data_7I6U
# 
_entry.id   7I6U 
# 
_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   7I6U         pdb_00007i6u 10.2210/pdb7i6u/pdb 
WWPDB D_1001408389 ?            ?                   
# 
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                        7I6U 
_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)-1-{[4-(methylsulfanyl)pyrimidin-5-yl]acetyl}piperidine-3-carboxamide' 294.373   2   ?         ? ? ? 
3 non-polymer syn GLYCEROL                                                                    92.094    1   ?         ? ? ? 
4 non-polymer syn 'ZINC ION'                                                                  65.409    2   ?         ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                        78.133    5   ?         ? ? ? 
6 water       nat water                                                                       18.015    241 ?         ? ? ? 
# 
_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)-1-{[4-(methylsulfanyl)pyrimidin-5-yl]acetyl}piperidine-3-carboxamide' A1B5A 
3 GLYCEROL                                                                    GOL   
4 'ZINC ION'                                                                  ZN    
5 'DIMETHYL SULFOXIDE'                                                        DMS   
6 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 
A1B5A non-polymer         . '(3S)-1-{[4-(methylsulfanyl)pyrimidin-5-yl]acetyl}piperidine-3-carboxamide' ? 'C13 H18 N4 O2 S' 
294.373 
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 
GOL   non-polymer         . GLYCEROL                                                                    
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'        92.094  
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        A1B5A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B5A 
_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 A1B5A 1   201 201 A1B5A LIG A . 
D 3 GOL   1   202 202 GOL   GOL A . 
E 4 ZN    1   203 1   ZN    ZN  A . 
F 5 DMS   1   204 6   DMS   DMS A . 
G 5 DMS   1   205 8   DMS   DMS A . 
H 2 A1B5A 1   201 201 A1B5A LIG C . 
I 5 DMS   1   202 7   DMS   DMS C . 
J 5 DMS   1   203 9   DMS   DMS C . 
K 4 ZN    1   204 1   ZN    ZN  C . 
L 5 DMS   1   205 6   DMS   DMS C . 
M 6 HOH   1   301 95  HOH   HOH A . 
M 6 HOH   2   302 244 HOH   HOH A . 
M 6 HOH   3   303 174 HOH   HOH A . 
M 6 HOH   4   304 63  HOH   HOH A . 
M 6 HOH   5   305 103 HOH   HOH A . 
M 6 HOH   6   306 64  HOH   HOH A . 
M 6 HOH   7   307 28  HOH   HOH A . 
M 6 HOH   8   308 93  HOH   HOH A . 
M 6 HOH   9   309 84  HOH   HOH A . 
M 6 HOH   10  310 228 HOH   HOH A . 
M 6 HOH   11  311 14  HOH   HOH A . 
M 6 HOH   12  312 148 HOH   HOH A . 
M 6 HOH   13  313 145 HOH   HOH A . 
M 6 HOH   14  314 155 HOH   HOH A . 
M 6 HOH   15  315 59  HOH   HOH A . 
M 6 HOH   16  316 61  HOH   HOH A . 
M 6 HOH   17  317 62  HOH   HOH A . 
M 6 HOH   18  318 14  HOH   HOH A . 
M 6 HOH   19  319 109 HOH   HOH A . 
M 6 HOH   20  320 22  HOH   HOH A . 
M 6 HOH   21  321 140 HOH   HOH A . 
M 6 HOH   22  322 235 HOH   HOH A . 
M 6 HOH   23  323 5   HOH   HOH A . 
M 6 HOH   24  324 113 HOH   HOH A . 
M 6 HOH   25  325 13  HOH   HOH A . 
M 6 HOH   26  326 23  HOH   HOH A . 
M 6 HOH   27  327 233 HOH   HOH A . 
M 6 HOH   28  328 250 HOH   HOH A . 
M 6 HOH   29  329 268 HOH   HOH A . 
M 6 HOH   30  330 19  HOH   HOH A . 
M 6 HOH   31  331 231 HOH   HOH A . 
M 6 HOH   32  332 115 HOH   HOH A . 
M 6 HOH   33  333 33  HOH   HOH A . 
M 6 HOH   34  334 48  HOH   HOH A . 
M 6 HOH   35  335 128 HOH   HOH A . 
M 6 HOH   36  336 259 HOH   HOH A . 
M 6 HOH   37  337 260 HOH   HOH A . 
M 6 HOH   38  338 256 HOH   HOH A . 
M 6 HOH   39  339 119 HOH   HOH A . 
M 6 HOH   40  340 56  HOH   HOH A . 
M 6 HOH   41  341 116 HOH   HOH A . 
M 6 HOH   42  342 88  HOH   HOH A . 
M 6 HOH   43  343 252 HOH   HOH A . 
M 6 HOH   44  344 158 HOH   HOH A . 
M 6 HOH   45  345 49  HOH   HOH A . 
M 6 HOH   46  346 6   HOH   HOH A . 
M 6 HOH   47  347 144 HOH   HOH A . 
M 6 HOH   48  348 7   HOH   HOH A . 
M 6 HOH   49  349 99  HOH   HOH A . 
M 6 HOH   50  350 38  HOH   HOH A . 
M 6 HOH   51  351 66  HOH   HOH A . 
M 6 HOH   52  352 71  HOH   HOH A . 
M 6 HOH   53  353 66  HOH   HOH A . 
M 6 HOH   54  354 53  HOH   HOH A . 
M 6 HOH   55  355 245 HOH   HOH A . 
M 6 HOH   56  356 281 HOH   HOH A . 
M 6 HOH   57  357 247 HOH   HOH A . 
M 6 HOH   58  358 265 HOH   HOH A . 
M 6 HOH   59  359 149 HOH   HOH A . 
M 6 HOH   60  360 261 HOH   HOH A . 
M 6 HOH   61  361 154 HOH   HOH A . 
M 6 HOH   62  362 70  HOH   HOH A . 
M 6 HOH   63  363 227 HOH   HOH A . 
M 6 HOH   64  364 278 HOH   HOH A . 
M 6 HOH   65  365 151 HOH   HOH A . 
M 6 HOH   66  366 10  HOH   HOH A . 
M 6 HOH   67  367 271 HOH   HOH A . 
M 6 HOH   68  368 72  HOH   HOH A . 
M 6 HOH   69  369 150 HOH   HOH A . 
M 6 HOH   70  370 230 HOH   HOH A . 
M 6 HOH   71  371 73  HOH   HOH A . 
M 6 HOH   72  372 243 HOH   HOH A . 
M 6 HOH   73  373 26  HOH   HOH A . 
M 6 HOH   74  374 156 HOH   HOH A . 
M 6 HOH   75  375 85  HOH   HOH A . 
M 6 HOH   76  376 115 HOH   HOH A . 
M 6 HOH   77  377 23  HOH   HOH A . 
M 6 HOH   78  378 107 HOH   HOH A . 
M 6 HOH   79  379 149 HOH   HOH A . 
M 6 HOH   80  380 249 HOH   HOH A . 
M 6 HOH   81  381 75  HOH   HOH A . 
M 6 HOH   82  382 141 HOH   HOH A . 
M 6 HOH   83  383 197 HOH   HOH A . 
