.373   17.166 1.00 15.67 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.132 7.401   17.161 1.00 16.67 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.114 4.748   15.200 1.00 11.63 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.178 5.431   14.440 1.00 11.11 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 21.905 6.939   14.402 1.00 12.24 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.762 7.337   14.177 1.00 12.10 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.242 4.885   13.003 1.00 11.08 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.235 5.691   12.139 1.00 12.47 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.625 3.387   13.010 1.00 13.25 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 22.930 7.756   14.635 1.00 13.00 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.752 9.197   14.634 1.00 13.32 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 23.855 9.921   13.838 1.00 15.54 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.636 11.032  13.381 1.00 15.94 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.777 9.686   16.084 1.00 14.06 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.696 11.097  16.205 1.00 16.15 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.075 9.309   13.741 1.00 14.76 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.194 9.990   13.044 1.00 16.25 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.012 8.911   12.330 1.00 16.53 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 26.740 7.728   12.487 1.00 15.61 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.168 10.700  14.097 1.00 20.80 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.004 9.720   14.752 1.00 23.46 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.515 11.585  15.063 1.00 22.25 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.061 9.306   11.616 1.00 17.66 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 29.023 8.355   11.093 1.00 20.21 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.988 9.032   10.148 1.00 22.21 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 30.074 10.258  10.108 1.00 22.57 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.621 8.222   9.328  1.00 23.63 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.481 8.722   8.263  1.00 25.27 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 32.768 7.958   8.236  1.00 24.89 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.223 7.530   9.287  1.00 25.64 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.381 7.809   7.068  1.00 24.15 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 34.682 7.177   6.884  1.00 23.74 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 34.889 5.864   7.626  1.00 21.35 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 35.972 5.650   8.202  1.00 22.10 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 35.761 8.194   7.262  1.00 28.18 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 35.703 9.401   6.370  1.00 36.68 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 35.489 9.263   5.165  1.00 39.65 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.840 10.608  6.938  1.00 38.35 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 33.927 4.944   7.532  1.00 18.35 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.059 3.662   8.194  1.00 16.88 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.689 3.695   9.666  1.00 16.24 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 33.912 2.696   10.340 1.00 17.55 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.046 4.797   10.137 1.00 14.95 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.564 4.873   11.518 1.00 13.94 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.028 4.963   11.521 1.00 13.75 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.422 5.485   10.583 1.00 14.78 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.109 6.124   12.229 1.00 14.95 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 34.628 6.077   12.493 1.00 17.39 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.110 7.487   12.931 1.00 19.26 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 34.938 5.063   13.665 1.00 17.16 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.429 4.534   12.631 1.00 12.35 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 28.981 4.674   12.813 1.00 11.96 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 28.791 5.088   14.284 1.00 12.47 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.430 4.511   15.180 1.00 13.09 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.168 3.401   12.439 1.00 13.98 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.702 2.147   13.136 1.00 14.54 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 26.676 3.631   12.709 1.00 14.72 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 27.971 6.123   14.510 1.00 12.03 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.704 6.588   15.871 1.00 12.82 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.260 6.399   16.274 1.00 13.08 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.369 6.645   15.462 1.00 13.15 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.020 5.970   17.527 1.00 12.13 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.656 5.656   17.981 1.00 12.23 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.293 6.554   19.189 1.00 12.37 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.074 6.707   20.123 1.00 12.51 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.584 4.181   18.447 1.00 11.83 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.106 3.172   17.440 1.00 12.14 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.284 2.684   16.448 1.00 12.36 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.418 2.696   17.521 1.00 13.63 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 24.767 1.757   15.516 1.00 12.36 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 26.904 1.750   16.623 1.00 14.00 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.084 1.295   15.598 1.00 13.53 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.076 7.100   19.146 1.00 11.43 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.569 7.858   20.278 1.00 11.77 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.065 6.796   21.280 1.00 12.19 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.128 6.046   20.938 1.00 13.26 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.413 8.750   19.800 1.00 13.38 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.622 6.779   22.496 1.00 12.19 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.205 5.834   23.519 1.00 13.17 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 20.828 6.205   24.016 1.00 13.57 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.511 7.404   24.158 1.00 14.11 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.171 5.901   24.707 1.00 14.12 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 22.900 4.877   25.803 1.00 18.14 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 22.665 3.704   25.474 1.00 16.88 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 22.828 5.278   26.993 1.00 22.42 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.005 5.177   24.380 1.00 13.03 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 18.716 5.427   25.044 1.00 12.87 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.593 4.692   26.382 1.00 14.08 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.543 4.779   27.039 1.00 14.98 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.487 5.112   24.172 1.00 13.99 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.488 5.976   22.888 1.00 13.77 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.411 3.616   23.840 1.00 14.15 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 19.643 3.933   26.791 1.00 13.46 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.542 3.078   27.983 1.00 13.56 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.394 3.803   29.268 1.00 16.63 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 18.956 3.207   30.260 1.00 17.55 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 20.736 2.103   28.074 1.00 13.01 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 20.782 1.144   26.890 1.00 14.73 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.048 0.340   26.987 1.00 14.88 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.195 1.165   26.665 1.00 13.71 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.449 0.705   26.589 1.00 15.18 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 24.720 -0.569  26.877 1.00 15.55 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.428 1.495   26.157 1.00 14.89 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 19.822 5.080   29.306 1.00 16.08 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 19.675 5.866   30.537 1.00 17.19 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.278 6.477   30.717 1.00 18.16 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.014 7.059   31.773 1.00 18.64 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 20.695 7.004   30.596 1.00 17.94 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.541 8.011   29.473 1.00 21.36 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.293 7.590   28.321 1.00 20.67 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 20.651 9.235   29.747 1.00 24.20 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.433 6.427   29.681 1.00 17.51 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.101 7.049   29.752 1.00 16.86 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.153 6.089   30.419 1.00 17.05 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.351 5.401   29.771 1.00 16.82 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.633 7.424   28.335 1.00 16.09 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.606 8.379   27.583 1.00 16.90 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.147 8.593   26.149 1.00 18.17 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 16.781 9.704   28.343 1.00 16.41 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.232 6.021   31.762 1.00 17.13 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.438 5.004   32.484 1.00 17.89 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 12.929 5.212   32.369 1.00 19.05 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.149 4.234   32.440 1.00 20.49 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 14.877 4.946   33.964 1.00 18.41 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.417 4.854   34.177 1.00 20.25 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 16.739 4.620   35.683 1.00 21.49 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.048 3.668   33.364 1.00 21.36 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.520 6.473   32.178 1.00 19.44 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.100 6.787   32.087 1.00 20.06 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.418 6.205   30.854 1.00 20.63 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.174  6.185   30.796 1.00 21.92 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 10.897 8.307   32.179 1.00 19.69 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 11.722 9.102   31.194 1.00 17.98 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 12.969 9.625   31.386 1.00 17.97 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.351 9.429   29.844 1.00 17.94 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.378 10.305  30.250 1.00 18.25 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.394 10.206  29.295 1.00 18.61 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.206 9.185   29.067 1.00 18.98 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.343 10.703  27.995 1.00 19.08 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.138 9.718   27.790 1.00 19.73 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.178 10.514  27.294 1.00 19.66 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.194 5.747   29.847 1.00 19.20 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 10.577 5.158   28.653 1.00 20.36 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 9.764  3.908   29.001 1.00 25.57 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 8.839  3.588   28.254 1.00 26.39 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 11.639 4.770   27.606 1.00 18.99 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.270 5.920   26.876 1.00 19.93 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.388 5.390   25.970 1.00 20.71 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.227 6.644   25.971 1.00 19.83 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.152 3.188   30.099 1.00 29.73 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.569  1.924   30.598 1.00 34.76 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 8.313  2.101   31.428 1.00 39.42 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 7.744  1.089   31.835 1.00 40.66 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.558 1.203   31.554 1.00 38.26 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.827 0.649   30.980 1.00 45.70 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 11.875 0.442   29.755 1.00 47.50 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.783 0.400   31.770 1.00 49.44 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 7.947  3.332   31.795 1.00 42.11 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 6.773  3.551   32.637 1.00 45.22 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 5.754  4.440   31.930 1.00 47.45 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 4.550  4.281   32.143 1.00 49.00 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 7.190  4.150   33.994 1.00 48.11 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 7.904  5.484   33.864 1.00 54.18 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 8.823  5.854   35.014 1.00 60.77 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 8.963  7.067   35.298 1.00 61.35 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 9.416  4.932   35.621 1.00 63.58 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.489 -24.817 23.969 1.00 22.29 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.604 -24.688 23.012 1.00 22.12 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.610 -25.828 21.975 1.00 21.35 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 19.938 -26.851 22.174 1.00 22.05 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 21.940 -24.695 23.755 1.00 24.83 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.110 -25.958 24.383 1.00 29.28 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.366 -25.641 20.881 1.00 19.04 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.524 -26.675 19.866 1.00 18.06 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.835 -26.079 18.503 1.00 17.32 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.476 -24.931 18.222 1.00 18.97 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.467 -26.862 17.629 1.00 17.28 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.793 -26.386 16.271 1.00 17.43 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.754 -27.533 15.266 1.00 17.05 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.832 -28.706 15.649 1.00 17.82 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.208 -25.776 16.270 1.00 18.78 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.673 -27.194 13.973 1.00 16.03 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.763 -28.139 12.870 1.00 14.93 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.129 -27.887 12.195 1.00 15.57 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.486 -26.753 11.941 1.00 15.47 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.647 -27.874 11.847 1.00 15.25 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.253 -27.901 12.536 1.00 16.42 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.766 -28.911 10.686 1.00 15.46 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.161 -27.291 11.637 1.00 18.68 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.892 -28.952 11.898 1.00 17.51 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.187 -28.849 11.260 1.00 18.02 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.106 -29.557 9.931  1.00 18.28 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 26.018 -30.781 9.905  1.00 19.17 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.266 -29.512 12.165 1.00 18.08 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.466 -28.737 13.459 1.00 17.97 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.283 -27.612 13.502 1.00 19.53 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.770 -29.077 14.612 1.00 19.95 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.448 -26.886 14.680 1.00 21.63 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.901 -28.337 15.784 1.00 21.43 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.746 -27.248 15.818 1.00 22.70 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.851 -26.513 16.984 1.00 24.55 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.106 -28.822 8.828  1.00 18.20 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 25.984 -29.413 7.501  1.00 19.31 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.046 -28.780 6.598  1.00 21.14 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.167 -27.555 6.558  1.00 21.61 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.527 -29.217 6.957  1.00 19.98 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.076 -27.766 7.041  1.00 21.15 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.418 -29.752 5.541  1.00 20.96 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 27.910 -29.596 5.974  1.00 22.09 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 28.975 -29.072 5.123  1.00 23.28 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 29.880 -28.142 5.913  1.00 23.57 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.215 -28.469 7.053  1.00 24.64 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.196 -26.949 5.383  1.00 23.38 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 30.980 -25.982 6.160  1.00 23.41 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.077 -24.910 6.798  1.00 20.75 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.491 -23.740 6.946  1.00 22.50 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.087 -25.347 5.334  1.00 27.19 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.173 -26.345 5.028  1.00 35.02 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 34.002 -26.676 5.890  1.00 38.14 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.173 -26.870 3.815  1.00 37.18 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 28.860 -25.318 7.228  1.00 18.85 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 27.927 -24.376 7.860  1.00 18.22 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.453 -24.865 9.217  1.00 17.01 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.317 -26.074 9.450  1.00 17.22 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.660 -24.271 6.998  1.00 18.86 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 26.913 -23.694 5.624  1.00 20.46 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.509 -22.448 5.473  1.00 22.01 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.544 -24.385 4.480  1.00 22.17 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 27.753 -21.911 4.212  1.00 23.93 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 26.764 -23.848 3.205  1.00 23.89 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.374 -22.611 3.081  1.00 25.96 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.593 -22.047 1.839  1.00 28.70 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.155 -23.897 10.099 1.00 16.02 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.566 -24.132 11.432 1.00 16.50 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.258 -23.311 11.461 1.00 15.11 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.306 -22.112 11.207 1.00 15.54 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.526 -23.674 12.547 1.00 17.49 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 26.900 -23.474 13.926 1.00 16.60 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 27.918 -23.226 15.059 1.00 15.63 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.491 -22.231 16.044 1.00 17.83 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.085 -22.516 17.282 1.00 22.38 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 27.016 -23.781 17.694 1.00 23.65 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.742 -21.534 18.123 1.00 20.36 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.104 -23.962 11.671 1.00 15.00 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.808 -23.289 11.730 1.00 14.20 ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.362 -23.208 13.183 1.00 14.98 ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.259 -24.239 13.854 1.00 15.19 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.730 -24.071 10.923 1.00 15.50 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.426 -23.235 10.809 1.00 15.03 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.240 -24.499 9.546  1.00 15.95 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.066 -21.996 13.670 1.00 14.09 ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.650 -21.822 15.059 1.00 13.63 ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.457 -20.868 15.119 1.00 13.15 ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.220 -20.105 14.158 1.00 13.93 ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 22.803 -21.206 15.919 1.00 15.85 ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 23.915 -22.214 16.120 1.00 19.59 ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.327 -19.899 15.319 1.00 14.96 ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.765 -20.816 16.286 1.00 12.25 ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.761 -19.770 16.489 1.00 12.41 ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.495 -18.422 16.468 1.00 13.67 ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.544 -18.284 17.133 1.00 13.96 ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.124 -19.902 17.863 1.00 12.19 ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.278 -21.157 18.018 1.00 14.07 ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.771 -22.213 18.452 1.00 14.86 ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 15.999 -21.055 17.634 1.00 13.05 ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 18.972 -17.451 15.715 1.00 12.49 ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.682 -16.162 15.615 1.00 11.95 ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 19.875 -15.514 17.021 1.00 13.94 ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 20.946 -14.949 17.309 1.00 14.80 ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 18.915 -15.240 14.692 1.00 12.63 ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.621 -13.900 14.349 1.00 13.80 ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.656 -13.026 13.538 1.00 14.17 ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.248 -11.772 13.012 1.00 13.75 ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.350 -10.651 13.702 1.00 15.50 ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.067 -10.630 14.998 1.00 15.94 ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 19.820 -9.546  13.122 1.00 15.27 ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 18.859 -15.691 17.906 1.00 12.73 ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 18.969 -15.102 19.245 1.00 13.38 ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 20.003 -15.799 20.130 1.00 14.57 ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.381 -15.224 21.159 1.00 15.34 ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.592 -14.992 19.957 1.00 14.28 ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.011 -16.295 20.455 1.00 14.38 ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.286 -17.137 19.618 1.00 14.78 ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.024 -16.821 21.707 1.00 15.83 ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 15.871 -18.161 20.389 1.00 14.77 ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.317 -18.037 21.653 1.00 16.17 ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.461 -16.997 19.761 1.00 14.07 ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.488 -17.690 20.556 1.00 15.27 ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 22.863 -17.645 19.877 1.00 16.70 ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.795 -18.242 20.400 1.00 17.35 ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 21.100 -19.162 20.842 1.00 15.05 ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.781 -19.305 21.632 1.00 15.66 ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.436 -20.796 21.846 1.00 15.96 ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.869 -18.541 23.017 1.00 17.49 ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 22.992 -16.951 18.715 1.00 15.13 ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.289 -16.869 18.025 1.00 15.89 ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.331 -16.214 18.897 1.00 16.80 ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.016 -15.256 19.594 1.00 17.17 ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.153 -16.071 16.728 1.00 16.23 ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.548 -16.771 18.898 1.00 16.70 ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.633 -16.257 19.731 1.00 16.96 ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.405 -15.135 19.011 1.00 18.07 ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.203 -14.906 17.814 1.00 17.84 ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.580 -17.437 20.042 1.00 18.49 ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.166 -17.873 18.813 1.00 19.78 ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 27.884 -18.572 20.739 1.00 19.32 ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.428 -14.518 19.691 1.00 18.46 ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.295 -13.555 19.014 1.00 19.10 ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 30.993 -14.231 17.807 1.00 18.15 ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.107 -13.630 16.739 1.00 18.89 ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.381 -13.054 20.006 1.00 22.13 ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 30.831 -12.281 21.169 1.00 28.27 ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.114 -11.104 20.980 1.00 31.56 ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 30.960 -12.500 22.502 1.00 30.94 ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 29.833 -10.646 22.192 1.00 32.27 ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.286 -11.469 23.142 1.00 32.77 ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.404 -15.504 17.965 1.00 18.44 ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.094 -16.199 16.853 1.00 19.00 ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.171 -16.434 15.670 1.00 19.12 ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.591 -16.337 14.506 1.00 19.21 ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.681 -17.518 17.344 1.00 20.52 ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.541 -18.227 16.324 1.00 27.39 ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.644 -17.767 15.981 1.00 28.69 ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.065 -19.366 15.827 1.00 29.43 ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 29.879 -16.752 15.952 1.00 18.50 ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 28.929 -16.923 14.838 1.00 18.04 ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 28.788 -15.618 14.038 1.00 18.36 ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 28.811 -15.642 12.816 1.00 18.50 ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.538 -17.306 15.361 1.00 16.94 ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.432 -18.728 15.864 1.00 17.97 ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.017 -19.640 15.215 1.00 18.37 ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.792 -18.934 16.937 1.00 16.87 ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.670 -14.475 14.726 1.00 18.20 ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.516 -13.194 14.036 1.00 18.67 ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 29.824 -12.802 13.308 1.00 20.34 ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 29.764 -12.173 12.255 1.00 21.81 ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.091 -12.116 15.048 1.00 18.82 ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.620 -12.109 15.312 1.00 17.22 ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 25.975 -12.623 16.398 1.00 18.03 ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.605 -11.564 14.452 1.00 16.60 ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.615 -12.430 16.275 1.00 18.23 ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.364 -11.782 15.085 1.00 16.57 ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 25.625 -10.934 13.200 1.00 16.82 ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.158 -11.347 14.524 1.00 17.00 ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.425 -10.521 12.636 1.00 17.87 ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.217 -10.724 13.307 1.00 17.13 ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 30.982 -13.189 13.855 1.00 19.55 ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.260 -12.870 13.204 1.00 20.98 ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.501 -13.750 11.947 1.00 22.10 ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.427 -13.459 11.171 1.00 24.03 ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.412 -13.071 14.195 1.00 20.39 ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 31.759 -14.871 11.804 1.00 19.66 ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 31.883 -15.778 10.656 1.00 19.42 ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.505 -15.914 9.972  1.00 20.21 ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.136 -16.975 9.511  1.00 19.42 ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.369 -17.150 11.137 1.00 20.80 ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 33.808 -17.089 11.609 1.00 25.95 ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 34.735 -17.029 10.785 1.00 26.22 ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.012 -17.028 12.942 1.00 26.12 ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 29.762 -14.812 9.908  1.00 20.64 ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.422 -14.776 9.369  1.00 19.66 ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.334 -15.128 7.890  1.00 20.41 ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.010 -14.511 7.060  1.00 22.12 ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 27.833 -13.379 9.627  1.00 20.00 ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.426 -13.132 9.114  1.00 20.51 ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.429 -14.037 9.849  1.00 20.22 ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.022 -11.670 9.308  1.00 20.86 ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.410 -16.041 7.545  1.00 19.20 ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.124 -16.380 6.154  1.00 18.86 ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 25.780 -15.737 5.775  1.00 20.26 ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 25.646 -15.112 4.708  1.00 21.82 ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.069 -17.921 5.951  1.00 20.16 ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.496 -18.288 4.574  1.00 21.28 ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.472 -18.527 6.136  1.00 20.27 ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 24.762 -15.922 6.640  1.00 17.84 ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.416 -15.445 6.372  1.00 17.26 ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.630 -15.384 7.668  1.00 16.66 ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 22.810 -16.236 8.550  1.00 16.93 ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 22.712 -16.411 5.381  1.00 18.11 ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.221 -16.225 5.197  1.00 18.93 ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.591 -15.367 4.340  1.00 21.46 ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.179 -16.973 5.849  1.00 17.83 ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.219 -15.513 4.449  1.00 21.83 ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 18.945 -16.512 5.348  1.00 19.30 ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.173 -18.005 6.790  1.00 17.99 ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 17.721 -17.041 5.773  1.00 19.11 ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 18.964 -18.537 7.191  1.00 18.46 ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.757 -18.064 6.679  1.00 17.69 ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 21.759 -14.389 7.811  1.00 16.62 ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 20.870 -14.329 8.962  1.00 17.17 ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.538 -13.754 8.529  1.00 16.19 ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.496 -12.923 7.591  1.00 16.40 ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.479 -13.559 10.144 1.00 17.82 ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 21.993 -12.162 9.808  1.00 18.05 ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 20.962 -11.054 9.722  1.00 20.55 ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.210 -10.064 8.988  1.00 20.83 ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 19.930 -11.136 10.422 1.00 17.33 ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.464 -14.133 9.226  1.00 14.37 ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.155 -13.577 8.947  1.00 14.49 ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.404 -13.455 10.273 1.00 14.52 ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.028 -14.466 10.877 1.00 14.18 ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.434 -14.469 7.922  1.00 16.23 ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.088 -13.960 7.448  1.00 20.73 ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.444 -13.238 8.193  1.00 24.60 ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.651 -14.364 6.331  1.00 21.48 ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.230 -12.219 10.744 1.00 15.43 ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.559 -11.952 11.999 0.50 15.51 ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.554 -11.962 12.009 0.50 15.13 ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.105 -12.443 11.965 1.00 16.07 ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.628 -12.963 12.970 1.00 16.74 ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.611 -10.456 12.306 0.50 18.15 ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.600 -10.473 12.364 0.50 16.75 ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 14.859 -10.148 13.460 0.50 22.96 ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.117 -9.693  11.282 0.50 20.10 ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.442 -12.330 10.792 1.00 15.42 ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.048 -12.791 10.720 1.00 15.84 ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 11.921 -14.282 10.887 1.00 15.46 ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 10.814 -14.724 11.209 1.00 17.41 ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.364 -12.343 9.423  1.00 19.42 ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 11.768 -13.110 8.295  1.00 24.43 ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 12.996 -15.043 10.668 1.00 13.36 ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 12.905 -16.508 10.832 1.00 12.75 ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.631 -16.994 12.115 1.00 13.15 ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.615 -18.193 12.405 1.00 12.78 ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.604 -17.207 9.640  1.00 13.52 ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 12.920 -16.946 8.312  1.00 13.57 ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.691 -17.567 7.146  1.00 14.29 ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.669 -19.025 7.225  1.00 14.50 ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.723 -19.831 6.170  1.00 15.22 ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 13.803 -19.325 4.930  1.00 15.81 ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.646 -21.149 6.334  1.00 14.80 ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.277 -16.092 12.867 1.00 13.82 ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.085 -16.477 14.025 1.00 13.27 ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.185 -17.481 13.629 1.00 12.39 ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.546 -18.359 14.438 1.00 12.66 ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.282 -17.022 15.225 1.00 13.96 ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.119 -17.347 16.475 1.00 13.84 ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 16.029 -16.525 16.832 1.00 14.37 ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 14.851 -18.419 17.133 1.00 13.03 ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 16.787 -17.290 12.431 1.00 12.73 ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 17.885 -18.154 11.996 1.00 12.98 ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.167 -17.387 11.708 1.00 13.54 ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.114 -16.274 11.197 1.00 13.36 ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.559 -18.932 10.729 1.00 13.26 ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.522 -20.039 10.867 1.00 14.55 ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.334 -20.737 9.492  1.00 14.88 ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 16.939 -21.075 11.937 1.00 15.81 ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.306 -18.011 12.001 1.00 12.98 ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.601 -17.474 11.623 1.00 13.45 ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.474 -18.674 11.205 1.00 12.95 ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.395 -19.762 11.822 1.00 13.48 ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.238 -16.689 12.779 1.00 14.23 ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.596 -16.021 12.446 1.00 14.72 ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 23.770 -14.692 13.198 1.00 14.27 ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 24.776 -16.995 12.778 1.00 15.32 ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.249 -18.501 10.129 1.00 13.41 ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.166 -19.517 9.635  1.00 13.74 ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.585 -18.910 9.636  1.00 14.74 ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 25.786 -17.809 9.107  1.00 15.40 ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 23.793 -19.979 8.204  1.00 14.68 ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 24.834 -20.976 7.673  1.00 16.05 ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.401 -20.631 8.226  1.00 14.67 ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.531 -19.615 10.262 1.00 15.87 ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 27.938 -19.174 10.276 1.00 15.90 ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 28.816 -20.245 9.590  1.00 17.44 ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.387 -21.389 9.382  1.00 17.45 ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.407 -18.937 11.705 1.00 16.62 ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.262 -20.108 12.503 1.00 18.52 ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.052 -19.847 9.217  1.00 17.78 ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 30.925 -20.819 8.543  1.00 20.15 ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 31.814 -21.551 9.540  1.00 22.86 ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.174 -21.010 10.603 1.00 23.47 ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 31.774 -20.131 7.485  1.00 21.87 ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.536 -19.119 8.100  1.00 25.68 ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.139 -22.805 9.201  1.00 24.41 ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 32.973 -23.667 10.052 1.00 26.94 ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.201 -24.134 9.244  1.00 30.42 ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.180 -24.141 8.006  1.00 30.72 ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.174 -24.929 10.485 1.00 27.75 ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 31.918 -25.742 9.333  1.00 29.21 ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 30.846 -24.605 11.173 1.00 27.59 ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.252 -24.545 9.945  1.00 32.88 ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.439 -25.107 9.298  1.00 35.68 ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.297 -26.638 9.164  1.00 37.26 ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.874 -27.224 8.249  1.00 39.16 ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.699 -24.716 10.079 1.00 38.50 ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.524 -25.081 11.448 1.00 40.92 ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 37.999 -23.220 9.993  1.00 39.14 ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.542 -27.289 10.063 1.00 36.49 ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.357 -28.743 10.010 1.00 36.83 ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.088 -29.115 9.251  1.00 37.06 ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.126 -28.348 9.243  1.00 37.15 ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.297 -29.314 11.416 1.00 37.13 ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.074 -30.292 8.633  1.00 36.48 ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 32.924 -30.753 7.871  1.00 36.86 ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.824 -31.239 8.804  1.00 35.02 ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 32.082 -31.974 9.763  1.00 35.89 ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.339 -31.871 6.897  1.00 40.50 ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.678 -31.759 5.520  1.00 48.15 ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 33.198 -30.559 4.762  1.00 56.00 ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 34.365 -30.147 4.911  1.00 59.11 ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 32.345 -29.969 3.929  1.00 56.63 ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.603 -30.813 8.497  1.00 31.97 ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.413 -31.182 9.242  1.00 30.88 ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.779 -32.412 8.645  1.00 29.90 ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.770 -32.588 7.423  1.00 30.52 ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.202 -33.223 9.505  1.00 28.14 ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.670 -34.522 9.155  1.00 29.10 ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.168 -34.610 8.956  1.00 26.09 ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.695 -35.698 8.582  1.00 27.24 ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.087 -35.504 10.240 1.00 34.12 ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 27.111 -35.348 11.774 1.00 49.62 ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.412 -33.603 9.399  1.00 21.52 ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.963 -33.672 9.401  1.00 19.47 ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.405 -33.621 7.994  1.00 19.98 ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.970 -32.977 7.092  1.00 21.73 ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.357 -32.517 10.225 1.00 20.20 ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.680 -32.605 11.714 1.00 25.03 ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 24.040 -33.720 12.184 1.00 27.82 ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.577 -31.555 12.422 1.00 24.61 ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.330 -34.351 7.788  1.00 18.68 ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.645 -34.358 6.505  1.00 18.88 ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.382 -33.527 6.659  1.00 17.70 ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.640 -33.763 7.595  1.00 18.51 ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.273 -35.816 6.130  1.00 23.00 ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.474 -36.520 5.766  1.00 24.30 ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.240 -35.896 4.984  1.00 25.07 ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.114 -32.588 5.742  1.00 16.18 ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.890 -31.787 5.816  1.00 15.67 ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.783 -32.487 5.040  1.00 15.54 ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 18.003 -32.963 3.902  1.00 15.65 ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.106 -30.390 5.194  1.00 16.69 ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.328 -29.698 5.795  1.00 18.65 ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 17.843 -29.502 5.352  1.00 15.33 ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.192 -29.479 7.337  1.00 21.27 ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.586 -32.569 5.618  1.00 15.03 ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.443 -33.166 4.936  1.00 14.84 ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 15.011 -32.262 3.765  1.00 14.01 ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.033 -31.029 3.896  1.00 14.27 ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.265 -33.283 5.915  1.00 15.54 ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.607 -32.879 2.616  1.00 13.35 ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.104 -32.117 1.453  1.00 13.91 ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.763 -32.782 1.174  1.00 13.80 ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.711 -33.797 0.452  1.00 15.45 ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.106 -32.217 0.285  1.00 14.76 ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.472 -31.633 0.592  1.00 15.83 ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.483 -30.140 0.979  1.00 15.57 ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 17.859 -29.692 1.237  1.00 18.02 ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.178 -28.572 1.879  1.00 19.40 ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.228 -27.767 2.337  1.00 15.69 ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.456 -28.252 2.080  1.00 19.62 ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.694 -32.245 1.759  1.00 13.92 ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.401 -32.919 1.793  1.00 13.96 ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.280  -32.023 2.296  1.00 14.90 ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.542  -30.912 2.757  1.00 15.19 ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.528 -34.133 2.704  1.00 14.06 ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.710 -33.681 4.478  1.00 14.47 ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 8.016  -32.573 2.285  1.00 14.98 ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.906  -31.849 2.894  1.00 16.32 ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.285  -32.664 4.033  1.00 16.31 ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.074  -32.544 4.301  1.00 16.76 ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.841  -31.487 1.843  1.00 19.65 ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.168  -32.669 1.214  1.00 25.83 ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.592  -33.838 1.489  1.00 26.10 ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.185  -32.451 0.477  1.00 30.59 ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.114  -33.451 4.758  1.00 13.83 ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.631  -34.190 5.947  1.00 13.41 ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 5.949  -33.256 6.918  1.00 13.96 ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.370  -32.092 7.104  1.00 13.95 ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.780  -34.891 6.664  1.00 12.35 ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.346  -36.370 5.798  1.00 16.15 ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.948  -33.816 7.584  1.00 12.59 ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.268  -33.152 8.689  1.00 12.18 ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.249  -34.056 9.931  1.00 12.91 ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.448  -33.811 10.843 1.00 13.02 ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.820  -32.766 8.362  1.00 13.09 ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.785  -31.548 7.451  1.00 15.34 ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.372  -31.104 7.159  1.00 17.77 ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.886  -31.263 6.020  1.00 19.18 ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.657  -30.593 8.200  1.00 14.55 ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.104  -35.118 9.983  1.00 12.28 ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.304  -35.880 11.207 1.00 13.94 ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.818  -36.014 11.404 1.00 13.73 ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.581  -36.086 10.426 1.00 14.84 ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.624  -37.226 11.257 1.00 18.98 ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.254  -38.083 10.299 1.00 21.65 ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.124  -37.144 10.999 1.00 19.99 ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.226  -36.043 12.677 1.00 12.93 ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.647  -36.151 12.976 1.00 12.88 ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.875  -36.284 14.473 1.00 12.12 ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.937  -36.554 15.200 1.00 13.62 ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.136 -36.200 14.908 1.00 11.57 ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.493 -36.370 16.332 1.00 12.01 ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.397 -35.178 16.693 1.00 11.69 ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.342 -34.907 15.976 1.00 11.94 ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.244 -37.721 16.562 1.00 13.18 ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.709 -37.865 18.025 1.00 13.18 ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.356 -38.925 16.171 1.00 14.11 ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.132 -34.536 17.871 1.00 10.85 ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 12.019 -33.436 18.299 1.00 11.27 ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.602 -33.726 19.683 1.00 12.45 ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 12.033 -34.487 20.470 1.00 12.53 ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.344 -32.030 18.328 1.00 11.52 ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.404 -31.806 19.500 1.00 10.90 ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.117  -32.341 19.493 1.00 13.05 ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.749 -30.947 20.547 1.00 11.96 ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.216  -32.092 20.529 1.00 15.24 ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 9.845  -30.678 21.594 1.00 13.56 ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.577  -31.256 21.578 1.00 14.57 ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.652  -31.014 22.597 1.00 15.07 ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.768 -33.145 19.949 1.00 13.14 ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.411 -33.283 21.234 1.00 13.13 ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 13.989 -32.128 22.131 1.00 13.02 ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.124 -30.960 21.759 1.00 12.78 ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 15.964 -33.360 21.110 1.00 13.54 ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.599 -33.527 22.477 1.00 14.73 ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.395 -34.680 23.220 1.00 15.80 ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.357 -32.511 23.044 1.00 15.92 ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 16.926 -34.824 24.504 1.00 16.75 ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 17.871 -32.636 24.330 1.00 16.54 ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.680 -33.804 25.038 1.00 18.21 ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.211 -33.949 26.312 1.00 20.93 ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.530 -32.489 23.357 1.00 13.10 ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.074 -31.515 24.347 1.00 12.95 ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 14.030 -31.555 25.583 1.00 13.86 ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 13.924 -32.458 26.429 1.00 15.08 ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.647 -31.852 24.742 1.00 12.91 ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 10.985 -30.793 26.063 1.00 15.58 ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 14.974 -30.590 25.660 1.00 13.47 ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 15.933 -30.627 26.744 1.00 14.85 ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.322 -30.483 28.119 1.00 15.60 ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 15.825 -31.143 29.040 1.00 16.40 ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.029 -29.597 26.528 1.00 19.32 ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.503 -28.292 26.559 1.00 27.17 ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.206 -29.742 28.249 1.00 15.49 ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.543 -29.588 29.569 1.00 15.67 ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 12.851 -30.867 30.056 1.00 16.83 ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.377 -30.902 31.190 1.00 16.94 ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.555 -28.425 29.560 1.00 17.18 ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.478 -28.658 28.669 1.00 16.91 ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 12.802 -31.923 29.243 1.00 15.51 ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.277 -33.216 29.664 1.00 15.10 ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.343 -34.327 29.435 1.00 15.75 ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.050 -35.500 29.694 1.00 16.90 ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.007 -33.544 28.858 1.00 15.91 ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 9.830  -32.617 29.152 1.00 17.55 ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.217  -32.946 30.521 1.00 18.37 ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.101  -32.057 30.856 1.00 20.96 ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.224  -30.897 31.493 1.00 24.36 ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.429  -30.442 31.844 1.00 23.31 ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.147  -30.170 31.774 1.00 25.89 ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.559 -33.979 28.895 1.00 16.26 ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.577 -34.995 28.529 1.00 16.50 ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 14.973 -36.112 27.683 1.00 18.08 ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.210 -37.294 27.940 1.00 19.52 ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.315 -35.562 29.765 1.00 18.90 ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.264 -34.558 30.405 1.00 22.42 ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.035 -35.213 31.537 1.00 30.76 ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 18.639 -34.204 32.413 1.00 37.24 ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 18.428 -34.122 33.723 1.00 41.67 ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 17.623 -34.985 34.328 1.00 42.53 ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 19.011 -33.159 34.440 1.00 41.62 ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.062 -35.737 26.744 1.00 16.73 ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.334 -36.761 25.989 1.00 17.19 ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.064 -36.315 24.580 1.00 14.89 ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 12.966 -35.115 24.336 1.00 15.01 ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.903 -36.935 26.604 1.00 21.68 ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.768 -37.937 27.727 1.00 33.36 ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.280 -38.189 27.977 1.00 40.18 ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 10.015 -39.398 28.859 1.00 46.48 ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.049 -39.050 30.308 1.00 48.65 ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.904 -37.271 23.678 1.00 14.43 ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.406 -37.013 22.330 1.00 12.62 ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.910 -37.282 22.288 1.00 15.05 ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.426 -38.241 22.940 1.00 18.60 ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.065 -37.947 21.316 1.00 12.81 ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.547 -37.747 21.259 1.00 14.93 ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.164 -36.977 20.276 1.00 16.91 ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.504 -38.283 22.051 1.00 15.65 ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.476 -37.097 20.493 1.00 15.88 ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.716 -37.801 21.575 1.00 18.60 ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.175 -36.463 21.535 1.00 13.11 ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.730  -36.650 21.391 1.00 13.32 ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.360  -36.721 19.919 1.00 12.67 ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.773  -35.852 19.125 1.00 12.76 ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.972  -35.438 21.957 1.00 14.44 ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.031  -35.343 23.462 1.00 15.71 ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.293  -36.202 24.256 1.00 16.59 ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.743  -34.322 24.092 1.00 15.97 ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.330  -36.106 25.648 1.00 17.77 ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 8.794  -34.224 25.472 1.00 16.75 ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.048  -35.090 26.245 1.00 18.52 ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.078  -34.956 27.623 1.00 22.25 ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.531  -37.725 19.546 1.00 12.60 ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 7.011  -37.763 18.170 1.00 12.86 ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.832  -36.783 18.061 1.00 14.20 ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.990  -36.771 18.966 1.00 14.64 ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.525  -39.223 18.016 1.00 13.26 ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.253  -39.672 19.399 1.00 13.96 ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 7.024  -38.840 20.393 1.00 12.81 ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.757  -35.994 16.978 1.00 12.69 ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.654  -35.025 16.840 1.00 13.44 ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.210  -34.908 15.383 1.00 13.58 ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 5.003  -35.115 14.443 1.00 14.95 ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.055  -33.607 17.338 1.00 14.97 ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.164  -33.575 18.870 1.00 16.77 ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.345  -33.131 16.677 1.00 14.78 ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 2.943  -34.456 15.207 1.00 12.78 ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.496  -33.927 13.942 1.00 13.09 ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.798  -32.398 13.980 1.00 12.17 ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.773  -31.782 15.063 1.00 12.97 ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 0.974  -34.089 13.807 1.00 16.38 ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.705  -35.472 13.702 1.00 23.96 ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.160  -31.788 12.827 1.00 11.58 ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.456  -30.355 12.814 1.00 12.40 ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 2.876  -29.724 11.542 1.00 12.18 ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.563  -30.410 10.557 1.00 13.56 ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 4.946  -30.077 13.025 1.00 12.56 ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 5.858  -30.781 12.051 1.00 12.31 ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.382  -32.018 12.340 1.00 11.61 ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.269  -30.147 10.887 1.00 12.57 ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.258  -32.662 11.431 1.00 12.21 ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.149  -30.760 10.002 1.00 13.32 ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.651  -32.015 10.295 1.00 12.31 ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.643  -28.416 11.608 1.00 11.51 ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 1.985  -27.705 10.517 1.00 13.23 ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 2.915  -27.408 9.337  1.00 14.67 ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.096  -27.757 9.363  1.00 15.62 ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.360  -26.418 11.064 1.00 14.28 ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.353  -25.463 11.424 1.00 15.58 ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.393  -26.750 8.295  1.00 14.78 ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.232  -26.324 7.177  1.00 15.80 ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 3.912  -25.006 7.581  1.00 16.34 ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.320  -24.199 8.303  1.00 18.40 ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.360  -26.074 5.940  1.00 19.29 ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.690  -27.352 5.476  1.00 24.01 ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 0.949  -27.152 4.151  1.00 31.08 ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 0.037  -28.316 3.838  1.00 38.60 ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? -0.930 -27.961 2.761  1.00 41.73 ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.077  -24.685 7.008  1.00 15.80 ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 5.757  -23.420 7.384  1.00 16.47 ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 4.894  -22.212 7.105  1.00 18.16 ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.303  -22.103 6.014  1.00 19.25 ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.026  -23.392 6.511  1.00 17.44 ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.264  -24.867 6.165  1.00 18.44 ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 5.897  -25.509 6.093  1.00 16.31 ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 4.776  -21.324 8.093  1.00 17.68 ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 3.891  -20.166 7.899  1.00 19.69 ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.272  -18.998 8.794  1.00 18.83 ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.214  -19.089 9.584  1.00 17.37 ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.449  -20.593 8.163  1.00 24.99 ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.208  -20.743 9.554  1.00 30.00 ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.542  -17.883 8.651  1.00 18.52 ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 3.774  -16.668 9.428  1.00 20.33 ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 2.940  -16.791 10.698 1.00 21.66 ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.697  -16.893 10.611 1.00 23.36 ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.202  -15.493 8.644  1.00 22.33 ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.116  -14.756 7.712  1.00 27.00 ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.300  -13.703 6.931  1.00 29.45 ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.223  -14.057 8.485  1.00 28.36 ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.589  -16.756 11.875 1.00 19.89 ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 2.905  -16.890 13.167 1.00 21.01 ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.274  -15.763 14.115 1.00 20.69 ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.445  -15.424 14.208 1.00 20.05 ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.194  -18.281 13.757 1.00 23.27 ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.475  -19.360 12.904 1.00 26.81 ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.830  -18.373 15.253 1.00 24.18 ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 2.982  -20.611 13.027 1.00 31.14 ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.286  -15.130 14.783 1.00 20.80 ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.575  -14.056 15.726 1.00 22.55 ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.309  -14.553 16.981 1.00 22.46 ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 2.911  -15.552 17.588 1.00 24.09 ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.262  -13.334 16.155 1.00 24.53 ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.445  -12.204 17.148 1.00 26.26 ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.308  -12.425 18.512 1.00 28.22 ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 1.812  -10.945 16.723 1.00 27.49 ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.483  -11.380 19.422 1.00 29.11 ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 1.984  -9.896  17.636 1.00 29.02 ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 1.848  -10.135 18.975 1.00 28.70 ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.355  -13.806 17.369 1.00 22.44 ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.175  -14.044 18.560 1.00 21.72 ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.272  -12.738 19.356 1.00 22.31 ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.664  -11.714 18.806 1.00 21.98 ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.596  -14.501 18.125 1.00 20.74 ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.456  -14.770 19.351 1.00 20.78 ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.516  -15.764 17.251 1.00 20.24 ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 4.999  -12.788 20.666 1.00 23.18 ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.072  -11.604 21.514 1.00 24.43 ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.494  -11.048 21.629 1.00 22.87 ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.459  -11.757 21.367 1.00 21.68 ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.520  -11.914 22.913 1.00 29.94 ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.046  -12.282 22.897 1.00 39.25 ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.194  -11.661 23.984 1.00 51.00 ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 0.994  -12.012 24.055 1.00 55.54 ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.711  -10.808 24.742 1.00 54.51 ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.630  -9.779  22.040 1.00 21.87 ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 7.937  -9.165  22.206 1.00 21.82 ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.742  -9.899  23.262 1.00 20.99 ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.196  -10.478 24.216 1.00 21.66 ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.792  -7.696  22.620 1.00 23.17 ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 10.054 -9.859  23.102 1.00 20.17 ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 10.960 -10.440 24.071 1.00 19.85 ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.191 -9.510  24.142 1.00 21.32 ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.226 -8.456  23.458 1.00 21.85 ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.385 -11.839 23.634 1.00 20.04 ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.180 -11.761 22.463 1.00 18.55 ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.191 -9.881  24.939 1.00 22.05 ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.412 -9.063  25.008 1.00 23.86 ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.168 -9.062  23.673 1.00 23.89 ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 15.881 -8.086  23.369 1.00 23.70 ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.319 -9.540  26.152 1.00 28.72 ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 14.647 -9.461  27.516 1.00 37.30 ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 14.122 -10.802 28.005 1.00 50.17 ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 14.170 -11.045 29.234 1.00 53.90 ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 13.669 -11.613 27.157 1.00 51.54 ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 14.983 -10.113 22.851 1.00 22.54 ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.678 -10.185 21.575 1.00 21.91 ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 14.916 -9.649  20.361 1.00 21.51 ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.553 -9.249  19.374 1.00 23.98 ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 16.101 -11.630 21.295 1.00 21.54 ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 17.195 -12.144 22.196 1.00 23.37 ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 18.539 -12.032 21.835 1.00 23.49 ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 16.894 -12.847 23.349 1.00 25.05 ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 19.543 -12.577 22.623 1.00 25.13 ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 17.893 -13.371 24.161 1.00 26.49 ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 19.217 -13.242 23.789 1.00 26.88 ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 20.198 -13.775 24.588 1.00 30.88 ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.584 -9.614  20.403 1.00 19.95 ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 12.796 -9.216  19.247 1.00 20.67 ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.612 -8.386  19.635 1.00 23.00 ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 10.967 -8.659  20.643 1.00 23.14 ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.211 -10.454 18.518 1.00 19.88 ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.221 -11.383 17.928 1.00 18.57 ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.392 -12.660 18.435 1.00 19.02 ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 13.995 -11.001 16.840 1.00 17.85 ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.274 -13.552 17.855 1.00 18.25 ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 14.905 -11.870 16.276 1.00 16.72 ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 15.041 -13.147 16.790 1.00 17.46 ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 15.986 -13.973 16.267 1.00 16.18 ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 11.209 -7.448  18.767 1.00 24.16 ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 9.936  -6.786  18.988 1.00 24.38 ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 8.781  -7.771  18.739 1.00 24.24 ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 8.966  -8.821  18.102 1.00 23.45 ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 9.933  -5.677  17.906 1.00 25.44 ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 10.749 -6.275  16.802 1.00 26.14 ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 11.827 -7.067  17.473 1.00 24.74 ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.555  -7.408  19.106 1.00 24.66 ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.355  -8.203  18.784 1.00 24.58 ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.259  -8.233  17.235 1.00 24.49 ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.521  -7.199  16.599 1.00 25.28 ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 5.102  -7.538  19.360 1.00 25.61 ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.104  -9.436  16.641 1.00 23.05 ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.188  -9.537  15.184 1.00 22.52 ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.629  -10.859 14.702 1.00 23.54 ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.322  -11.742 15.510 1.00 24.48 ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.688  -9.459  14.778 1.00 21.85 ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.463  -10.778 15.115 1.00 20.67 ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 9.945  -10.569 15.317 1.00 21.58 ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 10.774 -11.712 14.893 1.00 20.98 ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 10.866 -12.882 15.523 1.00 23.36 ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.699 -13.814 15.076 1.00 20.24 ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.083 -13.151 16.574 1.00 22.95 ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.529  -11.005 13.380 1.00 23.84 ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.182  -12.289 12.798 1.00 24.26 ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.508  -12.963 12.456 1.00 20.69 ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.352  -12.370 11.745 1.00 20.77 ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.436  -12.093 11.490 1.00 27.46 ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.069  -11.508 11.717 1.00 32.80 ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 1.986  -12.320 12.003 1.00 35.83 ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.872  -10.135 11.716 1.00 36.13 ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.725  -11.784 12.236 1.00 38.32 ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.618  -9.587  11.952 1.00 38.14 ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.551  -10.416 12.225 1.00 40.20 ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.692 -9.871  12.452 1.00 44.22 ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 6.695  -14.167 12.971 1.00 17.19 ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 7.885  -14.927 12.610 1.00 15.93 ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.477  -15.805 11.424 1.00 15.74 ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.417  -16.453 11.453 1.00 17.20 ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.364  -15.759 13.801 1.00 15.97 ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.548  -16.650 13.396 1.00 17.38 ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.320 -17.179 14.590 1.00 16.57 ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.578 -16.435 15.537 1.00 17.95 ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 10.771 -18.442 14.484 1.00 14.82 ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.295  -15.806 10.368 1.00 14.80 ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.001  -16.566 9.163  1.00 14.49 ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.648  -17.957 9.178  1.00 15.11 ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.553  -18.225 9.988  1.00 14.32 ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.474  -15.785 7.928  1.00 16.30 ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 9.885  -15.591 7.987  1.00 18.27 ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.167  -18.851 8.249  1.00 13.62 ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 8.739  -20.198 8.072  1.00 14.03 ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.673  -20.997 9.384  1.00 14.14 ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.540  -21.838 9.644  1.00 14.76 ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.183 -20.122 7.521  1.00 14.77 ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.273 -19.438 6.175  1.00 15.13 ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.210 -20.173 4.992  1.00 18.39 ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.329 -18.115 5.856  1.00 16.44 ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.287 -19.277 3.999  1.00 18.94 ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.380 -18.033 4.465  1.00 19.02 ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.615  -20.756 10.194 1.00 14.84 ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.474  -21.430 11.489 1.00 14.21 ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.427  -22.562 11.372 1.00 14.26 ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.389  -22.372 10.739 1.00 14.60 ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.026  -20.394 12.564 1.00 15.36 ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.040  -20.821 14.019 1.00 18.20 ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.492  -21.072 14.477 1.00 16.88 ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.492  -19.714 14.905 1.00 21.89 ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.664  -23.703 12.034 1.00 13.81 ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.721  -24.832 12.054 1.00 13.18 ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.343  -25.115 13.489 1.00 13.28 ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.239  -25.091 14.343 1.00 14.47 ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.439  -26.067 11.512 1.00 13.93 ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.828  -25.820 10.098 1.00 18.23 ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 7.842  -27.092 9.422  1.00 18.92 ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.382  -26.919 10.418 1.00 17.45 ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.044  -25.269 13.779 1.00 12.97 ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.625  -25.534 15.155 1.00 13.00 ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.217  -26.981 15.357 1.00 12.59 ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.747  -27.649 14.442 1.00 12.13 ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.408  -24.664 15.569 1.00 14.58 ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.585  -23.184 15.478 1.00 16.56 ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.310  -22.425 15.992 1.00 18.89 ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 3.828  -22.717 16.271 1.00 16.51 ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.467  -27.457 16.574 1.00 11.68 ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.003  -28.790 17.004 1.00 12.30 ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.457  -28.654 18.441 1.00 12.34 ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 2.803  -27.702 19.165 1.00 12.76 ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.162  -29.793 17.034 1.00 12.69 ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.613  -29.600 18.855 1.00 12.78 ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.156  -29.682 20.227 1.00 13.57 ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.235  -30.447 20.991 1.00 14.02 ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.435  -31.632 20.754 1.00 13.93 ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? -0.209 -30.380 20.291 1.00 15.01 ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.664 -30.553 21.755 1.00 15.35 ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.232 -29.572 19.491 1.00 15.19 ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 2.916  -29.751 21.883 1.00 15.57 ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 3.969  -30.382 22.671 1.00 16.73 ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.599  -29.416 23.648 1.00 16.89 ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.398  -28.190 23.576 1.00 17.31 ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.376  -29.964 24.587 1.00 15.81 ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.014  -29.162 25.602 1.00 16.27 ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.273  -28.478 25.125 1.00 15.85 ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.067  -29.073 24.400 1.00 15.14 ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.420  -30.073 26.774 1.00 16.73 ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.051  -29.303 27.890 1.00 17.08 ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.323  -28.321 28.596 1.00 18.44 ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.366  -29.219 28.264 1.00 18.27 ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.194  -27.771 29.432 1.00 19.85 ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.436  -28.270 29.265 1.00 20.37 ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.470  -27.253 25.595 1.00 15.44 ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 8.711  -26.542 25.399 1.00 15.98 ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 8.812  -25.411 26.411 1.00 16.71 ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 7.809  -24.932 26.951 1.00 17.45 ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 8.868  -26.044 23.962 1.00 18.55 ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 7.892  -25.076 23.642 1.00 19.77 ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.069 -24.996 26.654 1.00 16.80 ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.493 -23.879 27.513 1.00 18.06 ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.591 -23.092 26.783 1.00 17.78 ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.155 -23.584 25.820 1.00 17.58 ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.031 -24.458 28.821 1.00 20.91 ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 9.936  -25.178 29.563 1.00 24.82 ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.340 -25.803 30.882 1.00 28.63 ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 11.188 -25.217 31.589 1.00 33.40 ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 9.792  -26.880 31.209 1.00 27.42 ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 11.914 -21.848 27.196 1.00 17.72 ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 12.900 -21.060 26.423 1.00 17.66 ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.234 -21.758 26.125 1.00 16.85 ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 14.740 -21.706 24.986 1.00 18.51 ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.070 -19.799 27.265 1.00 19.01 ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 11.693 -19.608 27.927 1.00 20.37 ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.293 -21.049 28.286 1.00 18.96 ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 14.759 -22.481 27.123 1.00 16.46 ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.017 -23.198 26.982 1.00 16.06 ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 15.981 -24.374 26.033 1.00 15.78 ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.029 -24.951 25.694 1.00 16.31 ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 14.748 -24.750 25.601 1.00 13.92 ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.617 -25.816 24.606 1.00 13.87 ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 14.959 -25.363 23.186 1.00 13.12 ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.095 -26.212 22.323 1.00 13.72 ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.174 -26.391 24.599 1.00 14.40 ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 12.935 -27.202 25.862 1.00 17.99 ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 13.887 -27.868 26.321 1.00 17.08 ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 11.790 -27.173 26.387 1.00 17.01 ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.095 -24.040 22.958 1.00 12.67 ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.457 -23.546 21.618 1.00 12.75 ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.746 -24.205 21.133 1.00 13.53 ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.680 -24.334 21.922 1.00 14.34 ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.601 -22.033 21.616 1.00 14.54 ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.004 -21.172 21.692 1.00 16.99 ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.754 -24.616 19.882 1.00 13.73 ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 17.892 -25.312 19.302 1.00 13.73 ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.744 -26.820 19.232 1.00 15.04 ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.484 -27.495 18.498 1.00 15.62 ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.743 -27.361 19.946 1.00 13.49 ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.462 -28.789 19.840 1.00 12.28 ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.041 -29.137 18.407 1.00 12.90 ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.280 -28.398 17.787 1.00 13.55 ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.580 -30.243 17.862 1.00 12.69 ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.323 -30.575 16.482 1.00 13.66 ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.023 -31.321 16.308 1.00 11.92 ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.722 -32.237 17.109 1.00 13.11 ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.555 -31.353 15.906 1.00 16.39 ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.725 -30.361 15.627 1.00 19.22 ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.228 -32.124 14.597 1.00 18.81 ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.061 -31.175 15.222 1.00 22.97 ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.302 -31.023 15.198 1.00 11.54 ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.115 -31.771 14.722 1.00 11.78 ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.626 -32.556 13.499 1.00 12.42 ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.213 -31.942 12.602 1.00 12.01 ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 11.993 -30.781 14.309 1.00 11.96 ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.761 -31.385 13.585 1.00 12.62 ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 9.995  -32.352 14.515 1.00 12.64 ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.839  -30.265 13.091 1.00 12.23 ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.445 -33.891 13.502 1.00 12.68 ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.862 -34.760 12.398 1.00 12.66 ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.663 -35.532 11.871 1.00 13.69 ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.794 -35.968 12.620 1.00 14.71 ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.878 -35.813 12.909 1.00 15.93 ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.234 -35.232 13.144 1.00 21.60 ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.195 -36.273 13.736 1.00 26.90 ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 18.445 -36.250 12.972 1.00 38.38 ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 19.525 -35.566 13.325 1.00 44.94 ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.548 -34.891 14.473 1.00 46.99 ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 20.601 -35.567 12.548 1.00 46.68 ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.726 -35.859 10.590 1.00 13.68 ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.774 -36.817 9.996  1.00 15.91 ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.600 -37.965 9.395  1.00 16.61 ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.822 -37.995 9.545  1.00 14.71 ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.917 -36.132 8.935  1.00 15.64 ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.886 -35.557 7.497  1.00 13.90 ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.945 -38.867 8.640  1.00 18.45 ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.680 -39.979 8.035  1.00 21.10 ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.717 -39.504 7.001  1.00 20.34 ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.590 -40.276 6.617  1.00 22.95 ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.702 -40.978 7.386  1.00 25.09 ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.988 -40.402 6.165  1.00 28.72 ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.883  -41.296 5.650  1.00 38.19 ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.691  -41.029 5.854  1.00 41.17 ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.260 -42.354 4.950  1.00 39.18 ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.640 -38.245 6.536  1.00 16.79 ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.528 -37.725 5.492  1.00 17.57 ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.710 -36.961 6.033  1.00 18.19 ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.599 -36.640 5.259  1.00 20.81 ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.773 -36.838 4.489  1.00 17.27 ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.569 -37.516 3.906  1.00 17.42 ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.271 -37.165 4.248  1.00 17.05 ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.525 -38.520 2.987  1.00 19.69 ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.473 -37.995 3.575  1.00 20.44 ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.175 -38.831 2.802  1.00 21.89 ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.696 -36.607 7.332  1.00 16.58 ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.788 -35.842 7.907  1.00 15.67 ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.290 -34.717 8.807  1.00 14.35 ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.172 -34.763 9.331  1.00 14.77 ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.128 -33.707 8.990  1.00 13.57 ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.775 -32.582 9.844  1.00 13.54 ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.753 -31.671 9.173  1.00 13.00 ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 15.950 -31.223 8.021  1.00 13.86 ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.055 -31.787 10.170 1.00 14.94 ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.696 -30.554 10.961 1.00 14.30 ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 19.050 -32.650 10.955 1.00 15.68 ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.659 -31.349 9.883  1.00 12.60 ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.583 -30.485 9.367  1.00 12.15 ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.722 -29.047 9.865  1.00 12.59 ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.519 -28.115 9.083  1.00 13.11 ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.223 -31.034 9.864  1.00 12.72 ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.060 -30.096 9.520  1.00 14.17 ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 12.014 -32.439 9.332  1.00 13.17 ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.129 -28.872 11.132 1.00 11.42 ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.234 -27.527 11.691 1.00 12.45 ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.668 -27.581 13.142 1.00 11.95 ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.075 -28.637 13.642 1.00 12.15 ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.600 -26.407 13.812 1.00 12.37 ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.007 -26.322 15.221 1.00 12.58 ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 13.941 -25.634 16.037 1.00 12.51 ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.295 -24.696 15.568 1.00 13.02 ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.341 -25.580 15.434 1.00 14.93 ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.346 -24.245 14.696 1.00 15.76 ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.524 -26.485 15.001 1.00 16.59 ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.730 -23.468 14.992 1.00 18.43 ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.822 -26.022 17.329 1.00 10.76 ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 12.856 -25.325 18.213 1.00 11.56 ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.209 -23.821 18.273 1.00 11.75 ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.382 -23.487 18.428 1.00 12.08 ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 12.911 -25.911 19.629 1.00 11.39 ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.051 -25.101 20.601 1.00 12.65 ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.490 -27.393 19.619 1.00 13.35 ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.196 -22.953 18.138 1.00 12.00 ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.433 -21.520 18.121 1.00 11.11 ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.462 -20.769 19.027 1.00 13.70 ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 11.803 -19.699 19.534 1.00 13.21 ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.313 -21.003 16.681 1.00 11.66 ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.433 -19.585 16.621 1.00 13.50 ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.239 -21.276 19.222 1.00 13.10 ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.262  -20.573 20.090 1.00 15.21 ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.347  -21.593 20.761 1.00 14.31 ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.409  -22.786 20.424 1.00 13.83 ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.431  -19.590 19.233 1.00 19.39 ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.749  -18.682 20.167 1.00 21.12 ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 7.418  -20.348 18.376 1.00 21.00 ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.557  -21.145 21.718 1.00 15.65 ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.577  -22.039 22.323 1.00 17.74 ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 5.704  -21.282 23.286 1.00 18.51 ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 5.964  -20.122 23.605 1.00 18.73 ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 4.689  -21.969 23.785 1.00 19.15 ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 3.772  -21.354 24.737 1.00 19.65 ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.424  -22.028 24.626 1.00 20.35 ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.091  -22.538 23.559 1.00 19.18 ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.643  -22.012 25.717 1.00 21.75 ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.285  -22.562 25.733 1.00 23.07 ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.208  -23.996 25.231 1.00 22.49 ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.790 -24.370 24.600 1.00 23.59 ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.644 -21.677 24.915 1.00 26.46 ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.823 -20.301 25.472 1.00 33.69 ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.727 -20.079 26.672 1.00 36.43 ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -1.107 -19.369 24.594 1.00 35.72 ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.243  -24.793 25.493 1.00 19.62 ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.215  -26.189 25.071 1.00 18.25 ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.512  -26.418 23.599 1.00 17.02 ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.233  -27.498 23.084 1.00 17.17 ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.055  -25.416 22.924 1.00 15.60 ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.412  -25.469 21.518 1.00 15.61 ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 3.917  -25.211 21.410 1.00 16.45 ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.452  -24.349 22.142 1.00 17.91 ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.637  -24.394 20.732 1.00 16.36 ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.113  -24.618 20.746 1.00 18.58 ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.632 -23.309 20.547 1.00 20.21 ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.323 -25.611 19.697 1.00 18.59 ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.571  -25.875 20.461 1.00 13.59 ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.014  -25.679 20.229 1.00 13.43 ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.167  -25.270 18.755 1.00 13.49 ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.506  -25.861 17.876 1.00 12.99 ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 6.858  -26.946 20.576 1.00 15.13 ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.329  -28.241 19.988 1.00 15.97 ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.356  -26.749 20.255 1.00 15.10 ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.030  -24.280 18.501 1.00 12.03 ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.249  -23.811 17.137 1.00 12.86 ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.659  -24.102 16.667 1.00 12.80 ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.608  -23.865 17.412 1.00 12.34 ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 8.793  -24.614 15.433 1.00 11.40 ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.101 -24.966 14.871 1.00 11.10 ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.380 -24.062 13.682 1.00 12.09 ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.522  -23.921 12.796 1.00 13.08 ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.065 -26.440 14.383 1.00 11.92 ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.611  -27.446 15.419 1.00 12.47 ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.503 -27.973 16.336 1.00 11.26 ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.286  -27.839 15.487 1.00 13.63 ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.064 -28.888 17.298 1.00 11.76 ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 7.860  -28.790 16.422 1.00 14.11 ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.750  -29.294 17.323 1.00 13.26 ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.620 -23.560 13.609 1.00 11.07 ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.034 -22.798 12.447 1.00 10.66 ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.405 -23.809 11.379 1.00 11.16 ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.344 -24.600 11.605 1.00 11.80 ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.263 -21.959 12.810 1.00 12.20 ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.731 -23.773 10.215 1.00 11.03 ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.025 -24.730 9.148  1.00 11.51 ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.357 -24.406 8.538  1.00 12.22 ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.684 -23.219 8.354  1.00 13.01 ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 10.939 -24.562 8.047  1.00 12.46 ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.039 -25.575 6.914  1.00 16.75 ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.239 -26.756 7.205  1.00 16.05 ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 10.995 -25.147 5.734  1.00 19.54 ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.096 -25.453 8.068  1.00 12.42 ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.320 -25.204 7.279  1.00 13.28 ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.276 -25.946 5.932  1.00 14.29 ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.250 -25.881 5.168  1.00 14.03 ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.633 -25.595 8.033  1.00 13.30 ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.815 -24.738 9.307  1.00 14.26 ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.699 -27.087 8.339  1.00 14.11 ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.148 -26.640 5.619  1.00 13.92 ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.086 -27.473 4.439  1.00 13.09 ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.133 -26.723 3.142  1.00 13.97 ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.419 -27.336 2.107  1.00 15.04 ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 12.849 -28.372 4.477  1.00 12.49 ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 12.895 -29.370 5.617  1.00 13.53 ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.571 -30.105 5.670  1.00 13.23 ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.483 -29.224 6.094  1.00 13.11 ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.230  -29.636 6.290  1.00 13.63 ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.881  -30.897 6.008  1.00 13.99 ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.324  -28.810 6.812  1.00 14.21 ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 13.767 -25.441 3.146  1.00 13.61 ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 13.821 -24.635 1.925  1.00 13.77 ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.200 -24.052 1.641  1.00 14.80 ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.382 -23.480 0.547  1.00 16.30 ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 12.822 -23.476 1.992  1.00 14.92 ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.138 -22.476 3.097  1.00 18.64 ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.497 -22.923 4.222  1.00 17.91 ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.038 -21.236 2.835  1.00 20.36 ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.138 -24.150 2.573  1.00 14.58 ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.478 -23.557 2.401  1.00 14.17 ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.336 -24.530 1.631  1.00 15.08 ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.205 -25.208 2.181  1.00 16.50 ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.090 -23.218 3.796  1.00 14.54 ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.243 -22.271 4.639  1.00 16.51 ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 17.871 -22.120 6.036  1.00 16.65 ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.035 -20.950 3.968  1.00 16.91 ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.119 -24.576 0.310  1.00 14.57 ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 18.791 -25.609 -0.511 1.00 15.86 ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.298 -25.412 -0.592 1.00 17.49 ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.036 -26.373 -0.800 1.00 19.45 ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.177 -25.680 -1.925 1.00 15.85 ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.664 -25.719 -1.997 1.00 17.83 ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.193 -25.870 -3.454 1.00 19.52 ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.073 -26.865 -1.139 1.00 18.18 ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 20.745 -24.164 -0.439 1.00 17.27 ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.170 -23.847 -0.513 1.00 18.26 ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 22.990 -24.453 0.631  1.00 19.87 ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.223 -24.500 0.527  1.00 19.84 ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.370 -22.319 -0.597 1.00 17.72 ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 21.691 -21.544 0.497  1.00 16.92 ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.432 -21.015 0.477  1.00 17.37 ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.229 -21.266 1.813  1.00 16.62 ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.170 -20.374 1.683  1.00 17.84 ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.276 -20.491 2.498  1.00 16.85 ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.476 -21.497 2.423  1.00 17.55 ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.490 -20.041 3.806  1.00 18.30 ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 23.698 -21.023 3.710  1.00 18.66 ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 22.732 -20.265 4.366  1.00 18.51 ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.331 -24.941 1.711  1.00 18.97 ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.078 -25.562 2.805  1.00 19.97 ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 23.810 -26.815 2.327  1.00 24.01 ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 24.835 -27.139 2.931  1.00 25.53 ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.135 -25.965 3.961  1.00 18.16 ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.614 -24.807 4.801  1.00 18.41 ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.579 -25.321 5.795  1.00 17.64 ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.767 -24.127 5.573  1.00 18.64 ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.274 -27.506 1.267  1.00 26.17 ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 23.772 -28.766 0.686  1.00 29.62 ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 24.926 -28.578 -0.296 1.00 32.96 ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.423 -29.586 -0.813 1.00 33.69 ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 22.662 -29.468 -0.128 1.00 31.17 ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 21.440 -30.004 0.608  1.00 34.81 ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 21.524 -30.215 1.823  1.00 34.84 ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 20.387 -30.229 -0.060 1.00 37.18 ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.267 -27.337 -0.665 1.00 33.67 ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.333 -27.112 -1.643 1.00 36.73 ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.452 -26.258 -1.052 1.00 39.26 ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.608 -26.417 -1.464 1.00 41.32 ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.761 -26.478 -2.925 1.00 39.33 ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 25.107 -25.131 -2.683 1.00 45.28 ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.069 -24.710 -3.709 1.00 53.81 ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 23.925 -23.486 -3.941 1.00 54.08 ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.395 -25.603 -4.273 1.00 56.71 ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1B4W C 2 .   ? 25.207 13.884  10.287 1.00 24.08 ? 201 A1B4W A N1  1 
HETATM 2156 C  C4  . A1B4W C 2 .   ? 27.571 11.191  7.425  1.00 24.41 ? 201 A1B4W A C4  1 
HETATM 2157 C  C5  . A1B4W C 2 .   ? 26.485 10.999  8.255  1.00 23.85 ? 201 A1B4W A C5  1 
HETATM 2158 C  C6  . A1B4W C 2 .   ? 25.530 12.115  8.604  1.00 24.85 ? 201 A1B4W A C6  1 
HETATM 2159 C  C7  . A1B4W C 2 .   ? 25.914 12.785  9.909  1.00 24.18 ? 201 A1B4W A C7  1 
HETATM 2160 C  C8  . A1B4W C 2 .   ? 25.369 14.445  11.630 1.00 23.60 ? 201 A1B4W A C8  1 
HETATM 2161 C  C10 . A1B4W C 2 .   ? 24.156 14.602  13.883 1.00 22.39 ? 201 A1B4W A C10 1 
HETATM 2162 C  C13 . A1B4W C 2 .   ? 21.853 15.567  9.519  1.00 26.02 ? 201 A1B4W A C13 1 
HETATM 2163 C  C15 . A1B4W C 2 .   ? 23.319 15.572  7.427  1.00 28.17 ? 201 A1B4W A C15 1 
HETATM 2164 C  C17 . A1B4W C 2 .   ? 24.090 14.460  9.503  1.00 25.41 ? 201 A1B4W A C17 1 
HETATM 2165 O  O2  . A1B4W C 2 .   ? 24.545 15.742  14.166 1.00 22.77 ? 201 A1B4W A O2  1 
HETATM 2166 N  N2  . A1B4W C 2 .   ? 23.778 13.720  14.797 1.00 20.35 ? 201 A1B4W A N2  1 
HETATM 2167 C  C9  . A1B4W C 2 .   ? 24.111 14.122  12.443 1.00 22.38 ? 201 A1B4W A C9  1 
HETATM 2168 C  C11 . A1B4W C 2 .   ? 22.844 14.591  11.692 1.00 23.28 ? 201 A1B4W A C11 1 
HETATM 2169 C  C12 . A1B4W C 2 .   ? 23.109 15.282  10.351 1.00 25.22 ? 201 A1B4W A C12 1 
HETATM 2170 C  C16 . A1B4W C 2 .   ? 24.549 15.316  8.323  1.00 26.98 ? 201 A1B4W A C16 1 
HETATM 2171 C  C14 . A1B4W C 2 .   ? 22.197 16.291  8.193  1.00 27.42 ? 201 A1B4W A C14 1 
HETATM 2172 O  O1  . A1B4W C 2 .   ? 26.805 12.322  10.612 1.00 23.04 ? 201 A1B4W A O1  1 
HETATM 2173 C  C1  . A1B4W C 2 .   ? 26.239 9.689   8.667  1.00 22.91 ? 201 A1B4W A C1  1 
HETATM 2174 O  O   . A1B4W C 2 .   ? 25.134 9.538   9.468  1.00 21.57 ? 201 A1B4W A O   1 
HETATM 2175 C  C   . A1B4W C 2 .   ? 24.707 8.216   9.803  1.00 20.53 ? 201 A1B4W A C   1 
HETATM 2176 N  N   . A1B4W C 2 .   ? 28.369 10.221  6.976  1.00 24.53 ? 201 A1B4W A N   1 
HETATM 2177 C  C3  . A1B4W C 2 .   ? 28.096 8.978   7.379  1.00 23.54 ? 201 A1B4W A C3  1 
HETATM 2178 C  C2  . A1B4W C 2 .   ? 27.057 8.656   8.235  1.00 23.50 ? 201 A1B4W A C2  1 
HETATM 2179 ZN ZN  . ZN    D 3 .   ? 22.961 -5.434  26.975 1.00 15.49 2 202 ZN    A ZN  1 
HETATM 2180 S  S   . DMS   E 4 .   ? 19.829 20.431  25.041 0.00 40.25 ? 203 DMS   A S   1 
HETATM 2181 O  O   . DMS   E 4 .   ? 20.634 20.686  23.801 0.00 32.08 ? 203 DMS   A O   1 
HETATM 2182 C  C1  . DMS   E 4 .   ? 20.988 20.323  26.431 0.00 36.78 ? 203 DMS   A C1  1 
HETATM 2183 C  C2  . DMS   E 4 .   ? 19.087 22.007  25.543 0.00 36.72 ? 203 DMS   A C2  1 
HETATM 2184 S  S   . DMS   F 4 .   ? 14.742 -0.706  12.136 0.00 37.29 ? 204 DMS   A S   1 
HETATM 2185 O  O   . DMS   F 4 .   ? 16.205 -0.941  12.377 0.00 22.04 ? 204 DMS   A O   1 
HETATM 2186 C  C1  . DMS   F 4 .   ? 14.558 -0.089  10.442 0.00 36.15 ? 204 DMS   A C1  1 
HETATM 2187 C  C2  . DMS   F 4 .   ? 14.300 0.849   12.953 0.00 36.55 ? 204 DMS   A C2  1 
HETATM 2188 N  N1  . A1B4W G 2 .   ? 10.664 -16.896 22.876 1.00 18.10 ? 201 A1B4W C N1  1 
HETATM 2189 C  C4  . A1B4W G 2 .   ? 8.532  -19.597 25.975 1.00 20.77 ? 201 A1B4W C C4  1 
HETATM 2190 C  C5  . A1B4W G 2 .   ? 9.425  -19.788 24.945 1.00 18.63 ? 201 A1B4W C C5  1 
HETATM 2191 C  C6  . A1B4W G 2 .   ? 10.392 -18.707 24.520 1.00 19.36 ? 201 A1B4W C C6  1 
HETATM 2192 C  C7  . A1B4W G 2 .   ? 9.936  -17.977 23.268 1.00 18.96 ? 201 A1B4W C C7  1 
HETATM 2193 C  C8  . A1B4W G 2 .   ? 10.412 -16.297 21.562 1.00 16.87 ? 201 A1B4W C C8  1 
HETATM 2194 C  C10 . A1B4W G 2 .   ? 11.348 -16.140 19.230 1.00 16.28 ? 201 A1B4W C C10 1 
HETATM 2195 C  C13 . A1B4W G 2 .   ? 14.198 -15.462 23.273 1.00 18.52 ? 201 A1B4W C C13 1 
HETATM 2196 C  C15 . A1B4W G 2 .   ? 12.961 -15.313 25.505 1.00 20.77 ? 201 A1B4W C C15 1 
HETATM 2197 C  C17 . A1B4W G 2 .   ? 11.892 -16.382 23.535 1.00 19.25 ? 201 A1B4W C C17 1 
HETATM 2198 O  O2  . A1B4W G 2 .   ? 10.969 -14.967 19.062 1.00 16.40 ? 201 A1B4W C O2  1 
HETATM 2199 N  N2  . A1B4W G 2 .   ? 11.598 -16.980 18.235 1.00 15.45 ? 201 A1B4W C N2  1 
HETATM 2200 C  C9  . A1B4W G 2 .   ? 11.545 -16.705 20.625 1.00 17.32 ? 201 A1B4W C C9  1 
HETATM 2201 C  C11 . A1B4W G 2 .   ? 12.906 -16.292 21.215 1.00 18.03 ? 201 A1B4W C C11 1 
HETATM 2202 C  C12 . A1B4W G 2 .   ? 12.835 -15.622 22.591 1.00 19.01 ? 201 A1B4W C C12 1 
HETATM 2203 C  C16 . A1B4W G 2 .   ? 11.620 -15.498 24.750 1.00 20.30 ? 201 A1B4W C C16 1 
HETATM 2204 C  C14 . A1B4W G 2 .   ? 14.054 -14.693 24.603 1.00 19.24 ? 201 A1B4W C C14 1 
HETATM 2205 O  O1  . A1B4W G 2 .   ? 8.968  -18.374 22.620 1.00 17.85 ? 201 A1B4W C O1  1 
HETATM 2206 C  C1  . A1B4W G 2 .   ? 9.520  -21.083 24.439 1.00 18.69 ? 201 A1B4W C C1  1 
HETATM 2207 O  O   . A1B4W G 2 .   ? 10.471 -21.265 23.478 1.00 17.18 ? 201 A1B4W C O   1 
HETATM 2208 C  C   . A1B4W G 2 .   ? 10.735 -22.602 23.037 1.00 17.68 ? 201 A1B4W C C   1 
HETATM 2209 N  N   . A1B4W G 2 .   ? 7.765  -20.547 26.508 1.00 21.04 ? 201 A1B4W C N   1 
HETATM 2210 C  C3  . A1B4W G 2 .   ? 7.882  -21.770 26.005 1.00 20.77 ? 201 A1B4W C C3  1 
HETATM 2211 C  C2  . A1B4W G 2 .   ? 8.739  -22.098 24.971 1.00 20.08 ? 201 A1B4W C C2  1 
HETATM 2212 N  N1  . A1B4W H 2 .   ? 3.431  -16.888 21.449 1.00 33.59 ? 202 A1B4W C N1  1 
HETATM 2213 C  C4  . A1B4W H 2 .   ? 5.549  -17.548 25.020 1.00 35.74 ? 202 A1B4W C C4  1 
HETATM 2214 C  C5  . A1B4W H 2 .   ? 6.048  -16.824 23.951 1.00 35.77 ? 202 A1B4W C C5  1 
HETATM 2215 C  C6  . A1B4W H 2 .   ? 5.672  -17.126 22.519 1.00 35.23 ? 202 A1B4W C C6  1 
HETATM 2216 C  C7  . A1B4W H 2 .   ? 4.485  -16.290 22.072 1.00 34.70 ? 202 A1B4W C C7  1 
HETATM 2217 C  C8  . A1B4W H 2 .   ? 2.208  -16.116 21.180 1.00 33.59 ? 202 A1B4W C C8  1 
HETATM 2218 C  C10 . A1B4W H 2 .   ? -0.254 -16.034 21.345 1.00 32.83 ? 202 A1B4W C C10 1 
HETATM 2219 C  C13 . A1B4W H 2 .   ? 1.914  -20.266 20.369 1.00 32.58 ? 202 A1B4W C C13 1 
HETATM 2220 C  C15 . A1B4W H 2 .   ? 4.081  -19.880 19.054 1.00 32.29 ? 202 A1B4W C C15 1 
HETATM 2221 C  C17 . A1B4W H 2 .   ? 3.383  -18.289 20.968 1.00 33.18 ? 202 A1B4W C C17 1 
HETATM 2222 O  O2  . A1B4W H 2 .   ? -0.757 -16.364 20.266 1.00 30.86 ? 202 A1B4W C O2  1 
HETATM 2223 N  N2  . A1B4W H 2 .   ? -0.719 -15.037 22.079 1.00 33.83 ? 202 A1B4W C N2  1 
HETATM 2224 C  C9  . A1B4W H 2 .   ? 0.987  -16.729 21.881 1.00 33.26 ? 202 A1B4W C C9  1 
HETATM 2225 C  C11 . A1B4W H 2 .   ? 0.949  -18.253 21.652 1.00 33.59 ? 202 A1B4W C C11 1 
HETATM 2226 C  C12 . A1B4W H 2 .   ? 1.959  -18.747 20.606 1.00 33.00 ? 202 A1B4W C C12 1 
HETATM 2227 C  C16 . A1B4W H 2 .   ? 4.325  -18.547 19.791 1.00 32.62 ? 202 A1B4W C C16 1 
HETATM 2228 C  C14 . A1B4W H 2 .   ? 3.262  -20.864 19.888 1.00 32.49 ? 202 A1B4W C C14 1 
HETATM 2229 O  O1  . A1B4W H 2 .   ? 4.458  -15.095 22.322 1.00 35.07 ? 202 A1B4W C O1  1 
HETATM 2230 C  C1  . A1B4W H 2 .   ? 6.916  -15.777 24.263 1.00 36.64 ? 202 A1B4W C C1  1 
HETATM 2231 O  O   . A1B4W H 2 .   ? 7.274  -14.980 23.205 1.00 36.91 ? 202 A1B4W C O   1 
HETATM 2232 C  C   . A1B4W H 2 .   ? 8.301  -14.012 23.415 1.00 36.00 ? 202 A1B4W C C   1 
HETATM 2233 N  N   . A1B4W H 2 .   ? 5.847  -17.322 26.302 1.00 36.63 ? 202 A1B4W C N   1 
HETATM 2234 C  C3  . A1B4W H 2 .   ? 6.711  -16.337 26.559 1.00 36.36 ? 202 A1B4W C C3  1 
HETATM 2235 C  C2  . A1B4W H 2 .   ? 7.279  -15.542 25.583 1.00 36.62 ? 202 A1B4W C C2  1 
HETATM 2236 ZN ZN  . ZN    I 3 .   ? 10.614 -35.726 5.558  1.00 15.12 2 203 ZN    C ZN  1 
HETATM 2237 S  S   . DMS   J 4 .   ? 14.527 -10.158 7.551  0.00 40.25 ? 204 DMS   C S   1 
HETATM 2238 O  O   . DMS   J 4 .   ? 13.921 -10.027 8.917  0.00 32.08 ? 204 DMS   C O   1 
HETATM 2239 C  C1  . DMS   J 4 .   ? 13.165 -10.264 6.359  0.00 36.78 ? 204 DMS   C C1  1 
HETATM 2240 C  C2  . DMS   J 4 .   ? 15.087 -8.510  7.043  0.00 36.72 ? 204 DMS   C C2  1 
HETATM 2241 S  S   . DMS   K 4 .   ? 20.184 -31.955 19.545 0.00 37.29 ? 205 DMS   C S   1 
HETATM 2242 O  O   . DMS   K 4 .   ? 18.699 -32.104 19.390 0.00 22.04 ? 205 DMS   C O   1 
HETATM 2243 C  C1  . DMS   K 4 .   ? 20.522 -31.659 21.302 0.00 36.15 ? 205 DMS   C C1  1 
HETATM 2244 C  C2  . DMS   K 4 .   ? 20.625 -30.287 18.990 0.00 36.55 ? 205 DMS   C C2  1 
HETATM 2245 O  O   . HOH   L 5 .   ? 15.057 -6.043  20.890 1.00 23.13 ? 301 HOH   A O   1 
HETATM 2246 O  O   . HOH   L 5 .   ? 14.673 22.137  24.405 1.00 25.84 ? 302 HOH   A O   1 
HETATM 2247 O  O   . HOH   L 5 .   ? 23.677 7.456   28.045 1.00 21.79 ? 303 HOH   A O   1 
HETATM 2248 O  O   . HOH   L 5 .   ? 22.546 6.617   1.572  1.00 25.78 ? 304 HOH   A O   1 
HETATM 2249 O  O   . HOH   L 5 .   ? 31.632 7.252   23.005 1.00 26.32 ? 305 HOH   A O   1 
HETATM 2250 O  O   . HOH   L 5 .   ? 24.492 18.709  6.155  1.00 52.47 ? 306 HOH   A O   1 
HETATM 2251 O  O   . HOH   L 5 .   ? 17.673 -7.351  21.508 1.00 21.49 ? 307 HOH   A O   1 
HETATM 2252 O  O   . HOH   L 5 .   ? 6.306  2.964   28.709 1.00 45.62 ? 308 HOH   A O   1 
HETATM 2253 O  O   . HOH   L 5 .   ? 14.883 8.570   13.268 1.00 16.02 ? 309 HOH   A O   1 
HETATM 2254 O  O   . HOH   L 5 .   ? 29.793 6.835   4.542  1.00 39.50 ? 310 HOH   A O   1 
HETATM 2255 O  O   . HOH   L 5 .   ? 17.055 20.696  22.796 1.00 22.25 ? 311 HOH   A O   1 
HETATM 2256 O  O   . HOH   L 5 .   ? 25.101 -4.995  32.221 1.00 39.10 ? 312 HOH   A O   1 
HETATM 2257 O  O   . HOH   L 5 .   ? 25.336 17.983  12.700 1.00 26.16 ? 313 HOH   A O   1 
HETATM 2258 O  O   . HOH   L 5 .   ? 28.457 -6.188  3.640  1.00 31.33 ? 314 HOH   A O   1 
HETATM 2259 O  O   . HOH   L 5 .   ? 27.866 3.012   -0.223 1.00 22.28 ? 315 HOH   A O   1 
HETATM 2260 O  O   . HOH   L 5 .   ? 16.018 -0.786  4.661  1.00 27.59 ? 316 HOH   A O   1 
HETATM 2261 O  O   . HOH   L 5 .   ? 6.951  7.652   31.489 1.00 34.69 ? 317 HOH   A O   1 
HETATM 2262 O  O   . HOH   L 5 .   ? 6.570  15.959  28.705 1.00 45.24 ? 318 HOH   A O   1 
HETATM 2263 O  O   . HOH   L 5 .   ? 20.624 10.496  32.137 1.00 50.19 ? 319 HOH   A O   1 
HETATM 2264 O  O   . HOH   L 5 .   ? 18.614 -11.587 27.346 1.00 31.14 ? 320 HOH   A O   1 
HETATM 2265 O  O   . HOH   L 5 .   ? 3.706  19.777  21.011 1.00 27.13 ? 321 HOH   A O   1 
HETATM 2266 O  O   . HOH   L 5 .   ? 33.850 -3.271  13.112 1.00 31.45 ? 322 HOH   A O   1 
HETATM 2267 O  O   . HOH   L 5 .   ? 34.843 13.679  16.177 1.00 27.81 ? 323 HOH   A O   1 
HETATM 2268 O  O   . HOH   L 5 .   ? 23.783 3.962   29.178 1.00 20.35 ? 324 HOH   A O   1 
HETATM 2269 O  O   . HOH   L 5 .   ? 10.915 -0.145  15.924 1.00 22.03 ? 325 HOH   A O   1 
HETATM 2270 O  O   . HOH   L 5 .   ? -0.155 14.225  22.355 1.00 52.31 ? 326 HOH   A O   1 
HETATM 2271 O  O   . HOH   L 5 .   ? 20.555 1.406   31.548 1.00 19.35 ? 327 HOH   A O   1 
HETATM 2272 O  O   . HOH   L 5 .   ? 26.942 19.199  14.982 1.00 28.12 ? 328 HOH   A O   1 
HETATM 2273 O  O   . HOH   L 5 .   ? -1.937 15.512  20.488 1.00 34.01 ? 329 HOH   A O   1 
HETATM 2274 O  O   . HOH   L 5 .   ? 11.394 10.717  9.715  1.00 43.28 ? 330 HOH   A O   1 
HETATM 2275 O  O   . HOH   L 5 .   ? 30.952 -1.956  29.545 1.00 37.29 ? 331 HOH   A O   1 
HETATM 2276 O  O   . HOH   L 5 .   ? 23.400 10.977  21.238 1.00 15.02 ? 332 HOH   A O   1 
HETATM 2277 O  O   . HOH   L 5 .   ? 32.107 2.565   5.047  1.00 30.67 ? 333 HOH   A O   1 
HETATM 2278 O  O   . HOH   L 5 .   ? 20.028 11.819  8.458  1.00 21.64 ? 334 HOH   A O   1 
HETATM 2279 O  O   . HOH   L 5 .   ? 20.038 2.090   9.260  1.00 15.04 ? 335 HOH   A O   1 
HETATM 2280 O  O   . HOH   L 5 .   ? 4.649  10.572  14.580 1.00 43.32 ? 336 HOH   A O   1 
HETATM 2281 O  O   . HOH   L 5 .   ? 11.387 -1.588  27.941 1.00 24.33 ? 337 HOH   A O   1 
HETATM 2282 O  O   . HOH   L 5 .   ? 23.486 14.701  29.911 1.00 58.68 ? 338 HOH   A O   1 
HETATM 2283 O  O   . HOH   L 5 .   ? 29.657 6.484   29.740 1.00 33.29 ? 339 HOH   A O   1 
HETATM 2284 O  O   . HOH   L 5 .   ? 16.478 18.646  26.750 1.00 37.12 ? 340 HOH   A O   1 
HETATM 2285 O  O   . HOH   L 5 .   ? 25.236 1.704   29.765 1.00 20.16 ? 341 HOH   A O   1 
HETATM 2286 O  O   . HOH   L 5 .   ? 16.195 -3.339  13.793 1.00 33.50 ? 342 HOH   A O   1 
HETATM 2287 O  O   . HOH   L 5 .   ? 32.728 -6.819  17.434 1.00 37.72 ? 343 HOH   A O   1 
HETATM 2288 O  O   . HOH   L 5 .   ? 3.994  10.108  17.769 1.00 33.13 ? 344 HOH   A O   1 
HETATM 2289 O  O   . HOH   L 5 .   ? 34.412 -0.938  16.548 1.00 13.62 ? 345 HOH   A O   1 
HETATM 2290 O  O   . HOH   L 5 .   ? 4.902  3.199   20.918 1.00 24.21 ? 346 HOH   A O   1 
HETATM 2291 O  O   . HOH   L 5 .   ? 21.990 8.883   2.850  1.00 25.38 ? 347 HOH   A O   1 
HETATM 2292 O  O   . HOH   L 5 .   ? 17.162 2.073   9.242  1.00 21.32 ? 348 HOH   A O   1 
HETATM 2293 O  O   . HOH   L 5 .   ? 11.848 -2.797  15.992 1.00 32.39 ? 349 HOH   A O   1 
HETATM 2294 O  O   . HOH   L 5 .   ? 30.686 4.938   7.834  1.00 27.20 ? 350 HOH   A O   1 
HETATM 2295 O  O   . HOH   L 5 .   ? 23.690 1.811   -0.885 1.00 16.50 ? 351 HOH   A O   1 
HETATM 2296 O  O   . HOH   L 5 .   ? 11.415 13.227  8.504  1.00 52.19 ? 352 HOH   A O   1 
HETATM 2297 O  O   . HOH   L 5 .   ? 3.187  18.077  23.333 1.00 28.66 ? 353 HOH   A O   1 
HETATM 2298 O  O   . HOH   L 5 .   ? 8.797  3.889   11.831 1.00 35.23 ? 354 HOH   A O   1 
HETATM 2299 O  O   . HOH   L 5 .   ? 12.516 17.618  13.130 1.00 28.38 ? 355 HOH   A O   1 
HETATM 2300 O  O   . HOH   L 5 .   ? 34.966 14.754  24.909 1.00 38.90 ? 356 HOH   A O   1 
HETATM 2301 O  O   . HOH   L 5 .   ? 4.850  10.858  12.106 1.00 36.48 ? 357 HOH   A O   1 
HETATM 2302 O  O   . HOH   L 5 .   ? 22.374 -6.303  0.552  1.00 47.13 ? 358 HOH   A O   1 
HETATM 2303 O  O   . HOH   L 5 .   ? 17.669 16.694  28.335 1.00 42.11 ? 359 HOH   A O   1 
HETATM 2304 O  O   . HOH   L 5 .   ? 34.326 3.338   26.162 1.00 27.54 ? 360 HOH   A O   1 
HETATM 2305 O  O   . HOH   L 5 .   ? 28.185 0.894   26.678 1.00 19.46 ? 361 HOH   A O   1 
HETATM 2306 O  O   . HOH   L 5 .   ? 16.299 8.909   6.714  1.00 23.55 ? 362 HOH   A O   1 
HETATM 2307 O  O   . HOH   L 5 .   ? 4.201  4.359   27.987 1.00 36.43 ? 363 HOH   A O   1 
HETATM 2308 O  O   . HOH   L 5 .   ? 34.494 -6.460  21.815 1.00 31.24 ? 364 HOH   A O   1 
HETATM 2309 O  O   . HOH   L 5 .   ? 21.513 9.916   23.177 1.00 14.58 ? 365 HOH   A O   1 
HETATM 2310 O  O   . HOH   L 5 .   ? 30.209 -5.795  26.379 1.00 26.51 ? 366 HOH   A O   1 
HETATM 2311 O  O   . HOH   L 5 .   ? 17.152 18.498  15.345 1.00 18.07 ? 367 HOH   A O   1 
HETATM 2312 O  O   . HOH   L 5 .   ? 29.572 -2.245  8.512  1.00 22.13 ? 368 HOH   A O   1 
HETATM 2313 O  O   . HOH   L 5 .   ? 25.042 4.203   -1.239 1.00 19.30 ? 369 HOH   A O   1 
HETATM 2314 O  O   . HOH   L 5 .   ? 32.112 8.868   4.696  1.00 42.05 ? 370 HOH   A O   1 
HETATM 2315 O  O   . HOH   L 5 .   ? 19.732 -4.847  15.276 1.00 25.36 ? 371 HOH   A O   1 
HETATM 2316 O  O   . HOH   L 5 .   ? 17.720 21.127  14.310 1.00 34.15 ? 372 HOH   A O   1 
HETATM 2317 O  O   . HOH   L 5 .   ? 24.622 -8.544  24.726 1.00 25.11 ? 373 HOH   A O   1 
HETATM 2318 O  O   . HOH   L 5 .   ? 29.090 25.897  13.642 1.00 35.25 ? 374 HOH   A O   1 
HETATM 2319 O  O   . HOH   L 5 .   ? 31.987 22.426  11.468 1.00 40.86 ? 375 HOH   A O   1 
HETATM 2320 O  O   . HOH   L 5 .   ? 18.084 -5.177  30.523 1.00 26.21 ? 376 HOH   A O   1 
HETATM 2321 O  O   . HOH   L 5 .   ? 28.565 17.553  8.425  1.00 40.67 ? 377 HOH   A O   1 
HETATM 2322 O  O   . HOH   L 5 .   ? 30.493 -3.177  11.770 1.00 33.34 ? 378 HOH   A O   1 
HETATM 2323 O  O   . HOH   L 5 .   ? 16.667 4.392   5.670  1.00 27.10 ? 379 HOH   A O   1 
HETATM 2324 O  O   . HOH   L 5 .   ? 2.632  8.752   25.969 1.00 38.00 ? 380 HOH   A O   1 
HETATM 2325 O  O   . HOH   L 5 .   ? 15.626 12.180  30.709 1.00 32.16 ? 381 HOH   A O   1 
HETATM 2326 O  O   . HOH   L 5 .   ? 29.642 26.052  16.121 1.00 53.60 ? 382 HOH   A O   1 
HETATM 2327 O  O   . HOH   L 5 .   ? 32.547 12.432  27.539 1.00 31.49 ? 383 HOH   A O   1 
HETATM 2328 O  O   . HOH   L 5 .   ? 1.878  14.111  24.628 1.00 48.06 ? 384 HOH   A O   1 
HETATM 2329 O  O   . HOH   L 5 .   ? 6.851  16.113  8.567  1.00 34.05 ? 385 HOH   A O   1 
HETATM 2330 O  O   . HOH   L 5 .   ? 3.762  14.609  10.143 1.00 27.52 ? 386 HOH   A O   1 
HETATM 2331 O  O   . HOH   L 5 .   ? 15.288 23.284  16.890 1.00 22.82 ? 387 HOH   A O   1 
HETATM 2332 O  O   . HOH   L 5 .   ? 19.834 14.027  28.710 1.00 31.09 ? 388 HOH   A O   1 
HETATM 2333 O  O   . HOH   L 5 .   ? 27.683 11.897  27.499 1.00 24.84 ? 389 HOH   A O   1 
HETATM 2334 O  O   . HOH   L 5 .   ? 25.953 -8.519  22.488 1.00 40.30 ? 390 HOH   A O   1 
HETATM 2335 O  O   . HOH   L 5 .   ? 12.209 18.530  26.237 1.00 30.21 ? 391 HOH   A O   1 
HETATM 2336 O  O   . HOH   L 5 .   ? 28.776 21.963  22.042 1.00 38.31 ? 392 HOH   A O   1 
HETATM 2337 O  O   . HOH   L 5 .   ? 23.015 20.872  20.452 1.00 31.62 ? 393 HOH   A O   1 
HETATM 2338 O  O   . HOH   L 5 .   ? 3.260  2.518   18.736 1.00 30.66 ? 394 HOH   A O   1 
HETATM 2339 O  O   . HOH   L 5 .   ? 32.845 -2.753  15.410 1.00 22.49 ? 395 HOH   A O   1 
HETATM 2340 O  O   . HOH   L 5 .   ? 28.275 16.358  10.613 1.00 38.71 ? 396 HOH   A O   1 
HETATM 2341 O  O   . HOH   L 5 .   ? 32.628 5.149   4.727  1.00 46.04 ? 397 HOH   A O   1 
HETATM 2342 O  O   . HOH   L 5 .   ? 11.030 2.124   12.263 1.00 26.17 ? 398 HOH   A O   1 
HETATM 2343 O  O   . HOH   L 5 .   ? -0.740 10.811  19.577 1.00 46.28 ? 399 HOH   A O   1 
HETATM 2344 O  O   . HOH   L 5 .   ? 13.050 8.470   11.003 1.00 20.95 ? 400 HOH   A O   1 
HETATM 2345 O  O   . HOH   L 5 .   ? 30.117 -2.178  3.706  1.00 40.46 ? 401 HOH   A O   1 
HETATM 2346 O  O   . HOH   L 5 .   ? 29.992 13.432  9.768  1.00 50.21 ? 402 HOH   A O   1 
HETATM 2347 O  O   . HOH   L 5 .   ? 30.955 15.393  11.112 1.00 40.11 ? 403 HOH   A O   1 
HETATM 2348 O  O   . HOH   L 5 .   ? 5.427  2.699   12.064 1.00 57.59 ? 404 HOH   A O   1 
HETATM 2349 O  O   . HOH   L 5 .   ? 26.254 -6.439  29.767 1.00 31.98 ? 405 HOH   A O   1 
HETATM 2350 O  O   . HOH   L 5 .   ? 15.572 8.529   33.960 1.00 32.96 ? 406 HOH   A O   1 
HETATM 2351 O  O   . HOH   L 5 .   ? 25.527 22.282  5.865  1.00 48.47 ? 407 HOH   A O   1 
HETATM 2352 O  O   . HOH   L 5 .   ? 10.628 6.856   11.103 1.00 42.43 ? 408 HOH   A O   1 
HETATM 2353 O  O   . HOH   L 5 .   ? 8.853  17.885  8.437  1.00 40.62 ? 409 HOH   A O   1 
HETATM 2354 O  O   . HOH   L 5 .   ? 24.265 -12.414 30.746 1.00 60.01 ? 410 HOH   A O   1 
HETATM 2355 O  O   . HOH   L 5 .   ? 17.990 10.895  6.550  1.00 32.84 ? 411 HOH   A O   1 
HETATM 2356 O  O   . HOH   L 5 .   ? 13.902 21.647  14.587 1.00 28.10 ? 412 HOH   A O   1 
HETATM 2357 O  O   . HOH   L 5 .   ? 30.872 -2.935  5.992  1.00 33.45 ? 413 HOH   A O   1 
HETATM 2358 O  O   . HOH   L 5 .   ? 26.009 18.237  26.563 1.00 46.43 ? 414 HOH   A O   1 
HETATM 2359 O  O   . HOH   L 5 .   ? 27.852 1.716   29.294 1.00 25.39 ? 415 HOH   A O   1 
HETATM 2360 O  O   . HOH   L 5 .   ? 25.255 -9.046  19.776 1.00 28.50 ? 416 HOH   A O   1 
HETATM 2361 O  O   . HOH   L 5 .   ? 8.675  -2.181  27.643 1.00 51.66 ? 417 HOH   A O   1 
HETATM 2362 O  O   . HOH   L 5 .   ? 22.992 -11.804 21.704 1.00 46.96 ? 418 HOH   A O   1 
HETATM 2363 O  O   . HOH   L 5 .   ? 33.669 -2.357  9.134  1.00 28.63 ? 419 HOH   A O   1 
HETATM 2364 O  O   . HOH   L 5 .   ? 34.110 -9.288  20.380 1.00 39.19 ? 420 HOH   A O   1 
HETATM 2365 O  O   . HOH   L 5 .   ? 13.112 9.695   8.241  1.00 38.33 ? 421 HOH   A O   1 
HETATM 2366 O  O   . HOH   L 5 .   ? 28.340 4.187   30.497 1.00 33.46 ? 422 HOH   A O   1 
HETATM 2367 O  O   . HOH   L 5 .   ? 31.528 25.838  12.489 1.00 39.90 ? 423 HOH   A O   1 
HETATM 2368 O  O   . HOH   L 5 .   ? 2.637  4.035   16.625 1.00 39.60 ? 424 HOH   A O   1 
HETATM 2369 O  O   . HOH   M 5 .   ? 30.225 -10.543 10.298 1.00 44.32 ? 301 HOH   C O   1 
HETATM 2370 O  O   . HOH   M 5 .   ? 11.082 -40.325 24.357 1.00 29.02 ? 302 HOH   C O   1 
HETATM 2371 O  O   . HOH   M 5 .   ? 10.064 -22.859 4.873  1.00 20.41 ? 303 HOH   C O   1 
HETATM 2372 O  O   . HOH   M 5 .   ? 23.536 -31.372 15.032 1.00 25.87 ? 304 HOH   C O   1 
HETATM 2373 O  O   . HOH   M 5 .   ? 23.404 -9.233  7.810  1.00 24.27 ? 305 HOH   C O   1 
HETATM 2374 O  O   . HOH   M 5 .   ? 10.428 -27.409 33.710 1.00 29.08 ? 306 HOH   C O   1 
HETATM 2375 O  O   . HOH   M 5 .   ? 26.241 -22.663 -0.338 1.00 38.86 ? 307 HOH   C O   1 
HETATM 2376 O  O   . HOH   M 5 .   ? 20.387 -22.544 18.605 1.00 14.13 ? 308 HOH   C O   1 
HETATM 2377 O  O   . HOH   M 5 .   ? 6.632  -23.510 28.849 1.00 40.72 ? 309 HOH   C O   1 
HETATM 2378 O  O   . HOH   M 5 .   ? -2.877 -24.441 26.234 1.00 30.61 ? 310 HOH   C O   1 
HETATM 2379 O  O   . HOH   M 5 .   ? 17.507 -37.833 3.069  1.00 34.55 ? 311 HOH   C O   1 
HETATM 2380 O  O   . HOH   M 5 .   ? 23.172 -36.219 11.866 1.00 37.08 ? 312 HOH   C O   1 
HETATM 2381 O  O   . HOH   M 5 .   ? 34.337 -10.975 10.792 1.00 46.66 ? 313 HOH   C O   1 
HETATM 2382 O  O   . HOH   M 5 .   ? 3.689  -23.374 3.739  1.00 26.42 ? 314 HOH   C O   1 
HETATM 2383 O  O   . HOH   M 5 .   ? 26.281 -32.967 5.735  1.00 42.65 ? 315 HOH   C O   1 
HETATM 2384 O  O   . HOH   M 5 .   ? 10.518 -12.774 20.620 1.00 18.16 ? 316 HOH   C O   1 
HETATM 2385 O  O   . HOH   M 5 .   ? 33.007 -16.774 6.867  1.00 47.48 ? 317 HOH   C O   1 
HETATM 2386 O  O   . HOH   M 5 .   ? 9.840  -26.225 3.552  1.00 17.83 ? 318 HOH   C O   1 
HETATM 2387 O  O   . HOH   M 5 .   ? 30.829 -21.216 12.929 1.00 32.08 ? 319 HOH   C O   1 
HETATM 2388 O  O   . HOH   M 5 .   ? 22.285 -12.661 17.825 1.00 29.62 ? 320 HOH   C O   1 
HETATM 2389 O  O   . HOH   M 5 .   ? 14.060 -19.746 0.827  1.00 34.84 ? 321 HOH   C O   1 
HETATM 2390 O  O   . HOH   M 5 .   ? 31.157 -25.984 -2.259 1.00 54.36 ? 322 HOH   C O   1 
HETATM 2391 O  O   . HOH   M 5 .   ? 5.279  -25.590 24.418 1.00 23.68 ? 323 HOH   C O   1 
HETATM 2392 O  O   . HOH   M 5 .   ? 4.464  -36.399 21.617 1.00 23.93 ? 324 HOH   C O   1 
HETATM 2393 O  O   . HOH   M 5 .   ? 0.576  -16.931 17.921 1.00 27.16 ? 325 HOH   C O   1 
HETATM 2394 O  O   . HOH   M 5 .   ? 29.352 -27.881 9.715  1.00 26.57 ? 326 HOH   C O   1 
HETATM 2395 O  O   . HOH   M 5 .   ? 27.508 -14.966 2.709  1.00 41.14 ? 327 HOH   C O   1 
HETATM 2396 O  O   . HOH   M 5 .   ? 16.374 -14.148 4.217  1.00 38.33 ? 328 HOH   C O   1 
HETATM 2397 O  O   . HOH   M 5 .   ? 8.657  -11.496 18.623 1.00 21.04 ? 329 HOH   C O   1 
HETATM 2398 O  O   . HOH   M 5 .   ? 30.385 -20.327 19.025 1.00 26.60 ? 330 HOH   C O   1 
HETATM 2399 O  O   . HOH   M 5 .   ? 12.358 -6.056  22.122 1.00 25.97 ? 331 HOH   C O   1 
HETATM 2400 O  O   . HOH   M 5 .   ? 29.369 -9.817  18.663 1.00 40.08 ? 332 HOH   C O   1 
HETATM 2401 O  O   . HOH   M 5 .   ? 7.883  -35.006 0.502  1.00 21.54 ? 333 HOH   C O   1 
HETATM 2402 O  O   . HOH   M 5 .   ? 11.457 -36.040 -0.550 1.00 30.61 ? 334 HOH   C O   1 
HETATM 2403 O  O   . HOH   M 5 .   ? 17.616 -10.093 9.331  1.00 20.41 ? 335 HOH   C O   1 
HETATM 2404 O  O   . HOH   M 5 .   ? 19.138 -30.417 -2.520 1.00 33.53 ? 336 HOH   C O   1 
HETATM 2405 O  O   . HOH   M 5 .   ? 30.561 -20.469 16.244 1.00 30.46 ? 337 HOH   C O   1 
HETATM 2406 O  O   . HOH   M 5 .   ? 6.943  -37.065 29.012 1.00 33.94 ? 338 HOH   C O   1 
HETATM 2407 O  O   . HOH   M 5 .   ? 18.003 -10.104 18.404 1.00 33.77 ? 339 HOH   C O   1 