M 6 HOH   84  384 12  HOH   HOH A . 
M 6 HOH   85  385 102 HOH   HOH A . 
M 6 HOH   86  386 246 HOH   HOH A . 
M 6 HOH   87  387 19  HOH   HOH A . 
M 6 HOH   88  388 92  HOH   HOH A . 
M 6 HOH   89  389 91  HOH   HOH A . 
M 6 HOH   90  390 279 HOH   HOH A . 
M 6 HOH   91  391 96  HOH   HOH A . 
M 6 HOH   92  392 35  HOH   HOH A . 
M 6 HOH   93  393 40  HOH   HOH A . 
M 6 HOH   94  394 112 HOH   HOH A . 
M 6 HOH   95  395 21  HOH   HOH A . 
M 6 HOH   96  396 12  HOH   HOH A . 
M 6 HOH   97  397 202 HOH   HOH A . 
M 6 HOH   98  398 176 HOH   HOH A . 
M 6 HOH   99  399 241 HOH   HOH A . 
M 6 HOH   100 400 102 HOH   HOH A . 
M 6 HOH   101 401 232 HOH   HOH A . 
M 6 HOH   102 402 63  HOH   HOH A . 
M 6 HOH   103 403 16  HOH   HOH A . 
M 6 HOH   104 404 114 HOH   HOH A . 
M 6 HOH   105 405 153 HOH   HOH A . 
M 6 HOH   106 406 171 HOH   HOH A . 
M 6 HOH   107 407 157 HOH   HOH A . 
M 6 HOH   108 408 77  HOH   HOH A . 
M 6 HOH   109 409 52  HOH   HOH A . 
M 6 HOH   110 410 15  HOH   HOH A . 
M 6 HOH   111 411 136 HOH   HOH A . 
M 6 HOH   112 412 24  HOH   HOH A . 
M 6 HOH   113 413 104 HOH   HOH A . 
M 6 HOH   114 414 6   HOH   HOH A . 
M 6 HOH   115 415 172 HOH   HOH A . 
M 6 HOH   116 416 143 HOH   HOH A . 
M 6 HOH   117 417 154 HOH   HOH A . 
M 6 HOH   118 418 138 HOH   HOH A . 
M 6 HOH   119 419 135 HOH   HOH A . 
M 6 HOH   120 420 126 HOH   HOH A . 
M 6 HOH   121 421 129 HOH   HOH A . 
M 6 HOH   122 422 60  HOH   HOH A . 
M 6 HOH   123 423 226 HOH   HOH A . 
M 6 HOH   124 424 187 HOH   HOH A . 
M 6 HOH   125 425 222 HOH   HOH A . 
M 6 HOH   126 426 107 HOH   HOH A . 
M 6 HOH   127 427 82  HOH   HOH A . 
M 6 HOH   128 428 99  HOH   HOH A . 
M 6 HOH   129 429 206 HOH   HOH A . 
M 6 HOH   130 430 225 HOH   HOH A . 
N 6 HOH   1   301 103 HOH   HOH C . 
N 6 HOH   2   302 147 HOH   HOH C . 
N 6 HOH   3   303 8   HOH   HOH C . 
N 6 HOH   4   304 120 HOH   HOH C . 
N 6 HOH   5   305 152 HOH   HOH C . 
N 6 HOH   6   306 255 HOH   HOH C . 
N 6 HOH   7   307 157 HOH   HOH C . 
N 6 HOH   8   308 28  HOH   HOH C . 
N 6 HOH   9   309 70  HOH   HOH C . 
N 6 HOH   10  310 229 HOH   HOH C . 
N 6 HOH   11  311 2   HOH   HOH C . 
N 6 HOH   12  312 33  HOH   HOH C . 
N 6 HOH   13  313 276 HOH   HOH C . 
N 6 HOH   14  314 124 HOH   HOH C . 
N 6 HOH   15  315 50  HOH   HOH C . 
N 6 HOH   16  316 248 HOH   HOH C . 
N 6 HOH   17  317 51  HOH   HOH C . 
N 6 HOH   18  318 80  HOH   HOH C . 
N 6 HOH   19  319 43  HOH   HOH C . 
N 6 HOH   20  320 109 HOH   HOH C . 
N 6 HOH   21  321 264 HOH   HOH C . 
N 6 HOH   22  322 78  HOH   HOH C . 
N 6 HOH   23  323 67  HOH   HOH C . 
N 6 HOH   24  324 118 HOH   HOH C . 
N 6 HOH   25  325 20  HOH   HOH C . 
N 6 HOH   26  326 123 HOH   HOH C . 
N 6 HOH   27  327 39  HOH   HOH C . 
N 6 HOH   28  328 30  HOH   HOH C . 
N 6 HOH   29  329 234 HOH   HOH C . 
N 6 HOH   30  330 46  HOH   HOH C . 
N 6 HOH   31  331 257 HOH   HOH C . 
N 6 HOH   32  332 98  HOH   HOH C . 
N 6 HOH   33  333 238 HOH   HOH C . 
N 6 HOH   34  334 150 HOH   HOH C . 
N 6 HOH   35  335 122 HOH   HOH C . 
N 6 HOH   36  336 71  HOH   HOH C . 
N 6 HOH   37  337 13  HOH   HOH C . 
N 6 HOH   38  338 110 HOH   HOH C . 
N 6 HOH   39  339 65  HOH   HOH C . 
N 6 HOH   40  340 273 HOH   HOH C . 
N 6 HOH   41  341 31  HOH   HOH C . 
N 6 HOH   42  342 4   HOH   HOH C . 
N 6 HOH   43  343 269 HOH   HOH C . 
N 6 HOH   44  344 38  HOH   HOH C . 
N 6 HOH   45  345 280 HOH   HOH C . 
N 6 HOH   46  346 254 HOH   HOH C . 
N 6 HOH   47  347 37  HOH   HOH C . 
N 6 HOH   48  348 272 HOH   HOH C . 
N 6 HOH   49  349 242 HOH   HOH C . 
N 6 HOH   50  350 69  HOH   HOH C . 
N 6 HOH   51  351 79  HOH   HOH C . 
N 6 HOH   52  352 85  HOH   HOH C . 
N 6 HOH   53  353 140 HOH   HOH C . 
N 6 HOH   54  354 83  HOH   HOH C . 
N 6 HOH   55  355 83  HOH   HOH C . 
N 6 HOH   56  356 267 HOH   HOH C . 
N 6 HOH   57  357 16  HOH   HOH C . 
N 6 HOH   58  358 236 HOH   HOH C . 
N 6 HOH   59  359 89  HOH   HOH C . 
N 6 HOH   60  360 91  HOH   HOH C . 
N 6 HOH   61  361 11  HOH   HOH C . 
N 6 HOH   62  362 37  HOH   HOH C . 
N 6 HOH   63  363 146 HOH   HOH C . 
N 6 HOH   64  364 50  HOH   HOH C . 
N 6 HOH   65  365 7   HOH   HOH C . 
N 6 HOH   66  366 64  HOH   HOH C . 
N 6 HOH   67  367 240 HOH   HOH C . 
N 6 HOH   68  368 68  HOH   HOH C . 
N 6 HOH   69  369 1   HOH   HOH C . 