HETATM 2408 O  O   . HOH   M 5 .   ? 3.899  -27.184 27.883 1.00 34.53 ? 340 HOH   C O   1 
HETATM 2409 O  O   . HOH   M 5 .   ? 8.387  -28.397 2.977  1.00 19.66 ? 341 HOH   C O   1 
HETATM 2410 O  O   . HOH   M 5 .   ? 11.262 -19.647 11.656 1.00 14.94 ? 342 HOH   C O   1 
HETATM 2411 O  O   . HOH   M 5 .   ? 15.388 -28.921 23.167 1.00 14.68 ? 343 HOH   C O   1 
HETATM 2412 O  O   . HOH   M 5 .   ? 16.173 -19.251 24.153 1.00 20.07 ? 344 HOH   C O   1 
HETATM 2413 O  O   . HOH   M 5 .   ? 22.049 -32.225 3.679  1.00 23.61 ? 345 HOH   C O   1 
HETATM 2414 O  O   . HOH   M 5 .   ? 2.665  -31.226 3.820  1.00 36.26 ? 346 HOH   C O   1 
HETATM 2415 O  O   . HOH   M 5 .   ? 0.812  -31.769 17.048 1.00 13.21 ? 347 HOH   C O   1 
HETATM 2416 O  O   . HOH   M 5 .   ? 4.883  -31.135 -1.883 1.00 33.76 ? 348 HOH   C O   1 
HETATM 2417 O  O   . HOH   M 5 .   ? 18.190 -28.877 22.967 1.00 23.40 ? 349 HOH   C O   1 
HETATM 2418 O  O   . HOH   M 5 .   ? 1.125  -29.663 24.843 1.00 35.40 ? 350 HOH   C O   1 
HETATM 2419 O  O   . HOH   M 5 .   ? 9.717  -40.581 1.188  1.00 49.98 ? 351 HOH   C O   1 
HETATM 2420 O  O   . HOH   M 5 .   ? 5.676  -32.748 29.628 1.00 50.10 ? 352 HOH   C O   1 
HETATM 2421 O  O   . HOH   M 5 .   ? 18.027 -11.802 5.458  1.00 42.33 ? 353 HOH   C O   1 
HETATM 2422 O  O   . HOH   M 5 .   ? 14.344 -22.416 29.924 1.00 24.12 ? 354 HOH   C O   1 
HETATM 2423 O  O   . HOH   M 5 .   ? 19.787 -31.738 27.127 1.00 27.41 ? 355 HOH   C O   1 
HETATM 2424 O  O   . HOH   M 5 .   ? 19.714 -22.413 25.465 1.00 29.44 ? 356 HOH   C O   1 
HETATM 2425 O  O   . HOH   M 5 .   ? 19.372 -27.171 25.593 1.00 29.61 ? 357 HOH   C O   1 
HETATM 2426 O  O   . HOH   M 5 .   ? 12.909 -20.719 9.529  1.00 13.77 ? 358 HOH   C O   1 
HETATM 2427 O  O   . HOH   M 5 .   ? 31.116 -10.762 16.625 1.00 26.10 ? 359 HOH   C O   1 
HETATM 2428 O  O   . HOH   M 5 .   ? 18.278 -12.411 17.111 1.00 19.01 ? 360 HOH   C O   1 
HETATM 2429 O  O   . HOH   M 5 .   ? 5.602  -32.825 24.422 1.00 19.80 ? 361 HOH   C O   1 
HETATM 2430 O  O   . HOH   M 5 .   ? 5.526  -29.279 7.282  1.00 17.97 ? 362 HOH   C O   1 
HETATM 2431 O  O   . HOH   M 5 .   ? 8.379  -39.695 24.374 1.00 46.67 ? 363 HOH   C O   1 
HETATM 2432 O  O   . HOH   M 5 .   ? 21.354 -36.359 9.859  1.00 34.70 ? 364 HOH   C O   1 
HETATM 2433 O  O   . HOH   M 5 .   ? 16.490 -38.569 10.546 1.00 33.41 ? 365 HOH   C O   1 
HETATM 2434 O  O   . HOH   M 5 .   ? 4.005  -24.562 26.374 1.00 27.17 ? 366 HOH   C O   1 
HETATM 2435 O  O   . HOH   M 5 .   ? -2.237 -30.490 8.498  1.00 20.05 ? 367 HOH   C O   1 
HETATM 2436 O  O   . HOH   M 5 .   ? 3.738  -36.359 6.828  1.00 24.40 ? 368 HOH   C O   1 
HETATM 2437 O  O   . HOH   M 5 .   ? 13.369 -37.068 32.144 1.00 34.55 ? 369 HOH   C O   1 
HETATM 2438 O  O   . HOH   M 5 .   ? -0.459 -15.817 14.033 1.00 29.16 ? 370 HOH   C O   1 
HETATM 2439 O  O   . HOH   M 5 .   ? 31.185 -21.887 4.770  1.00 39.00 ? 371 HOH   C O   1 
HETATM 2440 O  O   . HOH   M 5 .   ? 28.934 -32.822 12.328 1.00 38.19 ? 372 HOH   C O   1 
HETATM 2441 O  O   . HOH   M 5 .   ? 6.392  -18.373 5.948  1.00 24.18 ? 373 HOH   C O   1 
HETATM 2442 O  O   . HOH   M 5 .   ? 14.982 -35.654 17.047 1.00 24.21 ? 374 HOH   C O   1 
HETATM 2443 O  O   . HOH   M 5 .   ? 31.216 -28.450 11.488 1.00 31.39 ? 375 HOH   C O   1 
HETATM 2444 O  O   . HOH   M 5 .   ? 14.055 -16.593 3.841  1.00 25.26 ? 376 HOH   C O   1 
HETATM 2445 O  O   . HOH   M 5 .   ? 1.522  -17.850 6.496  1.00 34.73 ? 377 HOH   C O   1 
HETATM 2446 O  O   . HOH   M 5 .   ? 7.737  -5.485  14.521 1.00 37.81 ? 378 HOH   C O   1 
HETATM 2447 O  O   . HOH   M 5 .   ? 19.264 -7.495  15.176 1.00 21.76 ? 379 HOH   C O   1 
HETATM 2448 O  O   . HOH   M 5 .   ? 11.007 -15.409 3.195  1.00 53.80 ? 380 HOH   C O   1 
HETATM 2449 O  O   . HOH   M 5 .   ? 17.927 -18.391 1.546  1.00 39.03 ? 381 HOH   C O   1 
HETATM 2450 O  O   . HOH   M 5 .   ? 1.649  -37.854 15.259 1.00 38.41 ? 382 HOH   C O   1 
HETATM 2451 O  O   . HOH   M 5 .   ? 4.189  -8.207  22.834 1.00 35.27 ? 383 HOH   C O   1 
HETATM 2452 O  O   . HOH   M 5 .   ? 3.937  -33.729 22.315 1.00 25.37 ? 384 HOH   C O   1 
HETATM 2453 O  O   . HOH   M 5 .   ? 15.206 -35.636 1.551  1.00 22.78 ? 385 HOH   C O   1 
HETATM 2454 O  O   . HOH   M 5 .   ? 6.023  -8.510  11.746 1.00 43.06 ? 386 HOH   C O   1 
HETATM 2455 O  O   . HOH   M 5 .   ? 26.611 -33.158 13.680 1.00 39.86 ? 387 HOH   C O   1 
HETATM 2456 O  O   . HOH   M 5 .   ? 16.529 -8.555  16.568 1.00 58.59 ? 388 HOH   C O   1 
HETATM 2457 O  O   . HOH   M 5 .   ? 4.772  -38.665 7.341  1.00 59.15 ? 389 HOH   C O   1 
HETATM 2458 O  O   . HOH   M 5 .   ? 22.191 -12.190 5.726  1.00 29.14 ? 390 HOH   C O   1 
HETATM 2459 O  O   . HOH   M 5 .   ? 8.734  -38.782 9.462  1.00 38.29 ? 391 HOH   C O   1 
HETATM 2460 O  O   . HOH   M 5 .   ? 32.060 -16.815 20.694 1.00 26.26 ? 392 HOH   C O   1 
HETATM 2461 O  O   . HOH   M 5 .   ? 24.085 -29.169 18.920 1.00 29.35 ? 393 HOH   C O   1 
HETATM 2462 O  O   . HOH   M 5 .   ? 22.382 -22.728 20.567 1.00 20.21 ? 394 HOH   C O   1 
HETATM 2463 O  O   . HOH   M 5 .   ? 11.889 -9.925  12.592 1.00 32.58 ? 395 HOH   C O   1 
HETATM 2464 O  O   . HOH   M 5 .   ? 16.935 -21.922 -1.656 1.00 30.89 ? 396 HOH   C O   1 
HETATM 2465 O  O   . HOH   M 5 .   ? 24.877 -24.170 19.934 1.00 34.57 ? 397 HOH   C O   1 
HETATM 2466 O  O   . HOH   M 5 .   ? 29.259 -15.255 22.722 1.00 39.68 ? 398 HOH   C O   1 
HETATM 2467 O  O   . HOH   M 5 .   ? 17.456 -34.596 17.890 1.00 38.88 ? 399 HOH   C O   1 
HETATM 2468 O  O   . HOH   M 5 .   ? 9.445  -9.997  11.223 1.00 41.74 ? 400 HOH   C O   1 
HETATM 2469 O  O   . HOH   M 5 .   ? 16.416 -7.424  14.307 1.00 44.26 ? 401 HOH   C O   1 
HETATM 2470 O  O   . HOH   M 5 .   ? 10.029 -22.133 32.056 1.00 54.33 ? 402 HOH   C O   1 
HETATM 2471 O  O   . HOH   M 5 .   ? -0.268 -36.094 16.839 1.00 46.33 ? 403 HOH   C O   1 
HETATM 2472 O  O   . HOH   M 5 .   ? -2.379 -35.591 15.080 1.00 34.10 ? 404 HOH   C O   1 
HETATM 2473 O  O   . HOH   M 5 .   ? 19.270 -22.010 -2.613 1.00 33.45 ? 405 HOH   C O   1 
HETATM 2474 O  O   . HOH   M 5 .   ? 2.227  -34.498 4.034  1.00 52.26 ? 406 HOH   C O   1 
HETATM 2475 O  O   . HOH   M 5 .   ? 12.730 -39.303 12.824 1.00 38.57 ? 407 HOH   C O   1 
HETATM 2476 O  O   . HOH   M 5 .   ? -2.345 -36.869 12.781 1.00 58.45 ? 408 HOH   C O   1 
HETATM 2477 O  O   . HOH   M 5 .   ? 4.671  -29.112 4.713  1.00 42.10 ? 409 HOH   C O   1 
HETATM 2478 O  O   . HOH   M 5 .   ? 30.020 -23.243 -1.036 1.00 68.15 ? 410 HOH   C O   1 
HETATM 2479 O  O   . HOH   M 5 .   ? 24.113 -15.734 22.964 1.00 50.83 ? 411 HOH   C O   1 
HETATM 2480 O  O   . HOH   M 5 .   ? 16.658 -20.204 0.201  1.00 38.34 ? 412 HOH   C O   1 
HETATM 2481 O  O   . HOH   M 5 .   ? 30.735 -31.207 12.950 1.00 43.72 ? 413 HOH   C O   1 
HETATM 2482 O  O   . HOH   M 5 .   ? 17.540 -9.683  29.276 1.00 46.61 ? 414 HOH   C O   1 
HETATM 2483 O  O   . HOH   M 5 .   ? 22.145 -34.849 35.306 1.00 59.78 ? 415 HOH   C O   1 
HETATM 2484 O  O   . HOH   M 5 .   ? -0.683 -34.889 10.274 1.00 50.53 ? 416 HOH   C O   1 
HETATM 2485 O  O   . HOH   M 5 .   ? 18.184 -20.410 25.805 1.00 26.35 ? 417 HOH   C O   1 
HETATM 2486 O  O   . HOH   M 5 .   ? 32.214 -19.455 20.851 1.00 34.65 ? 418 HOH   C O   1 
HETATM 2487 O  O   . HOH   M 5 .   ? 8.488  -23.974 2.813  1.00 31.49 ? 419 HOH   C O   1 
HETATM 2488 O  O   . HOH   M 5 .   ? 2.546  -29.029 27.368 1.00 36.12 ? 420 HOH   C O   1 
HETATM 2489 O  O   . HOH   M 5 .   ? 1.606  -39.014 17.993 1.00 36.08 ? 421 HOH   C O   1 
HETATM 2490 O  O   . HOH   M 5 .   ? 37.954 -14.666 9.210  1.00 47.42 ? 422 HOH   C O   1 
HETATM 2491 O  O   . HOH   M 5 .   ? 9.370  -39.752 12.328 1.00 35.94 ? 423 HOH   C O   1 
HETATM 2492 O  O   . HOH   M 5 .   ? 32.208 -27.085 13.427 1.00 35.18 ? 424 HOH   C O   1 
HETATM 2493 O  O   . HOH   M 5 .   ? 32.843 -9.137  12.064 1.00 41.68 ? 425 HOH   C O   1 
HETATM 2494 O  O   . HOH   M 5 .   ? 25.964 -32.838 16.195 1.00 46.13 ? 426 HOH   C O   1 
HETATM 2495 O  O   . HOH   M 5 .   ? 16.401 -17.406 26.178 1.00 34.58 ? 427 HOH   C O   1 
HETATM 2496 O  O   . HOH   M 5 .   ? 12.944 -19.895 -1.535 1.00 37.91 ? 428 HOH   C O   1 
HETATM 2497 O  O   . HOH   M 5 .   ? 29.664 -8.630  9.114  1.00 33.12 ? 429 HOH   C O   1 
HETATM 2498 O  O   . HOH   M 5 .   ? 5.157  -39.707 23.168 1.00 40.65 ? 430 HOH   C O   1 
HETATM 2499 O  O   . HOH   M 5 .   ? 20.663 -19.627 -3.035 1.00 34.75 ? 431 HOH   C O   1 
HETATM 2500 O  O   . HOH   M 5 .   ? 35.452 -9.727  8.700  1.00 47.46 ? 432 HOH   C 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   ? 0.2932 0.2345 0.2604 0.0069  -0.0159 0.0187  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2806 0.2232 0.2598 0.0052  -0.0184 0.0180  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2687 0.2134 0.2532 0.0036  -0.0185 0.0146  7   SER   A C   
4    O O   . SER   A 1   ? 0.2761 0.2205 0.2543 0.0042  -0.0188 0.0124  7   SER   A O   
5    C CB  . SER   A 1   ? 0.3127 0.2524 0.2918 0.0073  -0.0257 0.0188  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3430 0.2809 0.3162 0.0090  -0.0311 0.0158  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2421 0.1886 0.2379 0.0018  -0.0176 0.0144  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2300 0.1777 0.2313 0.0006  -0.0170 0.0123  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2235 0.1732 0.2342 -0.0008 -0.0124 0.0128  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2381 0.1887 0.2493 -0.0011 -0.0091 0.0137  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2038 0.1539 0.2217 -0.0014 -0.0116 0.0122  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2100 0.1615 0.2349 -0.0019 -0.0064 0.0128  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2071 0.1582 0.2334 -0.0018 -0.0035 0.0123  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2072 0.1571 0.2332 -0.0019 -0.0064 0.0116  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2139 0.1658 0.2508 -0.0022 -0.0077 0.0144  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1826 0.1342 0.2099 -0.0012 0.0023  0.0126  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1806 0.1311 0.2092 -0.0004 0.0064  0.0133  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1785 0.1293 0.2200 -0.0005 0.0096  0.0155  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1915 0.1433 0.2363 -0.0002 0.0115  0.0157  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1855 0.1358 0.2044 0.0016  0.0109  0.0121  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1932 0.1442 0.2018 0.0017  0.0079  0.0097  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1910 0.1391 0.2091 0.0033  0.0156  0.0137  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2219 0.1735 0.2231 0.0035  0.0105  0.0075  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1923 0.1421 0.2426 -0.0010 0.0107  0.0172  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2088 0.1592 0.2741 -0.0012 0.0147  0.0197  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2138 0.1620 0.2781 0.0005  0.0228  0.0221  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2435 0.1898 0.3088 0.0001  0.0227  0.0230  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2074 0.1585 0.2875 -0.0033 0.0088  0.0199  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2219 0.1743 0.3019 -0.0039 0.0009  0.0181  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2212 0.1756 0.3100 -0.0038 0.0008  0.0190  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2349 0.1863 0.3048 -0.0041 -0.0060 0.0159  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2348 0.1897 0.3224 -0.0038 -0.0063 0.0180  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2590 0.2107 0.3265 -0.0038 -0.0125 0.0149  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2674 0.2207 0.3434 -0.0036 -0.0127 0.0162  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3132 0.2662 0.3861 -0.0028 -0.0191 0.0160  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2184 0.1662 0.2784 0.0030  0.0297  0.0230  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2479 0.1927 0.3031 0.0058  0.0380  0.0256  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2614 0.2066 0.3264 0.0073  0.0457  0.0281  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2565 0.2033 0.3210 0.0080  0.0457  0.0263  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2788 0.2218 0.3139 0.0089  0.0388  0.0233  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2897 0.2345 0.3188 0.0095  0.0368  0.0197  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2901 0.2292 0.3182 0.0131  0.0477  0.0264  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2610 0.2048 0.3375 0.0076  0.0523  0.0325  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2531 0.1974 0.3407 0.0092  0.0607  0.0354  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2540 0.2027 0.3569 0.0067  0.0559  0.0337  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2527 0.2036 0.3659 0.0032  0.0477  0.0326  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2587 0.2082 0.3612 0.0090  0.0601  0.0331  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2610 0.2142 0.3767 0.0072  0.0552  0.0315  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2398 0.1933 0.3422 0.0071  0.0484  0.0272  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2450 0.1999 0.3524 0.0075  0.0475  0.0260  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3012 0.2556 0.4303 0.0093  0.0640  0.0338  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3812 0.3367 0.5306 0.0083  0.0695  0.0384  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4279 0.3867 0.5967 0.0049  0.0634  0.0386  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3857 0.3380 0.5308 0.0114  0.0809  0.0421  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2185 0.1706 0.3056 0.0064  0.0433  0.0251  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2110 0.1632 0.2869 0.0061  0.0376  0.0214  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1964 0.1495 0.2700 0.0032  0.0286  0.0204  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2047 0.1571 0.2776 0.0022  0.0272  0.0212  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2295 0.1791 0.2869 0.0090  0.0407  0.0191  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2519 0.1995 0.3061 0.0131  0.0491  0.0191  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2619 0.2102 0.3226 0.0139  0.0506  0.0178  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2780 0.2224 0.3217 0.0167  0.0556  0.0203  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2796 0.2255 0.3364 0.0183  0.0585  0.0173  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2920 0.2337 0.3300 0.0214  0.0635  0.0200  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2993 0.2419 0.3443 0.0222  0.0651  0.0184  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3361 0.2757 0.3746 0.0275  0.0730  0.0175  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1880 0.1420 0.2591 0.0023  0.0232  0.0185  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1883 0.1425 0.2544 0.0004  0.0156  0.0176  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1898 0.1433 0.2429 0.0010  0.0153  0.0151  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1907 0.1441 0.2453 0.0017  0.0169  0.0142  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1953 0.1508 0.2722 -0.0008 0.0096  0.0186  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2208 0.1757 0.2894 -0.0015 0.0026  0.0178  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2206 0.1759 0.2980 -0.0017 -0.0042 0.0190  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2370 0.1910 0.3068 -0.0013 -0.0077 0.0195  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2829 0.2354 0.3443 -0.0009 -0.0135 0.0195  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3025 0.2547 0.3617 -0.0011 -0.0174 0.0183  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2724 0.2232 0.3274 -0.0001 -0.0152 0.0209  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1832 0.1363 0.2253 0.0008  0.0136  0.0137  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1764 0.1294 0.2087 0.0011  0.0132  0.0111  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1719 0.1253 0.2017 -0.0005 0.0080  0.0114  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1872 0.1405 0.2144 -0.0010 0.0050  0.0119  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1911 0.1434 0.2130 0.0027  0.0153  0.0092  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2014 0.1542 0.2163 0.0033  0.0146  0.0058  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2083 0.1591 0.2304 0.0051  0.0210  0.0101  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1668 0.1203 0.1971 -0.0009 0.0072  0.0112  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1848 0.1380 0.2118 -0.0019 0.0035  0.0124  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1769 0.1302 0.2007 -0.0022 0.0051  0.0109  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1825 0.1359 0.2086 -0.0018 0.0078  0.0086  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1960 0.1482 0.2297 -0.0019 0.0005  0.0152  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2416 0.1939 0.2801 -0.0018 -0.0027 0.0162  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2054 0.1573 0.2471 -0.0017 0.0032  0.0154  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1743 0.1274 0.1938 -0.0027 0.0035  0.0122  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1693 0.1225 0.1896 -0.0035 0.0054  0.0116  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1791 0.1305 0.2072 -0.0037 0.0062  0.0132  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1881 0.1380 0.2183 -0.0032 0.0041  0.0165  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1658 0.1185 0.1806 -0.0036 0.0048  0.0140  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1910 0.1452 0.1983 -0.0031 0.0042  0.0124  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2161 0.1696 0.2187 -0.0022 0.0015  0.0130  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2002 0.1566 0.2076 -0.0035 0.0062  0.0098  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1724 0.1239 0.2056 -0.0042 0.0085  0.0106  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1709 0.1202 0.2123 -0.0042 0.0093  0.0117  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1873 0.1343 0.2297 -0.0046 0.0086  0.0169  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2028 0.1477 0.2497 -0.0038 0.0076  0.0198  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1735 0.1228 0.2196 -0.0045 0.0113  0.0071  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1646 0.1112 0.2198 -0.0042 0.0124  0.0070  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1824 0.1285 0.2421 -0.0045 0.0134  0.0016  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1826 0.1258 0.2509 -0.0038 0.0145  -0.0001 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1902 0.1305 0.2671 -0.0050 0.0151  0.0027  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2132 0.1530 0.2901 -0.0066 0.0153  0.0082  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1966 0.1339 0.2816 -0.0042 0.0160  0.0003  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1886 0.1358 0.2262 -0.0052 0.0094  0.0184  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1946 0.1386 0.2311 -0.0048 0.0098  0.0241  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2144 0.1569 0.2438 -0.0027 0.0058  0.0276  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2470 0.1860 0.2742 -0.0013 0.0054  0.0326  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2049 0.1492 0.2392 -0.0057 0.0131  0.0253  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2241 0.1705 0.2482 -0.0049 0.0124  0.0248  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2205 0.1707 0.2436 -0.0056 0.0121  0.0197  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2547 0.1993 0.2689 -0.0031 0.0120  0.0287  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2341 0.1848 0.2480 -0.0045 0.0116  0.0207  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2517 0.1991 0.2596 -0.0029 0.0116  0.0258  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2136 0.1582 0.2394 -0.0023 0.0029  0.0252  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2138 0.1570 0.2349 -0.0004 -0.0020 0.0275  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2287 0.1726 0.2587 -0.0001 -0.0047 0.0267  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2429 0.1863 0.2721 0.0013  -0.0096 0.0276  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2174 0.1619 0.2293 0.0001  -0.0041 0.0255  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2447 0.1888 0.2478 0.0004  -0.0013 0.0264  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2502 0.1953 0.2449 0.0012  -0.0036 0.0240  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2521 0.1920 0.2494 0.0025  -0.0011 0.0318  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2079 0.1529 0.2469 -0.0011 -0.0015 0.0247  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2064 0.1523 0.2550 -0.0006 -0.0025 0.0241  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2136 0.1573 0.2666 0.0010  -0.0064 0.0279  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2291 0.1698 0.2806 0.0016  -0.0059 0.0309  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1987 0.1452 0.2543 -0.0012 0.0022  0.0213  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2229 0.1679 0.2819 0.0019  -0.0104 0.0280  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2364 0.1794 0.3000 0.0040  -0.0157 0.0313  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2482 0.1914 0.3251 0.0044  -0.0133 0.0318  24  THR   A C   
137  O O   . THR   A 18  ? 0.2506 0.1953 0.3326 0.0032  -0.0077 0.0291  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2628 0.2075 0.3293 0.0049  -0.0221 0.0303  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2714 0.2198 0.3499 0.0035  -0.0192 0.0278  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2807 0.2247 0.3341 0.0049  -0.0249 0.0292  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2501 0.1915 0.3328 0.0067  -0.0180 0.0349  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2610 0.2028 0.3580 0.0074  -0.0161 0.0352  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2357 0.1820 0.3444 0.0065  -0.0136 0.0319  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2560 0.2031 0.3722 0.0063  -0.0078 0.0302  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3072 0.2469 0.4091 0.0105  -0.0232 0.0390  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3958 0.3300 0.4861 0.0124  -0.0251 0.0435  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4332 0.3641 0.5220 0.0117  -0.0193 0.0452  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4342 0.3655 0.5149 0.0154  -0.0321 0.0467  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4574 0.3833 0.5359 0.0140  -0.0219 0.0502  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4599 0.3856 0.5319 0.0167  -0.0296 0.0513  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2388 0.1877 0.3485 0.0062  -0.0175 0.0309  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2285 0.1815 0.3504 0.0054  -0.0142 0.0287  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2201 0.1737 0.3360 0.0039  -0.0058 0.0261  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2240 0.1792 0.3486 0.0042  0.0001  0.0249  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2878 0.2429 0.4132 0.0051  -0.0204 0.0281  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4171 0.3761 0.5581 0.0042  -0.0169 0.0269  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4544 0.4156 0.6121 0.0052  -0.0166 0.0276  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4741 0.4339 0.6106 0.0025  -0.0140 0.0253  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1953 0.1472 0.2959 0.0027  -0.0053 0.0252  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1929 0.1451 0.2871 0.0019  0.0015  0.0224  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2022 0.1531 0.3001 0.0028  0.0066  0.0211  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2051 0.1566 0.3046 0.0036  0.0123  0.0188  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1888 0.1398 0.2681 0.0008  0.0006  0.0215  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2336 0.1856 0.3076 0.0002  -0.0029 0.0215  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2256 0.1794 0.3054 0.0000  -0.0015 0.0207  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2285 0.1791 0.2930 0.0000  -0.0067 0.0223  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2028 0.1511 0.3011 0.0031  0.0047  0.0226  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1998 0.1462 0.3024 0.0039  0.0089  0.0209  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2223 0.1699 0.3388 0.0058  0.0113  0.0209  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2335 0.1803 0.3524 0.0071  0.0168  0.0179  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1918 0.1346 0.2931 0.0037  0.0065  0.0234  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1980 0.1395 0.2883 0.0020  0.0073  0.0222  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2103 0.1513 0.2917 0.0011  0.0043  0.0249  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1931 0.1339 0.2814 0.0013  0.0112  0.0179  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2102 0.1506 0.2858 -0.0004 0.0068  0.0229  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2038 0.1441 0.2839 -0.0004 0.0104  0.0183  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1980 0.1381 0.2904 0.0023  0.0150  0.0133  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2110 0.1510 0.2893 -0.0014 0.0128  0.0141  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2024 0.1415 0.2910 0.0017  0.0167  0.0088  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2029 0.1421 0.2856 -0.0004 0.0153  0.0092  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2221 0.1716 0.3479 0.0064  0.0074  0.0238  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2313 0.1828 0.3730 0.0082  0.0099  0.0240  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2426 0.1968 0.3867 0.0084  0.0164  0.0221  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2573 0.2130 0.4138 0.0103  0.0212  0.0219  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2349 0.1881 0.3874 0.0088  0.0028  0.0273  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2253 0.1801 0.3584 0.0070  0.0169  0.0211  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2254 0.1817 0.3588 0.0076  0.0235  0.0201  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2177 0.1716 0.3339 0.0078  0.0273  0.0170  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2144 0.1687 0.3241 0.0078  0.0299  0.0167  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2441 0.2031 0.3820 0.0059  0.0200  0.0221  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2758 0.2376 0.4328 0.0061  0.0163  0.0243  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2838 0.2477 0.4546 0.0073  0.0220  0.0250  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2838 0.2456 0.4420 0.0053  0.0069  0.0255  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2110 0.1622 0.3210 0.0083  0.0271  0.0145  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2087 0.1578 0.3044 0.0086  0.0288  0.0108  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2261 0.1745 0.3164 0.0115  0.0359  0.0082  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2373 0.1846 0.3333 0.0143  0.0410  0.0073  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2133 0.1597 0.3090 0.0086  0.0273  0.0086  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2336 0.1780 0.3175 0.0087  0.0278  0.0038  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2458 0.1915 0.3206 0.0063  0.0240  0.0046  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2324 0.1737 0.3203 0.0085  0.0265  0.0015  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2289 0.1770 0.3066 0.0116  0.0363  0.0070  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2422 0.1884 0.3104 0.0153  0.0425  0.0045  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2442 0.1878 0.3002 0.0164  0.0405  -0.0011 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2665 0.2072 0.3174 0.0202  0.0441  -0.0052 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2584 0.2056 0.3215 0.0151  0.0443  0.0072  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2839 0.2281 0.3329 0.0195  0.0500  0.0049  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2646 0.2142 0.3423 0.0143  0.0469  0.0121  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2208 0.1654 0.2725 0.0134  0.0346  -0.0017 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2259 0.1689 0.2686 0.0141  0.0320  -0.0071 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2002 0.1449 0.2446 0.0099  0.0263  -0.0060 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2140 0.1609 0.2593 0.0076  0.0244  -0.0019 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2476 0.1898 0.2761 0.0171  0.0337  -0.0092 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2591 0.2006 0.2787 0.0176  0.0295  -0.0146 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2824 0.2213 0.2972 0.0207  0.0286  -0.0213 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2432 0.1870 0.2585 0.0153  0.0252  -0.0143 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2834 0.2232 0.2931 0.0200  0.0234  -0.0252 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2621 0.2050 0.2715 0.0170  0.0219  -0.0207 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2414 0.1878 0.2574 0.0124  0.0237  -0.0098 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2596 0.2047 0.2652 0.0156  0.0175  -0.0222 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2556 0.2036 0.2664 0.0113  0.0199  -0.0112 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2502 0.1979 0.2565 0.0128  0.0171  -0.0171 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2157 0.1594 0.2609 0.0092  0.0237  -0.0099 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2105 0.1556 0.2571 0.0057  0.0197  -0.0088 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2016 0.1460 0.2458 0.0060  0.0176  -0.0148 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2098 0.1517 0.2547 0.0084  0.0182  -0.0200 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2210 0.1657 0.2778 0.0032  0.0186  -0.0043 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2273 0.1691 0.2930 0.0042  0.0200  -0.0059 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2487 0.1884 0.3179 0.0035  0.0187  -0.0105 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2934 0.2303 0.3667 0.0055  0.0201  -0.0146 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2295 0.1703 0.2983 0.0011  0.0166  -0.0104 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2012 0.1478 0.2441 0.0037  0.0149  -0.0145 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1917 0.1384 0.2357 0.0035  0.0123  -0.0203 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1964 0.1450 0.2465 -0.0003 0.0110  -0.0172 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1989 0.1500 0.2439 -0.0012 0.0105  -0.0143 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2086 0.1560 0.2413 0.0067  0.0110  -0.0249 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3018 0.2496 0.3358 0.0073  0.0070  -0.0321 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3327 0.2815 0.3776 0.0041  0.0055  -0.0326 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3123 0.2593 0.3366 0.0114  0.0053  -0.0372 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2046 0.1515 0.2656 -0.0023 0.0111  -0.0173 36  SER   A N   
241  C CA  A SER   A 30  ? 0.2138 0.1617 0.2812 -0.0055 0.0114  -0.0134 36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2114 0.1594 0.2788 -0.0055 0.0114  -0.0134 36  SER   A CA  
243  C C   . SER   A 30  ? 0.2168 0.1682 0.2836 -0.0062 0.0096  -0.0170 36  SER   A C   
244  O O   . SER   A 30  ? 0.2350 0.1885 0.3012 -0.0079 0.0105  -0.0129 36  SER   A O   
245  C CB  A SER   A 30  ? 0.2441 0.1888 0.3247 -0.0071 0.0125  -0.0131 36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2348 0.1795 0.3152 -0.0072 0.0125  -0.0128 36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2902 0.2355 0.3775 -0.0100 0.0139  -0.0092 36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2698 0.2131 0.3561 -0.0063 0.0108  -0.0207 36  SER   A OG  
249  N N   . SER   A 31  ? 0.2149 0.1666 0.2811 -0.0043 0.0068  -0.0248 37  SER   A N   
250  C CA  . SER   A 31  ? 0.2180 0.1734 0.2851 -0.0046 0.0041  -0.0287 37  SER   A CA  
251  C C   . SER   A 31  ? 0.2157 0.1739 0.2707 -0.0034 0.0040  -0.0261 37  SER   A C   
252  O O   . SER   A 31  ? 0.2397 0.2014 0.2965 -0.0041 0.0026  -0.0274 37  SER   A O   
253  C CB  . SER   A 31  ? 0.2656 0.2205 0.3342 -0.0021 -0.0003 -0.0383 37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3344 0.2882 0.3884 0.0024  -0.0017 -0.0413 37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1860 0.1429 0.2305 -0.0016 0.0054  -0.0228 38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1769 0.1358 0.2110 -0.0006 0.0053  -0.0204 38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1816 0.1404 0.2145 -0.0026 0.0076  -0.0130 38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1834 0.1435 0.2089 -0.0020 0.0074  -0.0109 38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1869 0.1439 0.2102 0.0032  0.0055  -0.0219 38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2131 0.1693 0.2327 0.0067  0.0027  -0.0294 38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2334 0.1867 0.2410 0.0110  0.0044  -0.0296 38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2173 0.1717 0.2161 0.0120  0.0051  -0.0260 38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2377 0.1900 0.2246 0.0163  0.0058  -0.0269 38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2530 0.2021 0.2336 0.0207  0.0058  -0.0314 38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2362 0.1892 0.2169 0.0168  0.0064  -0.0233 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1719 0.1288 0.2115 -0.0044 0.0093  -0.0093 39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1655 0.1217 0.2029 -0.0053 0.0104  -0.0028 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1663 0.1218 0.1966 -0.0036 0.0099  -0.0013 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1813 0.1370 0.2071 -0.0038 0.0093  0.0023  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1744 0.1323 0.2095 -0.0064 0.0109  0.0001  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1961 0.1522 0.2269 -0.0065 0.0113  0.0063  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1975 0.1509 0.2323 -0.0068 0.0117  0.0095  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1847 0.1418 0.2081 -0.0060 0.0107  0.0078  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1673 0.1216 0.1976 -0.0019 0.0105  -0.0040 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1566 0.1104 0.1830 -0.0004 0.0113  -0.0021 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1588 0.1106 0.1918 0.0001  0.0130  -0.0007 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1719 0.1223 0.2096 0.0006  0.0139  -0.0034 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1776 0.1314 0.1965 0.0023  0.0121  -0.0055 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1894 0.1450 0.2011 0.0026  0.0104  -0.0063 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2066 0.1613 0.2101 0.0062  0.0113  -0.0092 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1900 0.1462 0.2003 0.0012  0.0096  -0.0019 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1618 0.1136 0.1958 0.0002  0.0131  0.0029  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1619 0.1126 0.2033 0.0011  0.0149  0.0043  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1706 0.1219 0.2115 0.0020  0.0162  0.0062  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1708 0.1231 0.2085 0.0011  0.0140  0.0080  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1611 0.1110 0.2098 -0.0003 0.0128  0.0079  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1746 0.1236 0.2330 0.0008  0.0143  0.0093  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1965 0.1434 0.2615 0.0001  0.0129  0.0112  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1950 0.1453 0.2574 0.0008  0.0128  0.0127  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1760 0.1266 0.2204 0.0041  0.0203  0.0056  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1975 0.1486 0.2445 0.0051  0.0231  0.0080  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2059 0.1572 0.2659 0.0053  0.0247  0.0102  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2111 0.1612 0.2741 0.0068  0.0272  0.0085  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2127 0.1622 0.2511 0.0082  0.0281  0.0059  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2205 0.1701 0.2636 0.0092  0.0325  0.0094  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2094 0.1589 0.2358 0.0083  0.0256  0.0037  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2102 0.1631 0.2785 0.0041  0.0228  0.0135  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1991 0.1530 0.2822 0.0044  0.0237  0.0157  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2126 0.1677 0.3033 0.0050  0.0280  0.0178  43  SER   A C   
300  O O   . SER   A 37  ? 0.2045 0.1592 0.2891 0.0047  0.0288  0.0181  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2171 0.1718 0.3065 0.0026  0.0164  0.0177  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2259 0.1814 0.3125 0.0011  0.0116  0.0186  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2251 0.1815 0.3304 0.0060  0.0313  0.0194  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2412 0.1988 0.3567 0.0065  0.0365  0.0219  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2495 0.2097 0.3794 0.0040  0.0302  0.0239  44  SER   A C   
306  O O   . SER   A 38  ? 0.2534 0.2147 0.3886 0.0029  0.0229  0.0238  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2786 0.2363 0.4027 0.0094  0.0451  0.0225  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2896 0.2487 0.4252 0.0092  0.0415  0.0224  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2533 0.2140 0.3893 0.0032  0.0328  0.0258  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2798 0.2428 0.4308 0.0009  0.0263  0.0268  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3129 0.2780 0.4849 0.0011  0.0332  0.0297  45  THR   A C   
312  O O   . THR   A 39  ? 0.3229 0.2868 0.4932 0.0032  0.0439  0.0315  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2976 0.2589 0.4387 -0.0008 0.0224  0.0261  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3128 0.2724 0.4512 0.0001  0.0311  0.0280  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3018 0.2610 0.4222 -0.0008 0.0175  0.0237  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3289 0.2970 0.5208 -0.0007 0.0269  0.0301  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3427 0.3134 0.5587 -0.0011 0.0329  0.0329  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3587 0.3280 0.5781 -0.0030 0.0342  0.0341  46  THR   A C   
319  O O   . THR   A 40  ? 0.3747 0.3444 0.6078 -0.0028 0.0437  0.0375  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3607 0.3357 0.5995 -0.0018 0.0251  0.0322  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3828 0.3573 0.6174 -0.0035 0.0114  0.0294  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3671 0.3432 0.6065 0.0005  0.0263  0.0320  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3466 0.3139 0.5541 -0.0046 0.0253  0.0317  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3462 0.3116 0.5567 -0.0063 0.0256  0.0324  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3525 0.3136 0.5397 -0.0049 0.0325  0.0334  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3561 0.3159 0.5227 -0.0033 0.0322  0.0317  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3489 0.3143 0.5603 -0.0084 0.0117  0.0286  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3380 0.2968 0.5295 -0.0054 0.0383  0.0360  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3597 0.3140 0.5300 -0.0034 0.0444  0.0374  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3625 0.3149 0.5168 -0.0046 0.0346  0.0336  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3695 0.3224 0.5334 -0.0071 0.0259  0.0315  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4073 0.3591 0.5885 -0.0032 0.0544  0.0424  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5104 0.4582 0.6741 0.0010  0.0667  0.0460  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6247 0.5743 0.7900 0.0039  0.0746  0.0473  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6508 0.6044 0.8378 0.0026  0.0752  0.0479  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6574 0.6040 0.8001 0.0082  0.0803  0.0472  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3523 0.3027 0.4831 -0.0025 0.0356  0.0323  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3397 0.2888 0.4551 -0.0032 0.0273  0.0288  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3537 0.2995 0.4662 -0.0036 0.0272  0.0294  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3769 0.3203 0.4943 -0.0027 0.0353  0.0333  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3264 0.2714 0.4297 -0.0045 0.0184  0.0257  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3141 0.2557 0.4144 -0.0049 0.0164  0.0252  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3176 0.2567 0.3975 -0.0024 0.0200  0.0254  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3249 0.2606 0.4029 -0.0021 0.0205  0.0261  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3142 0.2562 0.4163 -0.0067 0.0049  0.0207  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3436 0.2877 0.4275 -0.0057 -0.0019 0.0169  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2973 0.2378 0.3626 -0.0005 0.0215  0.0244  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2819 0.2210 0.3283 0.0020  0.0225  0.0233  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2817 0.2183 0.3200 0.0056  0.0315  0.0263  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3149 0.2517 0.3603 0.0063  0.0376  0.0290  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2595 0.2017 0.2960 0.0019  0.0176  0.0195  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3006 0.2440 0.3391 -0.0003 0.0091  0.0167  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3168 0.2581 0.3534 -0.0006 0.0057  0.0155  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2677 0.2135 0.3089 -0.0013 0.0057  0.0156  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2743 0.2085 0.2973 0.0083  0.0321  0.0258  52  THR   A N   
356  C CA  . THR   A 46  ? 0.2941 0.2251 0.3037 0.0131  0.0385  0.0279  52  THR   A CA  
357  C C   . THR   A 46  ? 0.2714 0.2045 0.2659 0.0148  0.0341  0.0232  52  THR   A C   
358  O O   . THR   A 46  ? 0.2663 0.2012 0.2587 0.0132  0.0278  0.0201  52  THR   A O   
359  C CB  . THR   A 46  ? 0.3640 0.2901 0.3710 0.0147  0.0405  0.0310  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4281 0.3516 0.4492 0.0138  0.0468  0.0361  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3994 0.3219 0.3877 0.0204  0.0440  0.0319  52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2530 0.1857 0.2380 0.0184  0.0375  0.0224  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2364 0.1712 0.2099 0.0199  0.0328  0.0174  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2308 0.1624 0.1904 0.0245  0.0332  0.0174  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2481 0.1751 0.2014 0.0287  0.0393  0.0211  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2369 0.1727 0.2078 0.0215  0.0349  0.0153  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2491 0.1875 0.2346 0.0177  0.0354  0.0161  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2358 0.1742 0.1985 0.0224  0.0293  0.0095  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2576 0.1999 0.2502 0.0129  0.0281  0.0139  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2191 0.1529 0.1735 0.0243  0.0270  0.0137  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2179 0.1493 0.1595 0.0290  0.0259  0.0130  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2340 0.1643 0.1640 0.0340  0.0268  0.0104  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2303 0.1637 0.1625 0.0328  0.0250  0.0065  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2236 0.1589 0.1652 0.0274  0.0188  0.0088  54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2502 0.1755 0.1669 0.0402  0.0293  0.0123  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2587 0.1822 0.1619 0.0461  0.0288  0.0089  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2805 0.2029 0.1727 0.0505  0.0237  0.0071  55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3034 0.2201 0.1860 0.0553  0.0269  0.0115  55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2718 0.1893 0.1676 0.0507  0.0377  0.0136  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2701 0.1891 0.1792 0.0465  0.0433  0.0160  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3077 0.2314 0.2225 0.0437  0.0395  0.0101  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3029 0.2277 0.2310 0.0401  0.0448  0.0130  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3083 0.2372 0.2461 0.0362  0.0422  0.0097  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2955 0.2277 0.2320 0.0351  0.0350  0.0036  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2914 0.2211 0.2413 0.0336  0.0470  0.0126  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2709 0.1987 0.1661 0.0488  0.0159  0.0009  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2880 0.2164 0.1778 0.0517  0.0101  -0.0012 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2789 0.2138 0.1736 0.0502  0.0022  -0.0088 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2853 0.2240 0.1883 0.0463  0.0014  -0.0120 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2848 0.2132 0.1824 0.0480  0.0112  0.0030  56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2465 0.1822 0.1619 0.0393  0.0086  0.0006  56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2907 0.2271 0.1822 0.0531  -0.0035 -0.0115 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3014 0.2447 0.2012 0.0512  -0.0106 -0.0183 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2948 0.2421 0.2041 0.0476  -0.0122 -0.0176 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2982 0.2503 0.2121 0.0482  -0.0178 -0.0222 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3512 0.2940 0.2412 0.0581  -0.0173 -0.0239 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4850 0.4241 0.3640 0.0643  -0.0192 -0.0217 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5019 0.4375 0.3797 0.0636  -0.0142 -0.0151 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5769 0.5162 0.4489 0.0702  -0.0262 -0.0267 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2688 0.2145 0.1823 0.0438  -0.0073 -0.0122 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2447 0.1935 0.1662 0.0408  -0.0087 -0.0120 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2459 0.2019 0.1783 0.0368  -0.0115 -0.0166 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2339 0.1917 0.1713 0.0337  -0.0104 -0.0178 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2244 0.1703 0.1497 0.0370  -0.0039 -0.0068 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2643 0.2019 0.1811 0.0410  -0.0001 -0.0007 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2214 0.1813 0.1587 0.0370  -0.0145 -0.0188 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2122 0.1788 0.1613 0.0331  -0.0157 -0.0220 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2005 0.1680 0.1539 0.0305  -0.0134 -0.0198 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1974 0.1701 0.1593 0.0287  -0.0138 -0.0219 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2419 0.2137 0.1959 0.0357  -0.0211 -0.0277 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2954 0.2676 0.2487 0.0370  -0.0240 -0.0317 59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3573 0.3353 0.3187 0.0391  -0.0303 -0.0381 59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3735 0.3501 0.3278 0.0447  -0.0357 -0.0413 59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3008 0.2852 0.2777 0.0348  -0.0298 -0.0400 59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1926 0.1547 0.1404 0.0308  -0.0111 -0.0156 60  THR   A N   
416  C CA  . THR   A 54  ? 0.2027 0.1644 0.1534 0.0284  -0.0093 -0.0140 60  THR   A CA  
417  C C   . THR   A 54  ? 0.2011 0.1578 0.1501 0.0259  -0.0064 -0.0101 60  THR   A C   
418  O O   . THR   A 54  ? 0.2152 0.1680 0.1602 0.0270  -0.0050 -0.0078 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2386 0.1988 0.1869 0.0318  -0.0107 -0.0142 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2832 0.2368 0.2242 0.0346  -0.0101 -0.0109 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2361 0.2014 0.1874 0.0349  -0.0142 -0.0181 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1917 0.1487 0.1442 0.0228  -0.0055 -0.0096 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1914 0.1441 0.1443 0.0204  -0.0039 -0.0066 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1795 0.1328 0.1346 0.0182  -0.0043 -0.0072 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1866 0.1422 0.1413 0.0192  -0.0049 -0.0093 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1754 0.1260 0.1322 0.0157  -0.0042 -0.0054 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1705 0.1203 0.1272 0.0144  -0.0055 -0.0061 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1773 0.1281 0.1369 0.0117  -0.0051 -0.0047 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1850 0.1343 0.1479 0.0106  -0.0045 -0.0028 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1957 0.1400 0.1526 0.0149  -0.0074 -0.0059 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2197 0.1623 0.1754 0.0141  -0.0099 -0.0073 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2037 0.1464 0.1580 0.0179  -0.0076 -0.0071 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1736 0.1262 0.1317 0.0111  -0.0052 -0.0052 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1724 0.1250 0.1327 0.0090  -0.0052 -0.0035 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1797 0.1294 0.1361 0.0094  -0.0078 -0.0036 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1897 0.1382 0.1408 0.0113  -0.0086 -0.0053 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1715 0.1283 0.1338 0.0082  -0.0026 -0.0031 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1710 0.1296 0.1303 0.0091  -0.0009 -0.0034 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1815 0.1425 0.1400 0.0108  0.0004  -0.0054 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1813 0.1392 0.1390 0.0085  0.0000  -0.0014 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1872 0.1500 0.1440 0.0119  0.0032  -0.0054 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1900 0.1492 0.1446 0.0097  0.0030  -0.0009 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1993 0.1611 0.1540 0.0113  0.0050  -0.0029 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2193 0.1824 0.1717 0.0129  0.0092  -0.0020 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1797 0.1281 0.1388 0.0079  -0.0096 -0.0020 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1901 0.1354 0.1448 0.0088  -0.0131 -0.0023 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1904 0.1371 0.1404 0.0094  -0.0109 -0.0006 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1903 0.1392 0.1449 0.0077  -0.0087 0.0017  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1854 0.1283 0.1464 0.0074  -0.0171 -0.0016 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2063 0.1458 0.1621 0.0091  -0.0224 -0.0027 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2193 0.1553 0.1692 0.0113  -0.0260 -0.0060 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2247 0.1639 0.1804 0.0090  -0.0241 -0.0007 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2443 0.1765 0.1869 0.0138  -0.0314 -0.0077 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2407 0.1762 0.1892 0.0115  -0.0295 -0.0018 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2570 0.1890 0.1986 0.0140  -0.0334 -0.0056 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3094 0.2371 0.2421 0.0173  -0.0396 -0.0074 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.2013 0.1460 0.1419 0.0121  -0.0114 -0.0015 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1976 0.1426 0.1322 0.0134  -0.0082 0.0009  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2248 0.1647 0.1507 0.0159  -0.0128 0.0013  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2335 0.1700 0.1500 0.0191  -0.0154 -0.0012 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2003 0.1470 0.1301 0.0155  -0.0037 -0.0001 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2297 0.1760 0.1517 0.0178  0.0021  0.0036  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2200 0.1593 0.1488 0.0148  -0.0145 0.0041  66  SER   A N   
464  C CA  . SER   A 60  ? 0.2353 0.1698 0.1565 0.0175  -0.0201 0.0043  66  SER   A CA  
465  C C   . SER   A 60  ? 0.2375 0.1687 0.1432 0.0221  -0.0181 0.0055  66  SER   A C   
466  O O   . SER   A 60  ? 0.2543 0.1805 0.1496 0.0258  -0.0240 0.0035  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2707 0.2056 0.1991 0.0158  -0.0219 0.0073  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3474 0.2841 0.2765 0.0150  -0.0157 0.0115  66  SER   A OG  
469  N N   . SER   A 61  ? 0.2219 0.1555 0.1261 0.0221  -0.0099 0.0087  67  SER   A N   
470  C CA  . SER   A 61  ? 0.2378 0.1681 0.1274 0.0268  -0.0059 0.0108  67  SER   A CA  
471  C C   . SER   A 61  ? 0.2376 0.1660 0.1174 0.0303  -0.0063 0.0065  67  SER   A C   
472  O O   . SER   A 61  ? 0.2488 0.1737 0.1144 0.0351  -0.0028 0.0078  67  SER   A O   
473  C CB  . SER   A 61  ? 0.2615 0.1950 0.1550 0.0257  0.0038  0.0157  67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2596 0.1989 0.1637 0.0228  0.0082  0.0138  67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2289 0.1591 0.1157 0.0283  -0.0097 0.0018  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2328 0.1605 0.1116 0.0316  -0.0110 -0.0028 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2486 0.1731 0.1301 0.0312  -0.0207 -0.0078 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2679 0.1896 0.1442 0.0337  -0.0230 -0.0124 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2446 0.1777 0.1317 0.0298  -0.0050 -0.0036 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2495 0.1863 0.1367 0.0304  0.0046  0.0003  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2655 0.1984 0.1369 0.0363  0.0083  0.0003  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.2918 0.2280 0.1647 0.0370  0.0186  0.0048  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.2907 0.2253 0.1595 0.0378  0.0233  0.0105  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.2905 0.2205 0.1531 0.0382  0.0178  0.0123  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.2804 0.2181 0.1531 0.0382  0.0335  0.0147  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2710 0.1957 0.1618 0.0281  -0.0259 -0.0071 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2859 0.2084 0.1838 0.0269  -0.0339 -0.0113 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2817 0.2056 0.1861 0.0254  -0.0325 -0.0143 69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3019 0.2218 0.2050 0.0270  -0.0378 -0.0190 69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3289 0.2447 0.2153 0.0315  -0.0424 -0.0153 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3896 0.3038 0.2747 0.0322  -0.0472 -0.0131 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4174 0.3251 0.2950 0.0364  -0.0583 -0.0184 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4389 0.3444 0.3093 0.0391  -0.0620 -0.0156 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4599 0.3598 0.3098 0.0457  -0.0639 -0.0158 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4648 0.3608 0.2996 0.0503  -0.0625 -0.0193 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4476 0.3453 0.2910 0.0483  -0.0667 -0.0122 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2526 0.1817 0.1633 0.0229  -0.0254 -0.0118 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2461 0.1763 0.1614 0.0224  -0.0237 -0.0141 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2275 0.1628 0.1541 0.0187  -0.0196 -0.0114 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2279 0.1666 0.1570 0.0170  -0.0162 -0.0082 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.2999 0.2310 0.2061 0.0258  -0.0185 -0.0149 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4170 0.3425 0.3114 0.0305  -0.0219 -0.0193 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5120 0.4395 0.4012 0.0334  -0.0153 -0.0199 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5863 0.5081 0.4647 0.0383  -0.0181 -0.0250 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6259 0.5433 0.4879 0.0431  -0.0184 -0.0252 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2284 0.1635 0.1608 0.0180  -0.0199 -0.0129 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2126 0.1517 0.1525 0.0159  -0.0160 -0.0109 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2242 0.1661 0.1610 0.0179  -0.0121 -0.0120 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2560 0.1954 0.1876 0.0207  -0.0131 -0.0148 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2080 0.1447 0.1556 0.0146  -0.0180 -0.0111 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2275 0.1621 0.1814 0.0124  -0.0214 -0.0101 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2617 0.1985 0.2233 0.0099  -0.0193 -0.0069 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2535 0.1839 0.2083 0.0128  -0.0271 -0.0123 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2464 0.1808 0.2143 0.0086  -0.0234 -0.0070 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2910 0.2217 0.2553 0.0102  -0.0286 -0.0103 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1956 0.1426 0.1365 0.0168  -0.0082 -0.0103 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.1856 0.1362 0.1264 0.0186  -0.0051 -0.0115 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.1933 0.1465 0.1402 0.0180  -0.0046 -0.0112 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1939 0.1485 0.1448 0.0158  -0.0043 -0.0095 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.1951 0.1500 0.1360 0.0184  -0.0007 -0.0102 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2209 0.1733 0.1533 0.0205  0.0004  -0.0099 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2455 0.1965 0.1717 0.0240  0.0014  -0.0123 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2305 0.1817 0.1603 0.0195  0.0007  -0.0073 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2709 0.2187 0.1868 0.0269  0.0028  -0.0121 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2393 0.1873 0.1588 0.0223  0.0017  -0.0067 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2716 0.2180 0.1836 0.0262  0.0032  -0.0091 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3082 0.2507 0.2076 0.0299  0.0047  -0.0084 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.1858 0.1397 0.1329 0.0203  -0.0045 -0.0130 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1971 0.1534 0.1482 0.0207  -0.0045 -0.0128 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2250 0.1879 0.1808 0.0204  -0.0023 -0.0134 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2599 0.2258 0.2167 0.0209  0.0001  -0.0142 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2157 0.1699 0.1651 0.0239  -0.0056 -0.0145 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2272 0.1814 0.1735 0.0253  -0.0045 -0.0165 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.1960 0.1482 0.1390 0.0233  -0.0046 -0.0154 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1938 0.1587 0.1529 0.0198  -0.0029 -0.0132 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1873 0.1582 0.1529 0.0191  -0.0019 -0.0146 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1854 0.1579 0.1526 0.0212  -0.0045 -0.0164 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1908 0.1593 0.1531 0.0224  -0.0060 -0.0154 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2130 0.1845 0.1813 0.0158  -0.0004 -0.0129 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2148 0.1860 0.1821 0.0145  0.0024  -0.0112 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2280 0.1951 0.1931 0.0147  -0.0017 -0.0110 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1863 0.1646 0.1608 0.0219  -0.0049 -0.0191 75  SER   A N   
543  C CA  . SER   A 69  ? 0.1908 0.1714 0.1677 0.0240  -0.0085 -0.0219 75  SER   A CA  
544  C C   . SER   A 69  ? 0.1910 0.1749 0.1754 0.0209  -0.0077 -0.0229 75  SER   A C   
545  O O   . SER   A 69  ? 0.2012 0.1885 0.1933 0.0185  -0.0046 -0.0226 75  SER   A O   
546  C CB  . SER   A 69  ? 0.2078 0.1934 0.1910 0.0268  -0.0103 -0.0251 75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2733 0.2554 0.2499 0.0298  -0.0111 -0.0242 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1688 0.1507 0.1505 0.0211  -0.0098 -0.0235 76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1704 0.1542 0.1591 0.0181  -0.0090 -0.0245 76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1807 0.1664 0.1722 0.0203  -0.0136 -0.0292 76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1918 0.1754 0.1753 0.0245  -0.0172 -0.0307 76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1707 0.1499 0.1545 0.0156  -0.0063 -0.0207 76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1778 0.1516 0.1512 0.0177  -0.0070 -0.0189 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1828 0.1530 0.1505 0.0181  -0.0058 -0.0158 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1843 0.1560 0.1543 0.0193  -0.0083 -0.0201 76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1839 0.1489 0.1443 0.0198  -0.0054 -0.0135 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1875 0.1540 0.1483 0.0215  -0.0074 -0.0176 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1844 0.1477 0.1414 0.0215  -0.0057 -0.0140 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1709 0.1600 0.1735 0.0178  -0.0138 -0.0317 77  SER   A N   
560  C CA  . SER   A 71  ? 0.1855 0.1760 0.1915 0.0199  -0.0191 -0.0373 77  SER   A CA  
561  C C   . SER   A 71  ? 0.1983 0.1832 0.1935 0.0213  -0.0198 -0.0371 77  SER   A C   
562  O O   . SER   A 71  ? 0.2099 0.1910 0.2000 0.0191  -0.0155 -0.0325 77  SER   A O   
563  C CB  . SER   A 71  ? 0.1838 0.1794 0.2072 0.0166  -0.0190 -0.0403 77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2054 0.1990 0.2313 0.0124  -0.0140 -0.0366 77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1968 0.1810 0.1885 0.0253  -0.0253 -0.0422 78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2182 0.1969 0.1993 0.0274  -0.0253 -0.0425 78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2229 0.2017 0.2127 0.0231  -0.0228 -0.0428 78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2174 0.2006 0.2220 0.0198  -0.0235 -0.0452 78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2497 0.2277 0.2247 0.0334  -0.0325 -0.0489 78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2907 0.2669 0.2542 0.0386  -0.0347 -0.0476 78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3590 0.3331 0.3130 0.0458  -0.0423 -0.0538 78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.4440 0.4158 0.3863 0.0515  -0.0444 -0.0518 78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5092 0.4783 0.4400 0.0595  -0.0522 -0.0575 78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2254 0.1992 0.2071 0.0235  -0.0201 -0.0408 79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2295 0.2028 0.2195 0.0197  -0.0177 -0.0407 79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2246 0.2006 0.2255 0.0197  -0.0226 -0.0480 79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2331 0.2079 0.2283 0.0244  -0.0280 -0.0539 79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2499 0.2174 0.2281 0.0221  -0.0150 -0.0387 79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2757 0.2407 0.2414 0.0252  -0.0135 -0.0346 79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2392 0.2073 0.2050 0.0273  -0.0180 -0.0374 79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2024 0.1813 0.2189 0.0147  -0.0207 -0.0476 80  SER   A N   
582  C CA  . SER   A 74  ? 0.2174 0.1988 0.2479 0.0140  -0.0252 -0.0546 80  SER   A CA  
583  C C   . SER   A 74  ? 0.2262 0.2077 0.2708 0.0087  -0.0211 -0.0524 80  SER   A C   
584  O O   . SER   A 74  ? 0.2196 0.1993 0.2618 0.0060  -0.0151 -0.0454 80  SER   A O   
585  C CB  . SER   A 74  ? 0.2639 0.2512 0.3038 0.0145  -0.0292 -0.0580 80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3137 0.3047 0.3645 0.0099  -0.0239 -0.0528 80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2278 0.2111 0.2878 0.0074  -0.0247 -0.0585 81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2508 0.2338 0.3265 0.0025  -0.0209 -0.0567 81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2675 0.2557 0.3577 -0.0013 -0.0173 -0.0531 81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2889 0.2819 0.3904 -0.0009 -0.0213 -0.0581 81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2707 0.2532 0.3583 0.0031  -0.0269 -0.0658 81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.3217 0.2982 0.4020 0.0051  -0.0280 -0.0688 81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3432 0.3195 0.4359 0.0063  -0.0355 -0.0794 81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3281 0.3015 0.4123 0.0012  -0.0209 -0.0618 81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2618 0.2489 0.3522 -0.0045 -0.0098 -0.0447 82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2725 0.2635 0.3737 -0.0074 -0.0047 -0.0400 82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2732 0.2621 0.3857 -0.0113 0.0014  -0.0348 82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2571 0.2410 0.3616 -0.0117 0.0036  -0.0310 82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3086 0.3000 0.3946 -0.0058 -0.0018 -0.0344 82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3424 0.3366 0.4215 -0.0020 -0.0074 -0.0394 82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3162 0.3098 0.4093 -0.0082 0.0052  -0.0282 82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3750 0.3676 0.4379 0.0001  -0.0062 -0.0355 82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2690 0.2614 0.4014 -0.0142 0.0044  -0.0345 83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2804 0.2701 0.4239 -0.0177 0.0113  -0.0285 83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.2992 0.2863 0.4297 -0.0177 0.0186  -0.0185 83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3099 0.2997 0.4338 -0.0164 0.0210  -0.0158 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2821 0.2762 0.4517 -0.0208 0.0136  -0.0301 83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2992 0.2901 0.4815 -0.0242 0.0217  -0.0230 83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3225 0.3134 0.5041 -0.0250 0.0311  -0.0138 83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3137 0.3006 0.5074 -0.0262 0.0203  -0.0253 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3316 0.3187 0.5236 -0.0275 0.0392  -0.0064 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3237 0.3069 0.5295 -0.0292 0.0282  -0.0181 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3192 0.3024 0.5234 -0.0297 0.0378  -0.0083 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3066 0.2880 0.4335 -0.0187 0.0218  -0.0133 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.3189 0.2966 0.4339 -0.0183 0.0277  -0.0041 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.3242 0.2983 0.4518 -0.0208 0.0340  0.0018  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.3167 0.2878 0.4528 -0.0222 0.0322  -0.0004 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.3286 0.3022 0.4252 -0.0162 0.0243  -0.0032 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.3533 0.3230 0.4380 -0.0153 0.0290  0.0055  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.3284 0.3047 0.4134 -0.0136 0.0188  -0.0084 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.3410 0.3144 0.4683 -0.0208 0.0417  0.0095  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.3542 0.3236 0.4925 -0.0227 0.0490  0.0165  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.3587 0.3210 0.4878 -0.0219 0.0485  0.0209  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.3517 0.3126 0.4634 -0.0197 0.0438  0.0202  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.4181 0.3876 0.5533 -0.0216 0.0580  0.0246  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.5386 0.5153 0.6889 -0.0227 0.0603  0.0211  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.6948 0.6711 0.8497 -0.0223 0.0718  0.0298  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.7206 0.6916 0.8816 -0.0233 0.0788  0.0372  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.7379 0.7187 0.8896 -0.0207 0.0743  0.0294  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.3566 0.3145 0.4986 -0.0238 0.0533  0.0256  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.3694 0.3204 0.5035 -0.0227 0.0529  0.0303  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.3911 0.3388 0.5032 -0.0191 0.0551  0.0381  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.3992 0.3479 0.5051 -0.0177 0.0603  0.0426  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.3706 0.3168 0.5223 -0.0250 0.0587  0.0352  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.3922 0.3360 0.4925 -0.0173 0.0507  0.0390  87  SER   A N   
636  C CA  . SER   A 81  ? 0.4070 0.3472 0.4874 -0.0136 0.0509  0.0454  87  SER   A CA  
637  C C   . SER   A 81  ? 0.4217 0.3555 0.5010 -0.0126 0.0497  0.0497  87  SER   A C   
638  O O   . SER   A 81  ? 0.4259 0.3581 0.5202 -0.0149 0.0494  0.0478  87  SER   A O   
639  C CB  . SER   A 81  ? 0.4232 0.3670 0.4891 -0.0119 0.0442  0.0401  87  SER   A CB  
640  O OG  . SER   A 81  ? 0.4198 0.3638 0.4874 -0.0125 0.0379  0.0348  87  SER   A OG  
641  N N   . GLU   A 82  ? 0.4337 0.3636 0.4957 -0.0088 0.0482  0.0551  88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.4513 0.3754 0.5110 -0.0071 0.0461  0.0593  88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.4410 0.3670 0.5068 -0.0084 0.0393  0.0523  88  GLU   A C   
644  O O   . GLU   A 82  ? 0.4422 0.3641 0.5139 -0.0082 0.0385  0.0544  88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.5195 0.4397 0.5585 -0.0022 0.0442  0.0652  88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.6153 0.5398 0.6415 -0.0009 0.0384  0.0599  88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7546 0.6763 0.7612 0.0036  0.0386  0.0646  88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.8030 0.7198 0.7988 0.0073  0.0346  0.0684  88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7883 0.7125 0.7903 0.0038  0.0424  0.0639  88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.4260 0.3579 0.4905 -0.0095 0.0350  0.0443  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.4102 0.3437 0.4785 -0.0101 0.0297  0.0379  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.3722 0.3084 0.4549 -0.0129 0.0297  0.0305  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.3606 0.2959 0.4486 -0.0130 0.0270  0.0265  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.4208 0.3579 0.4768 -0.0086 0.0248  0.0344  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.4600 0.3944 0.5034 -0.0055 0.0220  0.0394  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.4898 0.4246 0.5201 -0.0037 0.0218  0.0414  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.4893 0.4206 0.5341 -0.0041 0.0189  0.0413  89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.5150 0.4471 0.5335 -0.0005 0.0178  0.0447  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.5178 0.4470 0.5522 -0.0010 0.0149  0.0449  89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.5419 0.4714 0.5629 0.0008  0.0140  0.0464  89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.5879 0.5147 0.5984 0.0043  0.0090  0.0493  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.3532 0.2925 0.4424 -0.0149 0.0324  0.0283  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.3309 0.2729 0.4333 -0.0170 0.0308  0.0201  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.3334 0.2756 0.4517 -0.0197 0.0354  0.0209  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.3287 0.2717 0.4454 -0.0198 0.0401  0.0260  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.3097 0.2574 0.4050 -0.0165 0.0271  0.0134  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.2766 0.2249 0.3582 -0.0141 0.0229  0.0118  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.2860 0.2330 0.3691 -0.0133 0.0200  0.0074  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.2792 0.2292 0.3472 -0.0126 0.0222  0.0141  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.2684 0.2162 0.3410 -0.0113 0.0173  0.0062  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.2673 0.2179 0.3255 -0.0108 0.0186  0.0125  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.2701 0.2197 0.3311 -0.0102 0.0166  0.0089  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.2485 0.1985 0.3019 -0.0085 0.0143  0.0079  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.3449 0.2867 0.4792 -0.0217 0.0339  0.0149  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.3434 0.2865 0.4963 -0.0246 0.0375  0.0141  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.3432 0.2933 0.4955 -0.0249 0.0356  0.0086  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3530 0.3063 0.4918 -0.0229 0.0307  0.0041  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.3525 0.2932 0.5211 -0.0261 0.0341  0.0069  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.3669 0.3085 0.5220 -0.0233 0.0275  0.0002  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.3501 0.2907 0.4865 -0.0210 0.0288  0.0075  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.3326 0.2854 0.5016 -0.0274 0.0392  0.0084  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3250 0.2848 0.4972 -0.0277 0.0368  0.0025  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3106 0.2724 0.4841 -0.0269 0.0277  -0.0092 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3251 0.2837 0.5094 -0.0278 0.0252  -0.0134 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3282 0.2904 0.5237 -0.0309 0.0423  0.0039  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2987 0.2647 0.4582 -0.0244 0.0229  -0.0136 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2775 0.2441 0.4334 -0.0224 0.0149  -0.0235 93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2800 0.2518 0.4249 -0.0199 0.0107  -0.0277 93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2870 0.2616 0.4261 -0.0198 0.0140  -0.0228 93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2835 0.2447 0.4250 -0.0204 0.0140  -0.0217 93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3034 0.2653 0.4234 -0.0180 0.0149  -0.0166 93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3049 0.2620 0.4157 -0.0171 0.0167  -0.0110 93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2880 0.2454 0.3811 -0.0143 0.0145  -0.0109 93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3002 0.2595 0.3818 -0.0134 0.0154  -0.0068 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2668 0.2259 0.3352 -0.0112 0.0135  -0.0068 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2869 0.2483 0.3708 -0.0146 0.0185  -0.0031 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2690 0.2412 0.4096 -0.0174 0.0035  -0.0365 94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2831 0.2588 0.4102 -0.0142 -0.0007 -0.0399 94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2701 0.2423 0.3763 -0.0115 -0.0002 -0.0366 94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2896 0.2576 0.3924 -0.0103 -0.0014 -0.0387 94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3112 0.2883 0.4427 -0.0118 -0.0090 -0.0510 94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3392 0.3206 0.4939 -0.0144 -0.0108 -0.0555 94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3643 0.3519 0.5233 -0.0142 -0.0118 -0.0564 94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3603 0.3396 0.5347 -0.0172 -0.0111 -0.0586 94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3762 0.3685 0.5595 -0.0167 -0.0131 -0.0604 94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3742 0.3577 0.5733 -0.0201 -0.0123 -0.0624 94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3890 0.3793 0.5929 -0.0198 -0.0133 -0.0633 94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.4196 0.4149 0.6503 -0.0226 -0.0146 -0.0674 94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2299 0.2037 0.3236 -0.0105 0.0019  -0.0317 95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2087 0.1796 0.2847 -0.0081 0.0020  -0.0290 95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2095 0.1818 0.2757 -0.0043 -0.0032 -0.0351 95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2227 0.1991 0.2904 -0.0036 -0.0053 -0.0375 95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2013 0.1723 0.2692 -0.0088 0.0063  -0.0209 95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2128 0.1812 0.2651 -0.0065 0.0058  -0.0188 95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2344 0.2015 0.2805 -0.0073 0.0091  -0.0113 95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2736 0.2390 0.3251 -0.0091 0.0122  -0.0067 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2011 0.1683 0.2356 -0.0055 0.0082  -0.0099 95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1914 0.1603 0.2479 -0.0014 -0.0048 -0.0375 96  SER   A N   
719  C CA  . SER   A 90  ? 0.1931 0.1619 0.2380 0.0032  -0.0092 -0.0427 96  SER   A CA  
720  C C   . SER   A 90  ? 0.2128 0.1809 0.2426 0.0050  -0.0070 -0.0376 96  SER   A C   
721  O O   . SER   A 90  ? 0.2038 0.1708 0.2320 0.0029  -0.0028 -0.0309 96  SER   A O   
722  C CB  . SER   A 90  ? 0.2192 0.1838 0.2607 0.0062  -0.0115 -0.0484 96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2466 0.2074 0.2836 0.0059  -0.0070 -0.0437 96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1990 0.1672 0.2181 0.0092  -0.0102 -0.0408 97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2108 0.1777 0.2163 0.0114  -0.0083 -0.0365 97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2031 0.1724 0.2109 0.0083  -0.0057 -0.0307 97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2064 0.1739 0.2069 0.0084  -0.0030 -0.0257 97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2290 0.1912 0.2270 0.0128  -0.0047 -0.0336 97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2534 0.2123 0.2462 0.0169  -0.0067 -0.0394 97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2867 0.2430 0.2651 0.0226  -0.0077 -0.0412 97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2613 0.2189 0.2611 0.0167  -0.0079 -0.0440 97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3029 0.2562 0.2784 0.0260  -0.0095 -0.0470 97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2841 0.2381 0.2727 0.0225  -0.0099 -0.0491 97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1811 0.1546 0.1993 0.0060  -0.0066 -0.0318 98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1753 0.1509 0.1948 0.0038  -0.0036 -0.0267 98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1791 0.1577 0.1953 0.0060  -0.0060 -0.0285 98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1857 0.1668 0.2061 0.0078  -0.0101 -0.0340 98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1879 0.1657 0.2214 0.0000  -0.0012 -0.0254 98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2211 0.1998 0.2550 -0.0019 0.0030  -0.0196 98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2247 0.1992 0.2494 -0.0023 0.0053  -0.0139 98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2578 0.2383 0.3063 -0.0050 0.0062  -0.0183 98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1803 0.1583 0.1896 0.0060  -0.0038 -0.0240 99  MET   A N   
743  C CA  . MET   A 93  ? 0.1707 0.1509 0.1764 0.0083  -0.0054 -0.0249 99  MET   A CA  
744  C C   . MET   A 93  ? 0.1752 0.1579 0.1856 0.0062  -0.0022 -0.0218 99  MET   A C   
745  O O   . MET   A 93  ? 0.1878 0.1681 0.1949 0.0046  0.0010  -0.0173 99  MET   A O   
746  C CB  . MET   A 93  ? 0.1880 0.1642 0.1803 0.0109  -0.0056 -0.0226 99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2003 0.1733 0.1862 0.0139  -0.0075 -0.0251 99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2460 0.2136 0.2184 0.0167  -0.0058 -0.0210 99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2699 0.2357 0.2459 0.0123  -0.0016 -0.0156 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1706 0.1581 0.1890 0.0066  -0.0028 -0.0243 100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1777 0.1672 0.1998 0.0051  0.0017  -0.0209 100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1801 0.1701 0.1952 0.0078  0.0011  -0.0208 100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1785 0.1698 0.1920 0.0106  -0.0030 -0.0243 100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1908 0.1856 0.2298 0.0033  0.0036  -0.0226 100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2406 0.2350 0.2898 0.0004  0.0044  -0.0231 100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2512 0.2509 0.3195 -0.0017 0.0072  -0.0242 100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2554 0.2450 0.2986 -0.0015 0.0085  -0.0173 100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1678 0.1567 0.1791 0.0074  0.0052  -0.0169 101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1752 0.1646 0.1812 0.0099  0.0053  -0.0170 101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1732 0.1637 0.1812 0.0094  0.0110  -0.0141 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1836 0.1729 0.1935 0.0073  0.0147  -0.0109 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2030 0.1865 0.1954 0.0112  0.0035  -0.0153 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1626 0.1550 0.1699 0.0118  0.0121  -0.0151 102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1662 0.1587 0.1723 0.0125  0.0181  -0.0123 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1941 0.1799 0.1841 0.0137  0.0174  -0.0100 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2158 0.1990 0.1987 0.0156  0.0135  -0.0118 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1703 0.1677 0.1827 0.0151  0.0193  -0.0149 102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1867 0.1835 0.1955 0.0167  0.0264  -0.0120 102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1625 0.1667 0.1927 0.0138  0.0186  -0.0178 102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1907 0.1734 0.1761 0.0128  0.0209  -0.0062 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2108 0.1872 0.1821 0.0141  0.0195  -0.0045 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2148 0.1884 0.1826 0.0134  0.0232  -0.0001 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2147 0.1908 0.1915 0.0113  0.0266  0.0020  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2206 0.1887 0.1751 0.0157  0.0224  0.0012  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2154 0.1799 0.1635 0.0162  0.0251  0.0056  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2210 0.1832 0.1706 0.0135  0.0213  0.0072  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2206 0.1812 0.1690 0.0127  0.0154  0.0050  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2256 0.1843 0.1574 0.0205  0.0242  0.0055  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2361 0.1902 0.1587 0.0221  0.0267  0.0102  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2604 0.2156 0.1846 0.0231  0.0353  0.0147  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2548 0.2035 0.1685 0.0229  0.0217  0.0115  104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2668 0.2165 0.1808 0.0248  0.0354  0.0189  104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2663 0.2122 0.1738 0.0249  0.0267  0.0168  104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2186 0.1804 0.1714 0.0124  0.0250  0.0113  105 SER   A N   
785  C CA  . SER   A 99  ? 0.2230 0.1820 0.1763 0.0106  0.0217  0.0133  105 SER   A CA  
786  C C   . SER   A 99  ? 0.2457 0.2022 0.1974 0.0112  0.0269  0.0190  105 SER   A C   
787  O O   . SER   A 99  ? 0.2694 0.2281 0.2257 0.0115  0.0340  0.0212  105 SER   A O   
788  C CB  . SER   A 99  ? 0.2250 0.1875 0.1910 0.0069  0.0194  0.0111  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.2542 0.2210 0.2322 0.0052  0.0242  0.0113  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.2203 0.1719 0.1651 0.0120  0.0235  0.0215  106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2413 0.1891 0.1831 0.0130  0.0267  0.0274  106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2548 0.2020 0.2044 0.0101  0.0224  0.0278  106 GLU   A C   
793  O O   . GLU   A 100 ? 0.2409 0.1898 0.1947 0.0083  0.0170  0.0237  106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.2843 0.2258 0.2073 0.0181  0.0247  0.0293  106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.2914 0.2329 0.2060 0.0215  0.0298  0.0290  106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.3035 0.2383 0.1973 0.0276  0.0279  0.0298  106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.3528 0.2822 0.2374 0.0301  0.0263  0.0338  106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.3054 0.2401 0.1917 0.0303  0.0279  0.0262  106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2696 0.2144 0.2224 0.0097  0.0256  0.0329  107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2630 0.2075 0.2249 0.0071  0.0221  0.0329  107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2723 0.2152 0.2298 0.0077  0.0138  0.0304  107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2797 0.2249 0.2463 0.0051  0.0108  0.0273  107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2761 0.2163 0.2376 0.0082  0.0266  0.0398  107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2913 0.2321 0.2517 0.0093  0.0350  0.0428  107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2757 0.2177 0.2251 0.0118  0.0335  0.0391  107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2505 0.1893 0.1943 0.0115  0.0101  0.0313  108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2457 0.1827 0.1866 0.0124  0.0018  0.0288  108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2454 0.1858 0.1904 0.0106  -0.0014 0.0231  108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2550 0.1947 0.2018 0.0105  -0.0076 0.0208  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2237 0.1676 0.1706 0.0095  0.0028  0.0208  109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2014 0.1480 0.1520 0.0082  0.0002  0.0161  109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.1976 0.1472 0.1604 0.0049  0.0001  0.0147  109 ASP   A C   