N 6 HOH   70  370 263 HOH   HOH C . 
N 6 HOH   71  371 62  HOH   HOH C . 
N 6 HOH   72  372 251 HOH   HOH C . 
N 6 HOH   73  373 258 HOH   HOH C . 
N 6 HOH   74  374 87  HOH   HOH C . 
N 6 HOH   75  375 41  HOH   HOH C . 
N 6 HOH   76  376 90  HOH   HOH C . 
N 6 HOH   77  377 17  HOH   HOH C . 
N 6 HOH   78  378 204 HOH   HOH C . 
N 6 HOH   79  379 54  HOH   HOH C . 
N 6 HOH   80  380 29  HOH   HOH C . 
N 6 HOH   81  381 54  HOH   HOH C . 
N 6 HOH   82  382 274 HOH   HOH C . 
N 6 HOH   83  383 44  HOH   HOH C . 
N 6 HOH   84  384 130 HOH   HOH C . 
N 6 HOH   85  385 117 HOH   HOH C . 
N 6 HOH   86  386 253 HOH   HOH C . 
N 6 HOH   87  387 41  HOH   HOH C . 
N 6 HOH   88  388 237 HOH   HOH C . 
N 6 HOH   89  389 45  HOH   HOH C . 
N 6 HOH   90  390 3   HOH   HOH C . 
N 6 HOH   91  391 97  HOH   HOH C . 
N 6 HOH   92  392 275 HOH   HOH C . 
N 6 HOH   93  393 9   HOH   HOH C . 
N 6 HOH   94  394 239 HOH   HOH C . 
N 6 HOH   95  395 124 HOH   HOH C . 
N 6 HOH   96  396 262 HOH   HOH C . 
N 6 HOH   97  397 47  HOH   HOH C . 
N 6 HOH   98  398 277 HOH   HOH C . 
N 6 HOH   99  399 95  HOH   HOH C . 
N 6 HOH   100 400 200 HOH   HOH C . 
N 6 HOH   101 401 266 HOH   HOH C . 
N 6 HOH   102 402 116 HOH   HOH C . 
N 6 HOH   103 403 146 HOH   HOH C . 
N 6 HOH   104 404 27  HOH   HOH C . 
N 6 HOH   105 405 139 HOH   HOH C . 
N 6 HOH   106 406 198 HOH   HOH C . 
N 6 HOH   107 407 93  HOH   HOH C . 
N 6 HOH   108 408 199 HOH   HOH C . 
N 6 HOH   109 409 132 HOH   HOH C . 
N 6 HOH   110 410 218 HOH   HOH C . 
N 6 HOH   111 411 142 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           7I6U 
_cell.length_a           72.534 
_cell.length_b           61.622 
_cell.length_c           65.197 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.91 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I6U 
_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          7I6U 
_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   46.27 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-02-07 
_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   0.92206 
_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        0.92206 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I6U 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.94 
_reflns.d_resolution_high            1.46 
_reflns.number_obs                   47046 
_reflns.percent_possible_obs         93.7 
_reflns.pdbx_Rmerge_I_obs            0.090 
_reflns.pdbx_netI_over_sigmaI        9.2 
_reflns.pdbx_redundancy              5.9 
_reflns.pdbx_Rrim_I_all              0.098 
_reflns.pdbx_Rpim_I_all              0.038 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     278595 
_reflns.pdbx_chi_squared             0.76 
_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                  1.46 
_reflns_shell.d_res_low                   1.53 
_reflns_shell.number_measured_all         19087 
_reflns_shell.number_unique_obs           5746 
_reflns_shell.Rmerge_I_obs                1.192 
_reflns_shell.pdbx_chi_squared            0.53 
_reflns_shell.pdbx_redundancy             3.3 
_reflns_shell.percent_possible_obs        78.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.389 
_reflns_shell.pdbx_Rpim_I_all             0.687 
_reflns_shell.pdbx_CC_half                0.467 
_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                                 7I6U 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     46782 
_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                             38.68 
_refine.ls_d_res_high                            1.456 
_refine.ls_percent_reflns_obs                    93.0 
_refine.ls_R_factor_obs                          0.1869 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1858 
_refine.ls_R_factor_R_free                       0.2092 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.920 
_refine.ls_number_reflns_R_free                  2301 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.959 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               21.95 
_refine.aniso_B[1][1]                            1.00800 
_refine.aniso_B[2][2]                            -1.53940 
_refine.aniso_B[3][3]                            0.53130 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.01160 
_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             0.071 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.071 
_refine.pdbx_overall_SU_R_Blow_DPI               0.074 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.073 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I6U 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_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         68 
_refine_hist.number_atoms_solvent             241 
_refine_hist.number_atoms_total               2457 
_refine_hist.d_res_high                       1.456 
_refine_hist.d_res_low                        38.68 
# 
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  2266 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.99  ? 2.00  3075 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  753  '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  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2266 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.51  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.82 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  275  '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  1854 '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                       1.46 
_refine_ls_shell.d_res_low                        1.47 
_refine_ls_shell.number_reflns_R_work             888 
_refine_ls_shell.R_factor_R_work                  0.3147 
_refine_ls_shell.percent_reflns_obs               62.82 
_refine_ls_shell.R_factor_R_free                  0.3493 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.13 
_refine_ls_shell.number_reflns_R_free             48 
_refine_ls_shell.number_reflns_all                936 
_refine_ls_shell.R_factor_all                     0.3165 
# 
_struct.entry_id                  7I6U 
_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-0036740-001 (A71EV2A-x5039)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I6U 
_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 5 ? 
G N N 5 ? 
H N N 2 ? 
I N N 5 ? 
J N N 5 ? 
K N N 4 ? 
L N N 5 ? 
M N N 6 ? 
N N N 6 ? 
# 
_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 7I6U A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I6U 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,G,M 
2 1 B,H,I,J,K,L,N 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 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 E ZN . ZN ? ? A CYS 56  A ZN 203 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 58  A ZN 203 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? A CYS 116 A ZN 203 1_555 ? ? ? ? ? ? ? 2.314 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? A HIS 118 A ZN 203 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 K ZN . ZN ? ? C CYS 56  C ZN 204 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 K ZN . ZN ? ? C CYS 58  C ZN 204 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 K ZN . ZN ? ? C CYS 116 C ZN 204 1_555 ? ? ? ? ? ? ? 2.321 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 K ZN . ZN ? ? C HIS 118 C ZN 204 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
# 
_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 ? E ZN . ? A ZN 203 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.3 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.2 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.3 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.6 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.7 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 113.6 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? K ZN . ? C ZN 204 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.3 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? K ZN . ? C ZN 204 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.6 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? K ZN . ? C ZN 204 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 116.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? K ZN . ? C ZN 204 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.7 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? K ZN . ? C ZN 204 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.9 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? K ZN . ? C ZN 204 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.5 ? 