813  O O   . ASP   A 103 ? 0.1997 0.1506 0.1652 0.0042  -0.0021 0.0116  109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.2015 0.1508 0.1501 0.0087  0.0042  0.0141  109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.2159 0.1618 0.1512 0.0125  0.0037  0.0140  109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.2382 0.1804 0.1670 0.0144  -0.0022 0.0128  109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.2249 0.1720 0.1571 0.0140  0.0091  0.0148  109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.1952 0.1452 0.1648 0.0034  0.0024  0.0171  110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.1916 0.1438 0.1716 0.0010  0.0025  0.0154  110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.2053 0.1563 0.1868 0.0010  -0.0021 0.0144  110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2259 0.1741 0.2043 0.0023  -0.0058 0.0161  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.2017 0.1534 0.1886 -0.0002 0.0051  0.0181  110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2327 0.1870 0.2250 -0.0015 0.0111  0.0181  110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.1811 0.1341 0.1672 0.0000  -0.0018 0.0117  111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.1953 0.1474 0.1849 -0.0001 -0.0047 0.0111  111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2014 0.1530 0.1872 0.0007  -0.0066 0.0091  111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2020 0.1532 0.1924 0.0003  -0.0075 0.0085  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.1835 0.1351 0.1616 0.0018  -0.0065 0.0081  112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.1789 0.1296 0.1535 0.0027  -0.0081 0.0059  112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.1763 0.1287 0.1545 0.0022  -0.0055 0.0046  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.1864 0.1413 0.1656 0.0020  -0.0025 0.0040  112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1643 0.1150 0.1443 0.0025  -0.0068 0.0041  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1670 0.1182 0.1487 0.0028  -0.0040 0.0037  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1586 0.1105 0.1343 0.0044  -0.0033 0.0018  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.1803 0.1308 0.1523 0.0052  -0.0054 0.0008  113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1919 0.1406 0.1800 0.0024  -0.0043 0.0050  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2142 0.1635 0.2101 0.0011  -0.0034 0.0069  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2147 0.1623 0.2018 0.0037  -0.0012 0.0053  113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2307 0.1780 0.2365 0.0004  -0.0037 0.0084  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1639 0.1175 0.1388 0.0053  -0.0009 0.0010  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1692 0.1234 0.1395 0.0075  -0.0007 -0.0008 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1767 0.1279 0.1466 0.0090  0.0008  0.0005  114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1827 0.1335 0.1544 0.0090  0.0030  0.0016  114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1768 0.1348 0.1470 0.0080  0.0002  -0.0030 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2036 0.1627 0.1701 0.0108  -0.0003 -0.0053 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2045 0.1642 0.1689 0.0117  -0.0015 -0.0061 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2041 0.1670 0.1730 0.0112  -0.0006 -0.0081 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1781 0.1267 0.1456 0.0103  0.0001  0.0007  115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1807 0.1256 0.1477 0.0120  0.0022  0.0030  115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.1934 0.1377 0.1539 0.0153  0.0019  0.0019  115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2186 0.1644 0.1774 0.0158  -0.0005 -0.0004 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2273 0.1684 0.1999 0.0106  0.0014  0.0047  115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2867 0.2278 0.2675 0.0080  0.0017  0.0063  115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3376 0.2753 0.3261 0.0065  -0.0005 0.0069  115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4369 0.3733 0.4350 0.0055  0.0027  0.0102  115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4973 0.4350 0.5039 0.0033  0.0016  0.0106  115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5511 0.4910 0.5566 0.0022  -0.0033 0.0082  115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.5360 0.4729 0.5527 0.0026  0.0055  0.0137  115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.1979 0.1394 0.1548 0.0181  0.0046  0.0039  116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2129 0.1523 0.1635 0.0219  0.0041  0.0039  116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.2193 0.1524 0.1711 0.0228  0.0073  0.0084  116 CYS   A C   
862  O O   . CYS   A 110 ? 0.2191 0.1504 0.1783 0.0201  0.0095  0.0108  116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2275 0.1683 0.1707 0.0255  0.0039  0.0023  116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.2146 0.1518 0.1538 0.0276  0.0089  0.0055  116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.2337 0.1631 0.1793 0.0269  0.0080  0.0099  117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.2416 0.1644 0.1894 0.0278  0.0121  0.0150  117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.2532 0.1735 0.2014 0.0284  0.0181  0.0192  117 GLN   A C   
868  O O   . GLN   A 111 ? 0.2776 0.1928 0.2311 0.0283  0.0227  0.0241  117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.2740 0.1927 0.2139 0.0328  0.0120  0.0164  117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.3470 0.2654 0.2745 0.0382  0.0129  0.0168  117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.4754 0.3909 0.3945 0.0435  0.0107  0.0171  117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.5019 0.4219 0.4176 0.0453  0.0055  0.0124  117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.4612 0.3692 0.3780 0.0464  0.0150  0.0228  117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.2306 0.1541 0.1737 0.0294  0.0186  0.0175  118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.2305 0.1516 0.1721 0.0310  0.0247  0.0211  118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.2267 0.1506 0.1797 0.0263  0.0261  0.0211  118 HIS   A C   
877  O O   . HIS   A 112 ? 0.2453 0.1669 0.2002 0.0271  0.0321  0.0246  118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.2425 0.1640 0.1704 0.0360  0.0245  0.0189  118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.2669 0.1859 0.1832 0.0413  0.0221  0.0185  118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.2688 0.1924 0.1814 0.0423  0.0152  0.0128  118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.3095 0.2217 0.2179 0.0462  0.0259  0.0235  118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.3032 0.2231 0.2062 0.0477  0.0142  0.0141  118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.3164 0.2290 0.2159 0.0503  0.0204  0.0207  118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.2053 0.1338 0.1654 0.0220  0.0209  0.0174  119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.2020 0.1331 0.1722 0.0181  0.0212  0.0173  119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.1970 0.1334 0.1669 0.0159  0.0162  0.0126  119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2101 0.1486 0.1748 0.0164  0.0122  0.0095  119 GLY   A O   
888  N N   . VAL   A 114 ? 0.1866 0.1252 0.1630 0.0136  0.0169  0.0126  120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.1847 0.1276 0.1619 0.0116  0.0131  0.0092  120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.1814 0.1261 0.1505 0.0141  0.0130  0.0063  120 VAL   A C   
891  O O   . VAL   A 114 ? 0.1949 0.1381 0.1602 0.0167  0.0165  0.0068  120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.1808 0.1248 0.1678 0.0089  0.0138  0.0104  120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.1818 0.1294 0.1689 0.0072  0.0108  0.0077  120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.1865 0.1292 0.1829 0.0064  0.0119  0.0121  120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.1841 0.1320 0.1509 0.0135  0.0091  0.0030  121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.1916 0.1419 0.1539 0.0153  0.0078  -0.0007 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1913 0.1445 0.1595 0.0127  0.0070  -0.0025 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2019 0.1555 0.1688 0.0141  0.0074  -0.0049 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.1961 0.1485 0.1555 0.0161  0.0044  -0.0031 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2168 0.1727 0.1752 0.0174  0.0019  -0.0077 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.1980 0.1470 0.1514 0.0191  0.0048  -0.0015 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1800 0.1346 0.1540 0.0094  0.0059  -0.0013 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1867 0.1434 0.1662 0.0071  0.0055  -0.0021 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1744 0.1315 0.1575 0.0045  0.0042  -0.0001 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1723 0.1278 0.1543 0.0044  0.0031  0.0015  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1776 0.1362 0.1648 0.0028  0.0040  -0.0001 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1850 0.1432 0.1733 0.0013  0.0027  0.0022  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1745 0.1348 0.1630 0.0006  0.0032  0.0016  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1695 0.1316 0.1617 0.0003  0.0044  -0.0003 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1899 0.1466 0.1837 0.0001  0.0026  0.0046  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1949 0.1523 0.1936 -0.0003 0.0047  0.0036  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2149 0.1697 0.2107 0.0004  0.0021  0.0059  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2242 0.1802 0.2292 -0.0012 0.0044  0.0063  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1657 0.1254 0.1508 0.0006  0.0024  0.0032  124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1584 0.1198 0.1441 0.0002  0.0044  0.0038  124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.1705 0.1316 0.1628 -0.0013 0.0060  0.0054  124 VAL   A C   
917  O O   . VAL   A 118 ? 0.1692 0.1279 0.1625 -0.0016 0.0050  0.0075  124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.1609 0.1204 0.1397 0.0013  0.0039  0.0059  124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.1779 0.1384 0.1573 0.0013  0.0076  0.0078  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.1903 0.1497 0.1633 0.0030  0.0023  0.0037  124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.1774 0.1409 0.1755 -0.0021 0.0084  0.0042  125 SER   A N   
922  C CA  . SER   A 119 ? 0.1792 0.1420 0.1850 -0.0037 0.0100  0.0055  125 SER   A CA  
923  C C   . SER   A 119 ? 0.2052 0.1692 0.2159 -0.0046 0.0137  0.0074  125 SER   A C   
924  O O   . SER   A 119 ? 0.2094 0.1714 0.2249 -0.0056 0.0158  0.0104  125 SER   A O   
925  C CB  . SER   A 119 ? 0.1861 0.1501 0.1978 -0.0040 0.0092  0.0012  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2100 0.1732 0.2305 -0.0054 0.0105  0.0014  125 SER   A OG  
927  N N   . THR   A 120 ? 0.1944 0.1615 0.2050 -0.0041 0.0150  0.0057  126 THR   A N   
928  C CA  . THR   A 120 ? 0.2103 0.1790 0.2280 -0.0049 0.0197  0.0077  126 THR   A CA  
929  C C   . THR   A 120 ? 0.2155 0.1858 0.2268 -0.0031 0.0214  0.0082  126 THR   A C   
930  O O   . THR   A 120 ? 0.2068 0.1769 0.2094 -0.0015 0.0183  0.0063  126 THR   A O   
931  C CB  . THR   A 120 ? 0.2618 0.2345 0.2939 -0.0067 0.0197  0.0030  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.2944 0.2710 0.3260 -0.0054 0.0174  -0.0016 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2788 0.2501 0.3165 -0.0078 0.0172  0.0005  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.2275 0.1994 0.2443 -0.0033 0.0268  0.0104  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.2601 0.2345 0.2734 -0.0014 0.0291  0.0100  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.2829 0.2581 0.3028 -0.0016 0.0369  0.0142  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.2842 0.2588 0.3145 -0.0037 0.0400  0.0167  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3030 0.2787 0.3162 0.0010  0.0404  0.0155  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3226 0.2983 0.3392 0.0018  0.0492  0.0206  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.3142 0.2952 0.3363 0.0031  0.0525  0.0182  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3192 0.3052 0.3499 0.0020  0.0479  0.0124  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.3068 0.2867 0.3241 0.0058  0.0604  0.0226  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2977 0.2827 0.3217 0.0074  0.0653  0.0212  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2671 0.2556 0.2885 0.0086  0.0586  0.0144  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2694 0.2645 0.3056 0.0080  0.0592  0.0108  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.3436 0.3344 0.3926 0.0040  0.0707  0.0216  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4516 0.4384 0.5034 0.0034  0.0794  0.0295  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.4965 0.4779 0.5323 0.0071  0.0854  0.0354  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4660 0.4544 0.5367 -0.0009 0.0799  0.0298  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2367 0.2205 0.2401 0.0108  0.0527  0.0129  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2184 0.2043 0.2188 0.0122  0.0468  0.0072  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2071 0.1953 0.2147 0.0095  0.0387  0.0026  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2233 0.2134 0.2300 0.0108  0.0342  -0.0017 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.1894 0.1765 0.2023 0.0064  0.0371  0.0037  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.1748 0.1630 0.1918 0.0046  0.0299  -0.0006 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.1783 0.1605 0.1837 0.0041  0.0262  0.0012  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.1945 0.1728 0.1942 0.0041  0.0289  0.0057  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.1803 0.1725 0.2152 0.0016  0.0304  -0.0021 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2035 0.2027 0.2543 0.0016  0.0323  -0.0051 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2197 0.2219 0.2901 -0.0017 0.0335  -0.0060 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.1999 0.2020 0.2499 0.0036  0.0249  -0.0114 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.1613 0.1432 0.1648 0.0040  0.0201  -0.0023 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.1604 0.1375 0.1566 0.0033  0.0169  -0.0010 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.1641 0.1428 0.1668 0.0021  0.0132  -0.0046 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1703 0.1518 0.1752 0.0033  0.0106  -0.0085 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.1917 0.1648 0.1748 0.0053  0.0140  -0.0007 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.1987 0.1735 0.1802 0.0072  0.0114  -0.0044 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.2035 0.1727 0.1831 0.0043  0.0108  0.0006  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.1584 0.1350 0.1639 0.0003  0.0129  -0.0033 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1667 0.1439 0.1766 -0.0002 0.0097  -0.0069 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1736 0.1468 0.1764 0.0001  0.0076  -0.0058 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.1766 0.1467 0.1764 -0.0007 0.0087  -0.0020 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1626 0.1355 0.1629 0.0016  0.0048  -0.0090 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1670 0.1362 0.1614 0.0021  0.0038  -0.0076 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1680 0.1365 0.1656 0.0024  0.0032  -0.0102 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1685 0.1389 0.1677 0.0039  0.0014  -0.0145 134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1650 0.1330 0.1516 0.0045  0.0023  -0.0082 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1699 0.1384 0.1530 0.0050  0.0024  -0.0070 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1749 0.1405 0.1542 0.0045  0.0025  -0.0040 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1874 0.1590 0.1714 0.0064  0.0020  -0.0095 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1766 0.1418 0.1514 0.0055  0.0023  -0.0037 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1932 0.1650 0.1737 0.0073  0.0025  -0.0088 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1902 0.1585 0.1654 0.0070  0.0028  -0.0060 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1567 0.1226 0.1550 0.0016  0.0042  -0.0079 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1610 0.1255 0.1608 0.0025  0.0041  -0.0103 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1697 0.1323 0.1611 0.0054  0.0039  -0.0107 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1848 0.1454 0.1735 0.0053  0.0050  -0.0072 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1805 0.1429 0.1848 0.0007  0.0058  -0.0072 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1710 0.1336 0.1587 0.0083  0.0025  -0.0149 136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1874 0.1474 0.1657 0.0119  0.0030  -0.0147 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.1937 0.1504 0.1714 0.0126  0.0064  -0.0126 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1989 0.1554 0.1816 0.0118  0.0069  -0.0142 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2010 0.1613 0.1743 0.0158  0.0000  -0.0200 136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2571 0.2139 0.2183 0.0206  0.0008  -0.0193 136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2426 0.1983 0.2006 0.0206  0.0022  -0.0154 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3143 0.2686 0.2690 0.0246  0.0004  -0.0224 136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.1897 0.1435 0.1620 0.0143  0.0090  -0.0092 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.1887 0.1396 0.1609 0.0157  0.0133  -0.0071 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2088 0.1560 0.1700 0.0208  0.0159  -0.0069 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2216 0.1659 0.1817 0.0227  0.0208  -0.0046 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2004 0.1509 0.1802 0.0127  0.0155  -0.0022 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.1939 0.1469 0.1825 0.0087  0.0130  -0.0020 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2035 0.1530 0.1812 0.0126  0.0156  0.0009  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2038 0.1509 0.1568 0.0235  0.0132  -0.0086 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2105 0.1533 0.1515 0.0289  0.0158  -0.0072 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.2533 0.1929 0.1855 0.0339  0.0174  -0.0102 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.2701 0.2050 0.1918 0.0389  0.0217  -0.0076 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.2056 0.1487 0.1399 0.0311  0.0118  -0.0085 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2247 0.1695 0.1656 0.0272  0.0112  -0.0052 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.2281 0.1738 0.1635 0.0295  0.0071  -0.0072 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.2102 0.1608 0.1498 0.0283  0.0020  -0.0126 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2284 0.1815 0.1670 0.0297  -0.0023 -0.0154 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2361 0.1868 0.1680 0.0328  -0.0025 -0.0133 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2205 0.1786 0.1666 0.0278  -0.0061 -0.0199 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2445 0.1862 0.1802 0.0333  0.0139  -0.0158 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2627 0.2010 0.1896 0.0385  0.0147  -0.0198 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2745 0.2105 0.2050 0.0383  0.0213  -0.0171 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2847 0.2170 0.2066 0.0433  0.0233  -0.0200 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2701 0.2110 0.2006 0.0381  0.0079  -0.0277 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3066 0.2513 0.2535 0.0316  0.0072  -0.0280 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.2943 0.2416 0.2495 0.0268  0.0086  -0.0232 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3414 0.2859 0.2923 0.0318  0.0053  -0.0332 139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.2612 0.1994 0.2045 0.0329  0.0242  -0.0124 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.2513 0.1882 0.2010 0.0325  0.0300  -0.0099 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.2568 0.1899 0.2012 0.0357  0.0376  -0.0042 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.2504 0.1845 0.2041 0.0325  0.0407  0.0014  140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.2348 0.1757 0.2007 0.0258  0.0286  -0.0075 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2420 0.1862 0.2138 0.0224  0.0223  -0.0120 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2528 0.1999 0.2376 0.0168  0.0213  -0.0086 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2367 0.1793 0.2074 0.0248  0.0214  -0.0179 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.2644 0.1927 0.1936 0.0427  0.0407  -0.0055 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.2777 0.2016 0.2004 0.0466  0.0492  0.0009  141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.2885 0.2123 0.2232 0.0451  0.0575  0.0058  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3061 0.2281 0.2443 0.0452  0.0642  0.0126  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.2934 0.2114 0.1946 0.0555  0.0510  -0.0015 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3203 0.2386 0.2103 0.0578  0.0414  -0.0076 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3461 0.2576 0.2129 0.0679  0.0431  -0.0091 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3321 0.2531 0.2265 0.0541  0.0378  -0.0044 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.2902 0.2158 0.2326 0.0436  0.0569  0.0024  142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.2938 0.2197 0.2489 0.0425  0.0643  0.0064  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.2933 0.2233 0.2671 0.0358  0.0638  0.0115  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3053 0.2359 0.2916 0.0350  0.0701  0.0157  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2875 0.2141 0.2464 0.0429  0.0632  0.0012  142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.2622 0.1928 0.2280 0.0379  0.0536  -0.0037 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.2651 0.1955 0.2223 0.0390  0.0466  -0.0103 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.2544 0.1895 0.2376 0.0313  0.0502  -0.0019 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.2633 0.1977 0.2325 0.0332  0.0403  -0.0122 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.2621 0.1991 0.2458 0.0288  0.0424  -0.0070 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.2617 0.1992 0.2604 0.0277  0.0529  0.0034  142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.2625 0.2031 0.2595 0.0232  0.0381  -0.0061 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.2657 0.2069 0.2771 0.0224  0.0473  0.0035  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.2652 0.2074 0.2746 0.0205  0.0406  -0.0010 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.2733 0.2063 0.2500 0.0313  0.0560  0.0107  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.2815 0.2178 0.2743 0.0257  0.0544  0.0146  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.3470 0.2810 0.3437 0.0266  0.0614  0.0209  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.3510 0.2872 0.3644 0.0228  0.0619  0.0242  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.2636 0.2025 0.2554 0.0219  0.0457  0.0126  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.2738 0.2156 0.2677 0.0193  0.0392  0.0080  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.2840 0.2279 0.2753 0.0166  0.0324  0.0066  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.2664 0.2108 0.2762 0.0157  0.0387  0.0096  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4062 0.3355 0.3881 0.0318  0.0662  0.0226  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4707 0.3964 0.4538 0.0336  0.0738  0.0292  144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.5287 0.4520 0.5171 0.0367  0.0852  0.0337  144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.5442 0.4645 0.5361 0.0380  0.0928  0.0400  144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5237 0.4443 0.4858 0.0392  0.0747  0.0295  144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6196 0.5414 0.5754 0.0375  0.0657  0.0265  144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6369 0.5627 0.6050 0.0316  0.0598  0.0258  144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6740 0.5925 0.6119 0.0426  0.0644  0.0249  144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.5626 0.4867 0.5506 0.0387  0.0873  0.0307  145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.6013 0.5231 0.5938 0.0424  0.0991  0.0348  145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.6208 0.5476 0.6344 0.0384  0.0988  0.0341  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.6354 0.5626 0.6636 0.0386  0.1075  0.0390  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.6473 0.5637 0.6170 0.0507  0.1037  0.0321  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.7257 0.6439 0.6888 0.0508  0.0954  0.0235  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.8195 0.7323 0.7571 0.0584  0.0946  0.0185  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.8282 0.7409 0.7618 0.0605  0.0922  0.0122  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.8617 0.7703 0.7837 0.0625  0.0956  0.0206  145 GLU   A OE2 
1078 N N   . SER   B 1   ? 0.3118 0.2623 0.2729 -0.0065 -0.0224 -0.0130 7   SER   C N   
1079 C CA  . SER   B 1   ? 0.3050 0.2598 0.2756 -0.0049 -0.0236 -0.0127 7   SER   C CA  
1080 C C   . SER   B 1   ? 0.2935 0.2496 0.2682 -0.0022 -0.0230 -0.0107 7   SER   C C   
1081 O O   . SER   B 1   ? 0.3048 0.2581 0.2748 -0.0017 -0.0230 -0.0091 7   SER   C O   
1082 C CB  . SER   B 1   ? 0.3381 0.2949 0.3103 -0.0059 -0.0289 -0.0126 7   SER   C CB  
1083 O OG  . SER   B 1   ? 0.3962 0.3514 0.3648 -0.0052 -0.0329 -0.0101 7   SER   C OG  
1084 N N   . GLY   B 2   ? 0.2603 0.2200 0.2432 -0.0010 -0.0220 -0.0109 8   GLY   C N   
1085 C CA  . GLY   B 2   ? 0.2462 0.2069 0.2330 0.0011  -0.0209 -0.0099 8   GLY   C CA  
1086 C C   . GLY   B 2   ? 0.2338 0.1977 0.2267 0.0011  -0.0175 -0.0108 8   GLY   C C   
1087 O O   . GLY   B 2   ? 0.2546 0.2187 0.2473 -0.0004 -0.0156 -0.0114 8   GLY   C O   
1088 N N   . ALA   B 3   ? 0.2310 0.1967 0.2289 0.0026  -0.0165 -0.0109 9   ALA   C N   
1089 C CA  . ALA   B 3   ? 0.2305 0.1990 0.2327 0.0019  -0.0127 -0.0118 9   ALA   C CA  
1090 C C   . ALA   B 3   ? 0.2258 0.1936 0.2285 0.0030  -0.0102 -0.0121 9   ALA   C C   
1091 O O   . ALA   B 3   ? 0.2362 0.2021 0.2390 0.0049  -0.0116 -0.0118 9   ALA   C O   
1092 C CB  . ALA   B 3   ? 0.2431 0.2165 0.2539 0.0016  -0.0134 -0.0130 9   ALA   C CB  
1093 N N   . ILE   B 4   ? 0.2124 0.1813 0.2152 0.0014  -0.0063 -0.0127 10  ILE   C N   
1094 C CA  . ILE   B 4   ? 0.1988 0.1671 0.2014 0.0015  -0.0030 -0.0139 10  ILE   C CA  
1095 C C   . ILE   B 4   ? 0.2026 0.1755 0.2135 0.0013  -0.0002 -0.0159 10  ILE   C C   
1096 O O   . ILE   B 4   ? 0.1998 0.1754 0.2125 -0.0006 0.0006  -0.0158 10  ILE   C O   
1097 C CB  . ILE   B 4   ? 0.2059 0.1723 0.2012 -0.0011 -0.0007 -0.0130 10  ILE   C CB  
1098 C CG1 . ILE   B 4   ? 0.2239 0.1870 0.2130 -0.0012 -0.0032 -0.0109 10  ILE   C CG1 
1099 C CG2 . ILE   B 4   ? 0.2096 0.1746 0.2031 -0.0019 0.0030  -0.0149 10  ILE   C CG2 
1100 C CD1 . ILE   B 4   ? 0.2543 0.2169 0.2385 -0.0038 -0.0021 -0.0092 10  ILE   C CD1 
1101 N N   . TYR   B 5   ? 0.2252 0.1988 0.2415 0.0033  0.0016  -0.0180 11  TYR   C N   
1102 C CA  . TYR   B 5   ? 0.2268 0.2053 0.2524 0.0033  0.0050  -0.0204 11  TYR   C CA  
1103 C C   . TYR   B 5   ? 0.2316 0.2084 0.2544 0.0020  0.0108  -0.0229 11  TYR   C C   
1104 O O   . TYR   B 5   ? 0.2439 0.2174 0.2670 0.0042  0.0115  -0.0243 11  TYR   C O   
1105 C CB  . TYR   B 5   ? 0.2228 0.2043 0.2598 0.0071  0.0020  -0.0209 11  TYR   C CB  
1106 C CG  . TYR   B 5   ? 0.2201 0.2036 0.2589 0.0073  -0.0039 -0.0187 11  TYR   C CG  
1107 C CD1 . TYR   B 5   ? 0.2361 0.2251 0.2810 0.0055  -0.0040 -0.0191 11  TYR   C CD1 
1108 C CD2 . TYR   B 5   ? 0.2484 0.2279 0.2815 0.0085  -0.0090 -0.0164 11  TYR   C CD2 
1109 C CE1 . TYR   B 5   ? 0.2621 0.2523 0.3076 0.0050  -0.0093 -0.0176 11  TYR   C CE1 
1110 C CE2 . TYR   B 5   ? 0.2670 0.2477 0.2997 0.0078  -0.0140 -0.0149 11  TYR   C CE2 
1111 C CZ  . TYR   B 5   ? 0.2793 0.2652 0.3181 0.0061  -0.0143 -0.0156 11  TYR   C CZ  
1112 O OH  . TYR   B 5   ? 0.3030 0.2894 0.3404 0.0048  -0.0192 -0.0146 11  TYR   C OH  
1113 N N   . VAL   B 6   ? 0.2314 0.2095 0.2505 -0.0018 0.0150  -0.0236 12  VAL   C N   
1114 C CA  . VAL   B 6   ? 0.2479 0.2239 0.2618 -0.0042 0.0207  -0.0261 12  VAL   C CA  
1115 C C   . VAL   B 6   ? 0.2680 0.2487 0.2866 -0.0069 0.0262  -0.0283 12  VAL   C C   
1116 O O   . VAL   B 6   ? 0.2732 0.2565 0.2915 -0.0093 0.0255  -0.0263 12  VAL   C O   
1117 C CB  . VAL   B 6   ? 0.2626 0.2338 0.2626 -0.0076 0.0197  -0.0238 12  VAL   C CB  
1118 C CG1 . VAL   B 6   ? 0.2781 0.2505 0.2749 -0.0099 0.0172  -0.0201 12  VAL   C CG1 
1119 C CG2 . VAL   B 6   ? 0.2783 0.2472 0.2711 -0.0112 0.0253  -0.0264 12  VAL   C CG2 
1120 N N   . GLY   B 7   ? 0.2775 0.2597 0.3021 -0.0062 0.0320  -0.0327 13  GLY   C N   
1121 C CA  . GLY   B 7   ? 0.2891 0.2764 0.3190 -0.0090 0.0382  -0.0353 13  GLY   C CA  
1122 C C   . GLY   B 7   ? 0.2866 0.2806 0.3282 -0.0078 0.0355  -0.0338 13  GLY   C C   
1123 O O   . GLY   B 7   ? 0.2965 0.2924 0.3473 -0.0033 0.0306  -0.0331 13  GLY   C O   
1124 N N   . ASN   B 8   ? 0.2837 0.2806 0.3239 -0.0122 0.0377  -0.0328 14  ASN   C N   
1125 C CA  . ASN   B 8   ? 0.2787 0.2814 0.3292 -0.0118 0.0346  -0.0314 14  ASN   C CA  
1126 C C   . ASN   B 8   ? 0.2488 0.2481 0.2915 -0.0131 0.0284  -0.0268 14  ASN   C C   
1127 O O   . ASN   B 8   ? 0.2691 0.2710 0.3147 -0.0156 0.0276  -0.0253 14  ASN   C O   
1128 C CB  . ASN   B 8   ? 0.3225 0.3310 0.3794 -0.0157 0.0411  -0.0335 14  ASN   C CB  
1129 C CG  . ASN   B 8   ? 0.4157 0.4294 0.4855 -0.0133 0.0468  -0.0384 14  ASN   C CG  
1130 O OD1 . ASN   B 8   ? 0.4484 0.4675 0.5334 -0.0090 0.0440  -0.0393 14  ASN   C OD1 
1131 N ND2 . ASN   B 8   ? 0.4456 0.4574 0.5097 -0.0159 0.0546  -0.0418 14  ASN   C ND2 
1132 N N   . TYR   B 9   ? 0.2297 0.2232 0.2634 -0.0113 0.0242  -0.0247 15  TYR   C N   
1133 C CA  . TYR   B 9   ? 0.2250 0.2151 0.2523 -0.0120 0.0190  -0.0209 15  TYR   C CA  
1134 C C   . TYR   B 9   ? 0.2100 0.1982 0.2382 -0.0079 0.0131  -0.0200 15  TYR   C C   
1135 O O   . TYR   B 9   ? 0.2130 0.1998 0.2416 -0.0049 0.0125  -0.0211 15  TYR   C O   
1136 C CB  . TYR   B 9   ? 0.2393 0.2239 0.2533 -0.0147 0.0198  -0.0187 15  TYR   C CB  
1137 C CG  . TYR   B 9   ? 0.2611 0.2460 0.2704 -0.0199 0.0249  -0.0185 15  TYR   C CG  
1138 C CD1 . TYR   B 9   ? 0.2789 0.2660 0.2914 -0.0228 0.0258  -0.0172 15  TYR   C CD1 
1139 C CD2 . TYR   B 9   ? 0.2864 0.2688 0.2872 -0.0224 0.0289  -0.0197 15  TYR   C CD2 
1140 C CE1 . TYR   B 9   ? 0.3051 0.2920 0.3123 -0.0282 0.0306  -0.0165 15  TYR   C CE1 
1141 C CE2 . TYR   B 9   ? 0.3103 0.2926 0.3049 -0.0280 0.0336  -0.0193 15  TYR   C CE2 
1142 C CZ  . TYR   B 9   ? 0.3347 0.3193 0.3325 -0.0308 0.0344  -0.0175 15  TYR   C CZ  
1143 O OH  . TYR   B 9   ? 0.3720 0.3559 0.3626 -0.0369 0.0389  -0.0165 15  TYR   C OH  
1144 N N   . ARG   B 10  ? 0.1979 0.1854 0.2255 -0.0081 0.0088  -0.0179 16  ARG   C N   
1145 C CA  . ARG   B 10  ? 0.2053 0.1904 0.2312 -0.0054 0.0034  -0.0168 16  ARG   C CA  
1146 C C   . ARG   B 10  ? 0.1922 0.1726 0.2092 -0.0069 0.0021  -0.0142 16  ARG   C C   
1147 O O   . ARG   B 10  ? 0.1977 0.1780 0.2147 -0.0094 0.0028  -0.0132 16  ARG   C O   
1148 C CB  . ARG   B 10  ? 0.2138 0.2028 0.2480 -0.0046 -0.0003 -0.0173 16  ARG   C CB  
1149 C CG  . ARG   B 10  ? 0.2049 0.1907 0.2350 -0.0036 -0.0056 -0.0161 16  ARG   C CG  
1150 C CD  . ARG   B 10  ? 0.1889 0.1786 0.2262 -0.0033 -0.0099 -0.0168 16  ARG   C CD  
1151 N NE  . ARG   B 10  ? 0.2194 0.2062 0.2520 -0.0050 -0.0131 -0.0164 16  ARG   C NE  
1152 C CZ  . ARG   B 10  ? 0.2795 0.2636 0.3073 -0.0041 -0.0174 -0.0159 16  ARG   C CZ  
1153 N NH1 . ARG   B 10  ? 0.2959 0.2796 0.3230 -0.0014 -0.0197 -0.0151 16  ARG   C NH1 
1154 N NH2 . ARG   B 10  ? 0.2563 0.2377 0.2796 -0.0063 -0.0192 -0.0164 16  ARG   C NH2 
1155 N N   . VAL   B 11  ? 0.1945 0.1709 0.2047 -0.0056 0.0008  -0.0132 17  VAL   C N   
1156 C CA  . VAL   B 11  ? 0.1877 0.1604 0.1915 -0.0065 -0.0004 -0.0108 17  VAL   C CA  
1157 C C   . VAL   B 11  ? 0.1984 0.1694 0.2015 -0.0047 -0.0040 -0.0108 17  VAL   C C   
1158 O O   . VAL   B 11  ? 0.2017 0.1719 0.2037 -0.0027 -0.0057 -0.0113 17  VAL   C O   
1159 C CB  . VAL   B 11  ? 0.2073 0.1775 0.2042 -0.0069 0.0008  -0.0097 17  VAL   C CB  
1160 C CG1 . VAL   B 11  ? 0.2037 0.1713 0.1962 -0.0081 -0.0004 -0.0068 17  VAL   C CG1 
1161 C CG2 . VAL   B 11  ? 0.2129 0.1843 0.2087 -0.0090 0.0046  -0.0107 17  VAL   C CG2 
1162 N N   . VAL   B 12  ? 0.1875 0.1571 0.1906 -0.0057 -0.0049 -0.0102 18  VAL   C N   
1163 C CA  . VAL   B 12  ? 0.1829 0.1505 0.1843 -0.0047 -0.0075 -0.0108 18  VAL   C CA  
1164 C C   . VAL   B 12  ? 0.1789 0.1431 0.1776 -0.0053 -0.0068 -0.0096 18  VAL   C C   
1165 O O   . VAL   B 12  ? 0.1886 0.1524 0.1884 -0.0066 -0.0052 -0.0079 18  VAL   C O   
1166 C CB  . VAL   B 12  ? 0.2090 0.1785 0.2149 -0.0055 -0.0094 -0.0126 18  VAL   C CB  
1167 C CG1 . VAL   B 12  ? 0.2536 0.2268 0.2638 -0.0043 -0.0111 -0.0135 18  VAL   C CG1 
1168 C CG2 . VAL   B 12  ? 0.1962 0.1663 0.2060 -0.0079 -0.0078 -0.0126 18  VAL   C CG2 
1169 N N   . ASN   B 13  ? 0.1692 0.1310 0.1651 -0.0046 -0.0079 -0.0104 19  ASN   C N   
1170 C CA  . ASN   B 13  ? 0.1723 0.1311 0.1680 -0.0048 -0.0067 -0.0101 19  ASN   C CA  
1171 C C   . ASN   B 13  ? 0.1872 0.1452 0.1869 -0.0064 -0.0063 -0.0109 19  ASN   C C   
1172 O O   . ASN   B 13  ? 0.1902 0.1492 0.1910 -0.0074 -0.0077 -0.0131 19  ASN   C O   
1173 C CB  . ASN   B 13  ? 0.1715 0.1281 0.1635 -0.0043 -0.0071 -0.0119 19  ASN   C CB  
1174 C CG  . ASN   B 13  ? 0.1967 0.1534 0.1845 -0.0032 -0.0072 -0.0110 19  ASN   C CG  
1175 O OD1 . ASN   B 13  ? 0.2075 0.1648 0.1925 -0.0029 -0.0090 -0.0113 19  ASN   C OD1 
1176 N ND2 . ASN   B 13  ? 0.1839 0.1400 0.1720 -0.0027 -0.0056 -0.0095 19  ASN   C ND2 
1177 N N   . ARG   B 14  ? 0.1721 0.1282 0.1743 -0.0069 -0.0049 -0.0090 20  ARG   C N   
1178 C CA  . ARG   B 14  ? 0.1646 0.1190 0.1706 -0.0088 -0.0043 -0.0095 20  ARG   C CA  
1179 C C   . ARG   B 14  ? 0.1908 0.1424 0.1965 -0.0093 -0.0047 -0.0133 20  ARG   C C   
1180 O O   . ARG   B 14  ? 0.2010 0.1528 0.2087 -0.0114 -0.0054 -0.0151 20  ARG   C O   
1181 C CB  . ARG   B 14  ? 0.1733 0.1249 0.1817 -0.0089 -0.0032 -0.0062 20  ARG   C CB  
1182 C CG  . ARG   B 14  ? 0.1877 0.1366 0.2000 -0.0112 -0.0025 -0.0058 20  ARG   C CG  
1183 C CD  . ARG   B 14  ? 0.1928 0.1379 0.2076 -0.0109 -0.0020 -0.0017 20  ARG   C CD  
1184 N NE  . ARG   B 14  ? 0.1876 0.1292 0.2057 -0.0133 -0.0014 -0.0001 20  ARG   C NE  
1185 C CZ  . ARG   B 14  ? 0.2102 0.1469 0.2319 -0.0138 -0.0007 -0.0022 20  ARG   C CZ  
1186 N NH1 . ARG   B 14  ? 0.2164 0.1514 0.2378 -0.0124 -0.0001 -0.0066 20  ARG   C NH1 
1187 N NH2 . ARG   B 14  ? 0.2076 0.1404 0.2322 -0.0162 -0.0002 -0.0001 20  ARG   C NH2 
1188 N N   . HIS   B 15  ? 0.1773 0.1265 0.1799 -0.0079 -0.0041 -0.0147 21  HIS   C N   
1189 C CA  . HIS   B 15  ? 0.1873 0.1332 0.1878 -0.0091 -0.0039 -0.0188 21  HIS   C CA  
1190 C C   . HIS   B 15  ? 0.2030 0.1512 0.1995 -0.0106 -0.0068 -0.0209 21  HIS   C C   
1191 O O   . HIS   B 15  ? 0.2143 0.1601 0.2084 -0.0128 -0.0074 -0.0243 21  HIS   C O   
1192 C CB  . HIS   B 15  ? 0.2005 0.1430 0.1989 -0.0077 -0.0014 -0.0202 21  HIS   C CB  
1193 C CG  . HIS   B 15  ? 0.2029 0.1475 0.1960 -0.0067 -0.0019 -0.0200 21  HIS   C CG  
1194 N ND1 . HIS   B 15  ? 0.2067 0.1541 0.2007 -0.0048 -0.0019 -0.0166 21  HIS   C ND1 
1195 C CD2 . HIS   B 15  ? 0.2239 0.1675 0.2100 -0.0078 -0.0024 -0.0227 21  HIS   C CD2 
1196 C CE1 . HIS   B 15  ? 0.2083 0.1562 0.1966 -0.0047 -0.0021 -0.0174 21  HIS   C CE1 
1197 N NE2 . HIS   B 15  ? 0.2286 0.1743 0.2117 -0.0064 -0.0025 -0.0208 21  HIS   C NE2 
1198 N N   . LEU   B 16  ? 0.1953 0.1480 0.1913 -0.0097 -0.0089 -0.0191 22  LEU   C N   
1199 C CA  . LEU   B 16  ? 0.2103 0.1657 0.2043 -0.0106 -0.0125 -0.0203 22  LEU   C CA  
1200 C C   . LEU   B 16  ? 0.2246 0.1846 0.2253 -0.0115 -0.0140 -0.0196 22  LEU   C C   
1201 O O   . LEU   B 16  ? 0.2315 0.1948 0.2330 -0.0119 -0.0174 -0.0201 22  LEU   C O   
1202 C CB  . LEU   B 16  ? 0.2085 0.1651 0.1981 -0.0088 -0.0139 -0.0189 22  LEU   C CB  
1203 C CG  . LEU   B 16  ? 0.2198 0.1724 0.2026 -0.0085 -0.0122 -0.0197 22  LEU   C CG  
1204 C CD1 . LEU   B 16  ? 0.2249 0.1782 0.2033 -0.0071 -0.0136 -0.0178 22  LEU   C CD1 
1205 C CD2 . LEU   B 16  ? 0.2461 0.1950 0.2236 -0.0113 -0.0126 -0.0233 22  LEU   C CD2 
1206 N N   . ALA   B 17  ? 0.2029 0.1634 0.2086 -0.0119 -0.0115 -0.0183 23  ALA   C N   
1207 C CA  . ALA   B 17  ? 0.2088 0.1741 0.2210 -0.0133 -0.0119 -0.0180 23  ALA   C CA  
1208 C C   . ALA   B 17  ? 0.2191 0.1854 0.2339 -0.0161 -0.0145 -0.0205 23  ALA   C C   
1209 O O   . ALA   B 17  ? 0.2262 0.1879 0.2383 -0.0179 -0.0144 -0.0225 23  ALA   C O   
1210 C CB  . ALA   B 17  ? 0.2124 0.1766 0.2276 -0.0143 -0.0086 -0.0161 23  ALA   C CB  
1211 N N   . THR   B 18  ? 0.2139 0.1864 0.2343 -0.0164 -0.0169 -0.0207 24  THR   C N   
1212 C CA  . THR   B 18  ? 0.2152 0.1902 0.2390 -0.0194 -0.0204 -0.0228 24  THR   C CA  
1213 C C   . THR   B 18  ? 0.2264 0.2029 0.2572 -0.0226 -0.0182 -0.0232 24  THR   C C   
1214 O O   . THR   B 18  ? 0.2230 0.1991 0.2558 -0.0223 -0.0142 -0.0215 24  THR   C O   
1215 C CB  . THR   B 18  ? 0.2307 0.2125 0.2595 -0.0180 -0.0244 -0.0221 24  THR   C CB  
1216 O OG1 . THR   B 18  ? 0.2425 0.2296 0.2795 -0.0166 -0.0216 -0.0209 24  THR   C OG1 
1217 C CG2 . THR   B 18  ? 0.2442 0.2239 0.2659 -0.0152 -0.0267 -0.0211 24  THR   C CG2 
1218 N N   . HIS   B 19  ? 0.2292 0.2081 0.2641 -0.0261 -0.0213 -0.0253 25  HIS   C N   
1219 C CA  . HIS   B 19  ? 0.2339 0.2151 0.2765 -0.0296 -0.0193 -0.0257 25  HIS   C CA  
1220 C C   . HIS   B 19  ? 0.2167 0.2053 0.2677 -0.0283 -0.0168 -0.0238 25  HIS   C C   
1221 O O   . HIS   B 19  ? 0.2253 0.2134 0.2789 -0.0300 -0.0125 -0.0227 25  HIS   C O   
1222 C CB  . HIS   B 19  ? 0.2699 0.2543 0.3164 -0.0337 -0.0240 -0.0283 25  HIS   C CB  
1223 C CG  . HIS   B 19  ? 0.3532 0.3300 0.3910 -0.0362 -0.0258 -0.0311 25  HIS   C CG  
1224 N ND1 . HIS   B 19  ? 0.3990 0.3672 0.4329 -0.0378 -0.0219 -0.0322 25  HIS   C ND1 
1225 C CD2 . HIS   B 19  ? 0.3890 0.3653 0.4213 -0.0377 -0.0309 -0.0331 25  HIS   C CD2 
1226 C CE1 . HIS   B 19  ? 0.4122 0.3750 0.4390 -0.0401 -0.0240 -0.0355 25  HIS   C CE1 
1227 N NE2 . HIS   B 19  ? 0.4178 0.3851 0.4422 -0.0403 -0.0294 -0.0362 25  HIS   C NE2 
1228 N N   . ASN   B 20  ? 0.2172 0.2118 0.2717 -0.0253 -0.0191 -0.0233 26  ASN   C N   
1229 C CA  . ASN   B 20  ? 0.2192 0.2206 0.2822 -0.0240 -0.0159 -0.0224 26  ASN   C CA  
1230 C C   . ASN   B 20  ? 0.2239 0.2213 0.2813 -0.0223 -0.0106 -0.0206 26  ASN   C C   
1231 O O   . ASN   B 20  ? 0.2228 0.2230 0.2842 -0.0236 -0.0060 -0.0201 26  ASN   C O   
1232 C CB  . ASN   B 20  ? 0.2345 0.2421 0.3033 -0.0207 -0.0196 -0.0223 26  ASN   C CB  
1233 C CG  . ASN   B 20  ? 0.3153 0.3304 0.3950 -0.0192 -0.0160 -0.0224 26  ASN   C CG  
1234 O OD1 . ASN   B 20  ? 0.3260 0.3478 0.4165 -0.0218 -0.0148 -0.0234 26  ASN   C OD1 
1235 N ND2 . ASN   B 20  ? 0.3421 0.3563 0.4197 -0.0153 -0.0140 -0.0216 26  ASN   C ND2 
1236 N N   . ASP   B 21  ? 0.2215 0.2124 0.2689 -0.0199 -0.0111 -0.0197 27  ASP   C N   
1237 C CA  . ASP   B 21  ? 0.2188 0.2060 0.2606 -0.0188 -0.0069 -0.0177 27  ASP   C CA  
1238 C C   . ASP   B 21  ? 0.2243 0.2081 0.2652 -0.0223 -0.0037 -0.0165 27  ASP   C C   
1239 O O   . ASP   B 21  ? 0.2258 0.2103 0.2666 -0.0233 0.0002  -0.0149 27  ASP   C O   
1240 C CB  . ASP   B 21  ? 0.2099 0.1912 0.2425 -0.0161 -0.0083 -0.0168 27  ASP   C CB  
1241 C CG  . ASP   B 21  ? 0.2228 0.2059 0.2542 -0.0127 -0.0106 -0.0170 27  ASP   C CG  
1242 O OD1 . ASP   B 21  ? 0.2248 0.2123 0.2609 -0.0114 -0.0092 -0.0170 27  ASP   C OD1 
1243 O OD2 . ASP   B 21  ? 0.2117 0.1915 0.2376 -0.0116 -0.0135 -0.0173 27  ASP   C OD2 
1244 N N   . TRP   B 22  ? 0.2240 0.2035 0.2640 -0.0244 -0.0052 -0.0172 28  TRP   C N   
1245 C CA  . TRP   B 22  ? 0.2316 0.2066 0.2712 -0.0276 -0.0025 -0.0157 28  TRP   C CA  
1246 C C   . TRP   B 22  ? 0.2485 0.2288 0.2957 -0.0315 -0.0002 -0.0158 28  TRP   C C   
1247 O O   . TRP   B 22  ? 0.2681 0.2461 0.3143 -0.0340 0.0032  -0.0135 28  TRP   C O   
1248 C CB  . TRP   B 22  ? 0.2364 0.2049 0.2738 -0.0288 -0.0045 -0.0172 28  TRP   C CB  
1249 C CG  . TRP   B 22  ? 0.2206 0.1824 0.2512 -0.0258 -0.0045 -0.0162 28  TRP   C CG  
1250 C CD1 . TRP   B 22  ? 0.2329 0.1932 0.2591 -0.0233 -0.0066 -0.0180 28  TRP   C CD1 
1251 C CD2 . TRP   B 22  ? 0.2155 0.1719 0.2435 -0.0253 -0.0022 -0.0128 28  TRP   C CD2 
1252 N NE1 . TRP   B 22  ? 0.2386 0.1934 0.2607 -0.0211 -0.0052 -0.0165 28  TRP   C NE1 
1253 C CE2 . TRP   B 22  ? 0.2179 0.1703 0.2415 -0.0221 -0.0029 -0.0131 28  TRP   C CE2 
1254 C CE3 . TRP   B 22  ? 0.2185 0.1731 0.2474 -0.0274 0.0002  -0.0093 28  TRP   C CE3 
1255 C CZ2 . TRP   B 22  ? 0.2255 0.1729 0.2475 -0.0206 -0.0017 -0.0101 28  TRP   C CZ2 
1256 C CZ3 . TRP   B 22  ? 0.2348 0.1837 0.2606 -0.0261 0.0008  -0.0057 28  TRP   C CZ3 
1257 C CH2 . TRP   B 22  ? 0.2273 0.1730 0.2507 -0.0225 -0.0002 -0.0062 28  TRP   C CH2 
1258 N N   . ALA   B 23  ? 0.2334 0.2211 0.2884 -0.0321 -0.0020 -0.0183 29  ALA   C N   
1259 C CA  . ALA   B 23  ? 0.2464 0.2405 0.3104 -0.0358 0.0006  -0.0188 29  ALA   C CA  
1260 C C   . ALA   B 23  ? 0.2584 0.2573 0.3240 -0.0349 0.0053  -0.0179 29  ALA   C C   
1261 O O   . ALA   B 23  ? 0.2791 0.2828 0.3511 -0.0384 0.0092  -0.0181 29  ALA   C O   
1262 C CB  . ALA   B 23  ? 0.2333 0.2349 0.3067 -0.0365 -0.0034 -0.0216 29  ALA   C CB  
1263 N N   . ASN   B 24  ? 0.2296 0.2276 0.2900 -0.0307 0.0053  -0.0173 30  ASN   C N   
1264 C CA  . ASN   B 24  ? 0.2254 0.2266 0.2858 -0.0299 0.0100  -0.0171 30  ASN   C CA  
1265 C C   . ASN   B 24  ? 0.2419 0.2358 0.2901 -0.0290 0.0112  -0.0144 30  ASN   C C   
1266 O O   . ASN   B 24  ? 0.2328 0.2272 0.2777 -0.0267 0.0126  -0.0146 30  ASN   C O   
1267 C CB  . ASN   B 24  ? 0.2388 0.2461 0.3055 -0.0257 0.0084  -0.0194 30  ASN   C CB  
1268 C CG  . ASN   B 24  ? 0.2964 0.3124 0.3770 -0.0268 0.0073  -0.0216 30  ASN   C CG  
1269 O OD1 . ASN   B 24  ? 0.2952 0.3172 0.3837 -0.0292 0.0122  -0.0227 30  ASN   C OD1 
1270 N ND2 . ASN   B 24  ? 0.2972 0.3143 0.3810 -0.0256 0.0009  -0.0222 30  ASN   C ND2 
1271 N N   . LEU   B 25  ? 0.2515 0.2386 0.2940 -0.0309 0.0104  -0.0118 31  LEU   C N   
1272 C CA  . LEU   B 25  ? 0.2446 0.2252 0.2773 -0.0301 0.0104  -0.0086 31  LEU   C CA  
1273 C C   . LEU   B 25  ? 0.2557 0.2366 0.2833 -0.0324 0.0147  -0.0067 31  LEU   C C   
1274 O O   . LEU   B 25  ? 0.2767 0.2585 0.3052 -0.0368 0.0182  -0.0058 31  LEU   C O   
1275 C CB  . LEU   B 25  ? 0.2519 0.2255 0.2825 -0.0317 0.0087  -0.0063 31  LEU   C CB  
1276 C CG  . LEU   B 25  ? 0.2631 0.2301 0.2860 -0.0308 0.0080  -0.0023 31  LEU   C CG  
1277 C CD1 . LEU   B 25  ? 0.2607 0.2271 0.2806 -0.0261 0.0053  -0.0033 31  LEU   C CD1 
1278 C CD2 . LEU   B 25  ? 0.2698 0.2298 0.2931 -0.0324 0.0069  -0.0001 31  LEU   C CD2 
1279 N N   . VAL   B 26  ? 0.2432 0.2224 0.2639 -0.0300 0.0144  -0.0059 32  VAL   C N   
1280 C CA  . VAL   B 26  ? 0.2417 0.2199 0.2549 -0.0327 0.0178  -0.0040 32  VAL   C CA  
1281 C C   . VAL   B 26  ? 0.2644 0.2358 0.2694 -0.0334 0.0152  0.0009  32  VAL   C C   
1282 O O   . VAL   B 26  ? 0.2870 0.2556 0.2866 -0.0376 0.0168  0.0045  32  VAL   C O   
1283 C CB  . VAL   B 26  ? 0.2578 0.2388 0.2693 -0.0302 0.0194  -0.0068 32  VAL   C CB  
1284 C CG1 . VAL   B 26  ? 0.2763 0.2548 0.2773 -0.0334 0.0222  -0.0049 32  VAL   C CG1 
1285 C CG2 . VAL   B 26  ? 0.2536 0.2417 0.2750 -0.0296 0.0225  -0.0113 32  VAL   C CG2 
1286 N N   . TRP   B 27  ? 0.2349 0.2037 0.2393 -0.0293 0.0112  0.0013  33  TRP   C N   
1287 C CA  . TRP   B 27  ? 0.2311 0.1947 0.2302 -0.0291 0.0084  0.0058  33  TRP   C CA  
1288 C C   . TRP   B 27  ? 0.2230 0.1848 0.2253 -0.0247 0.0049  0.0048  33  TRP   C C   
1289 O O   . TRP   B 27  ? 0.2248 0.1893 0.2293 -0.0217 0.0043  0.0012  33  TRP   C O   
1290 C CB  . TRP   B 27  ? 0.2445 0.2082 0.2353 -0.0299 0.0089  0.0073  33  TRP   C CB  
1291 C CG  . TRP   B 27  ? 0.2576 0.2176 0.2442 -0.0289 0.0051  0.0117  33  TRP   C CG  
1292 C CD1 . TRP   B 27  ? 0.2921 0.2483 0.2748 -0.0317 0.0035  0.0173  33  TRP   C CD1 
1293 C CD2 . TRP   B 27  ? 0.2436 0.2037 0.2301 -0.0251 0.0025  0.0110  33  TRP   C CD2 
1294 N NE1 . TRP   B 27  ? 0.2977 0.2524 0.2793 -0.0294 -0.0003 0.0201  33  TRP   C NE1 
1295 C CE2 . TRP   B 27  ? 0.2641 0.2213 0.2478 -0.0256 -0.0006 0.0161  33  TRP   C CE2 
1296 C CE3 . TRP   B 27  ? 0.2443 0.2067 0.2327 -0.0215 0.0023  0.0069  33  TRP   C CE3 
1297 C CZ2 . TRP   B 27  ? 0.2617 0.2190 0.2455 -0.0227 -0.0033 0.0168  33  TRP   C CZ2 
1298 C CZ3 . TRP   B 27  ? 0.2509 0.2126 0.2380 -0.0190 -0.0002 0.0077  33  TRP   C CZ3 
1299 C CH2 . TRP   B 27  ? 0.2425 0.2021 0.2277 -0.0197 -0.0027 0.0124  33  TRP   C CH2 
1300 N N   . GLU   B 28  ? 0.2240 0.1809 0.2268 -0.0242 0.0028  0.0080  34  GLU   C N   
1301 C CA  . GLU   B 28  ? 0.2307 0.1856 0.2359 -0.0203 0.0005  0.0069  34  GLU   C CA  
1302 C C   . GLU   B 28  ? 0.2200 0.1709 0.2243 -0.0196 -0.0015 0.0117  34  GLU   C C   
1303 O O   . GLU   B 28  ? 0.2239 0.1719 0.2273 -0.0224 -0.0017 0.0160  34  GLU   C O   
1304 C CB  . GLU   B 28  ? 0.2376 0.1912 0.2484 -0.0198 0.0004  0.0036  34  GLU   C CB  
1305 C CG  . GLU   B 28  ? 0.2407 0.1905 0.2546 -0.0229 0.0012  0.0054  34  GLU   C CG  
1306 C CD  . GLU   B 28  ? 0.2741 0.2172 0.2894 -0.0222 0.0000  0.0090  34  GLU   C CD  
1307 O OE1 . GLU   B 28  ? 0.2786 0.2181 0.2947 -0.0251 0.0005  0.0125  34  GLU   C OE1 
1308 O OE2 . GLU   B 28  ? 0.2334 0.1749 0.2500 -0.0187 -0.0012 0.0084  34  GLU   C OE2 
1309 N N   . ASP   B 29  ? 0.1967 0.1474 0.2020 -0.0162 -0.0030 0.0111  35  ASP   C N   
1310 C CA  . ASP   B 29  ? 0.1985 0.1463 0.2056 -0.0149 -0.0050 0.0154  35  ASP   C CA  
1311 C C   . ASP   B 29  ? 0.1977 0.1443 0.2096 -0.0111 -0.0051 0.0125  35  ASP   C C   
1312 O O   . ASP   B 29  ? 0.1931 0.1426 0.2032 -0.0093 -0.0050 0.0099  35  ASP   C O   
1313 C CB  . ASP   B 29  ? 0.2215 0.1719 0.2232 -0.0159 -0.0066 0.0187  35  ASP   C CB  
1314 C CG  . ASP   B 29  ? 0.2782 0.2268 0.2824 -0.0150 -0.0097 0.0242  35  ASP   C CG  
1315 O OD1 . ASP   B 29  ? 0.3257 0.2720 0.3371 -0.0120 -0.0101 0.0242  35  ASP   C OD1 
1316 O OD2 . ASP   B 29  ? 0.2891 0.2390 0.2881 -0.0174 -0.0117 0.0283  35  ASP   C OD2 
1317 N N   . SER   B 30  ? 0.2089 0.1507 0.2265 -0.0102 -0.0047 0.0126  36  SER   C N   
1318 C CA  A SER   B 30  ? 0.2091 0.1491 0.2312 -0.0071 -0.0037 0.0091  36  SER   C CA  
1319 C CA  B SER   B 30  ? 0.2043 0.1443 0.2263 -0.0071 -0.0037 0.0091  36  SER   C CA  
1320 C C   . SER   B 30  ? 0.2148 0.1567 0.2390 -0.0044 -0.0047 0.0112  36  SER   C C   
1321 O O   . SER   B 30  ? 0.2228 0.1660 0.2472 -0.0025 -0.0034 0.0075  36  SER   C O   
1322 C CB  A SER   B 30  ? 0.2427 0.1762 0.2709 -0.0070 -0.0027 0.0090  36  SER   C CB  
1323 C CB  B SER   B 30  ? 0.2249 0.1585 0.2532 -0.0069 -0.0026 0.0088  36  SER   C CB  
1324 O OG  A SER   B 30  ? 0.3029 0.2341 0.3355 -0.0042 -0.0009 0.0054  36  SER   C OG  
1325 O OG  B SER   B 30  ? 0.2671 0.1978 0.2989 -0.0073 -0.0043 0.0151  36  SER   C OG  
1326 N N   . SER   B 31  ? 0.2061 0.1486 0.2314 -0.0049 -0.0072 0.0172  37  SER   C N   
1327 C CA  . SER   B 31  ? 0.2092 0.1547 0.2379 -0.0026 -0.0087 0.0195  37  SER   C CA  
1328 C C   . SER   B 31  ? 0.2048 0.1553 0.2273 -0.0029 -0.0086 0.0172  37  SER   C C   
1329 O O   . SER   B 31  ? 0.2276 0.1806 0.2532 -0.0010 -0.0089 0.0174  37  SER   C O   
1330 C CB  . SER   B 31  ? 0.2538 0.1990 0.2849 -0.0035 -0.0124 0.0269  37  SER   C CB  
1331 O OG  . SER   B 31  ? 0.3195 0.2673 0.3416 -0.0071 -0.0144 0.0297  37  SER   C OG  
1332 N N   . ARG   B 32  ? 0.1804 0.1322 0.1951 -0.0052 -0.0081 0.0152  38  ARG   C N   
1333 C CA  . ARG   B 32  ? 0.1732 0.1289 0.1824 -0.0054 -0.0080 0.0131  38  ARG   C CA  
1334 C C   . ARG   B 32  ? 0.1790 0.1345 0.1862 -0.0044 -0.0059 0.0074  38  ARG   C C   
1335 O O   . ARG   B 32  ? 0.1750 0.1326 0.1779 -0.0043 -0.0058 0.0055  38  ARG   C O   
1336 C CB  . ARG   B 32  ? 0.1849 0.1421 0.1868 -0.0086 -0.0088 0.0146  38  ARG   C CB  
1337 C CG  . ARG   B 32  ? 0.1857 0.1432 0.1865 -0.0107 -0.0115 0.0204  38  ARG   C CG  
1338 C CD  . ARG   B 32  ? 0.1975 0.1559 0.1897 -0.0146 -0.0112 0.0211  38  ARG   C CD  
1339 N NE  . ARG   B 32  ? 0.2010 0.1619 0.1881 -0.0149 -0.0105 0.0180  38  ARG   C NE  
1340 C CZ  . ARG   B 32  ? 0.2123 0.1741 0.1918 -0.0181 -0.0107 0.0188  38  ARG   C CZ  
1341 N NH1 . ARG   B 32  ? 0.2217 0.1825 0.1967 -0.0219 -0.0119 0.0228  38  ARG   C NH1 
1342 N NH2 . ARG   B 32  ? 0.2079 0.1709 0.1836 -0.0180 -0.0098 0.0157  38  ARG   C NH2 
1343 N N   . ASP   B 33  ? 0.1876 0.1402 0.1974 -0.0041 -0.0045 0.0048  39  ASP   C N   
1344 C CA  . ASP   B 33  ? 0.1815 0.1340 0.1886 -0.0039 -0.0035 -0.0001 39  ASP   C CA  
1345 C C   . ASP   B 33  ? 0.1709 0.1263 0.1735 -0.0054 -0.0041 -0.0008 39  ASP   C C   
1346 O O   . ASP   B 33  ? 0.1749 0.1315 0.1747 -0.0048 -0.0043 -0.0036 39  ASP   C O   
1347 C CB  . ASP   B 33  ? 0.1906 0.1432 0.1967 -0.0022 -0.0026 -0.0028 39  ASP   C CB  
1348 C CG  . ASP   B 33  ? 0.1906 0.1425 0.1928 -0.0027 -0.0022 -0.0072 39  ASP   C CG  
1349 O OD1 . ASP   B 33  ? 0.1977 0.1475 0.2009 -0.0038 -0.0021 -0.0092 39  ASP   C OD1 
1350 O OD2 . ASP   B 33  ? 0.1814 0.1344 0.1791 -0.0023 -0.0024 -0.0085 39  ASP   C OD2 
1351 N N   . LEU   B 34  ? 0.1751 0.1312 0.1773 -0.0073 -0.0042 0.0015  40  LEU   C N   
1352 C CA  . LEU   B 34  ? 0.1782 0.1372 0.1777 -0.0086 -0.0038 0.0002  40  LEU   C CA  
1353 C C   . LEU   B 34  ? 0.1844 0.1436 0.1864 -0.0107 -0.0028 -0.0004 40  LEU   C C   
1354 O O   . LEU   B 34  ? 0.1823 0.1392 0.1862 -0.0122 -0.0025 0.0019  40  LEU   C O   
1355 C CB  . LEU   B 34  ? 0.1827 0.1432 0.1780 -0.0100 -0.0037 0.0027  40  LEU   C CB  
1356 C CG  . LEU   B 34  ? 0.1998 0.1611 0.1920 -0.0087 -0.0046 0.0028  40  LEU   C CG  
1357 C CD1 . LEU   B 34  ? 0.2053 0.1676 0.1925 -0.0111 -0.0045 0.0049  40  LEU   C CD1 
1358 C CD2 . LEU   B 34  ? 0.2158 0.1778 0.2071 -0.0069 -0.0045 -0.0007 40  LEU   C CD2 
1359 N N   . LEU   B 35  ? 0.1761 0.1382 0.1788 -0.0109 -0.0024 -0.0033 41  LEU   C N   
1360 C CA  . LEU   B 35  ? 0.1803 0.1442 0.1864 -0.0132 -0.0011 -0.0040 41  LEU   C CA  
1361 C C   . LEU   B 35  ? 0.1725 0.1407 0.1787 -0.0132 0.0002  -0.0058 41  LEU   C C   
1362 O O   . LEU   B 35  ? 0.1791 0.1485 0.1846 -0.0109 -0.0010 -0.0074 41  LEU   C O   
1363 C CB  . LEU   B 35  ? 0.1890 0.1522 0.1993 -0.0134 -0.0021 -0.0066 41  LEU   C CB  
1364 C CG  . LEU   B 35  ? 0.1930 0.1584 0.2080 -0.0163 -0.0010 -0.0074 41  LEU   C CG  
1365 C CD1 . LEU   B 35  ? 0.1874 0.1493 0.2053 -0.0177 -0.0017 -0.0085 41  LEU   C CD1 
1366 C CD2 . LEU   B 35  ? 0.1974 0.1687 0.2161 -0.0158 -0.0014 -0.0102 41  LEU   C CD2 
1367 N N   . VAL   B 36  ? 0.1774 0.1476 0.1846 -0.0159 0.0028  -0.0053 42  VAL   C N   
1368 C CA  . VAL   B 36  ? 0.1795 0.1540 0.1884 -0.0161 0.0052  -0.0075 42  VAL   C CA  
1369 C C   . VAL   B 36  ? 0.1885 0.1668 0.2048 -0.0181 0.0068  -0.0092 42  VAL   C C   
1370 O O   . VAL   B 36  ? 0.1972 0.1743 0.2137 -0.0213 0.0082  -0.0075 42  VAL   C O   
1371 C CB  . VAL   B 36  ? 0.1938 0.1676 0.1963 -0.0183 0.0081  -0.0061 42  VAL   C CB  
1372 C CG1 . VAL   B 36  ? 0.2090 0.1868 0.2142 -0.0186 0.0118  -0.0093 42  VAL   C CG1 
1373 C CG2 . VAL   B 36  ? 0.1968 0.1675 0.1929 -0.0167 0.0060  -0.0045 42  VAL   C CG2 
1374 N N   . SER   B 37  ? 0.1991 0.1819 0.2220 -0.0162 0.0064  -0.0121 43  SER   C N   
1375 C CA  . SER   B 37  ? 0.1948 0.1828 0.2267 -0.0180 0.0078  -0.0140 43  SER   C CA  
1376 C C   . SER   B 37  ? 0.2108 0.2041 0.2478 -0.0175 0.0115  -0.0163 43  SER   C C   
1377 O O   . SER   B 37  ? 0.2123 0.2045 0.2461 -0.0151 0.0122  -0.0170 43  SER   C O   
1378 C CB  . SER   B 37  ? 0.2014 0.1910 0.2389 -0.0166 0.0033  -0.0153 43  SER   C CB  
1379 O OG  . SER   B 37  ? 0.2251 0.2155 0.2630 -0.0128 0.0003  -0.0163 43  SER   C OG  
1380 N N   . SER   B 38  ? 0.2105 0.2093 0.2559 -0.0199 0.0145  -0.0179 44  SER   C N   
1381 C CA  . SER   B 38  ? 0.2366 0.2406 0.2884 -0.0193 0.0192  -0.0207 44  SER   C CA  
1382 C C   . SER   B 38  ? 0.2649 0.2747 0.3289 -0.0154 0.0162  -0.0229 44  SER   C C   
1383 O O   . SER   B 38  ? 0.2703 0.2820 0.3395 -0.0151 0.0112  -0.0224 44  SER   C O   
1384 C CB  . SER   B 38  ? 0.2562 0.2637 0.3112 -0.0241 0.0251  -0.0214 44  SER   C CB  
1385 O OG  . SER   B 38  ? 0.3006 0.3116 0.3636 -0.0260 0.0231  -0.0212 44  SER   C OG  
1386 N N   . THR   B 39  ? 0.2824 0.2944 0.3508 -0.0126 0.0188  -0.0251 45  THR   C N   
1387 C CA  . THR   B 39  ? 0.3085 0.3257 0.3895 -0.0083 0.0158  -0.0267 45  THR   C CA  
1388 C C   . THR   B 39  ? 0.3458 0.3704 0.4397 -0.0083 0.0222  -0.0301 45  THR   C C   
1389 O O   . THR   B 39  ? 0.3512 0.3750 0.4409 -0.0112 0.0295  -0.0318 45  THR   C O   
1390 C CB  . THR   B 39  ? 0.3222 0.3343 0.3980 -0.0039 0.0130  -0.0262 45  THR   C CB  
1391 O OG1 . THR   B 39  ? 0.3427 0.3525 0.4145 -0.0039 0.0193  -0.0283 45  THR   C OG1 
1392 C CG2 . THR   B 39  ? 0.3268 0.3318 0.3896 -0.0039 0.0081  -0.0233 45  THR   C CG2 
1393 N N   . THR   B 40  ? 0.3694 0.4011 0.4790 -0.0054 0.0195  -0.0312 46  THR   C N   
1394 C CA  . THR   B 40  ? 0.3971 0.4366 0.5220 -0.0044 0.0256  -0.0348 46  THR   C CA  
1395 C C   . THR   B 40  ? 0.4170 0.4541 0.5446 0.0008  0.0272  -0.0366 46  THR   C C   
1396 O O   . THR   B 40  ? 0.4377 0.4777 0.5724 0.0012  0.0349  -0.0404 46  THR   C O   
1397 C CB  . THR   B 40  ? 0.4235 0.4730 0.5664 -0.0039 0.0216  -0.0347 46  THR   C CB  
1398 O OG1 . THR   B 40  ? 0.4540 0.5025 0.5984 -0.0002 0.0120  -0.0321 46  THR   C OG1 
1399 C CG2 . THR   B 40  ? 0.4310 0.4832 0.5729 -0.0098 0.0219  -0.0339 46  THR   C CG2 
1400 N N   . ALA   B 41  ? 0.4112 0.4425 0.5329 0.0045  0.0204  -0.0342 47  ALA   C N   
1401 C CA  . ALA   B 41  ? 0.4160 0.4436 0.5398 0.0093  0.0214  -0.0355 47  ALA   C CA  
1402 C C   . ALA   B 41  ? 0.4280 0.4461 0.5339 0.0077  0.0249  -0.0359 47  ALA   C C   
1403 O O   . ALA   B 41  ? 0.4355 0.4490 0.5271 0.0044  0.0231  -0.0335 47  ALA   C O   
1404 C CB  . ALA   B 41  ? 0.4187 0.4453 0.5466 0.0138  0.0119  -0.0322 47  ALA   C CB  
1405 N N   . GLN   B 42  ? 0.4211 0.4363 0.5286 0.0101  0.0298  -0.0390 48  GLN   C N   
1406 C CA  . GLN   B 42  ? 0.4344 0.4407 0.5255 0.0082  0.0332  -0.0399 48  GLN   C CA  
1407 C C   . GLN   B 42  ? 0.4165 0.4157 0.4983 0.0105  0.0259  -0.0363 48  GLN   C C   
1408 O O   . GLN   B 42  ? 0.4250 0.4239 0.5147 0.0151  0.0208  -0.0349 48  GLN   C O   
1409 C CB  . GLN   B 42  ? 0.4792 0.4843 0.5753 0.0095  0.0415  -0.0453 48  GLN   C CB  
1410 C CG  . GLN   B 42  ? 0.5827 0.5831 0.6634 0.0040  0.0490  -0.0479 48  GLN   C CG  
1411 C CD  . GLN   B 42  ? 0.6806 0.6867 0.7606 -0.0014 0.0538  -0.0485 48  GLN   C CD  
1412 O OE1 . GLN   B 42  ? 0.7121 0.7266 0.8071 -0.0008 0.0553  -0.0496 48  GLN   C OE1 
1413 N NE2 . GLN   B 42  ? 0.6957 0.6973 0.7586 -0.0072 0.0559  -0.0475 48  GLN   C NE2 
1414 N N   . GLY   B 43  ? 0.3853 0.3788 0.4506 0.0069  0.0254  -0.0345 49  GLY   C N   
1415 C CA  . GLY   B 43  ? 0.3771 0.3639 0.4321 0.0080  0.0196  -0.0313 49  GLY   C CA  
1416 C C   . GLY   B 43  ? 0.3690 0.3491 0.4178 0.0086  0.0229  -0.0334 49  GLY   C C   
1417 O O   . GLY   B 43  ? 0.3787 0.3576 0.4233 0.0058  0.0296  -0.0368 49  GLY   C O   
1418 N N   . CYS   B 44  ? 0.3492 0.3243 0.3959 0.0115  0.0180  -0.0314 50  CYS   C N   
1419 C CA  . CYS   B 44  ? 0.3651 0.3331 0.4076 0.0126  0.0201  -0.0332 50  CYS   C CA  
1420 C C   . CYS   B 44  ? 0.3344 0.2959 0.3609 0.0094  0.0189  -0.0316 50  CYS   C C   
1421 O O   . CYS   B 44  ? 0.3524 0.3077 0.3747 0.0095  0.0210  -0.0334 50  CYS   C O   
1422 C CB  . CYS   B 44  ? 0.4262 0.3923 0.4780 0.0179  0.0155  -0.0318 50  CYS   C CB  
1423 S SG  . CYS   B 44  ? 0.6263 0.5890 0.6700 0.0184  0.0061  -0.0257 50  CYS   C SG  
1424 N N   . ASP   B 45  ? 0.2785 0.2412 0.2979 0.0072  0.0149  -0.0279 51  ASP   C N   
1425 C CA  . ASP   B 45  ? 0.2584 0.2161 0.2652 0.0047  0.0129  -0.0258 51  ASP   C CA  
1426 C C   . ASP   B 45  ? 0.2685 0.2245 0.2662 0.0002  0.0177  -0.0278 51  ASP   C C   
1427 O O   . ASP   B 45  ? 0.2893 0.2488 0.2876 -0.0023 0.0217  -0.0295 51  ASP   C O   
1428 C CB  . ASP   B 45  ? 0.2681 0.2281 0.2715 0.0038  0.0081  -0.0218 51  ASP   C CB  
1429 C CG  . ASP   B 45  ? 0.3272 0.2877 0.3360 0.0072  0.0026  -0.0196 51  ASP   C CG  
1430 O OD1 . ASP   B 45  ? 0.3620 0.3198 0.3751 0.0103  0.0014  -0.0199 51  ASP   C OD1 
1431 O OD2 . ASP   B 45  ? 0.3212 0.2843 0.3295 0.0066  -0.0005 -0.0175 51  ASP   C OD2 
1432 N N   . THR   B 46  ? 0.2568 0.2072 0.2457 -0.0014 0.0171  -0.0276 52  THR   C N   
1433 C CA  . THR   B 46  ? 0.2634 0.2118 0.2421 -0.0064 0.0204  -0.0290 52  THR   C CA  
1434 C C   . THR   B 46  ? 0.2509 0.2000 0.2218 -0.0091 0.0161  -0.0246 52  THR   C C   
1435 O O   . THR   B 46  ? 0.2618 0.2093 0.2323 -0.0075 0.0120  -0.0221 52  THR   C O   
1436 C CB  . THR   B 46  ? 0.3192 0.2607 0.2938 -0.0069 0.0226  -0.0321 52  THR   C CB  
1437 O OG1 . THR   B 46  ? 0.3334 0.2741 0.3157 -0.0047 0.0279  -0.0369 52  THR   C OG1 
1438 C CG2 . THR   B 46  ? 0.3508 0.2894 0.3123 -0.0129 0.0240  -0.0327 52  THR   C CG2 
1439 N N   . ILE   B 47  ? 0.2326 0.1841 0.1980 -0.0132 0.0171  -0.0234 53  ILE   C N   
1440 C CA  . ILE   B 47  ? 0.2277 0.1800 0.1875 -0.0154 0.0129  -0.0190 53  ILE   C CA  
1441 C C   . ILE   B 47  ? 0.2306 0.1793 0.1807 -0.0193 0.0127  -0.0191 53  ILE   C C   
1442 O O   . ILE   B 47  ? 0.2347 0.1812 0.1787 -0.0229 0.0165  -0.0221 53  ILE   C O   
1443 C CB  . ILE   B 47  ? 0.2397 0.1957 0.1986 -0.0179 0.0133  -0.0168 53  ILE   C CB  
1444 C CG1 . ILE   B 47  ? 0.2602 0.2198 0.2286 -0.0150 0.0142  -0.0174 53  ILE   C CG1 
1445 C CG2 . ILE   B 47  ? 0.2233 0.1802 0.1789 -0.0193 0.0087  -0.0118 53  ILE   C CG2 
1446 C CD1 . ILE   B 47  ? 0.2909 0.2514 0.2657 -0.0107 0.0098  -0.0155 53  ILE   C CD1 
1447 N N   . ALA   B 48  ? 0.2249 0.1729 0.1732 -0.0193 0.0085  -0.0161 54  ALA   C N   
1448 C CA  . ALA   B 48  ? 0.2261 0.1717 0.1661 -0.0235 0.0074  -0.0157 54  ALA   C CA  
1449 C C   . ALA   B 48  ? 0.2169 0.1649 0.1504 -0.0284 0.0066  -0.0132 54  ALA   C C   
1450 O O   . ALA   B 48  ? 0.2180 0.1696 0.1547 -0.0277 0.0048  -0.0098 54  ALA   C O   
1451 C CB  . ALA   B 48  ? 0.2343 0.1802 0.1759 -0.0222 0.0031  -0.0126 54  ALA   C CB  
1452 N N   . ARG   B 49  ? 0.2128 0.1581 0.1366 -0.0337 0.0077  -0.0148 55  ARG   C N   
1453 C CA  . ARG   B 49  ? 0.2219 0.1689 0.1377 -0.0393 0.0059  -0.0117 55  ARG   C CA  
1454 C C   . ARG   B 49  ? 0.2229 0.1687 0.1328 -0.0430 0.0022  -0.0104 55  ARG   C C   
1455 O O   . ARG   B 49  ? 0.2479 0.1895 0.1496 -0.0470 0.0044  -0.0142 55  ARG   C O   
1456 C CB  . ARG   B 49  ? 0.2357 0.1807 0.1445 -0.0432 0.0114  -0.0155 55  ARG   C CB  
1457 C CG  . ARG   B 49  ? 0.2460 0.1930 0.1623 -0.0396 0.0154  -0.0172 55  ARG   C CG  
1458 C CD  . ARG   B 49  ? 0.2395 0.1909 0.1613 -0.0379 0.0122  -0.0119 55  ARG   C CD  
1459 N NE  . ARG   B 49  ? 0.2674 0.2208 0.1965 -0.0353 0.0163  -0.0141 55  ARG   C NE  
1460 C CZ  . ARG   B 49  ? 0.2813 0.2379 0.2179 -0.0325 0.0145  -0.0112 55  ARG   C CZ  
1461 N NH1 . ARG   B 49  ? 0.2334 0.1912 0.1716 -0.0317 0.0092  -0.0061 55  ARG   C NH1 
1462 N NH2 . ARG   B 49  ? 0.2812 0.2398 0.2245 -0.0307 0.0183  -0.0135 55  ARG   C NH2 
1463 N N   . CYS   B 50  ? 0.2216 0.1710 0.1362 -0.0418 -0.0030 -0.0055 56  CYS   C N   
1464 C CA  . CYS   B 50  ? 0.2228 0.1722 0.1353 -0.0443 -0.0067 -0.0042 56  CYS   C CA  
1465 C C   . CYS   B 50  ? 0.2305 0.1855 0.1500 -0.0430 -0.0121 0.0017  56  CYS   C C   
1466 O O   . CYS   B 50  ? 0.2311 0.1890 0.1573 -0.0395 -0.0126 0.0044  56  CYS   C O   
1467 C CB  . CYS   B 50  ? 0.2244 0.1699 0.1398 -0.0413 -0.0043 -0.0081 56  CYS   C CB  
1468 S SG  . CYS   B 50  ? 0.2247 0.1724 0.1526 -0.0337 -0.0048 -0.0065 56  CYS   C SG  
1469 N N   . ASP   B 51  ? 0.2314 0.1877 0.1502 -0.0458 -0.0156 0.0033  57  ASP   C N   
1470 C CA  . ASP   B 51  ? 0.2433 0.2055 0.1713 -0.0439 -0.0200 0.0083  57  ASP   C CA  
1471 C C   . ASP   B 51  ? 0.2415 0.2035 0.1748 -0.0417 -0.0194 0.0069  57  ASP   C C   
1472 O O   . ASP   B 51  ? 0.2437 0.2104 0.1826 -0.0424 -0.0228 0.0100  57  ASP   C O   
1473 C CB  . ASP   B 51  ? 0.2852 0.2513 0.2102 -0.0493 -0.0257 0.0130  57  ASP   C CB  
1474 C CG  . ASP   B 51  ? 0.3666 0.3311 0.2838 -0.0553 -0.0272 0.0113  57  ASP   C CG  
1475 O OD1 . ASP   B 51  ? 0.3732 0.3323 0.2862 -0.0554 -0.0232 0.0059  57  ASP   C OD1 
1476 O OD2 . ASP   B 51  ? 0.4260 0.3945 0.3417 -0.0599 -0.0327 0.0154  57  ASP   C OD2 
1477 N N   . CYS   B 52  ? 0.2120 0.1690 0.1446 -0.0388 -0.0152 0.0025  58  CYS   C N   
1478 C CA  . CYS   B 52  ? 0.2056 0.1616 0.1425 -0.0367 -0.0145 0.0016  58  CYS   C CA  
1479 C C   . CYS   B 52  ? 0.2075 0.1690 0.1541 -0.0333 -0.0160 0.0050  58  CYS   C C   
1480 O O   . CYS   B 52  ? 0.2050 0.1689 0.1561 -0.0303 -0.0160 0.0066  58  CYS   C O   
1481 C CB  . CYS   B 52  ? 0.1944 0.1444 0.1305 -0.0331 -0.0105 -0.0023 58  CYS   C CB  
1482 S SG  . CYS   B 52  ? 0.2483 0.1905 0.1750 -0.0366 -0.0078 -0.0073 58  CYS   C SG  
1483 N N   . GLN   B 53  ? 0.1885 0.1514 0.1382 -0.0341 -0.0166 0.0056  59  GLN   C N   
1484 C CA  . GLN   B 53  ? 0.1789 0.1463 0.1377 -0.0311 -0.0166 0.0076  59  GLN   C CA  
1485 C C   . GLN   B 53  ? 0.1895 0.1532 0.1479 -0.0298 -0.0139 0.0056  59  GLN   C C   
1486 O O   . GLN   B 53  ? 0.1877 0.1549 0.1521 -0.0289 -0.0133 0.0068  59  GLN   C O   
1487 C CB  . GLN   B 53  ? 0.1858 0.1604 0.1511 -0.0336 -0.0200 0.0113  59  GLN   C CB  
1488 C CG  . GLN   B 53  ? 0.2119 0.1907 0.1802 -0.0335 -0.0231 0.0147  59  GLN   C CG  
1489 C CD  . GLN   B 53  ? 0.2371 0.2237 0.2142 -0.0353 -0.0272 0.0190  59  GLN   C CD  
1490 O OE1 . GLN   B 53  ? 0.2553 0.2441 0.2293 -0.0399 -0.0315 0.0214  59  GLN   C OE1 
1491 N NE2 . GLN   B 53  ? 0.1911 0.1822 0.1795 -0.0320 -0.0258 0.0199  59  GLN   C NE2 
1492 N N   . THR   B 54  ? 0.1862 0.1428 0.1377 -0.0300 -0.0121 0.0025  60  THR   C N   
1493 C CA  . THR   B 54  ? 0.2091 0.1611 0.1596 -0.0283 -0.0100 0.0013  60  THR   C CA  
1494 C C   . THR   B 54  ? 0.2090 0.1556 0.1568 -0.0249 -0.0085 -0.0010 60  THR   C C   
1495 O O   . THR   B 54  ? 0.2248 0.1696 0.1696 -0.0252 -0.0082 -0.0026 60  THR   C O   
1496 C CB  . THR   B 54  ? 0.2754 0.2236 0.2222 -0.0321 -0.0099 0.0006  60  THR   C CB  
1497 O OG1 . THR   B 54  ? 0.3134 0.2557 0.2536 -0.0340 -0.0097 -0.0019 60  THR   C OG1 
1498 C CG2 . THR   B 54  ? 0.2848 0.2394 0.2355 -0.0360 -0.0117 0.0028  60  THR   C CG2 
1499 N N   . GLY   B 55  ? 0.1993 0.1438 0.1482 -0.0218 -0.0075 -0.0010 61  GLY   C N   
1500 C CA  . GLY   B 55  ? 0.2003 0.1407 0.1483 -0.0184 -0.0068 -0.0026 61  GLY   C CA  
1501 C C   . GLY   B 55  ? 0.1916 0.1296 0.1395 -0.0162 -0.0067 -0.0019 61  GLY   C C   
1502 O O   . GLY   B 55  ? 0.2108 0.1489 0.1579 -0.0179 -0.0065 -0.0006 61  GLY   C O   
1503 N N   . VAL   B 56  ? 0.1852 0.1208 0.1338 -0.0130 -0.0070 -0.0027 62  VAL   C N   
1504 C CA  . VAL   B 56  ? 0.1920 0.1249 0.1394 -0.0113 -0.0078 -0.0016 62  VAL   C CA  
1505 C C   . VAL   B 56  ? 0.1857 0.1220 0.1364 -0.0084 -0.0084 -0.0020 62  VAL   C C   
1506 O O   . VAL   B 56  ? 0.1876 0.1249 0.1412 -0.0068 -0.0084 -0.0033 62  VAL   C O   
1507 C CB  . VAL   B 56  ? 0.2101 0.1355 0.1551 -0.0103 -0.0087 -0.0018 62  VAL   C CB  
1508 C CG1 . VAL   B 56  ? 0.2119 0.1342 0.1548 -0.0088 -0.0106 0.0001  62  VAL   C CG1 
1509 C CG2 . VAL   B 56  ? 0.2247 0.1455 0.1660 -0.0135 -0.0079 -0.0017 62  VAL   C CG2 
1510 N N   . TYR   B 57  ? 0.1750 0.1125 0.1248 -0.0083 -0.0085 -0.0012 63  TYR   C N   
1511 C CA  . TYR   B 57  ? 0.1786 0.1187 0.1311 -0.0062 -0.0093 -0.0019 63  TYR   C CA  
1512 C C   . TYR   B 57  ? 0.1959 0.1325 0.1446 -0.0056 -0.0112 -0.0011 63  TYR   C C   
1513 O O   . TYR   B 57  ? 0.2000 0.1328 0.1433 -0.0073 -0.0114 0.0003  63  TYR   C O   
1514 C CB  . TYR   B 57  ? 0.1791 0.1242 0.1346 -0.0066 -0.0077 -0.0022 63  TYR   C CB  
1515 C CG  . TYR   B 57  ? 0.1722 0.1172 0.1249 -0.0081 -0.0063 -0.0020 63  TYR   C CG  
1516 C CD1 . TYR   B 57  ? 0.1996 0.1450 0.1514 -0.0104 -0.0046 -0.0011 63  TYR   C CD1 
1517 C CD2 . TYR   B 57  ? 0.1860 0.1310 0.1375 -0.0076 -0.0060 -0.0030 63  TYR   C CD2 
1518 C CE1 . TYR   B 57  ? 0.2276 0.1737 0.1777 -0.0120 -0.0022 -0.0013 63  TYR   C CE1 
1519 C CE2 . TYR   B 57  ? 0.2072 0.1522 0.1558 -0.0094 -0.0036 -0.0035 63  TYR   C CE2 
1520 C CZ  . TYR   B 57  ? 0.2199 0.1655 0.1681 -0.0115 -0.0014 -0.0027 63  TYR   C CZ  
1521 O OH  . TYR   B 57  ? 0.2268 0.1729 0.1728 -0.0135 0.0019  -0.0035 63  TYR   C OH  
1522 N N   . TYR   B 58  ? 0.2035 0.1411 0.1545 -0.0036 -0.0130 -0.0017 64  TYR   C N   
1523 C CA  . TYR   B 58  ? 0.2054 0.1404 0.1528 -0.0034 -0.0158 -0.0007 64  TYR   C CA  
1524 C C   . TYR   B 58  ? 0.2044 0.1413 0.1490 -0.0050 -0.0148 -0.0016 64  TYR   C C   
1525 O O   . TYR   B 58  ? 0.1987 0.1395 0.1476 -0.0044 -0.0135 -0.0034 64  TYR   C O   
1526 C CB  . TYR   B 58  ? 0.2088 0.1444 0.1613 -0.0007 -0.0189 -0.0008 64  TYR   C CB  
1527 C CG  . TYR   B 58  ? 0.2261 0.1591 0.1745 -0.0010 -0.0230 0.0010  64  TYR   C CG  
1528 C CD1 . TYR   B 58  ? 0.2435 0.1707 0.1860 -0.0018 -0.0252 0.0037  64  TYR   C CD1 
1529 C CD2 . TYR   B 58  ? 0.2397 0.1757 0.1893 -0.0010 -0.0250 0.0001  64  TYR   C CD2 
1530 C CE1 . TYR   B 58  ? 0.2582 0.1828 0.1955 -0.0027 -0.0297 0.0060  64  TYR   C CE1 
1531 C CE2 . TYR   B 58  ? 0.2501 0.1837 0.1945 -0.0021 -0.0293 0.0018  64  TYR   C CE2 
1532 C CZ  . TYR   B 58  ? 0.2752 0.2033 0.2134 -0.0029 -0.0319 0.0050  64  TYR   C CZ  
1533 O OH  . TYR   B 58  ? 0.3126 0.2381 0.2446 -0.0045 -0.0369 0.0074  64  TYR   C OH  
1534 N N   . CYS   B 59  ? 0.2091 0.1426 0.1459 -0.0073 -0.0152 -0.0005 65  CYS   C N   
1535 C CA  . CYS   B 59  ? 0.2085 0.1427 0.1409 -0.0094 -0.0133 -0.0021 65  CYS   C CA  
1536 C C   . CYS   B 59  ? 0.2232 0.1543 0.1491 -0.0104 -0.0174 -0.0012 65  CYS   C C   
1537 O O   . CYS   B 59  ? 0.2429 0.1694 0.1609 -0.0123 -0.0193 0.0011  65  CYS   C O   
1538 C CB  . CYS   B 59  ? 0.2098 0.1429 0.1378 -0.0121 -0.0096 -0.0019 65  CYS   C CB  
1539 S SG  . CYS   B 59  ? 0.2456 0.1788 0.1675 -0.0151 -0.0058 -0.0045 65  CYS   C SG  
1540 N N   . SER   B 60  ? 0.2163 0.1500 0.1454 -0.0095 -0.0192 -0.0029 66  SER   C N   
1541 C CA  . SER   B 60  ? 0.2364 0.1679 0.1600 -0.0108 -0.0240 -0.0019 66  SER   C CA  
1542 C C   . SER   B 60  ? 0.2511 0.1789 0.1626 -0.0150 -0.0231 -0.0023 66  SER   C C   
1543 O O   . SER   B 60  ? 0.2651 0.1892 0.1688 -0.0168 -0.0277 0.0005  66  SER   C O   
1544 C CB  . SER   B 60  ? 0.2895 0.2249 0.2194 -0.0096 -0.0260 -0.0038 66  SER   C CB  
1545 O OG  . SER   B 60  ? 0.3884 0.3254 0.3186 -0.0108 -0.0218 -0.0073 66  SER   C OG  
1546 N N   . SER   B 61  ? 0.2501 0.1788 0.1598 -0.0168 -0.0171 -0.0053 67  SER   C N   
1547 C CA  . SER   B 61  ? 0.2576 0.1826 0.1552 -0.0214 -0.0147 -0.0065 67  SER   C CA  
1548 C C   . SER   B 61  ? 0.2764 0.1972 0.1659 -0.0237 -0.0145 -0.0032 67  SER   C C   
1549 O O   . SER   B 61  ? 0.2828 0.2001 0.1607 -0.0281 -0.0127 -0.0036 67  SER   C O   
1550 C CB  . SER   B 61  ? 0.2752 0.2024 0.1753 -0.0221 -0.0076 -0.0110 67  SER   C CB  
1551 O OG  . SER   B 61  ? 0.2683 0.1984 0.1759 -0.0204 -0.0034 -0.0108 67  SER   C OG  
1552 N N   . ARG   B 62  ? 0.2581 0.1786 0.1526 -0.0213 -0.0160 -0.0001 68  ARG   C N   
1553 C CA  . ARG   B 62  ? 0.2570 0.1726 0.1442 -0.0236 -0.0165 0.0035  68  ARG   C CA  
1554 C C   . ARG   B 62  ? 0.2657 0.1780 0.1545 -0.0212 -0.0234 0.0079  68  ARG   C C   
1555 O O   . ARG   B 62  ? 0.2838 0.1909 0.1675 -0.0226 -0.0247 0.0115  68  ARG   C O   
1556 C CB  . ARG   B 62  ? 0.2648 0.1824 0.1572 -0.0234 -0.0111 0.0029  68  ARG   C CB  
1557 C CG  . ARG   B 62  ? 0.2845 0.2055 0.1768 -0.0256 -0.0041 -0.0009 68  ARG   C CG  
1558 C CD  . ARG   B 62  ? 0.3008 0.2173 0.1797 -0.0311 -0.0016 -0.0005 68  ARG   C CD  
1559 N NE  . ARG   B 62  ? 0.3323 0.2521 0.2120 -0.0331 0.0060  -0.0048 68  ARG   C NE  
1560 C CZ  . ARG   B 62  ? 0.3760 0.2965 0.2532 -0.0342 0.0086  -0.0088 68  ARG   C CZ  
1561 N NH1 . ARG   B 62  ? 0.3647 0.2832 0.2379 -0.0338 0.0037  -0.0091 68  ARG   C NH1 
1562 N NH2 . ARG   B 62  ? 0.3938 0.3170 0.2731 -0.0358 0.0163  -0.0129 68  ARG   C NH2 
1563 N N   . ARG   B 63  ? 0.2685 0.1838 0.1657 -0.0175 -0.0275 0.0076  69  ARG   C N   
1564 C CA  . ARG   B 63  ? 0.2705 0.1837 0.1728 -0.0143 -0.0331 0.0112  69  ARG   C CA  
1565 C C   . ARG   B 63  ? 0.2902 0.2007 0.1960 -0.0129 -0.0311 0.0125  69  ARG   C C   
1566 O O   . ARG   B 63  ? 0.3113 0.2160 0.2146 -0.0127 -0.0345 0.0164  69  ARG   C O   
1567 C CB  . ARG   B 63  ? 0.3055 0.2136 0.1992 -0.0162 -0.0399 0.0155  69  ARG   C CB  
1568 C CG  . ARG   B 63  ? 0.3493 0.2605 0.2419 -0.0171 -0.0438 0.0143  69  ARG   C CG  
1569 C CD  . ARG   B 63  ? 0.4591 0.3657 0.3439 -0.0190 -0.0518 0.0194  69  ARG   C CD  
1570 N NE  . ARG   B 63  ? 0.5424 0.4511 0.4215 -0.0221 -0.0549 0.0179  69  ARG   C NE  
1571 C CZ  . ARG   B 63  ? 0.6051 0.5095 0.4685 -0.0278 -0.0570 0.0193  69  ARG   C CZ  
1572 N NH1 . ARG   B 63  ? 0.6222 0.5200 0.4740 -0.0311 -0.0560 0.0225  69  ARG   C NH1 
1573 N NH2 . ARG   B 63  ? 0.6056 0.5119 0.4639 -0.0309 -0.0598 0.0173  69  ARG   C NH2 
1574 N N   . LYS   B 64  ? 0.2703 0.1845 0.1808 -0.0126 -0.0254 0.0095  70  LYS   C N   
1575 C CA  . LYS   B 64  ? 0.2765 0.1881 0.1887 -0.0125 -0.0232 0.0104  70  LYS   C CA  
1576 C C   . LYS   B 64  ? 0.2425 0.1594 0.1640 -0.0104 -0.0198 0.0074  70  LYS   C C   
1577 O O   . LYS   B 64  ? 0.2410 0.1634 0.1659 -0.0100 -0.0177 0.0047  70  LYS   C O   
1578 C CB  . LYS   B 64  ? 0.3365 0.2464 0.2406 -0.0171 -0.0191 0.0107  70  LYS   C CB  
1579 C CG  . LYS   B 64  ? 0.4906 0.3929 0.3839 -0.0203 -0.0213 0.0147  70  LYS   C CG  
1580 C CD  . LYS   B 64  ? 0.5789 0.4806 0.4670 -0.0247 -0.0160 0.0144  70  LYS   C CD  
1581 C CE  . LYS   B 64  ? 0.6650 0.5583 0.5426 -0.0285 -0.0176 0.0188  70  LYS   C CE  
1582 N NZ  . LYS   B 64  ? 0.6975 0.5883 0.5628 -0.0325 -0.0182 0.0201  70  LYS   C NZ  
1583 N N   . HIS   B 65  ? 0.2363 0.1509 0.1611 -0.0095 -0.0193 0.0078  71  HIS   C N   
1584 C CA  . HIS   B 65  ? 0.2099 0.1287 0.1409 -0.0089 -0.0161 0.0054  71  HIS   C CA  
1585 C C   . HIS   B 65  ? 0.2418 0.1605 0.1695 -0.0124 -0.0127 0.0055  71  HIS   C C   
1586 O O   . HIS   B 65  ? 0.2905 0.2039 0.2122 -0.0149 -0.0129 0.0077  71  HIS   C O   
1587 C CB  . HIS   B 65  ? 0.2116 0.1275 0.1474 -0.0066 -0.0170 0.0051  71  HIS   C CB  
1588 C CG  . HIS   B 65  ? 0.2364 0.1532 0.1777 -0.0029 -0.0198 0.0048  71  HIS   C CG  
1589 N ND1 . HIS   B 65  ? 0.2573 0.1795 0.2056 -0.0009 -0.0186 0.0021  71  HIS   C ND1 
1590 C CD2 . HIS   B 65  ? 0.2468 0.1599 0.1880 -0.0012 -0.0240 0.0071  71  HIS   C CD2 
1591 C CE1 . HIS   B 65  ? 0.2427 0.1647 0.1959 0.0020  -0.0215 0.0026  71  HIS   C CE1 
1592 N NE2 . HIS   B 65  ? 0.2800 0.1971 0.2295 0.0021  -0.0252 0.0056  71  HIS   C NE2 
1593 N N   . TYR   B 66  ? 0.2136 0.1385 0.1459 -0.0129 -0.0098 0.0035  72  TYR   C N   
1594 C CA  . TYR   B 66  ? 0.2159 0.1425 0.1476 -0.0161 -0.0069 0.0037  72  TYR   C CA  
1595 C C   . TYR   B 66  ? 0.2049 0.1346 0.1420 -0.0161 -0.0063 0.0026  72  TYR   C C   
1596 O O   . TYR   B 66  ? 0.2029 0.1369 0.1451 -0.0141 -0.0064 0.0013  72  TYR   C O   
1597 C CB  . TYR   B 66  ? 0.2278 0.1600 0.1609 -0.0170 -0.0040 0.0025  72  TYR   C CB  
1598 C CG  . TYR   B 66  ? 0.2473 0.1765 0.1731 -0.0186 -0.0035 0.0030  72  TYR   C CG  
1599 C CD1 . TYR   B 66  ? 0.2619 0.1873 0.1810 -0.0222 -0.0021 0.0046  72  TYR   C CD1 
1600 C CD2 . TYR   B 66  ? 0.2505 0.1808 0.1755 -0.0172 -0.0041 0.0017  72  TYR   C CD2 
1601 C CE1 . TYR   B 66  ? 0.2808 0.2031 0.1913 -0.0245 -0.0015 0.0052  72  TYR   C CE1 
1602 C CE2 . TYR   B 66  ? 0.2641 0.1914 0.1807 -0.0194 -0.0037 0.0019  72  TYR   C CE2 
1603 C CZ  . TYR   B 66  ? 0.2904 0.2138 0.1994 -0.0232 -0.0022 0.0036  72  TYR   C CZ  
1604 O OH  . TYR   B 66  ? 0.3421 0.2622 0.2411 -0.0262 -0.0016 0.0038  72  TYR   C OH  
1605 N N   . PRO   B 67  ? 0.2052 0.1327 0.1408 -0.0190 -0.0056 0.0033  73  PRO   C N   
1606 C CA  . PRO   B 67  ? 0.2062 0.1369 0.1456 -0.0202 -0.0052 0.0023  73  PRO   C CA  
1607 C C   . PRO   B 67  ? 0.2188 0.1575 0.1632 -0.0216 -0.0035 0.0025  73  PRO   C C   
1608 O O   . PRO   B 67  ? 0.2243 0.1642 0.1680 -0.0235 -0.0016 0.0032  73  PRO   C O   
1609 C CB  . PRO   B 67  ? 0.2146 0.1394 0.1500 -0.0233 -0.0052 0.0030  73  PRO   C CB  
1610 C CG  . PRO   B 67  ? 0.2264 0.1472 0.1568 -0.0248 -0.0046 0.0048  73  PRO   C CG  
1611 C CD  . PRO   B 67  ? 0.2119 0.1335 0.1413 -0.0219 -0.0052 0.0051  73  PRO   C CD  
1612 N N   . VAL   B 68  ? 0.1961 0.1402 0.1457 -0.0208 -0.0042 0.0019  74  VAL   C N   
1613 C CA  . VAL   B 68  ? 0.2009 0.1527 0.1571 -0.0216 -0.0031 0.0026  74  VAL   C CA  
1614 C C   . VAL   B 68  ? 0.2002 0.1560 0.1599 -0.0232 -0.0050 0.0032  74  VAL   C C   
1615 O O   . VAL   B 68  ? 0.2192 0.1725 0.1762 -0.0228 -0.0065 0.0025  74  VAL   C O   
1616 C CB  . VAL   B 68  ? 0.2179 0.1728 0.1781 -0.0184 -0.0023 0.0020  74  VAL   C CB  
1617 C CG1 . VAL   B 68  ? 0.2428 0.1951 0.1993 -0.0181 -0.0002 0.0014  74  VAL   C CG1 
1618 C CG2 . VAL   B 68  ? 0.2160 0.1696 0.1759 -0.0157 -0.0041 0.0013  74  VAL   C CG2 
1619 N N   . SER   B 69  ? 0.1855 0.1481 0.1518 -0.0249 -0.0049 0.0046  75  SER   C N   
1620 C CA  . SER   B 69  ? 0.1861 0.1540 0.1572 -0.0259 -0.0074 0.0060  75  SER   C CA  
1621 C C   . SER   B 69  ? 0.1711 0.1428 0.1484 -0.0222 -0.0074 0.0066  75  SER   C C   
1622 O O   . SER   B 69  ? 0.1800 0.1523 0.1603 -0.0199 -0.0048 0.0058  75  SER   C O   
1623 C CB  . SER   B 69  ? 0.2235 0.1978 0.2010 -0.0292 -0.0079 0.0078  75  SER   C CB  
1624 O OG  . SER   B 69  ? 0.3229 0.2932 0.2944 -0.0332 -0.0081 0.0072  75  SER   C OG  
1625 N N   . PHE   B 70  ? 0.1629 0.1361 0.1410 -0.0219 -0.0100 0.0078  76  PHE   C N   
1626 C CA  . PHE   B 70  ? 0.1704 0.1463 0.1544 -0.0186 -0.0100 0.0087  76  PHE   C CA  
1627 C C   . PHE   B 70  ? 0.1645 0.1453 0.1532 -0.0200 -0.0137 0.0120  76  PHE   C C   
1628 O O   . PHE   B 70  ? 0.1830 0.1643 0.1679 -0.0237 -0.0163 0.0131  76  PHE   C O   
1629 C CB  . PHE   B 70  ? 0.1758 0.1467 0.1548 -0.0161 -0.0091 0.0067  76  PHE   C CB  
1630 C CG  . PHE   B 70  ? 0.1763 0.1434 0.1480 -0.0176 -0.0103 0.0059  76  PHE   C CG  
1631 C CD1 . PHE   B 70  ? 0.1713 0.1331 0.1365 -0.0183 -0.0093 0.0037  76  PHE   C CD1 
1632 C CD2 . PHE   B 70  ? 0.1794 0.1475 0.1506 -0.0182 -0.0120 0.0071  76  PHE   C CD2 
1633 C CE1 . PHE   B 70  ? 0.1821 0.1401 0.1415 -0.0194 -0.0095 0.0022  76  PHE   C CE1 
1634 C CE2 . PHE   B 70  ? 0.1925 0.1570 0.1567 -0.0198 -0.0120 0.0056  76  PHE   C CE2 
1635 C CZ  . PHE   B 70  ? 0.1831 0.1427 0.1420 -0.0201 -0.0105 0.0029  76  PHE   C CZ  
1636 N N   . SER   B 71  ? 0.1520 0.1363 0.1492 -0.0174 -0.0139 0.0138  77  SER   C N   
1637 C CA  . SER   B 71  ? 0.1701 0.1593 0.1733 -0.0184 -0.0180 0.0180  77  SER   C CA  
1638 C C   . SER   B 71  ? 0.1915 0.1779 0.1879 -0.0196 -0.0206 0.0193  77  SER   C C   
1639 O O   . SER   B 71  ? 0.2081 0.1891 0.1962 -0.0194 -0.0187 0.0165  77  SER   C O   
1640 C CB  . SER   B 71  ? 0.1777 0.1710 0.1939 -0.0148 -0.0171 0.0195  77  SER   C CB  
1641 O OG  . SER   B 71  ? 0.1957 0.1850 0.2113 -0.0116 -0.0152 0.0182  77  SER   C OG  
1642 N N   . LYS   B 72  ? 0.1905 0.1804 0.1905 -0.0211 -0.0249 0.0238  78  LYS   C N   
1643 C CA  . LYS   B 72  ? 0.2066 0.1938 0.1998 -0.0227 -0.0271 0.0255  78  LYS   C CA  
1644 C C   . LYS   B 72  ? 0.2125 0.1979 0.2106 -0.0186 -0.0254 0.0258  78  LYS   C C   
1645 O O   . LYS   B 72  ? 0.2340 0.2220 0.2430 -0.0153 -0.0247 0.0268  78  LYS   C O   
1646 C CB  . LYS   B 72  ? 0.2489 0.2404 0.2435 -0.0264 -0.0331 0.0309  78  LYS   C CB  
1647 C CG  . LYS   B 72  ? 0.3100 0.3031 0.2990 -0.0313 -0.0351 0.0304  78  LYS   C CG  
1648 C CD  . LYS   B 72  ? 0.3987 0.3956 0.3867 -0.0360 -0.0419 0.0359  78  LYS   C CD  
1649 C CE  . LYS   B 72  ? 0.4938 0.4936 0.4793 -0.0409 -0.0444 0.0355  78  LYS   C CE  
1650 N NZ  . LYS   B 72  ? 0.5305 0.5362 0.5189 -0.0450 -0.0521 0.0418  78  LYS   C NZ  
1651 N N   . PRO   B 73  ? 0.2094 0.1908 0.2004 -0.0193 -0.0249 0.0254  79  PRO   C N   
1652 C CA  . PRO   B 73  ? 0.2169 0.1963 0.2126 -0.0160 -0.0233 0.0257  79  PRO   C CA  
1653 C C   . PRO   B 73  ? 0.2339 0.2161 0.2400 -0.0146 -0.0266 0.0309  79  PRO   C C   
1654 O O   . PRO   B 73  ? 0.2471 0.2317 0.2527 -0.0176 -0.0314 0.0359  79  PRO   C O   
1655 C CB  . PRO   B 73  ? 0.2337 0.2092 0.2196 -0.0184 -0.0228 0.0252  79  PRO   C CB  
1656 C CG  . PRO   B 73  ? 0.2500 0.2244 0.2262 -0.0216 -0.0219 0.0220  79  PRO   C CG  
1657 C CD  . PRO   B 73  ? 0.2210 0.1992 0.1996 -0.0232 -0.0247 0.0238  79  PRO   C CD  
1658 N N   . SER   B 74  ? 0.2247 0.2066 0.2404 -0.0104 -0.0242 0.0299  80  SER   C N   
1659 C CA  . SER   B 74  ? 0.2453 0.2297 0.2733 -0.0083 -0.0269 0.0347  80  SER   C CA  
1660 C C   . SER   B 74  ? 0.2331 0.2141 0.2684 -0.0041 -0.0234 0.0328  80  SER   C C   
1661 O O   . SER   B 74  ? 0.2175 0.1948 0.2479 -0.0032 -0.0193 0.0278  80  SER   C O   
1662 C CB  . SER   B 74  ? 0.3073 0.2979 0.3444 -0.0078 -0.0283 0.0360  80  SER   C CB  
1663 O OG  . SER   B 74  ? 0.3688 0.3598 0.4111 -0.0048 -0.0230 0.0311  80  SER   C OG  
1664 N N   . LEU   B 75  ? 0.2247 0.2067 0.2723 -0.0016 -0.0254 0.0369  81  LEU   C N   
1665 C CA  . LEU   B 75  ? 0.2461 0.2243 0.3020 0.0023  -0.0221 0.0352  81  LEU   C CA  
1666 C C   . LEU   B 75  ? 0.2589 0.2399 0.3240 0.0054  -0.0177 0.0309  81  LEU   C C   
1667 O O   . LEU   B 75  ? 0.2752 0.2618 0.3506 0.0064  -0.0193 0.0335  81  LEU   C O   
1668 C CB  . LEU   B 75  ? 0.2680 0.2460 0.3345 0.0036  -0.0265 0.0420  81  LEU   C CB  
1669 C CG  . LEU   B 75  ? 0.3309 0.3037 0.3912 0.0016  -0.0292 0.0459  81  LEU   C CG  
1670 C CD1 . LEU   B 75  ? 0.3580 0.3312 0.4299 0.0029  -0.0346 0.0540  81  LEU   C CD1 
1671 C CD2 . LEU   B 75  ? 0.3509 0.3172 0.4093 0.0030  -0.0243 0.0411  81  LEU   C CD2 
1672 N N   . ILE   B 76  ? 0.2391 0.2162 0.3007 0.0067  -0.0122 0.0246  82  ILE   C N   
1673 C CA  . ILE   B 76  ? 0.2506 0.2294 0.3182 0.0088  -0.0070 0.0198  82  ILE   C CA  
1674 C C   . ILE   B 76  ? 0.2469 0.2203 0.3190 0.0116  -0.0023 0.0157  82  ILE   C C   
1675 O O   . ILE   B 76  ? 0.2431 0.2111 0.3075 0.0107  -0.0018 0.0138  82  ILE   C O   
1676 C CB  . ILE   B 76  ? 0.2828 0.2625 0.3389 0.0063  -0.0050 0.0158  82  ILE   C CB  
1677 C CG1 . ILE   B 76  ? 0.3262 0.3116 0.3809 0.0037  -0.0090 0.0195  82  ILE   C CG1 
1678 C CG2 . ILE   B 76  ? 0.2939 0.2732 0.3519 0.0076  0.0012  0.0100  82  ILE   C CG2 
1679 C CD1 . ILE   B 76  ? 0.3853 0.3698 0.4279 0.0010  -0.0087 0.0172  82  ILE   C CD1 
1680 N N   . PHE   B 77  ? 0.2434 0.2182 0.3288 0.0147  0.0013  0.0141  83  PHE   C N   
1681 C CA  . PHE   B 77  ? 0.2662 0.2351 0.3557 0.0170  0.0065  0.0093  83  PHE   C CA  
1682 C C   . PHE   B 77  ? 0.2702 0.2358 0.3475 0.0152  0.0114  0.0021  83  PHE   C C   
1683 O O   . PHE   B 77  ? 0.2911 0.2601 0.3639 0.0138  0.0136  -0.0004 83  PHE   C O   
1684 C CB  . PHE   B 77  ? 0.2843 0.2558 0.3919 0.0209  0.0101  0.0087  83  PHE   C CB  
1685 C CG  . PHE   B 77  ? 0.3068 0.2716 0.4194 0.0233  0.0164  0.0029  83  PHE   C CG  
1686 C CD1 . PHE   B 77  ? 0.3331 0.2969 0.4423 0.0228  0.0237  -0.0047 83  PHE   C CD1 
1687 C CD2 . PHE   B 77  ? 0.3222 0.2811 0.4413 0.0253  0.0151  0.0050  83  PHE   C CD2 
1688 C CE1 . PHE   B 77  ? 0.3456 0.3025 0.4580 0.0243  0.0298  -0.0107 83  PHE   C CE1 
1689 C CE2 . PHE   B 77  ? 0.3425 0.2942 0.4658 0.0271  0.0212  -0.0009 83  PHE   C CE2 
1690 C CZ  . PHE   B 77  ? 0.3400 0.2908 0.4595 0.0264  0.0285  -0.0090 83  PHE   C CZ  
1691 N N   . VAL   B 78  ? 0.2739 0.2326 0.3462 0.0148  0.0129  -0.0010 84  VAL   C N   
1692 C CA  . VAL   B 78  ? 0.2699 0.2245 0.3309 0.0128  0.0166  -0.0075 84  VAL   C CA  
1693 C C   . VAL   B 78  ? 0.2778 0.2260 0.3440 0.0143  0.0214  -0.0123 84  VAL   C C   
1694 O O   . VAL   B 78  ? 0.2733 0.2174 0.3446 0.0154  0.0198  -0.0103 84  VAL   C O   
1695 C CB  . VAL   B 78  ? 0.2624 0.2150 0.3108 0.0101  0.0125  -0.0064 84  VAL   C CB  
1696 C CG1 . VAL   B 78  ? 0.2677 0.2168 0.3051 0.0079  0.0152  -0.0124 84  VAL   C CG1 
1697 C CG2 . VAL   B 78  ? 0.2558 0.2138 0.2993 0.0086  0.0083  -0.0022 84  VAL   C CG2 
1698 N N   . GLU   B 79  ? 0.2902 0.2367 0.3536 0.0137  0.0274  -0.0188 85  GLU   C N   
1699 C CA  . GLU   B 79  ? 0.3072 0.2469 0.3742 0.0145  0.0328  -0.0245 85  GLU   C CA  
1700 C C   . GLU   B 79  ? 0.2926 0.2257 0.3507 0.0121  0.0309  -0.0264 85  GLU   C C   
1701 O O   . GLU   B 79  ? 0.2807 0.2150 0.3281 0.0095  0.0266  -0.0246 85  GLU   C O   
1702 C CB  . GLU   B 79  ? 0.3785 0.3179 0.4414 0.0131  0.0399  -0.0315 85  GLU   C CB  
1703 C CG  . GLU   B 79  ? 0.4904 0.4364 0.5647 0.0154  0.0431  -0.0305 85  GLU   C CG  
1704 C CD  . GLU   B 79  ? 0.6374 0.5814 0.7188 0.0165  0.0523  -0.0374 85  GLU   C CD  
1705 O OE1 . GLU   B 79  ? 0.6895 0.6398 0.7810 0.0181  0.0555  -0.0370 85  GLU   C OE1 
1706 O OE2 . GLU   B 79  ? 0.6858 0.6221 0.7634 0.0155  0.0564  -0.0434 85  GLU   C OE2 
1707 N N   . ALA   B 80  ? 0.2806 0.2067 0.3437 0.0129  0.0345  -0.0303 86  ALA   C N   
1708 C CA  . ALA   B 80  ? 0.2846 0.2042 0.3402 0.0102  0.0331  -0.0325 86  ALA   C CA  
1709 C C   . ALA   B 80  ? 0.2796 0.1988 0.3192 0.0058  0.0335  -0.0374 86  ALA   C C   
1710 O O   . ALA   B 80  ? 0.2894 0.2099 0.3238 0.0048  0.0374  -0.0413 86  ALA   C O   
1711 C CB  . ALA   B 80  ? 0.3017 0.2130 0.3655 0.0115  0.0378  -0.0368 86  ALA   C CB  
1712 N N   . SER   B 81  ? 0.2724 0.1897 0.3042 0.0031  0.0294  -0.0369 87  SER   C N   
1713 C CA  . SER   B 81  ? 0.2733 0.1899 0.2909 -0.0012 0.0285  -0.0409 87  SER   C CA  
1714 C C   . SER   B 81  ? 0.2946 0.2056 0.3098 -0.0038 0.0269  -0.0430 87  SER   C C   
1715 O O   . SER   B 81  ? 0.2995 0.2069 0.3240 -0.0023 0.0271  -0.0414 87  SER   C O   
1716 C CB  . SER   B 81  ? 0.2758 0.1990 0.2866 -0.0019 0.0234  -0.0364 87  SER   C CB  
1717 O OG  . SER   B 81  ? 0.2553 0.1803 0.2691 -0.0015 0.0185  -0.0314 87  SER   C OG  
1718 N N   . GLU   B 82  ? 0.3080 0.2184 0.3115 -0.0080 0.0248  -0.0461 88  GLU   C N   
1719 C CA  . GLU   B 82  ? 0.3329 0.2392 0.3346 -0.0111 0.0227  -0.0480 88  GLU   C CA  
1720 C C   . GLU   B 82  ? 0.3303 0.2400 0.3375 -0.0102 0.0178  -0.0418 88  GLU   C C   
1721 O O   . GLU   B 82  ? 0.3280 0.2338 0.3386 -0.0118 0.0171  -0.0421 88  GLU   C O   
1722 C CB  . GLU   B 82  ? 0.3990 0.3050 0.3873 -0.0160 0.0205  -0.0521 88  GLU   C CB  
1723 C CG  . GLU   B 82  ? 0.5117 0.4133 0.4922 -0.0181 0.0257  -0.0587 88  GLU   C CG  
1724 C CD  . GLU   B 82  ? 0.6758 0.5821 0.6483 -0.0182 0.0254  -0.0576 88  GLU   C CD  
1725 O OE1 . GLU   B 82  ? 0.7279 0.6317 0.6883 -0.0223 0.0265  -0.0621 88  GLU   C OE1 
1726 O OE2 . GLU   B 82  ? 0.6896 0.6017 0.6672 -0.0147 0.0238  -0.0520 88  GLU   C OE2 
1727 N N   . TYR   B 83  ? 0.3106 0.2271 0.3186 -0.0081 0.0149  -0.0363 89  TYR   C N   
1728 C CA  . TYR   B 83  ? 0.3003 0.2201 0.3122 -0.0078 0.0110  -0.0308 89  TYR   C CA  
1729 C C   . TYR   B 83  ? 0.2921 0.2115 0.3138 -0.0048 0.0115  -0.0257 89  TYR   C C   
1730 O O   . TYR   B 83  ? 0.3224 0.2417 0.3472 -0.0055 0.0093  -0.0220 89  TYR   C O   
1731 C CB  . TYR   B 83  ? 0.2950 0.2220 0.3015 -0.0080 0.0074  -0.0279 89  TYR   C CB  
1732 C CG  . TYR   B 83  ? 0.3205 0.2487 0.3188 -0.0111 0.0048  -0.0309 89  TYR   C CG  
1733 C CD1 . TYR   B 83  ? 0.3211 0.2513 0.3201 -0.0134 0.0015  -0.0301 89  TYR   C CD1 
1734 C CD2 . TYR   B 83  ? 0.3444 0.2726 0.3347 -0.0120 0.0052  -0.0339 89  TYR   C CD2 
1735 C CE1 . TYR   B 83  ? 0.3430 0.2755 0.3361 -0.0160 -0.0017 -0.0322 89  TYR   C CE1 
1736 C CE2 . TYR   B 83  ? 0.3647 0.2942 0.3474 -0.0151 0.0018  -0.0357 89  TYR   C CE2 
1737 C CZ  . TYR   B 83  ? 0.3682 0.3002 0.3530 -0.0168 -0.0020 -0.0347 89  TYR   C CZ  
1738 O OH  . TYR   B 83  ? 0.4201 0.3542 0.3991 -0.0196 -0.0062 -0.0360 89  TYR   C OH  
1739 N N   . TYR   B 84  ? 0.2707 0.1898 0.2976 -0.0016 0.0143  -0.0252 90  TYR   C N   
1740 C CA  . TYR   B 84  ? 0.2764 0.1959 0.3130 0.0013  0.0136  -0.0195 90  TYR   C CA  
1741 C C   . TYR   B 84  ? 0.3041 0.2196 0.3500 0.0044  0.0178  -0.0213 90  TYR   C C   
1742 O O   . TYR   B 84  ? 0.3064 0.2220 0.3509 0.0049  0.0216  -0.0259 90  TYR   C O   
1743 C CB  . TYR   B 84  ? 0.2642 0.1913 0.2998 0.0028  0.0111  -0.0147 90  TYR   C CB  
1744 C CG  . TYR   B 84  ? 0.2487 0.1801 0.2769 0.0005  0.0073  -0.0124 90  TYR   C CG  