# 
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 SER B 119 ? N SER C 125 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                   7I6U 
_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_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 19.6506 6.7664   18.2753 -0.0226 -0.0154 -0.0083 -0.0015 0.0149 -0.0038 0.6562 0.9709 0.4372 
-0.2242 -0.0843 -0.0955 0.0083  -0.0077 0.0804 0.0259 0.0197 0.0397  0.0203 0.0353  -0.0281 
'X-RAY DIFFRACTION' 2 ? refined 15.3764 -23.9247 14.1019 -0.0191 -0.0118 -0.0142 0.0014  0.0102 -0.0034 0.6373 0.9512 0.4642 
0.2373  0.2070  0.1481  -0.0247 0.0317  0.0406 0.0271 0.0534 -0.0531 0.0202 -0.0001 -0.0287 
# 
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|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       430 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   8.66 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
# 
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 
A1B5A N1   N  Y N 1   
A1B5A N3   N  N N 2   
A1B5A C4   C  Y N 3   
A1B5A C5   C  N N 4   
A1B5A C6   C  N N 5   
A1B5A C7   C  N N 6   
A1B5A C8   C  N N 7   
A1B5A C10  C  N S 8   
A1B5A O1   O  N N 9   
A1B5A C11  C  N N 10  
A1B5A C9   C  N N 11  
A1B5A C12  C  N N 12  
A1B5A N2   N  N N 13  
A1B5A O    O  N N 14  
A1B5A C1   C  Y N 15  
A1B5A S    S  N N 16  
A1B5A C    C  N N 17  
A1B5A C3   C  Y N 18  
A1B5A C2   C  Y N 19  
A1B5A N    N  Y N 20  
A1B5A H14  H  N N 21  
A1B5A H15  H  N N 22  
A1B5A H6   H  N N 23  
A1B5A H7   H  N N 24  
A1B5A H8   H  N N 25  
A1B5A H9   H  N N 26  
A1B5A H10  H  N N 27  
A1B5A H11  H  N N 28  
A1B5A H    H  N N 29  
A1B5A H12  H  N N 30  
A1B5A H13  H  N N 31  
A1B5A H16  H  N N 32  
A1B5A H17  H  N N 33  
A1B5A H1   H  N N 34  
A1B5A H3   H  N N 35  
A1B5A H2   H  N N 36  
A1B5A H5   H  N N 37  
A1B5A H4   H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
GOL   C1   C  N N 185 
GOL   O1   O  N N 186 
GOL   C2   C  N N 187 
GOL   O2   O  N N 188 
GOL   C3   C  N N 189 
GOL   O3   O  N N 190 
GOL   H11  H  N N 191 
GOL   H12  H  N N 192 
GOL   HO1  H  N N 193 
GOL   H2   H  N N 194 
GOL   HO2  H  N N 195 
GOL   H31  H  N N 196 
GOL   H32  H  N N 197 
GOL   HO3  H  N N 198 
HIS   N    N  N N 199 
HIS   CA   C  N S 200 
HIS   C    C  N N 201 
HIS   O    O  N N 202 
HIS   CB   C  N N 203 
HIS   CG   C  Y N 204 
HIS   ND1  N  Y N 205 
HIS   CD2  C  Y N 206 
HIS   CE1  C  Y N 207 
HIS   NE2  N  Y N 208 
HIS   OXT  O  N N 209 
HIS   H    H  N N 210 
HIS   H2   H  N N 211 
HIS   HA   H  N N 212 
HIS   HB2  H  N N 213 
HIS   HB3  H  N N 214 
HIS   HD1  H  N N 215 
HIS   HD2  H  N N 216 
HIS   HE1  H  N N 217 
HIS   HE2  H  N N 218 
HIS   HXT  H  N N 219 
HOH   O    O  N N 220 
HOH   H1   H  N N 221 
HOH   H2   H  N N 222 
ILE   N    N  N N 223 
ILE   CA   C  N S 224 
ILE   C    C  N N 225 
ILE   O    O  N N 226 
ILE   CB   C  N S 227 
ILE   CG1  C  N N 228 
ILE   CG2  C  N N 229 
ILE   CD1  C  N N 230 
ILE   OXT  O  N N 231 
ILE   H    H  N N 232 
ILE   H2   H  N N 233 
ILE   HA   H  N N 234 
ILE   HB   H  N N 235 
ILE   HG12 H  N N 236 
ILE   HG13 H  N N 237 
ILE   HG21 H  N N 238 
ILE   HG22 H  N N 239 
ILE   HG23 H  N N 240 
ILE   HD11 H  N N 241 
ILE   HD12 H  N N 242 
ILE   HD13 H  N N 243 
ILE   HXT  H  N N 244 
LEU   N    N  N N 245 
LEU   CA   C  N S 246 
LEU   C    C  N N 247 
LEU   O    O  N N 248 
LEU   CB   C  N N 249 
LEU   CG   C  N N 250 
LEU   CD1  C  N N 251 
LEU   CD2  C  N N 252 
LEU   OXT  O  N N 253 
LEU   H    H  N N 254 
LEU   H2   H  N N 255 
LEU   HA   H  N N 256 
LEU   HB2  H  N N 257 
LEU   HB3  H  N N 258 
LEU   HG   H  N N 259 
LEU   HD11 H  N N 260 
LEU   HD12 H  N N 261 
LEU   HD13 H  N N 262 
LEU   HD21 H  N N 263 
LEU   HD22 H  N N 264 
LEU   HD23 H  N N 265 
LEU   HXT  H  N N 266 
LYS   N    N  N N 267 
LYS   CA   C  N S 268 
LYS   C    C  N N 269 
LYS   O    O  N N 270 
LYS   CB   C  N N 271 
LYS   CG   C  N N 272 
LYS   CD   C  N N 273 
LYS   CE   C  N N 274 
LYS   NZ   N  N N 275 
LYS   OXT  O  N N 276 
LYS   H    H  N N 277 
LYS   H2   H  N N 278 
LYS   HA   H  N N 279 
LYS   HB2  H  N N 280 
LYS   HB3  H  N N 281 
LYS   HG2  H  N N 282 
LYS   HG3  H  N N 283 
LYS   HD2  H  N N 284 
LYS   HD3  H  N N 285 
LYS   HE2  H  N N 286 
LYS   HE3  H  N N 287 
LYS   HZ1  H  N N 288 
LYS   HZ2  H  N N 289 
LYS   HZ3  H  N N 290 
LYS   HXT  H  N N 291 
MET   N    N  N N 292 
MET   CA   C  N S 293 
MET   C    C  N N 294 
MET   O    O  N N 295 
MET   CB   C  N N 296 
MET   CG   C  N N 297 
MET   SD   S  N N 298 
MET   CE   C  N N 299 
MET   OXT  O  N N 300 
MET   H    H  N N 301 
MET   H2   H  N N 302 
MET   HA   H  N N 303 
MET   HB2  H  N N 304 
MET   HB3  H  N N 305 
MET   HG2  H  N N 306 
MET   HG3  H  N N 307 
MET   HE1  H  N N 308 
MET   HE2  H  N N 309 
MET   HE3  H  N N 310 
MET   HXT  H  N N 311 
PHE   N    N  N N 312 
PHE   CA   C  N S 313 
PHE   C    C  N N 314 
PHE   O    O  N N 315 
PHE   CB   C  N N 316 
PHE   CG   C  Y N 317 
PHE   CD1  C  Y N 318 
PHE   CD2  C  Y N 319 
PHE   CE1  C  Y N 320 
PHE   CE2  C  Y N 321 
PHE   CZ   C  Y N 322 
PHE   OXT  O  N N 323 
PHE   H    H  N N 324 
PHE   H2   H  N N 325 
PHE   HA   H  N N 326 
PHE   HB2  H  N N 327 
PHE   HB3  H  N N 328 
PHE   HD1  H  N N 329 
PHE   HD2  H  N N 330 
PHE   HE1  H  N N 331 
PHE   HE2  H  N N 332 
PHE   HZ   H  N N 333 
PHE   HXT  H  N N 334 
PRO   N    N  N N 335 
PRO   CA   C  N S 336 
PRO   C    C  N N 337 
PRO   O    O  N N 338 
PRO   CB   C  N N 339 
PRO   CG   C  N N 340 
PRO   CD   C  N N 341 
PRO   OXT  O  N N 342 
PRO   H    H  N N 343 
PRO   HA   H  N N 344 
PRO   HB2  H  N N 345 
PRO   HB3  H  N N 346 
PRO   HG2  H  N N 347 
PRO   HG3  H  N N 348 
PRO   HD2  H  N N 349 
PRO   HD3  H  N N 350 
PRO   HXT  H  N N 351 
SER   N    N  N N 352 
SER   CA   C  N S 353 
SER   C    C  N N 354 
SER   O    O  N N 355 
SER   CB   C  N N 356 
SER   OG   O  N N 357 
SER   OXT  O  N N 358 
SER   H    H  N N 359 
SER   H2   H  N N 360 
SER   HA   H  N N 361 
SER   HB2  H  N N 362 
SER   HB3  H  N N 363 
SER   HG   H  N N 364 
SER   HXT  H  N N 365 
THR   N    N  N N 366 
THR   CA   C  N S 367 
THR   C    C  N N 368 
THR   O    O  N N 369 
THR   CB   C  N R 370 
THR   OG1  O  N N 371 
THR   CG2  C  N N 372 
THR   OXT  O  N N 373 
THR   H    H  N N 374 
THR   H2   H  N N 375 
THR   HA   H  N N 376 
THR   HB   H  N N 377 
THR   HG1  H  N N 378 
THR   HG21 H  N N 379 
THR   HG22 H  N N 380 
THR   HG23 H  N N 381 
THR   HXT  H  N N 382 
TRP   N    N  N N 383 
TRP   CA   C  N S 384 
TRP   C    C  N N 385 
TRP   O    O  N N 386 
TRP   CB   C  N N 387 
TRP   CG   C  Y N 388 
TRP   CD1  C  Y N 389 
TRP   CD2  C  Y N 390 
TRP   NE1  N  Y N 391 
TRP   CE2  C  Y N 392 
TRP   CE3  C  Y N 393 
TRP   CZ2  C  Y N 394 
TRP   CZ3  C  Y N 395 
TRP   CH2  C  Y N 396 