1745 C CD1 . TYR   B 84  ? 0.2555 0.1911 0.2760 -0.0002 0.0066  -0.0141 90  TYR   C CD1 
1746 C CD2 . TYR   B 84  ? 0.2393 0.1704 0.2685 -0.0009 0.0048  -0.0085 90  TYR   C CD2 
1747 C CE1 . TYR   B 84  ? 0.2462 0.1856 0.2615 -0.0017 0.0035  -0.0121 90  TYR   C CE1 
1748 C CE2 . TYR   B 84  ? 0.2255 0.1609 0.2489 -0.0028 0.0023  -0.0070 90  TYR   C CE2 
1749 C CZ  . TYR   B 84  ? 0.2355 0.1751 0.2526 -0.0029 0.0017  -0.0089 90  TYR   C CZ  
1750 O OH  . TYR   B 84  ? 0.2195 0.1629 0.2324 -0.0045 -0.0003 -0.0078 90  TYR   C OH  
1751 N N   . PRO   B 85  ? 0.3165 0.2290 0.3727 0.0065  0.0172  -0.0170 91  PRO   C N   
1752 C CA  . PRO   B 85  ? 0.3161 0.2262 0.3842 0.0104  0.0208  -0.0176 91  PRO   C CA  
1753 C C   . PRO   B 85  ? 0.3106 0.2285 0.3820 0.0129  0.0202  -0.0146 91  PRO   C C   
1754 O O   . PRO   B 85  ? 0.3005 0.2247 0.3659 0.0117  0.0162  -0.0106 91  PRO   C O   
1755 C CB  . PRO   B 85  ? 0.3279 0.2332 0.4056 0.0118  0.0184  -0.0117 91  PRO   C CB  
1756 C CG  . PRO   B 85  ? 0.3377 0.2473 0.4084 0.0091  0.0128  -0.0058 91  PRO   C CG  
1757 C CD  . PRO   B 85  ? 0.3234 0.2353 0.3812 0.0055  0.0129  -0.0105 91  PRO   C CD  
1758 N N   . ALA   B 86  ? 0.3122 0.2301 0.3948 0.0164  0.0241  -0.0160 92  ALA   C N   
1759 C CA  . ALA   B 86  ? 0.3064 0.2322 0.3951 0.0188  0.0234  -0.0126 92  ALA   C CA  
1760 C C   . ALA   B 86  ? 0.3028 0.2318 0.3961 0.0196  0.0165  -0.0032 92  ALA   C C   
1761 O O   . ALA   B 86  ? 0.3126 0.2364 0.4118 0.0204  0.0146  0.0003  92  ALA   C O   
1762 C CB  . ALA   B 86  ? 0.3149 0.2397 0.4183 0.0228  0.0291  -0.0155 92  ALA   C CB  
1763 N N   . ARG   B 87  ? 0.2839 0.2204 0.3715 0.0183  0.0126  0.0006  93  ARG   C N   
1764 C CA  . ARG   B 87  ? 0.2762 0.2151 0.3642 0.0176  0.0061  0.0089  93  ARG   C CA  
1765 C C   . ARG   B 87  ? 0.2876 0.2349 0.3720 0.0166  0.0031  0.0119  93  ARG   C C   
1766 O O   . ARG   B 87  ? 0.2996 0.2504 0.3802 0.0162  0.0060  0.0076  93  ARG   C O   
1767 C CB  . ARG   B 87  ? 0.2729 0.2081 0.3494 0.0139  0.0040  0.0092  93  ARG   C CB  
1768 C CG  . ARG   B 87  ? 0.2613 0.2003 0.3236 0.0108  0.0039  0.0060  93  ARG   C CG  
1769 C CD  . ARG   B 87  ? 0.2772 0.2122 0.3307 0.0078  0.0041  0.0031  93  ARG   C CD  
1770 N NE  . ARG   B 87  ? 0.2718 0.2109 0.3146 0.0050  0.0016  0.0038  93  ARG   C NE  
1771 C CZ  . ARG   B 87  ? 0.3031 0.2457 0.3389 0.0044  0.0024  0.0006  93  ARG   C CZ  
1772 N NH1 . ARG   B 87  ? 0.2652 0.2107 0.2930 0.0022  0.0003  0.0013  93  ARG   C NH1 
1773 N NH2 . ARG   B 87  ? 0.2971 0.2404 0.3343 0.0058  0.0054  -0.0031 93  ARG   C NH2 
1774 N N   . TYR   B 88  ? 0.2904 0.2403 0.3749 0.0155  -0.0027 0.0192  94  TYR   C N   
1775 C CA  . TYR   B 88  ? 0.2954 0.2523 0.3741 0.0135  -0.0060 0.0219  94  TYR   C CA  
1776 C C   . TYR   B 88  ? 0.2557 0.2113 0.3190 0.0097  -0.0072 0.0209  94  TYR   C C   
1777 O O   . TYR   B 88  ? 0.2591 0.2109 0.3190 0.0080  -0.0092 0.0235  94  TYR   C O   
1778 C CB  . TYR   B 88  ? 0.3327 0.2928 0.4179 0.0136  -0.0121 0.0303  94  TYR   C CB  
1779 C CG  . TYR   B 88  ? 0.3935 0.3563 0.4963 0.0178  -0.0117 0.0321  94  TYR   C CG  
1780 C CD1 . TYR   B 88  ? 0.4277 0.3980 0.5358 0.0185  -0.0112 0.0315  94  TYR   C CD1 
1781 C CD2 . TYR   B 88  ? 0.4333 0.3910 0.5483 0.0210  -0.0113 0.0340  94  TYR   C CD2 
1782 C CE1 . TYR   B 88  ? 0.4520 0.4258 0.5783 0.0226  -0.0103 0.0329  94  TYR   C CE1 
1783 C CE2 . TYR   B 88  ? 0.4518 0.4122 0.5851 0.0254  -0.0105 0.0354  94  TYR   C CE2 
1784 C CZ  . TYR   B 88  ? 0.4730 0.4420 0.6124 0.0263  -0.0099 0.0347  94  TYR   C CZ  
1785 O OH  . TYR   B 88  ? 0.5160 0.4887 0.6754 0.0308  -0.0087 0.0360  94  TYR   C OH  
1786 N N   . GLN   B 89  ? 0.2132 0.1718 0.2680 0.0082  -0.0057 0.0171  95  GLN   C N   
1787 C CA  . GLN   B 89  ? 0.2017 0.1598 0.2438 0.0050  -0.0069 0.0162  95  GLN   C CA  
1788 C C   . GLN   B 89  ? 0.1990 0.1615 0.2374 0.0028  -0.0111 0.0210  95  GLN   C C   
1789 O O   . GLN   B 89  ? 0.2149 0.1820 0.2565 0.0033  -0.0118 0.0220  95  GLN   C O   
1790 C CB  . GLN   B 89  ? 0.2045 0.1625 0.2396 0.0046  -0.0035 0.0100  95  GLN   C CB  
1791 C CG  . GLN   B 89  ? 0.2259 0.1843 0.2501 0.0019  -0.0049 0.0094  95  GLN   C CG  
1792 C CD  . GLN   B 89  ? 0.2182 0.1751 0.2362 0.0016  -0.0025 0.0038  95  GLN   C CD  
1793 O OE1 . GLN   B 89  ? 0.2361 0.1899 0.2559 0.0024  -0.0001 0.0004  95  GLN   C OE1 
1794 N NE2 . GLN   B 89  ? 0.1979 0.1567 0.2084 0.0002  -0.0034 0.0032  95  GLN   C NE2 
1795 N N   . SER   B 90  ? 0.1898 0.1511 0.2214 0.0000  -0.0135 0.0238  96  SER   C N   
1796 C CA  . SER   B 90  ? 0.1866 0.1512 0.2128 -0.0030 -0.0173 0.0280  96  SER   C CA  
1797 C C   . SER   B 90  ? 0.1977 0.1635 0.2130 -0.0052 -0.0161 0.0244  96  SER   C C   
1798 O O   . SER   B 90  ? 0.1895 0.1535 0.2013 -0.0047 -0.0130 0.0196  96  SER   C O   
1799 C CB  . SER   B 90  ? 0.2111 0.1731 0.2350 -0.0054 -0.0203 0.0333  96  SER   C CB  
1800 O OG  . SER   B 90  ? 0.2393 0.1978 0.2569 -0.0069 -0.0177 0.0304  96  SER   C OG  
1801 N N   . HIS   B 91  ? 0.1794 0.1483 0.1897 -0.0080 -0.0189 0.0270  97  HIS   C N   
1802 C CA  . HIS   B 91  ? 0.1879 0.1572 0.1882 -0.0104 -0.0178 0.0239  97  HIS   C CA  
1803 C C   . HIS   B 91  ? 0.1890 0.1587 0.1898 -0.0082 -0.0148 0.0189  97  HIS   C C   
1804 O O   . HIS   B 91  ? 0.1994 0.1677 0.1937 -0.0088 -0.0130 0.0153  97  HIS   C O   
1805 C CB  . HIS   B 91  ? 0.2007 0.1670 0.1936 -0.0125 -0.0163 0.0226  97  HIS   C CB  
1806 C CG  . HIS   B 91  ? 0.2064 0.1719 0.1964 -0.0158 -0.0189 0.0277  97  HIS   C CG  
1807 N ND1 . HIS   B 91  ? 0.2504 0.2167 0.2315 -0.0201 -0.0206 0.0294  97  HIS   C ND1 
1808 C CD2 . HIS   B 91  ? 0.2222 0.1856 0.2167 -0.0156 -0.0203 0.0316  97  HIS   C CD2 
1809 C CE1 . HIS   B 91  ? 0.2586 0.2234 0.2378 -0.0228 -0.0230 0.0344  97  HIS   C CE1 
1810 N NE2 . HIS   B 91  ? 0.2575 0.2203 0.2448 -0.0201 -0.0230 0.0361  97  HIS   C NE2 
1811 N N   . LEU   B 92  ? 0.1944 0.1661 0.2032 -0.0058 -0.0144 0.0188  98  LEU   C N   
1812 C CA  . LEU   B 92  ? 0.1866 0.1582 0.1950 -0.0044 -0.0113 0.0145  98  LEU   C CA  
1813 C C   . LEU   B 92  ? 0.1863 0.1615 0.1939 -0.0059 -0.0124 0.0152  98  LEU   C C   
1814 O O   . LEU   B 92  ? 0.1876 0.1664 0.2008 -0.0065 -0.0150 0.0189  98  LEU   C O   
1815 C CB  . LEU   B 92  ? 0.1984 0.1695 0.2157 -0.0012 -0.0088 0.0130  98  LEU   C CB  
1816 C CG  . LEU   B 92  ? 0.2353 0.2053 0.2509 -0.0002 -0.0051 0.0081  98  LEU   C CG  
1817 C CD1 . LEU   B 92  ? 0.2227 0.1888 0.2300 -0.0007 -0.0042 0.0049  98  LEU   C CD1 
1818 C CD2 . LEU   B 92  ? 0.2795 0.2487 0.3037 0.0023  -0.0021 0.0065  98  LEU   C CD2 
1819 N N   . MET   B 93  ? 0.1830 0.1571 0.1846 -0.0065 -0.0106 0.0119  99  MET   C N   
1820 C CA  . MET   B 93  ? 0.1746 0.1511 0.1750 -0.0083 -0.0111 0.0121  99  MET   C CA  
1821 C C   . MET   B 93  ? 0.1754 0.1516 0.1774 -0.0070 -0.0077 0.0091  99  MET   C C   
1822 O O   . MET   B 93  ? 0.1931 0.1656 0.1909 -0.0058 -0.0056 0.0061  99  MET   C O   
1823 C CB  . MET   B 93  ? 0.1884 0.1622 0.1787 -0.0108 -0.0117 0.0108  99  MET   C CB  
1824 C CG  . MET   B 93  ? 0.2439 0.2178 0.2311 -0.0129 -0.0143 0.0132  99  MET   C CG  
1825 S SD  . MET   B 93  ? 0.2575 0.2276 0.2337 -0.0156 -0.0137 0.0107  99  MET   C SD  
1826 C CE  . MET   B 93  ? 0.2405 0.2068 0.2158 -0.0123 -0.0105 0.0069  99  MET   C CE  
1827 N N   . LEU   B 94  ? 0.1681 0.1484 0.1764 -0.0073 -0.0071 0.0100  100 LEU   C N   
1828 C CA  . LEU   B 94  ? 0.1684 0.1484 0.1773 -0.0067 -0.0031 0.0070  100 LEU   C CA  
1829 C C   . LEU   B 94  ? 0.1651 0.1450 0.1682 -0.0096 -0.0028 0.0065  100 LEU   C C   
1830 O O   . LEU   B 94  ? 0.1588 0.1409 0.1614 -0.0120 -0.0056 0.0087  100 LEU   C O   
1831 C CB  . LEU   B 94  ? 0.1825 0.1673 0.2039 -0.0050 -0.0009 0.0075  100 LEU   C CB  
1832 C CG  . LEU   B 94  ? 0.2053 0.1897 0.2344 -0.0020 -0.0006 0.0080  100 LEU   C CG  
1833 C CD1 . LEU   B 94  ? 0.2285 0.2175 0.2718 0.0001  0.0025  0.0078  100 LEU   C CD1 
1834 C CD2 . LEU   B 94  ? 0.2088 0.1871 0.2313 -0.0008 0.0017  0.0043  100 LEU   C CD2 
1835 N N   . ALA   B 95  ? 0.1565 0.1331 0.1543 -0.0097 0.0003  0.0037  101 ALA   C N   
1836 C CA  . ALA   B 95  ? 0.1664 0.1420 0.1589 -0.0125 0.0011  0.0033  101 ALA   C CA  
1837 C C   . ALA   B 95  ? 0.1667 0.1423 0.1599 -0.0126 0.0058  0.0010  101 ALA   C C   
1838 O O   . ALA   B 95  ? 0.1720 0.1464 0.1664 -0.0106 0.0082  -0.0010 101 ALA   C O   
1839 C CB  . ALA   B 95  ? 0.1772 0.1464 0.1587 -0.0132 -0.0003 0.0024  101 ALA   C CB  
1840 N N   . VAL   B 96  ? 0.1724 0.1490 0.1643 -0.0155 0.0075  0.0012  102 VAL   C N   
1841 C CA  . VAL   B 96  ? 0.1833 0.1591 0.1731 -0.0167 0.0124  -0.0010 102 VAL   C CA  
1842 C C   . VAL   B 96  ? 0.1962 0.1640 0.1725 -0.0176 0.0118  -0.0019 102 VAL   C C   
1843 O O   . VAL   B 96  ? 0.1982 0.1627 0.1682 -0.0196 0.0097  -0.0006 102 VAL   C O   
1844 C CB  . VAL   B 96  ? 0.1985 0.1790 0.1930 -0.0199 0.0145  -0.0001 102 VAL   C CB  
1845 C CG1 . VAL   B 96  ? 0.2045 0.1836 0.1952 -0.0219 0.0204  -0.0025 102 VAL   C CG1 
1846 C CG2 . VAL   B 96  ? 0.1927 0.1820 0.2025 -0.0185 0.0140  0.0014  102 VAL   C CG2 
1847 N N   . GLY   B 97  ? 0.2181 0.1828 0.1905 -0.0163 0.0135  -0.0042 103 GLY   C N   
1848 C CA  . GLY   B 97  ? 0.2392 0.1969 0.1995 -0.0172 0.0121  -0.0045 103 GLY   C CA  
1849 C C   . GLY   B 97  ? 0.2432 0.1986 0.2002 -0.0162 0.0138  -0.0073 103 GLY   C C   
1850 O O   . GLY   B 97  ? 0.2451 0.2034 0.2094 -0.0143 0.0160  -0.0091 103 GLY   C O   
1851 N N   . HIS   B 98  ? 0.2351 0.1847 0.1809 -0.0178 0.0126  -0.0074 104 HIS   C N   
1852 C CA  . HIS   B 98  ? 0.2437 0.1905 0.1841 -0.0180 0.0137  -0.0100 104 HIS   C CA  
1853 C C   . HIS   B 98  ? 0.2379 0.1840 0.1802 -0.0151 0.0098  -0.0103 104 HIS   C C   
1854 O O   . HIS   B 98  ? 0.2292 0.1744 0.1716 -0.0137 0.0054  -0.0081 104 HIS   C O   
1855 C CB  . HIS   B 98  ? 0.2561 0.1968 0.1828 -0.0213 0.0126  -0.0091 104 HIS   C CB  
1856 C CG  . HIS   B 98  ? 0.2641 0.2017 0.1834 -0.0226 0.0132  -0.0118 104 HIS   C CG  
1857 N ND1 . HIS   B 98  ? 0.2806 0.2195 0.2005 -0.0240 0.0194  -0.0159 104 HIS   C ND1 
1858 C CD2 . HIS   B 98  ? 0.2823 0.2164 0.1955 -0.0223 0.0084  -0.0114 104 HIS   C CD2 
1859 C CE1 . HIS   B 98  ? 0.3025 0.2375 0.2144 -0.0253 0.0182  -0.0179 104 HIS   C CE1 
1860 N NE2 . HIS   B 98  ? 0.3112 0.2437 0.2191 -0.0243 0.0112  -0.0151 104 HIS   C NE2 
1861 N N   . SER   B 99  ? 0.2322 0.1785 0.1760 -0.0146 0.0119  -0.0134 105 SER   C N   
1862 C CA  . SER   B 99  ? 0.2393 0.1844 0.1836 -0.0128 0.0086  -0.0141 105 SER   C CA  
1863 C C   . SER   B 99  ? 0.2501 0.1932 0.1916 -0.0140 0.0117  -0.0182 105 SER   C C   
1864 O O   . SER   B 99  ? 0.2588 0.2025 0.2016 -0.0151 0.0173  -0.0209 105 SER   C O   
1865 C CB  . SER   B 99  ? 0.2670 0.2158 0.2220 -0.0096 0.0070  -0.0128 105 SER   C CB  
1866 O OG  . SER   B 99  ? 0.2784 0.2304 0.2423 -0.0085 0.0108  -0.0140 105 SER   C OG  
1867 N N   . GLU   B 100 ? 0.2531 0.1940 0.1912 -0.0140 0.0081  -0.0190 106 GLU   C N   
1868 C CA  . GLU   B 100 ? 0.2711 0.2094 0.2058 -0.0155 0.0097  -0.0231 106 GLU   C CA  
1869 C C   . GLU   B 100 ? 0.2651 0.2044 0.2061 -0.0133 0.0062  -0.0231 106 GLU   C C   
1870 O O   . GLU   B 100 ? 0.2604 0.2018 0.2057 -0.0112 0.0025  -0.0199 106 GLU   C O   
1871 C CB  . GLU   B 100 ? 0.3133 0.2472 0.2338 -0.0194 0.0076  -0.0234 106 GLU   C CB  
1872 C CG  . GLU   B 100 ? 0.3658 0.2982 0.2792 -0.0223 0.0116  -0.0235 106 GLU   C CG  
1873 C CD  . GLU   B 100 ? 0.4209 0.3484 0.3185 -0.0270 0.0096  -0.0231 106 GLU   C CD  
1874 O OE1 . GLU   B 100 ? 0.4845 0.4092 0.3755 -0.0290 0.0074  -0.0252 106 GLU   C OE1 
1875 O OE2 . GLU   B 100 ? 0.4081 0.3341 0.2996 -0.0289 0.0100  -0.0205 106 GLU   C OE2 
1876 N N   . PRO   B 101 ? 0.2648 0.2021 0.2065 -0.0140 0.0079  -0.0268 107 PRO   C N   
1877 C CA  . PRO   B 101 ? 0.2613 0.1997 0.2099 -0.0123 0.0051  -0.0266 107 PRO   C CA  
1878 C C   . PRO   B 101 ? 0.2513 0.1909 0.1981 -0.0122 -0.0013 -0.0238 107 PRO   C C   
1879 O O   . PRO   B 101 ? 0.2688 0.2113 0.2233 -0.0098 -0.0033 -0.0216 107 PRO   C O   
1880 C CB  . PRO   B 101 ? 0.2804 0.2150 0.2266 -0.0144 0.0078  -0.0316 107 PRO   C CB  
1881 C CG  . PRO   B 101 ? 0.2987 0.2318 0.2435 -0.0152 0.0145  -0.0346 107 PRO   C CG  
1882 C CD  . PRO   B 101 ? 0.2831 0.2171 0.2203 -0.0165 0.0134  -0.0318 107 PRO   C CD  
1883 N N   . GLY   B 102 ? 0.2503 0.1879 0.1873 -0.0147 -0.0045 -0.0235 108 GLY   C N   
1884 C CA  . GLY   B 102 ? 0.2449 0.1839 0.1816 -0.0143 -0.0108 -0.0207 108 GLY   C CA  
1885 C C   . GLY   B 102 ? 0.2392 0.1805 0.1801 -0.0115 -0.0125 -0.0167 108 GLY   C C   
1886 O O   . GLY   B 102 ? 0.2444 0.1873 0.1880 -0.0103 -0.0169 -0.0146 108 GLY   C O   
1887 N N   . ASP   B 103 ? 0.2151 0.1567 0.1572 -0.0106 -0.0087 -0.0160 109 ASP   C N   
1888 C CA  . ASP   B 103 ? 0.2126 0.1559 0.1584 -0.0085 -0.0098 -0.0128 109 ASP   C CA  
1889 C C   . ASP   B 103 ? 0.1988 0.1456 0.1543 -0.0061 -0.0096 -0.0123 109 ASP   C C   
1890 O O   . ASP   B 103 ? 0.2051 0.1530 0.1631 -0.0047 -0.0107 -0.0102 109 ASP   C O   
1891 C CB  . ASP   B 103 ? 0.2201 0.1630 0.1641 -0.0091 -0.0061 -0.0121 109 ASP   C CB  
1892 C CG  . ASP   B 103 ? 0.2704 0.2094 0.2037 -0.0118 -0.0067 -0.0115 109 ASP   C CG  
1893 O OD1 . ASP   B 103 ? 0.2611 0.1980 0.1898 -0.0123 -0.0113 -0.0098 109 ASP   C OD1 
1894 O OD2 . ASP   B 103 ? 0.2593 0.1975 0.1894 -0.0137 -0.0025 -0.0126 109 ASP   C OD2 
1895 N N   . CYS   B 104 ? 0.1912 0.1390 0.1513 -0.0059 -0.0080 -0.0142 110 CYS   C N   
1896 C CA  . CYS   B 104 ? 0.1886 0.1392 0.1567 -0.0043 -0.0079 -0.0132 110 CYS   C CA  
1897 C C   . CYS   B 104 ? 0.1973 0.1496 0.1673 -0.0035 -0.0113 -0.0121 110 CYS   C C   
1898 O O   . CYS   B 104 ? 0.2083 0.1602 0.1762 -0.0042 -0.0142 -0.0127 110 CYS   C O   
1899 C CB  . CYS   B 104 ? 0.2100 0.1602 0.1822 -0.0047 -0.0063 -0.0153 110 CYS   C CB  
1900 S SG  . CYS   B 104 ? 0.2406 0.1897 0.2155 -0.0043 -0.0015 -0.0162 110 CYS   C SG  
1901 N N   . GLY   B 105 ? 0.1978 0.1520 0.1717 -0.0023 -0.0108 -0.0105 111 GLY   C N   
1902 C CA  . GLY   B 105 ? 0.1963 0.1523 0.1731 -0.0014 -0.0127 -0.0099 111 GLY   C CA  
1903 C C   . GLY   B 105 ? 0.2142 0.1688 0.1884 -0.0005 -0.0137 -0.0085 111 GLY   C C   
1904 O O   . GLY   B 105 ? 0.2201 0.1758 0.1976 0.0006  -0.0141 -0.0083 111 GLY   C O   
1905 N N   . GLY   B 106 ? 0.1975 0.1494 0.1658 -0.0012 -0.0134 -0.0079 112 GLY   C N   
1906 C CA  . GLY   B 106 ? 0.1838 0.1334 0.1493 -0.0008 -0.0140 -0.0064 112 GLY   C CA  
1907 C C   . GLY   B 106 ? 0.1904 0.1412 0.1586 -0.0006 -0.0119 -0.0061 112 GLY   C C   
1908 O O   . GLY   B 106 ? 0.1976 0.1502 0.1671 -0.0013 -0.0099 -0.0060 112 GLY   C O   
1909 N N   . ILE   B 107 ? 0.1879 0.1374 0.1570 0.0004  -0.0125 -0.0059 113 ILE   C N   
1910 C CA  . ILE   B 107 ? 0.1995 0.1496 0.1698 0.0000  -0.0104 -0.0062 113 ILE   C CA  
1911 C C   . ILE   B 107 ? 0.1797 0.1277 0.1456 -0.0016 -0.0095 -0.0052 113 ILE   C C   
1912 O O   . ILE   B 107 ? 0.1971 0.1415 0.1594 -0.0017 -0.0105 -0.0044 113 ILE   C O   
1913 C CB  . ILE   B 107 ? 0.2330 0.1827 0.2071 0.0016  -0.0103 -0.0074 113 ILE   C CB  
1914 C CG1 . ILE   B 107 ? 0.2653 0.2192 0.2456 0.0023  -0.0101 -0.0085 113 ILE   C CG1 
1915 C CG2 . ILE   B 107 ? 0.2645 0.2128 0.2373 0.0005  -0.0078 -0.0083 113 ILE   C CG2 
1916 C CD1 . ILE   B 107 ? 0.3107 0.2650 0.2971 0.0044  -0.0098 -0.0100 113 ILE   C CD1 
1917 N N   . LEU   B 108 ? 0.1742 0.1241 0.1402 -0.0032 -0.0079 -0.0050 114 LEU   C N   
1918 C CA  . LEU   B 108 ? 0.1788 0.1275 0.1415 -0.0054 -0.0073 -0.0042 114 LEU   C CA  
1919 C C   . LEU   B 108 ? 0.1877 0.1348 0.1494 -0.0061 -0.0063 -0.0056 114 LEU   C C   
1920 O O   . LEU   B 108 ? 0.1812 0.1305 0.1448 -0.0063 -0.0054 -0.0063 114 LEU   C O   
1921 C CB  . LEU   B 108 ? 0.1792 0.1317 0.1434 -0.0069 -0.0070 -0.0028 114 LEU   C CB  
1922 C CG  . LEU   B 108 ? 0.1880 0.1411 0.1503 -0.0097 -0.0070 -0.0017 114 LEU   C CG  
1923 C CD1 . LEU   B 108 ? 0.1901 0.1406 0.1497 -0.0105 -0.0069 -0.0014 114 LEU   C CD1 
1924 C CD2 . LEU   B 108 ? 0.1803 0.1380 0.1464 -0.0106 -0.0074 0.0003  114 LEU   C CD2 
1925 N N   . ARG   B 109 ? 0.1935 0.1362 0.1522 -0.0067 -0.0062 -0.0061 115 ARG   C N   
1926 C CA  . ARG   B 109 ? 0.1946 0.1346 0.1518 -0.0076 -0.0045 -0.0082 115 ARG   C CA  
1927 C C   . ARG   B 109 ? 0.2101 0.1479 0.1623 -0.0111 -0.0044 -0.0080 115 ARG   C C   
1928 O O   . ARG   B 109 ? 0.2240 0.1603 0.1746 -0.0120 -0.0054 -0.0065 115 ARG   C O   
1929 C CB  . ARG   B 109 ? 0.2370 0.1721 0.1961 -0.0049 -0.0045 -0.0096 115 ARG   C CB  
1930 C CG  . ARG   B 109 ? 0.3059 0.2437 0.2710 -0.0018 -0.0046 -0.0103 115 ARG   C CG  
1931 C CD  . ARG   B 109 ? 0.3733 0.3069 0.3421 0.0013  -0.0055 -0.0109 115 ARG   C CD  
1932 N NE  . ARG   B 109 ? 0.5160 0.4513 0.4911 0.0030  -0.0032 -0.0136 115 ARG   C NE  
1933 C CZ  . ARG   B 109 ? 0.5953 0.5349 0.5772 0.0054  -0.0041 -0.0137 115 ARG   C CZ  
1934 N NH1 . ARG   B 109 ? 0.6205 0.5622 0.6029 0.0061  -0.0077 -0.0112 115 ARG   C NH1 
1935 N NH2 . ARG   B 109 ? 0.6145 0.5564 0.6028 0.0065  -0.0011 -0.0165 115 ARG   C NH2 
1936 N N   . CYS   B 110 ? 0.2111 0.1480 0.1606 -0.0135 -0.0028 -0.0098 116 CYS   C N   
1937 C CA  . CYS   B 110 ? 0.2422 0.1760 0.1864 -0.0174 -0.0026 -0.0104 116 CYS   C CA  
1938 C C   . CYS   B 110 ? 0.2538 0.1813 0.1960 -0.0174 0.0001  -0.0142 116 CYS   C C   
1939 O O   . CYS   B 110 ? 0.2288 0.1552 0.1751 -0.0140 0.0016  -0.0159 116 CYS   C O   
1940 C CB  . CYS   B 110 ? 0.2382 0.1764 0.1796 -0.0214 -0.0035 -0.0092 116 CYS   C CB  
1941 S SG  . CYS   B 110 ? 0.2166 0.1560 0.1556 -0.0228 -0.0013 -0.0112 116 CYS   C SG  
1942 N N   . GLN   B 111 ? 0.2803 0.2039 0.2168 -0.0215 0.0008  -0.0159 117 GLN   C N   
1943 C CA  . GLN   B 111 ? 0.3168 0.2335 0.2514 -0.0217 0.0042  -0.0202 117 GLN   C CA  
1944 C C   . GLN   B 111 ? 0.3066 0.2250 0.2414 -0.0216 0.0075  -0.0233 117 GLN   C C   
1945 O O   . GLN   B 111 ? 0.3409 0.2544 0.2767 -0.0205 0.0112  -0.0275 117 GLN   C O   
1946 C CB  . GLN   B 111 ? 0.3714 0.2831 0.2987 -0.0270 0.0044  -0.0218 117 GLN   C CB  
1947 C CG  . GLN   B 111 ? 0.4181 0.3341 0.3392 -0.0326 0.0037  -0.0217 117 GLN   C CG  
1948 C CD  . GLN   B 111 ? 0.5415 0.4539 0.4557 -0.0385 0.0028  -0.0226 117 GLN   C CD  
1949 O OE1 . GLN   B 111 ? 0.5779 0.4946 0.4919 -0.0412 -0.0008 -0.0191 117 GLN   C OE1 
1950 N NE2 . GLN   B 111 ? 0.5583 0.4629 0.4675 -0.0408 0.0061  -0.0275 117 GLN   C NE2 
1951 N N   . HIS   B 112 ? 0.2596 0.1846 0.1938 -0.0229 0.0066  -0.0215 118 HIS   C N   
1952 C CA  . HIS   B 112 ? 0.2693 0.1961 0.2023 -0.0240 0.0100  -0.0240 118 HIS   C CA  
1953 C C   . HIS   B 112 ? 0.2731 0.2037 0.2145 -0.0192 0.0109  -0.0237 118 HIS   C C   
1954 O O   . HIS   B 112 ? 0.3057 0.2376 0.2475 -0.0198 0.0145  -0.0262 118 HIS   C O   
1955 C CB  . HIS   B 112 ? 0.2663 0.1974 0.1926 -0.0291 0.0084  -0.0218 118 HIS   C CB  
1956 C CG  . HIS   B 112 ? 0.2717 0.2002 0.1899 -0.0345 0.0067  -0.0218 118 HIS   C CG  
1957 N ND1 . HIS   B 112 ? 0.2658 0.1980 0.1841 -0.0362 0.0019  -0.0173 118 HIS   C ND1 
1958 C CD2 . HIS   B 112 ? 0.3049 0.2278 0.2153 -0.0389 0.0094  -0.0261 118 HIS   C CD2 
1959 C CE1 . HIS   B 112 ? 0.3122 0.2412 0.2232 -0.0414 0.0012  -0.0187 118 HIS   C CE1 
1960 N NE2 . HIS   B 112 ? 0.3346 0.2575 0.2398 -0.0435 0.0056  -0.0240 118 HIS   C NE2 
1961 N N   . GLY   B 113 ? 0.2499 0.1826 0.1975 -0.0152 0.0077  -0.0206 119 GLY   C N   
1962 C CA  . GLY   B 113 ? 0.2345 0.1710 0.1900 -0.0113 0.0078  -0.0202 119 GLY   C CA  
1963 C C   . GLY   B 113 ? 0.2156 0.1566 0.1732 -0.0102 0.0040  -0.0161 119 GLY   C C   
1964 O O   . GLY   B 113 ? 0.2218 0.1624 0.1768 -0.0111 0.0013  -0.0136 119 GLY   C O   
1965 N N   . VAL   B 114 ? 0.2026 0.1478 0.1653 -0.0084 0.0041  -0.0156 120 VAL   C N   
1966 C CA  . VAL   B 114 ? 0.2002 0.1490 0.1653 -0.0073 0.0011  -0.0125 120 VAL   C CA  
1967 C C   . VAL   B 114 ? 0.1938 0.1451 0.1550 -0.0106 0.0002  -0.0101 120 VAL   C C   
1968 O O   . VAL   B 114 ? 0.2052 0.1577 0.1639 -0.0132 0.0019  -0.0103 120 VAL   C O   
1969 C CB  . VAL   B 114 ? 0.2145 0.1666 0.1865 -0.0050 0.0016  -0.0131 120 VAL   C CB  
1970 C CG1 . VAL   B 114 ? 0.2049 0.1598 0.1785 -0.0045 -0.0010 -0.0105 120 VAL   C CG1 
1971 C CG2 . VAL   B 114 ? 0.2226 0.1731 0.2001 -0.0014 0.0012  -0.0147 120 VAL   C CG2 
1972 N N   . VAL   B 115 ? 0.1886 0.1406 0.1496 -0.0105 -0.0024 -0.0074 121 VAL   C N   
1973 C CA  . VAL   B 115 ? 0.1824 0.1372 0.1420 -0.0129 -0.0039 -0.0045 121 VAL   C CA  
1974 C C   . VAL   B 115 ? 0.1853 0.1431 0.1500 -0.0113 -0.0047 -0.0027 121 VAL   C C   
1975 O O   . VAL   B 115 ? 0.1912 0.1509 0.1559 -0.0129 -0.0052 -0.0007 121 VAL   C O   
1976 C CB  . VAL   B 115 ? 0.1902 0.1445 0.1485 -0.0137 -0.0056 -0.0031 121 VAL   C CB  
1977 C CG1 . VAL   B 115 ? 0.2067 0.1649 0.1667 -0.0154 -0.0076 0.0003  121 VAL   C CG1 
1978 C CG2 . VAL   B 115 ? 0.1989 0.1495 0.1519 -0.0160 -0.0048 -0.0049 121 VAL   C CG2 
1979 N N   . GLY   B 116 ? 0.1694 0.1269 0.1376 -0.0083 -0.0051 -0.0035 122 GLY   C N   
1980 C CA  . GLY   B 116 ? 0.1804 0.1399 0.1529 -0.0071 -0.0056 -0.0025 122 GLY   C CA  
1981 C C   . GLY   B 116 ? 0.1738 0.1322 0.1480 -0.0047 -0.0061 -0.0038 122 GLY   C C   
1982 O O   . GLY   B 116 ? 0.1776 0.1340 0.1502 -0.0038 -0.0064 -0.0051 122 GLY   C O   
1983 N N   . ILE   B 117 ? 0.1777 0.1371 0.1551 -0.0039 -0.0064 -0.0035 123 ILE   C N   
1984 C CA  . ILE   B 117 ? 0.1807 0.1389 0.1582 -0.0026 -0.0071 -0.0050 123 ILE   C CA  
1985 C C   . ILE   B 117 ? 0.1798 0.1378 0.1577 -0.0026 -0.0065 -0.0046 123 ILE   C C   
1986 O O   . ILE   B 117 ? 0.1847 0.1440 0.1659 -0.0028 -0.0058 -0.0035 123 ILE   C O   
1987 C CB  . ILE   B 117 ? 0.2091 0.1682 0.1898 -0.0020 -0.0075 -0.0063 123 ILE   C CB  
1988 C CG1 . ILE   B 117 ? 0.2181 0.1785 0.2023 -0.0028 -0.0065 -0.0054 123 ILE   C CG1 
1989 C CG2 . ILE   B 117 ? 0.2296 0.1892 0.2114 -0.0014 -0.0077 -0.0073 123 ILE   C CG2 
1990 C CD1 . ILE   B 117 ? 0.2503 0.2117 0.2382 -0.0028 -0.0068 -0.0070 123 ILE   C CD1 
1991 N N   . VAL   B 118 ? 0.1593 0.1155 0.1341 -0.0023 -0.0068 -0.0057 124 VAL   C N   
1992 C CA  . VAL   B 118 ? 0.1695 0.1253 0.1445 -0.0026 -0.0052 -0.0064 124 VAL   C CA  
1993 C C   . VAL   B 118 ? 0.1703 0.1265 0.1497 -0.0022 -0.0044 -0.0074 124 VAL   C C   
1994 O O   . VAL   B 118 ? 0.1747 0.1303 0.1541 -0.0021 -0.0056 -0.0085 124 VAL   C O   
1995 C CB  . VAL   B 118 ? 0.1701 0.1233 0.1392 -0.0032 -0.0054 -0.0076 124 VAL   C CB  
1996 C CG1 . VAL   B 118 ? 0.1865 0.1390 0.1553 -0.0039 -0.0027 -0.0093 124 VAL   C CG1 
1997 C CG2 . VAL   B 118 ? 0.1969 0.1487 0.1618 -0.0038 -0.0061 -0.0063 124 VAL   C CG2 
1998 N N   . SER   B 119 ? 0.1718 0.1286 0.1555 -0.0018 -0.0025 -0.0070 125 SER   C N   
1999 C CA  . SER   B 119 ? 0.1591 0.1152 0.1476 -0.0014 -0.0017 -0.0078 125 SER   C CA  
2000 C C   . SER   B 119 ? 0.1916 0.1465 0.1826 -0.0009 0.0014  -0.0097 125 SER   C C   
2001 O O   . SER   B 119 ? 0.1855 0.1380 0.1783 -0.0009 0.0026  -0.0120 125 SER   C O   
2002 C CB  . SER   B 119 ? 0.1638 0.1216 0.1574 -0.0011 -0.0025 -0.0047 125 SER   C CB  
2003 O OG  . SER   B 119 ? 0.1860 0.1422 0.1847 -0.0007 -0.0017 -0.0048 125 SER   C OG  
2004 N N   . THR   B 120 ? 0.1832 0.1396 0.1750 -0.0008 0.0030  -0.0092 126 THR   C N   
2005 C CA  . THR   B 120 ? 0.2089 0.1646 0.2044 -0.0003 0.0070  -0.0115 126 THR   C CA  
2006 C C   . THR   B 120 ? 0.1982 0.1552 0.1902 -0.0014 0.0089  -0.0121 126 THR   C C   
2007 O O   . THR   B 120 ? 0.1933 0.1514 0.1808 -0.0024 0.0066  -0.0101 126 THR   C O   
2008 C CB  . THR   B 120 ? 0.2574 0.2151 0.2641 0.0016  0.0076  -0.0093 126 THR   C CB  
2009 O OG1 . THR   B 120 ? 0.2784 0.2344 0.2898 0.0025  0.0122  -0.0127 126 THR   C OG1 
2010 C CG2 . THR   B 120 ? 0.2751 0.2375 0.2854 0.0017  0.0062  -0.0056 126 THR   C CG2 
2011 N N   . GLY   B 121 ? 0.2149 0.1713 0.2084 -0.0016 0.0133  -0.0150 127 GLY   C N   
2012 C CA  . GLY   B 121 ? 0.2416 0.1997 0.2327 -0.0031 0.0159  -0.0154 127 GLY   C CA  
2013 C C   . GLY   B 121 ? 0.2503 0.2079 0.2451 -0.0031 0.0220  -0.0192 127 GLY   C C   
2014 O O   . GLY   B 121 ? 0.2530 0.2079 0.2508 -0.0022 0.0241  -0.0221 127 GLY   C O   
2015 N N   . GLY   B 122 ? 0.2578 0.2177 0.2522 -0.0046 0.0252  -0.0197 128 GLY   C N   
2016 C CA  . GLY   B 122 ? 0.2628 0.2228 0.2610 -0.0050 0.0322  -0.0239 128 GLY   C CA  
2017 C C   . GLY   B 122 ? 0.2676 0.2333 0.2723 -0.0055 0.0349  -0.0225 128 GLY   C C   
2018 O O   . GLY   B 122 ? 0.2494 0.2196 0.2599 -0.0046 0.0310  -0.0181 128 GLY   C O   
2019 N N   . ASN   B 123 ? 0.2856 0.2514 0.2893 -0.0075 0.0418  -0.0264 129 ASN   C N   
2020 C CA  . ASN   B 123 ? 0.2977 0.2697 0.3091 -0.0084 0.0455  -0.0257 129 ASN   C CA  
2021 C C   . ASN   B 123 ? 0.2915 0.2655 0.2975 -0.0106 0.0410  -0.0212 129 ASN   C C   
2022 O O   . ASN   B 123 ? 0.2999 0.2804 0.3160 -0.0104 0.0408  -0.0186 129 ASN   C O   
2023 C CB  . ASN   B 123 ? 0.3319 0.3102 0.3633 -0.0043 0.0466  -0.0245 129 ASN   C CB  
2024 C CG  . ASN   B 123 ? 0.4214 0.3977 0.4608 -0.0019 0.0525  -0.0294 129 ASN   C CG  
2025 O OD1 . ASN   B 123 ? 0.4602 0.4322 0.4916 -0.0042 0.0586  -0.0349 129 ASN   C OD1 
2026 N ND2 . ASN   B 123 ? 0.4411 0.4202 0.4960 0.0024  0.0507  -0.0273 129 ASN   C ND2 
2027 N N   . GLY   B 124 ? 0.2620 0.2305 0.2529 -0.0128 0.0371  -0.0202 130 GLY   C N   
2028 C CA  . GLY   B 124 ? 0.2464 0.2153 0.2317 -0.0150 0.0332  -0.0163 130 GLY   C CA  
2029 C C   . GLY   B 124 ? 0.2282 0.1995 0.2190 -0.0128 0.0267  -0.0121 130 GLY   C C   
2030 O O   . GLY   B 124 ? 0.2302 0.2028 0.2193 -0.0146 0.0242  -0.0093 130 GLY   C O   
2031 N N   . LEU   B 125 ? 0.2081 0.1797 0.2048 -0.0095 0.0244  -0.0119 131 LEU   C N   
2032 C CA  . LEU   B 125 ? 0.2063 0.1797 0.2070 -0.0079 0.0187  -0.0082 131 LEU   C CA  
2033 C C   . LEU   B 125 ? 0.2213 0.1894 0.2145 -0.0069 0.0153  -0.0086 131 LEU   C C   
2034 O O   . LEU   B 125 ? 0.2413 0.2063 0.2327 -0.0061 0.0173  -0.0115 131 LEU   C O   
2035 C CB  . LEU   B 125 ? 0.2089 0.1878 0.2249 -0.0051 0.0188  -0.0068 131 LEU   C CB  
2036 C CG  . LEU   B 125 ? 0.2313 0.2170 0.2578 -0.0059 0.0216  -0.0061 131 LEU   C CG  
2037 C CD1 . LEU   B 125 ? 0.2451 0.2350 0.2876 -0.0025 0.0238  -0.0062 131 LEU   C CD1 
2038 C CD2 . LEU   B 125 ? 0.2298 0.2194 0.2572 -0.0078 0.0170  -0.0020 131 LEU   C CD2 
2039 N N   . VAL   B 126 ? 0.1864 0.1538 0.1763 -0.0070 0.0106  -0.0059 132 VAL   C N   
2040 C CA  . VAL   B 126 ? 0.1873 0.1510 0.1720 -0.0060 0.0075  -0.0061 132 VAL   C CA  
2041 C C   . VAL   B 126 ? 0.1852 0.1514 0.1760 -0.0047 0.0043  -0.0034 132 VAL   C C   
2042 O O   . VAL   B 126 ? 0.1770 0.1463 0.1701 -0.0056 0.0027  -0.0008 132 VAL   C O   
2043 C CB  . VAL   B 126 ? 0.2138 0.1733 0.1878 -0.0075 0.0053  -0.0059 132 VAL   C CB  
2044 C CG1 . VAL   B 126 ? 0.2247 0.1849 0.1970 -0.0092 0.0040  -0.0037 132 VAL   C CG1 
2045 C CG2 . VAL   B 126 ? 0.2152 0.1722 0.1864 -0.0062 0.0022  -0.0061 132 VAL   C CG2 
2046 N N   . GLY   B 127 ? 0.1666 0.1314 0.1590 -0.0031 0.0035  -0.0038 133 GLY   C N   
2047 C CA  . GLY   B 127 ? 0.1752 0.1416 0.1719 -0.0024 0.0007  -0.0010 133 GLY   C CA  
2048 C C   . GLY   B 127 ? 0.1771 0.1411 0.1680 -0.0027 -0.0016 -0.0011 133 GLY   C C   
2049 O O   . GLY   B 127 ? 0.1733 0.1345 0.1609 -0.0023 -0.0012 -0.0034 133 GLY   C O   
2050 N N   . PHE   B 128 ? 0.1595 0.1246 0.1492 -0.0038 -0.0040 0.0012  134 PHE   C N   
2051 C CA  . PHE   B 128 ? 0.1578 0.1210 0.1428 -0.0041 -0.0053 0.0008  134 PHE   C CA  
2052 C C   . PHE   B 128 ? 0.1689 0.1333 0.1571 -0.0045 -0.0065 0.0029  134 PHE   C C   
2053 O O   . PHE   B 128 ? 0.1799 0.1465 0.1704 -0.0055 -0.0078 0.0059  134 PHE   C O   
2054 C CB  . PHE   B 128 ? 0.1702 0.1329 0.1499 -0.0057 -0.0062 0.0010  134 PHE   C CB  
2055 C CG  . PHE   B 128 ? 0.1789 0.1400 0.1552 -0.0061 -0.0054 -0.0001 134 PHE   C CG  
2056 C CD1 . PHE   B 128 ? 0.1660 0.1238 0.1380 -0.0053 -0.0053 -0.0019 134 PHE   C CD1 
2057 C CD2 . PHE   B 128 ? 0.1924 0.1555 0.1701 -0.0074 -0.0049 0.0010  134 PHE   C CD2 
2058 C CE1 . PHE   B 128 ? 0.1745 0.1301 0.1424 -0.0061 -0.0048 -0.0023 134 PHE   C CE1 
2059 C CE2 . PHE   B 128 ? 0.2004 0.1616 0.1743 -0.0083 -0.0038 0.0002  134 PHE   C CE2 
2060 C CZ  . PHE   B 128 ? 0.1927 0.1499 0.1612 -0.0077 -0.0038 -0.0013 134 PHE   C CZ  
2061 N N   . ALA   B 129 ? 0.1568 0.1197 0.1443 -0.0041 -0.0063 0.0018  135 ALA   C N   
2062 C CA  . ALA   B 129 ? 0.1509 0.1142 0.1398 -0.0051 -0.0071 0.0039  135 ALA   C CA  
2063 C C   . ALA   B 129 ? 0.1589 0.1226 0.1424 -0.0072 -0.0076 0.0043  135 ALA   C C   
2064 O O   . ALA   B 129 ? 0.1684 0.1310 0.1488 -0.0070 -0.0067 0.0018  135 ALA   C O   
2065 C CB  . ALA   B 129 ? 0.1704 0.1322 0.1608 -0.0045 -0.0062 0.0022  135 ALA   C CB  
2066 N N   . ASP   B 130 ? 0.1573 0.1222 0.1396 -0.0094 -0.0091 0.0074  136 ASP   C N   
2067 C CA  . ASP   B 130 ? 0.1657 0.1304 0.1414 -0.0121 -0.0091 0.0072  136 ASP   C CA  
2068 C C   . ASP   B 130 ? 0.1755 0.1393 0.1494 -0.0131 -0.0075 0.0062  136 ASP   C C   
2069 O O   . ASP   B 130 ? 0.1846 0.1484 0.1613 -0.0132 -0.0076 0.0078  136 ASP   C O   
2070 C CB  . ASP   B 130 ? 0.1775 0.1439 0.1520 -0.0150 -0.0118 0.0113  136 ASP   C CB  
2071 C CG  . ASP   B 130 ? 0.2349 0.2006 0.2010 -0.0188 -0.0119 0.0109  136 ASP   C CG  
2072 O OD1 . ASP   B 130 ? 0.2276 0.1918 0.1905 -0.0187 -0.0104 0.0076  136 ASP   C OD1 
2073 O OD2 . ASP   B 130 ? 0.2713 0.2373 0.2337 -0.0221 -0.0133 0.0137  136 ASP   C OD2 
2074 N N   . VAL   B 131 ? 0.1801 0.1429 0.1491 -0.0144 -0.0056 0.0035  137 VAL   C N   
2075 C CA  . VAL   B 131 ? 0.1915 0.1542 0.1589 -0.0160 -0.0033 0.0023  137 VAL   C CA  
2076 C C   . VAL   B 131 ? 0.2072 0.1690 0.1667 -0.0200 -0.0021 0.0019  137 VAL   C C   
2077 O O   . VAL   B 131 ? 0.2047 0.1664 0.1618 -0.0220 0.0008  0.0004  137 VAL   C O   
2078 C CB  . VAL   B 131 ? 0.1905 0.1532 0.1616 -0.0135 -0.0010 -0.0016 137 VAL   C CB  
2079 C CG1 . VAL   B 131 ? 0.2005 0.1637 0.1777 -0.0106 -0.0023 -0.0016 137 VAL   C CG1 
2080 C CG2 . VAL   B 131 ? 0.2020 0.1631 0.1712 -0.0123 -0.0002 -0.0045 137 VAL   C CG2 
2081 N N   . ARG   B 132 ? 0.2041 0.1654 0.1594 -0.0217 -0.0041 0.0031  138 ARG   C N   
2082 C CA  . ARG   B 132 ? 0.1970 0.1567 0.1436 -0.0260 -0.0029 0.0020  138 ARG   C CA  
2083 C C   . ARG   B 132 ? 0.2100 0.1700 0.1507 -0.0306 -0.0033 0.0048  138 ARG   C C   
2084 O O   . ARG   B 132 ? 0.2269 0.1852 0.1592 -0.0348 -0.0011 0.0028  138 ARG   C O   
2085 C CB  . ARG   B 132 ? 0.1906 0.1498 0.1343 -0.0272 -0.0054 0.0025  138 ARG   C CB  
2086 C CG  . ARG   B 132 ? 0.2031 0.1608 0.1502 -0.0237 -0.0044 -0.0005 138 ARG   C CG  
2087 C CD  . ARG   B 132 ? 0.2001 0.1576 0.1450 -0.0255 -0.0070 0.0006  138 ARG   C CD  
2088 N NE  . ARG   B 132 ? 0.1956 0.1568 0.1458 -0.0246 -0.0104 0.0049  138 ARG   C NE  
2089 C CZ  . ARG   B 132 ? 0.2012 0.1641 0.1525 -0.0257 -0.0129 0.0065  138 ARG   C CZ  
2090 N NH1 . ARG   B 132 ? 0.2083 0.1689 0.1542 -0.0285 -0.0126 0.0045  138 ARG   C NH1 
2091 N NH2 . ARG   B 132 ? 0.2049 0.1715 0.1634 -0.0241 -0.0151 0.0098  138 ARG   C NH2 
2092 N N   . ASP   B 133 ? 0.2038 0.1653 0.1481 -0.0304 -0.0061 0.0095  139 ASP   C N   
2093 C CA  . ASP   B 133 ? 0.2079 0.1691 0.1463 -0.0350 -0.0071 0.0132  139 ASP   C CA  
2094 C C   . ASP   B 133 ? 0.2211 0.1817 0.1594 -0.0358 -0.0029 0.0116  139 ASP   C C   
2095 O O   . ASP   B 133 ? 0.2427 0.2023 0.1742 -0.0405 -0.0028 0.0144  139 ASP   C O   
2096 C CB  . ASP   B 133 ? 0.2204 0.1829 0.1637 -0.0344 -0.0123 0.0196  139 ASP   C CB  
2097 C CG  . ASP   B 133 ? 0.2638 0.2267 0.2177 -0.0295 -0.0119 0.0199  139 ASP   C CG  
2098 O OD1 . ASP   B 133 ? 0.2528 0.2160 0.2117 -0.0255 -0.0097 0.0157  139 ASP   C OD1 
2099 O OD2 . ASP   B 133 ? 0.2849 0.2472 0.2416 -0.0299 -0.0138 0.0244  139 ASP   C OD2 
2100 N N   . LEU   B 134 ? 0.2158 0.1770 0.1612 -0.0318 0.0002  0.0076  140 LEU   C N   
2101 C CA  . LEU   B 134 ? 0.2098 0.1714 0.1573 -0.0324 0.0041  0.0060  140 LEU   C CA  
2102 C C   . LEU   B 134 ? 0.2233 0.1845 0.1651 -0.0351 0.0093  0.0013  140 LEU   C C   
2103 O O   . LEU   B 134 ? 0.2392 0.2014 0.1863 -0.0322 0.0127  -0.0035 140 LEU   C O   
2104 C CB  . LEU   B 134 ? 0.2103 0.1734 0.1686 -0.0271 0.0044  0.0040  140 LEU   C CB  
2105 C CG  . LEU   B 134 ? 0.2335 0.1964 0.1975 -0.0244 0.0002  0.0076  140 LEU   C CG  
2106 C CD1 . LEU   B 134 ? 0.2321 0.1959 0.2045 -0.0200 0.0007  0.0046  140 LEU   C CD1 
2107 C CD2 . LEU   B 134 ? 0.2392 0.2010 0.2024 -0.0270 -0.0014 0.0125  140 LEU   C CD2 
2108 N N   . LEU   B 135 ? 0.2210 0.1806 0.1520 -0.0410 0.0102  0.0027  141 LEU   C N   
2109 C CA  . LEU   B 135 ? 0.2400 0.1984 0.1641 -0.0442 0.0159  -0.0026 141 LEU   C CA  
2110 C C   . LEU   B 135 ? 0.2585 0.2188 0.1874 -0.0441 0.0222  -0.0065 141 LEU   C C   
2111 O O   . LEU   B 135 ? 0.2832 0.2434 0.2124 -0.0440 0.0277  -0.0123 141 LEU   C O   
2112 C CB  . LEU   B 135 ? 0.2456 0.2015 0.1550 -0.0516 0.0153  -0.0004 141 LEU   C CB  
2113 C CG  . LEU   B 135 ? 0.2724 0.2276 0.1776 -0.0527 0.0083  0.0044  141 LEU   C CG  
2114 C CD1 . LEU   B 135 ? 0.2998 0.2527 0.1894 -0.0608 0.0075  0.0063  141 LEU   C CD1 
2115 C CD2 . LEU   B 135 ? 0.2753 0.2304 0.1849 -0.0486 0.0070  0.0013  141 LEU   C CD2 
2116 N N   . TRP   B 136 ? 0.2536 0.2155 0.1871 -0.0441 0.0216  -0.0033 142 TRP   C N   
2117 C CA  . TRP   B 136 ? 0.2634 0.2279 0.2026 -0.0445 0.0273  -0.0065 142 TRP   C CA  
2118 C C   . TRP   B 136 ? 0.2784 0.2460 0.2307 -0.0384 0.0290  -0.0112 142 TRP   C C   
2119 O O   . TRP   B 136 ? 0.2749 0.2455 0.2332 -0.0385 0.0342  -0.0149 142 TRP   C O   
2120 C CB  . TRP   B 136 ? 0.2559 0.2207 0.1968 -0.0465 0.0257  -0.0015 142 TRP   C CB  
2121 C CG  . TRP   B 136 ? 0.2434 0.2080 0.1916 -0.0421 0.0194  0.0024  142 TRP   C CG  
2122 C CD1 . TRP   B 136 ? 0.2510 0.2131 0.1958 -0.0423 0.0136  0.0080  142 TRP   C CD1 
2123 C CD2 . TRP   B 136 ? 0.2346 0.2016 0.1952 -0.0369 0.0186  0.0006  142 TRP   C CD2 
2124 N NE1 . TRP   B 136 ? 0.2537 0.2161 0.2081 -0.0374 0.0101  0.0093  142 TRP   C NE1 
2125 C CE2 . TRP   B 136 ? 0.2373 0.2024 0.2004 -0.0345 0.0130  0.0048  142 TRP   C CE2 
2126 C CE3 . TRP   B 136 ? 0.2420 0.2127 0.2121 -0.0345 0.0220  -0.0040 142 TRP   C CE3 
2127 C CZ2 . TRP   B 136 ? 0.2522 0.2183 0.2250 -0.0301 0.0111  0.0039  142 TRP   C CZ2 
2128 C CZ3 . TRP   B 136 ? 0.2523 0.2245 0.2322 -0.0303 0.0191  -0.0042 142 TRP   C CZ3 
2129 C CH2 . TRP   B 136 ? 0.2512 0.2207 0.2314 -0.0285 0.0140  -0.0004 142 TRP   C CH2 
2130 N N   . LEU   B 137 ? 0.2656 0.2327 0.2225 -0.0333 0.0245  -0.0110 143 LEU   C N   
2131 C CA  . LEU   B 137 ? 0.2738 0.2432 0.2418 -0.0278 0.0251  -0.0148 143 LEU   C CA  
2132 C C   . LEU   B 137 ? 0.3246 0.2941 0.2934 -0.0277 0.0308  -0.0205 143 LEU   C C   
2133 O O   . LEU   B 137 ? 0.3391 0.3118 0.3189 -0.0242 0.0327  -0.0236 143 LEU   C O   
2134 C CB  . LEU   B 137 ? 0.2507 0.2186 0.2208 -0.0234 0.0195  -0.0133 143 LEU   C CB  
2135 C CG  . LEU   B 137 ? 0.2526 0.2209 0.2259 -0.0219 0.0147  -0.0092 143 LEU   C CG  
2136 C CD1 . LEU   B 137 ? 0.2434 0.2100 0.2169 -0.0185 0.0104  -0.0082 143 LEU   C CD1 
2137 C CD2 . LEU   B 137 ? 0.2511 0.2227 0.2345 -0.0199 0.0151  -0.0104 143 LEU   C CD2 
2138 N N   . ASP   B 138 ? 0.3570 0.3230 0.3146 -0.0317 0.0332  -0.0219 144 ASP   C N   
2139 C CA  . ASP   B 138 ? 0.4016 0.3660 0.3579 -0.0322 0.0392  -0.0278 144 ASP   C CA  
2140 C C   . ASP   B 138 ? 0.4431 0.4098 0.3996 -0.0360 0.0471  -0.0315 144 ASP   C C   
2141 O O   . ASP   B 138 ? 0.4528 0.4181 0.4091 -0.0364 0.0533  -0.0373 144 ASP   C O   
2142 C CB  . ASP   B 138 ? 0.4277 0.3868 0.3699 -0.0363 0.0386  -0.0279 144 ASP   C CB  
2143 C CG  . ASP   B 138 ? 0.4752 0.4316 0.4159 -0.0337 0.0323  -0.0255 144 ASP   C CG  
2144 O OD1 . ASP   B 138 ? 0.4720 0.4294 0.4224 -0.0280 0.0295  -0.0252 144 ASP   C OD1 
2145 O OD2 . ASP   B 138 ? 0.5100 0.4632 0.4393 -0.0380 0.0303  -0.0240 144 ASP   C OD2 
2146 N N   . GLU   B 139 ? 0.4515 0.4208 0.4069 -0.0394 0.0476  -0.0285 145 GLU   C N   
2147 C CA  . GLU   B 139 ? 0.4898 0.4613 0.4444 -0.0439 0.0557  -0.0318 145 GLU   C CA  
2148 C C   . GLU   B 139 ? 0.5151 0.4928 0.4837 -0.0417 0.0567  -0.0315 145 GLU   C C   
2149 O O   . GLU   B 139 ? 0.5377 0.5192 0.5129 -0.0428 0.0641  -0.0360 145 GLU   C O   
2150 C CB  . GLU   B 139 ? 0.5295 0.4977 0.4670 -0.0521 0.0566  -0.0286 145 GLU   C CB  
2151 C CG  . GLU   B 139 ? 0.6058 0.5737 0.5409 -0.0532 0.0496  -0.0208 145 GLU   C CG  
2152 C CD  . GLU   B 139 ? 0.7211 0.6844 0.6392 -0.0598 0.0466  -0.0158 145 GLU   C CD  
2153 O OE1 . GLU   B 139 ? 0.7255 0.6885 0.6408 -0.0627 0.0437  -0.0100 145 GLU   C OE1 
2154 O OE2 . GLU   B 139 ? 0.7624 0.7223 0.6702 -0.0622 0.0467  -0.0175 145 GLU   C OE2 
2155 N N1  . A1B4W C .   ? 0.3103 0.2666 0.3379 -0.0068 0.0318  0.0264  201 A1B4W A N1  
2156 C C4  . A1B4W C .   ? 0.3234 0.2813 0.3227 0.0009  0.0428  0.0321  201 A1B4W A C4  
2157 C C5  . A1B4W C .   ? 0.3168 0.2743 0.3149 -0.0001 0.0354  0.0284  201 A1B4W A C5  
2158 C C6  . A1B4W C .   ? 0.3285 0.2834 0.3324 -0.0018 0.0334  0.0300  201 A1B4W A C6  
2159 C C7  . A1B4W C .   ? 0.3132 0.2719 0.3337 -0.0053 0.0328  0.0255  201 A1B4W A C7  
2160 C C8  . A1B4W C .   ? 0.2989 0.2579 0.3398 -0.0094 0.0297  0.0207  201 A1B4W A C8  
2161 C C10 . A1B4W C .   ? 0.2817 0.2417 0.3273 -0.0103 0.0213  0.0113  201 A1B4W A C10 
2162 C C13 . A1B4W C .   ? 0.3413 0.2853 0.3621 -0.0047 0.0260  0.0352  201 A1B4W A C13 
2163 C C15 . A1B4W C .   ? 0.3732 0.3138 0.3832 -0.0016 0.0358  0.0447  201 A1B4W A C15 
2164 C C17 . A1B4W C .   ? 0.3313 0.2818 0.3525 -0.0054 0.0314  0.0319  201 A1B4W A C17 
2165 O O2  . A1B4W C .   ? 0.2825 0.2421 0.3406 -0.0121 0.0230  0.0105  201 A1B4W A O2  
2166 N N2  . A1B4W C .   ? 0.2573 0.2189 0.2971 -0.0092 0.0173  0.0069  201 A1B4W A N2  
2167 C C9  . A1B4W C .   ? 0.2854 0.2435 0.3212 -0.0088 0.0238  0.0176  201 A1B4W A C9  
2168 C C11 . A1B4W C .   ? 0.3004 0.2534 0.3307 -0.0077 0.0231  0.0228  201 A1B4W A C11 
2169 C C12 . A1B4W C .   ? 0.3266 0.2759 0.3555 -0.0069 0.0280  0.0300  201 A1B4W A C12 
2170 C C16 . A1B4W C .   ? 0.3522 0.2990 0.3738 -0.0045 0.0381  0.0394  201 A1B4W A C16 
2171 C C14 . A1B4W C .   ? 0.3617 0.3010 0.3790 -0.0030 0.0313  0.0431  201 A1B4W A C14 
2172 O O1  . A1B4W C .   ? 0.2951 0.2586 0.3217 -0.0062 0.0325  0.0208  201 A1B4W A O1  
2173 C C1  . A1B4W C .   ? 0.3069 0.2660 0.2975 0.0010  0.0301  0.0238  201 A1B4W A C1  
2174 O O   . A1B4W C .   ? 0.2902 0.2487 0.2806 0.0000  0.0240  0.0210  201 A1B4W A O   
2175 C C   . A1B4W C .   ? 0.2794 0.2383 0.2624 0.0012  0.0191  0.0174  201 A1B4W A C   
2176 N N   . A1B4W C .   ? 0.3263 0.2861 0.3196 0.0031  0.0452  0.0312  201 A1B4W A N   
2177 C C3  . A1B4W C .   ? 0.3158 0.2770 0.3016 0.0042  0.0394  0.0263  201 A1B4W A C3  
2178 C C2  . A1B4W C .   ? 0.3159 0.2767 0.3004 0.0031  0.0319  0.0226  201 A1B4W A C2  
2188 N N1  . A1B4W G .   ? 0.2505 0.1923 0.2447 -0.0020 0.0146  -0.0251 201 A1B4W C N1  
2189 C C4  . A1B4W G .   ? 0.2918 0.2341 0.2634 -0.0080 0.0231  -0.0304 201 A1B4W C C4  
2190 C C5  . A1B4W G .   ? 0.2634 0.2072 0.2373 -0.0065 0.0175  -0.0267 201 A1B4W C C5  
2191 C C6  . A1B4W G .   ? 0.2720 0.2139 0.2496 -0.0057 0.0155  -0.0273 201 A1B4W C C6  
2192 C C7  . A1B4W G .   ? 0.2621 0.2062 0.2522 -0.0025 0.0156  -0.0246 201 A1B4W C C7  
2193 C C8  . A1B4W G .   ? 0.2310 0.1745 0.2355 0.0004  0.0134  -0.0212 201 A1B4W C C8  
2194 C C10 . A1B4W G .   ? 0.2205 0.1670 0.2309 0.0014  0.0070  -0.0134 201 A1B4W C C10 
2195 C C13 . A1B4W G .   ? 0.2606 0.1960 0.2472 -0.0068 0.0081  -0.0290 201 A1B4W C C13 
2196 C C15 . A1B4W G .   ? 0.2943 0.2240 0.2710 -0.0095 0.0153  -0.0370 201 A1B4W C C15 
2197 C C17 . A1B4W G .   ? 0.2684 0.2064 0.2566 -0.0043 0.0134  -0.0283 201 A1B4W C C17 
2198 O O2  . A1B4W G .   ? 0.2204 0.1645 0.2384 0.0026  0.0086  -0.0134 201 A1B4W C O2  
2199 N N2  . A1B4W G .   ? 0.2095 0.1595 0.2181 0.0011  0.0038  -0.0097 201 A1B4W C N2  
2200 C C9  . A1B4W G .   ? 0.2369 0.1821 0.2391 -0.0002 0.0085  -0.0179 201 A1B4W C C9  
2201 C C11 . A1B4W G .   ? 0.2486 0.1907 0.2456 -0.0023 0.0072  -0.0208 201 A1B4W C C11 
2202 C C12 . A1B4W G .   ? 0.2637 0.2013 0.2571 -0.0039 0.0105  -0.0263 201 A1B4W C C12 
2203 C C16 . A1B4W G .   ? 0.2843 0.2172 0.2700 -0.0060 0.0181  -0.0342 201 A1B4W C C16 
2204 C C14 . A1B4W G .   ? 0.2730 0.2031 0.2550 -0.0091 0.0116  -0.0350 201 A1B4W C C14 
2205 O O1  . A1B4W G .   ? 0.2448 0.1927 0.2408 -0.0010 0.0161  -0.0218 201 A1B4W C O1  
2206 C C1  . A1B4W G .   ? 0.2642 0.2106 0.2351 -0.0065 0.0139  -0.0227 201 A1B4W C C1  
2207 O O   . A1B4W G .   ? 0.2442 0.1917 0.2168 -0.0054 0.0091  -0.0199 201 A1B4W C O   
2208 C C   . A1B4W G .   ? 0.2513 0.2003 0.2202 -0.0055 0.0057  -0.0167 201 A1B4W C C   
2209 N N   . A1B4W G .   ? 0.2964 0.2399 0.2631 -0.0096 0.0252  -0.0302 201 A1B4W C N   
2210 C C3  . A1B4W G .   ? 0.2931 0.2388 0.2570 -0.0097 0.0212  -0.0259 201 A1B4W C C3  
2211 C C2  . A1B4W G .   ? 0.2833 0.2304 0.2492 -0.0081 0.0155  -0.0223 201 A1B4W C C2  
2212 N N1  . A1B4W H .   ? 0.4224 0.3849 0.4689 0.0082  0.0279  -0.0176 202 A1B4W C N1  
2213 C C4  . A1B4W H .   ? 0.4678 0.4159 0.4742 -0.0009 0.0346  -0.0319 202 A1B4W C C4  
2214 C C5  . A1B4W H .   ? 0.4658 0.4137 0.4797 0.0016  0.0307  -0.0289 202 A1B4W C C5  
2215 C C6  . A1B4W H .   ? 0.4543 0.4074 0.4769 0.0040  0.0263  -0.0226 202 A1B4W C C6  
2216 C C7  . A1B4W H .   ? 0.4413 0.3972 0.4801 0.0072  0.0289  -0.0215 202 A1B4W C C7  
2217 C C8  . A1B4W H .   ? 0.4155 0.3814 0.4792 0.0115  0.0305  -0.0167 202 A1B4W C C8  
2218 C C10 . A1B4W H .   ? 0.3942 0.3707 0.4826 0.0147  0.0368  -0.0165 202 A1B4W C C10 
2219 C C13 . A1B4W H .   ? 0.4066 0.3832 0.4481 0.0039  0.0218  -0.0093 202 A1B4W C C13 
2220 C C15 . A1B4W H .   ? 0.4082 0.3787 0.4398 0.0041  0.0135  -0.0058 202 A1B4W C C15 
2221 C C17 . A1B4W H .   ? 0.4181 0.3847 0.4580 0.0062  0.0240  -0.0141 202 A1B4W C C17 
2222 O O2  . A1B4W H .   ? 0.3648 0.3471 0.4605 0.0155  0.0315  -0.0104 202 A1B4W C O2  
2223 N N2  . A1B4W H .   ? 0.4044 0.3786 0.5022 0.0170  0.0436  -0.0213 202 A1B4W C N2  
2224 C C9  . A1B4W H .   ? 0.4083 0.3793 0.4762 0.0109  0.0357  -0.0189 202 A1B4W C C9  
2225 C C11 . A1B4W H .   ? 0.4142 0.3892 0.4727 0.0078  0.0324  -0.0161 202 A1B4W C C11 
2226 C C12 . A1B4W H .   ? 0.4100 0.3838 0.4602 0.0069  0.0247  -0.0115 202 A1B4W C C12 
2227 C C16 . A1B4W H .   ? 0.4126 0.3788 0.4480 0.0059  0.0173  -0.0096 202 A1B4W C C16 
2228 C C14 . A1B4W H .   ? 0.4109 0.3838 0.4398 0.0023  0.0167  -0.0077 202 A1B4W C C14 
2229 O O1  . A1B4W H .   ? 0.4450 0.3971 0.4904 0.0089  0.0319  -0.0241 202 A1B4W C O1  
2230 C C1  . A1B4W H .   ? 0.4793 0.4215 0.4914 0.0013  0.0311  -0.0320 202 A1B4W C C1  
2231 O O   . A1B4W H .   ? 0.4800 0.4218 0.5005 0.0036  0.0280  -0.0289 202 A1B4W C O   
2232 C C   . A1B4W H .   ? 0.4711 0.4072 0.4893 0.0026  0.0275  -0.0315 202 A1B4W C C   
2233 N N   . A1B4W H .   ? 0.4840 0.4272 0.4807 -0.0038 0.0384  -0.0375 202 A1B4W C N   
2234 C C3  . A1B4W H .   ? 0.4830 0.4210 0.4776 -0.0042 0.0382  -0.0405 202 A1B4W C C3  
2235 C C2  . A1B4W H .   ? 0.4838 0.4211 0.4863 -0.0017 0.0347  -0.0380 202 A1B4W C C2  
# 