TRP   OXT  O  N N 397 
TRP   H    H  N N 398 
TRP   H2   H  N N 399 
TRP   HA   H  N N 400 
TRP   HB2  H  N N 401 
TRP   HB3  H  N N 402 
TRP   HD1  H  N N 403 
TRP   HE1  H  N N 404 
TRP   HE3  H  N N 405 
TRP   HZ2  H  N N 406 
TRP   HZ3  H  N N 407 
TRP   HH2  H  N N 408 
TRP   HXT  H  N N 409 
TYR   N    N  N N 410 
TYR   CA   C  N S 411 
TYR   C    C  N N 412 
TYR   O    O  N N 413 
TYR   CB   C  N N 414 
TYR   CG   C  Y N 415 
TYR   CD1  C  Y N 416 
TYR   CD2  C  Y N 417 
TYR   CE1  C  Y N 418 
TYR   CE2  C  Y N 419 
TYR   CZ   C  Y N 420 
TYR   OH   O  N N 421 
TYR   OXT  O  N N 422 
TYR   H    H  N N 423 
TYR   H2   H  N N 424 
TYR   HA   H  N N 425 
TYR   HB2  H  N N 426 
TYR   HB3  H  N N 427 
TYR   HD1  H  N N 428 
TYR   HD2  H  N N 429 
TYR   HE1  H  N N 430 
TYR   HE2  H  N N 431 
TYR   HH   H  N N 432 
TYR   HXT  H  N N 433 
VAL   N    N  N N 434 
VAL   CA   C  N S 435 
VAL   C    C  N N 436 
VAL   O    O  N N 437 
VAL   CB   C  N N 438 
VAL   CG1  C  N N 439 
VAL   CG2  C  N N 440 
VAL   OXT  O  N N 441 
VAL   H    H  N N 442 
VAL   H2   H  N N 443 
VAL   HA   H  N N 444 
VAL   HB   H  N N 445 
VAL   HG11 H  N N 446 
VAL   HG12 H  N N 447 
VAL   HG13 H  N N 448 
VAL   HG21 H  N N 449 
VAL   HG22 H  N N 450 
VAL   HG23 H  N N 451 
VAL   HXT  H  N N 452 
ZN    ZN   ZN N N 453 
# 
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 
A1B5A C   S    sing N N 1   
A1B5A S   C1   sing N N 2   
A1B5A C1  N    doub Y N 3   
A1B5A N   C2   sing Y N 4   
A1B5A C2  N1   doub Y N 5   
A1B5A N1  C3   sing Y N 6   
A1B5A C3  C4   doub Y N 7   
A1B5A C1  C4   sing Y N 8   
A1B5A C4  C5   sing N N 9   
A1B5A C5  C6   sing N N 10  
A1B5A O   C6   doub N N 11  
A1B5A C6  N2   sing N N 12  
A1B5A N2  C7   sing N N 13  
A1B5A C7  C8   sing N N 14  
A1B5A C8  C9   sing N N 15  
A1B5A C9  C10  sing N N 16  
A1B5A C10 C11  sing N N 17  
A1B5A N3  C11  sing N N 18  
A1B5A C11 O1   doub N N 19  
A1B5A C12 C10  sing N N 20  
A1B5A N2  C12  sing N N 21  
A1B5A N3  H14  sing N N 22  
A1B5A N3  H15  sing N N 23  
A1B5A C5  H6   sing N N 24  
A1B5A C5  H7   sing N N 25  
A1B5A C7  H8   sing N N 26  
A1B5A C7  H9   sing N N 27  
A1B5A C8  H10  sing N N 28  
A1B5A C8  H11  sing N N 29  
A1B5A C10 H    sing N N 30  
A1B5A C9  H12  sing N N 31  
A1B5A C9  H13  sing N N 32  
A1B5A C12 H16  sing N N 33  
A1B5A C12 H17  sing N N 34  
A1B5A C   H1   sing N N 35  
A1B5A C   H3   sing N N 36  
A1B5A C   H2   sing N N 37  
A1B5A C3  H5   sing N N 38  
A1B5A C2  H4   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
GOL   C1  O1   sing N N 177 
GOL   C1  C2   sing N N 178 
GOL   C1  H11  sing N N 179 
GOL   C1  H12  sing N N 180 
GOL   O1  HO1  sing N N 181 
GOL   C2  O2   sing N N 182 
GOL   C2  C3   sing N N 183 
GOL   C2  H2   sing N N 184 
GOL   O2  HO2  sing N N 185 
GOL   C3  O3   sing N N 186 
GOL   C3  H31  sing N N 187 
GOL   C3  H32  sing N N 188 
GOL   O3  HO3  sing N N 189 
HIS   N   CA   sing N N 190 
HIS   N   H    sing N N 191 
HIS   N   H2   sing N N 192 
HIS   CA  C    sing N N 193 
HIS   CA  CB   sing N N 194 
HIS   CA  HA   sing N N 195 
HIS   C   O    doub N N 196 
HIS   C   OXT  sing N N 197 
HIS   CB  CG   sing N N 198 
HIS   CB  HB2  sing N N 199 
HIS   CB  HB3  sing N N 200 
HIS   CG  ND1  sing Y N 201 
HIS   CG  CD2  doub Y N 202 
HIS   ND1 CE1  doub Y N 203 
HIS   ND1 HD1  sing N N 204 
HIS   CD2 NE2  sing Y N 205 
HIS   CD2 HD2  sing N N 206 
HIS   CE1 NE2  sing Y N 207 
HIS   CE1 HE1  sing N N 208 
HIS   NE2 HE2  sing N N 209 
HIS   OXT HXT  sing N N 210 
HOH   O   H1   sing N N 211 
HOH   O   H2   sing N N 212 
ILE   N   CA   sing N N 213 
ILE   N   H    sing N N 214 
ILE   N   H2   sing N N 215 
ILE   CA  C    sing N N 216 
ILE   CA  CB   sing N N 217 
ILE   CA  HA   sing N N 218 
ILE   C   O    doub N N 219 
ILE   C   OXT  sing N N 220 
ILE   CB  CG1  sing N N 221 
ILE   CB  CG2  sing N N 222 
ILE   CB  HB   sing N N 223 
ILE   CG1 CD1  sing N N 224 
ILE   CG1 HG12 sing N N 225 
ILE   CG1 HG13 sing N N 226 
ILE   CG2 HG21 sing N N 227 
ILE   CG2 HG22 sing N N 228 
ILE   CG2 HG23 sing N N 229 
ILE   CD1 HD11 sing N N 230 
ILE   CD1 HD12 sing N N 231 
ILE   CD1 HD13 sing N N 232 
ILE   OXT HXT  sing N N 233 
LEU   N   CA   sing N N 234 
LEU   N   H    sing N N 235 
LEU   N   H2   sing N N 236 
LEU   CA  C    sing N N 237 
LEU   CA  CB   sing N N 238 
LEU   CA  HA   sing N N 239 
LEU   C   O    doub N N 240 
LEU   C   OXT  sing N N 241 
LEU   CB  CG   sing N N 242 
LEU   CB  HB2  sing N N 243 
LEU   CB  HB3  sing N N 244 
LEU   CG  CD1  sing N N 245 
LEU   CG  CD2  sing N N 246 
LEU   CG  HG   sing N N 247 
LEU   CD1 HD11 sing N N 248 
LEU   CD1 HD12 sing N N 249 
LEU   CD1 HD13 sing N N 250 
LEU   CD2 HD21 sing N N 251 
LEU   CD2 HD22 sing N N 252 
LEU   CD2 HD23 sing N N 253 
LEU   OXT HXT  sing N N 254 
LYS   N   CA   sing N N 255 
LYS   N   H    sing N N 256 
LYS   N   H2   sing N N 257 
LYS   CA  C    sing N N 258 
LYS   CA  CB   sing N N 259 
LYS   CA  HA   sing N N 260 
LYS   C   O    doub N N 261 
LYS   C   OXT  sing N N 262 
LYS   CB  CG   sing N N 263 
LYS   CB  HB2  sing N N 264 
LYS   CB  HB3  sing N N 265 
LYS   CG  CD   sing N N 266 
LYS   CG  HG2  sing N N 267 
LYS   CG  HG3  sing N N 268 
LYS   CD  CE   sing N N 269 
LYS   CD  HD2  sing N N 270 
LYS   CD  HD3  sing N N 271 
LYS   CE  NZ   sing N N 272 
LYS   CE  HE2  sing N N 273 
LYS   CE  HE3  sing N N 274 
LYS   NZ  HZ1  sing N N 275 
LYS   NZ  HZ2  sing N N 276 
LYS   NZ  HZ3  sing N N 277 
LYS   OXT HXT  sing N N 278 
MET   N   CA   sing N N 279 
MET   N   H    sing N N 280 
MET   N   H2   sing N N 281 
MET   CA  C    sing N N 282 
MET   CA  CB   sing N N 283 
MET   CA  HA   sing N N 284 
MET   C   O    doub N N 285 
MET   C   OXT  sing N N 286 
MET   CB  CG   sing N N 287 
MET   CB  HB2  sing N N 288 
MET   CB  HB3  sing N N 289 
MET   CG  SD   sing N N 290 
MET   CG  HG2  sing N N 291 
MET   CG  HG3  sing N N 292 
MET   SD  CE   sing N N 293 
MET   CE  HE1  sing N N 294 
MET   CE  HE2  sing N N 295 
MET   CE  HE3  sing N N 296 
MET   OXT HXT  sing N N 297 
PHE   N   CA   sing N N 298 
PHE   N   H    sing N N 299 
PHE   N   H2   sing N N 300 
PHE   CA  C    sing N N 301 
PHE   CA  CB   sing N N 302 
PHE   CA  HA   sing N N 303 
PHE   C   O    doub N N 304 
PHE   C   OXT  sing N N 305 
PHE   CB  CG   sing N N 306 
PHE   CB  HB2  sing N N 307 
PHE   CB  HB3  sing N N 308 
PHE   CG  CD1  doub Y N 309 
PHE   CG  CD2  sing Y N 310 
PHE   CD1 CE1  sing Y N 311 
PHE   CD1 HD1  sing N N 312 
PHE   CD2 CE2  doub Y N 313 
PHE   CD2 HD2  sing N N 314 
PHE   CE1 CZ   doub Y N 315 
PHE   CE1 HE1  sing N N 316 
PHE   CE2 CZ   sing Y N 317 
PHE   CE2 HE2  sing N N 318 
PHE   CZ  HZ   sing N N 319 
PHE   OXT HXT  sing N N 320 
PRO   N   CA   sing N N 321 
PRO   N   CD   sing N N 322 
PRO   N   H    sing N N 323 
PRO   CA  C    sing N N 324 
PRO   CA  CB   sing N N 325 
PRO   CA  HA   sing N N 326 
PRO   C   O    doub N N 327 
PRO   C   OXT  sing N N 328 
PRO   CB  CG   sing N N 329 
PRO   CB  HB2  sing N N 330 
PRO   CB  HB3  sing N N 331 
PRO   CG  CD   sing N N 332 
PRO   CG  HG2  sing N N 333 
PRO   CG  HG3  sing N N 334 
PRO   CD  HD2  sing N N 335 
PRO   CD  HD3  sing N N 336 
PRO   OXT HXT  sing N N 337 
SER   N   CA   sing N N 338 
SER   N   H    sing N N 339 
SER   N   H2   sing N N 340 
SER   CA  C    sing N N 341 
SER   CA  CB   sing N N 342 
SER   CA  HA   sing N N 343 
SER   C   O    doub N N 344 
SER   C   OXT  sing N N 345 
SER   CB  OG   sing N N 346 
SER   CB  HB2  sing N N 347 
SER   CB  HB3  sing N N 348 
SER   OG  HG   sing N N 349 
SER   OXT HXT  sing N N 350 
THR   N   CA   sing N N 351 
THR   N   H    sing N N 352 
THR   N   H2   sing N N 353 
THR   CA  C    sing N N 354 
THR   CA  CB   sing N N 355 
THR   CA  HA   sing N N 356 
THR   C   O    doub N N 357 
THR   C   OXT  sing N N 358 
THR   CB  OG1  sing N N 359 
THR   CB  CG2  sing N N 360 
THR   CB  HB   sing N N 361 
THR   OG1 HG1  sing N N 362 
THR   CG2 HG21 sing N N 363 
THR   CG2 HG22 sing N N 364 
THR   CG2 HG23 sing N N 365 
THR   OXT HXT  sing N N 366 
TRP   N   CA   sing N N 367 
TRP   N   H    sing N N 368 
TRP   N   H2   sing N N 369 
TRP   CA  C    sing N N 370 
TRP   CA  CB   sing N N 371 
TRP   CA  HA   sing N N 372 
TRP   C   O    doub N N 373 
TRP   C   OXT  sing N N 374 
TRP   CB  CG   sing N N 375 
TRP   CB  HB2  sing N N 376 
TRP   CB  HB3  sing N N 377 
TRP   CG  CD1  doub Y N 378 
TRP   CG  CD2  sing Y N 379 
TRP   CD1 NE1  sing Y N 380 
TRP   CD1 HD1  sing N N 381 
TRP   CD2 CE2  doub Y N 382 
TRP   CD2 CE3  sing Y N 383 
TRP   NE1 CE2  sing Y N 384 
TRP   NE1 HE1  sing N N 385 
TRP   CE2 CZ2  sing Y N 386 
TRP   CE3 CZ3  doub Y N 387 
TRP   CE3 HE3  sing N N 388 
TRP   CZ2 CH2  doub Y N 389 
TRP   CZ2 HZ2  sing N N 390 
TRP   CZ3 CH2  sing Y N 391 
TRP   CZ3 HZ3  sing N N 392 
TRP   CH2 HH2  sing N N 393 
TRP   OXT HXT  sing N N 394 
TYR   N   CA   sing N N 395 
TYR   N   H    sing N N 396 
TYR   N   H2   sing N N 397 
TYR   CA  C    sing N N 398 
TYR   CA  CB   sing N N 399 
TYR   CA  HA   sing N N 400 
TYR   C   O    doub N N 401 
TYR   C   OXT  sing N N 402 
TYR   CB  CG   sing N N 403 
TYR   CB  HB2  sing N N 404 
TYR   CB  HB3  sing N N 405 
TYR   CG  CD1  doub Y N 406 
TYR   CG  CD2  sing Y N 407 
TYR   CD1 CE1  sing Y N 408 
TYR   CD1 HD1  sing N N 409 
TYR   CD2 CE2  doub Y N 410 
TYR   CD2 HD2  sing N N 411 
TYR   CE1 CZ   doub Y N 412 
TYR   CE1 HE1  sing N N 413 
TYR   CE2 CZ   sing Y N 414 
TYR   CE2 HE2  sing N N 415 
TYR   CZ  OH   sing N N 416 
TYR   OH  HH   sing N N 417 
TYR   OXT HXT  sing N N 418 
VAL   N   CA   sing N N 419 
VAL   N   H    sing N N 420 
VAL   N   H2   sing N N 421 
VAL   CA  C    sing N N 422 
VAL   CA  CB   sing N N 423 
VAL   CA  HA   sing N N 424 
VAL   C   O    doub N N 425 
VAL   C   OXT  sing N N 426 
VAL   CB  CG1  sing N N 427 
VAL   CB  CG2  sing N N 428 
VAL   CB  HB   sing N N 429 
VAL   CG1 HG11 sing N N 430 
VAL   CG1 HG12 sing N N 431 
VAL   CG1 HG13 sing N N 432 
VAL   CG2 HG21 sing N N 433 
VAL   CG2 HG22 sing N N 434 
VAL   CG2 HG23 sing N N 435 
VAL   OXT HXT  sing N N 436 
# 
_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                    7I6U 
_atom_sites.fract_transf_matrix[1][1]   0.013787 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000701 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016228 
_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]   0.015358 
_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   ? 16.439 6.496   8.161  1.00 19.28 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.213 6.661   8.939  1.00 19.71 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.009 5.488   9.908  1.00 19.83 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.602 4.429   9.741  1.00 20.36 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 14.025 6.780   7.987  1.00 23.35 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.871 5.559   7.279  1.00 28.22 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.181 5.688   10.937 1.00 18.49 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.870 4.611   11.872 1.00 17.84 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.449 5.131   13.231 1.00 16.73 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.768 6.273   13.572 1.00 17.38 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.711 4.318   14.002 1.00 15.48 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.293 4.760   15.329 1.00 16.33 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.242 3.557   16.271 1.00 16.25 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.135 2.404   15.805 1.00 16.23 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.892 5.384   15.250 1.00 17.20 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.264 3.828   17.602 1.00 14.48 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.021 2.815   18.612 1.00 13.56 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.595 3.034   19.085 1.00 15.07 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.238 4.166   19.426 1.00 15.79 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 12.973 2.993   19.814 1.00 13.97 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.453 2.935   19.315 1.00 14.08 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.730 1.905   20.861 1.00 15.57 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.432 3.472   20.410 1.00 16.93 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.794  1.964   19.170 1.00 14.75 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.424  2.088   19.693 1.00 16.22 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.350  1.314   20.983 1.00 16.27 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.413  0.086   20.935 1.00 17.42 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.410  1.508   18.685 1.00 17.64 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.315  2.340   17.440 1.00 19.60 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.443  3.419   17.368 1.00 22.24 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.124  2.078   16.348 1.00 21.68 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.383  4.215   16.235 1.00 23.70 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.082  2.869   15.219 1.00 23.45 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.208  3.931   15.163 1.00 24.88 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.199  4.724   14.046 1.00 27.25 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.250  1.995   22.143 1.00 16.35 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.203  1.333   23.455 1.00 17.75 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.082  1.912   24.281 1.00 18.85 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 6.961  3.122   24.412 1.00 19.35 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.561  1.438   24.202 1.00 19.83 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.051 2.892   24.252 1.00 20.30 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.441  0.871   25.626 1.00 22.50 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.191  1.053   24.795 1.00 19.87 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.024  1.515   25.540 1.00 20.00 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.214  2.480   24.687 1.00 20.22 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.006  2.205   23.521 1.00 20.55 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 3.886  3.666   25.203 1.00 20.30 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.190  4.684   24.402 1.00 21.39 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.142  5.790   23.939 1.00 19.47 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.748  6.959   23.839 1.00 19.64 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.004  5.272   25.153 1.00 23.70 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 0.915  4.258   25.375 1.00 31.91 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.281  3.779   24.430 1.00 35.48 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.693  3.910   26.620 1.00 34.10 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.393  5.424   23.661 1.00 17.74 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.397  6.387   23.219 1.00 16.91 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.010  5.945   21.879 1.00 15.97 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.148  4.739   21.613 1.00 16.10 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.550  6.456   24.239 1.00 17.45 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.149  7.009   25.594 1.00 18.50 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.511  8.235   25.707 1.00 20.08 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.401  6.301   26.759 1.00 20.01 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.141  8.752   26.949 1.00 21.23 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.022  6.796   28.002 1.00 20.74 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.395  8.030   28.093 1.00 22.20 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.052  8.556   29.317 1.00 23.75 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.472  6.931   21.083 1.00 14.86 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.200  6.740   19.831 1.00 14.75 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.521  7.548   20.000 1.00 15.49 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.463  8.743   20.297 1.00 16.68 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.360  7.255   18.646 1.00 16.36 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.136  7.489   17.362 1.00 18.34 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.207  7.844   16.214 1.00 19.78 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.781  8.866   15.340 1.00 22.13 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.160  8.651   14.084 1.00 24.94 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.039  7.440   13.543 1.00 24.96 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.665  9.641   13.357 1.00 22.95 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.678 6.904   19.824 1.00 14.23 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 11.986 7.548   19.975 1.00 14.23 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.571 7.711   18.591 1.00 14.12 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.734 6.709   17.869 1.00 14.36 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 12.953 6.719   20.873 1.00 15.58 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.240 7.522   21.145 1.00 16.09 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.295 6.301   22.186 1.00 15.14 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.915 8.933   18.204 1.00 12.56 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.484 9.185   16.869 1.00 13.86 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.709 10.093  16.972 1.00 14.04 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.924 10.773  17.995 1.00 13.96 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.444 9.840   15.919 1.00 15.75 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.292 8.896   15.657 1.00 17.91 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.928 11.158  16.508 1.00 17.06 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.497 10.194  15.879 1.00 12.73 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.553 11.207  15.834 1.00 12.71 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.855 12.574  15.830 1.00 13.65 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.905 12.782  15.053 1.00 14.07 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.331 11.076  14.527 1.00 12.92 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.107 9.792   14.455 1.00 15.04 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.621 8.786   13.902 1.00 16.07 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.332 9.807   14.980 1.00 16.78 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.294 13.489  16.692 1.00 13.12 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.662 14.810  16.758 1.00 12.91 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.693 15.529  15.386 1.00 13.76 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.682 16.117  14.998 1.00 14.97 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.333 15.635  17.863 1.00 14.35 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.582 16.947  18.198 1.00 14.99 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.518 17.810  19.022 1.00 15.30 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.899 19.050  19.529 1.00 16.57 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.857 20.198  18.858 1.00 17.84 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.328 20.268  17.619 1.00 17.45 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.353 21.295  19.432 1.00 16.82 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.794 15.371  14.623 1.00 13.69 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.907 16.040  13.322 1.00 14.54 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.957 15.481  12.259 1.00 15.96 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.786 16.128  11.221 1.00 18.32 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.375 16.096  12.824 1.00 15.19 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.959 14.801  12.321 1.00 15.68 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.514 13.865  13.187 1.00 16.00 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 19.149 14.384  11.046 1.00 17.24 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.985 12.887  12.411 1.00 16.79 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.773 13.158  11.111 1.00 17.51 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.374 14.285  12.496 1.00 15.64 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.415 13.660  11.566 1.00 16.68 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.983 13.664  12.105 1.00 17.80 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 12.099 13.083  11.453 1.00 18.84 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.862 12.227  11.264 1.00 16.15 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.261 12.104  10.634 1.00 17.69 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.606 10.626  10.395 1.00 17.27 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.338 12.897  9.292  1.00 18.02 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.724 14.328  13.261 1.00 16.58 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.360 14.314  13.819 1.00 16.37 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.373 15.003  12.879 1.00 16.85 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.731 15.954  12.199 1.00 16.75 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.341 14.962  15.186 1.00 16.38 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.162  14.484  12.811 1.00 18.29 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.139  15.011  11.914 1.00 19.81 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.324  16.098  12.604 1.00 20.76 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.414  16.276  13.822 1.00 20.52 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.208  13.850  11.462 1.00 21.40 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.458  13.371  12.584 1.00 22.65 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.954  12.702  10.811 1.00 21.37 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.411  16.782  11.849 1.00 21.19 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.491  17.757  12.458 1.00 23.50 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.632  17.032  13.547 1.00 21.84 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.380  17.593  14.621 1.00 22.73 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.561  18.380  11.372 1.00 28.10 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.250  19.276  10.377 1.00 36.40 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.406  20.643  10.598 1.00 40.65 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 5.741  18.978  9.154  1.00 39.39 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.041  21.103  9.531  1.00 41.76 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 6.263  20.137  8.637  1.00 41.65 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.230  15.751  13.277 1.00 21.70 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.440  14.985  14.245 1.00 21.55 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.229  14.665  15.520 1.00 20.01 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.681  14.731  16.624 1.00 20.88 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.852  13.706  13.634 1.00 24.16 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.551  13.917  12.899 1.00 30.25 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.665  14.660  13.342 1.00 30.77 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.434  13.300  11.745 1.00 31.95 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.536  14.363  15.396 1.00 17.52 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.371  14.134  16.593 1.00 16.91 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.392  15.401  17.461 1.00 17.65 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.250  15.313  18.681 1.00 18.60 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.805  13.782  16.174 1.00 15.95 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.965  12.378  15.640 1.00 19.67 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.391  11.436  16.250 1.00 20.17 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.646  12.214  14.587 1.00 20.53 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.625  16.566  16.832 1.00 17.60 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.665  17.822  17.597 1.00 17.86 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.319  18.203  18.202 1.00 20.24 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.278  18.739  19.311 1.00 21.54 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.223  18.961  16.727 1.00 18.03 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.733  18.943  16.636 1.00 19.01 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.489  18.503  15.595 1.00 20.62 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.653  19.458  17.610 1.00 19.20 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.838 18.701  15.869 1.00 20.91 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.957 19.267  17.106 1.00 20.30 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.500  20.006  18.888 1.00 19.92 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.102 19.665  17.816 1.00 19.81 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.637 20.400  19.586 1.00 20.19 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.914 20.187  19.068 1.00 20.02 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.217  17.862  17.528 1.00 20.91 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.869  18.143  18.052 1.00 22.59 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.483  17.216  19.238 1.00 23.04 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.527  17.497  19.987 1.00 24.29 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.850  17.991  16.933 1.00 23.41 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.174  16.085  19.371 1.00 20.75 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 2.954  15.127  20.458 1.00 20.63 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.244  14.981  21.301 1.00 19.34 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.537  13.917  21.830 1.00 17.90 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.513  13.782  19.867 1.00 22.39 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.161  13.888  19.199 1.00 25.25 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.131  13.911  19.867 1.00 27.68 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.141  13.977  17.881 1.00 25.81 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 4.995  16.076  21.438 1.00 18.89 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.298  16.053  22.120 1.00 19.20 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.227  15.649  23.610 1.00 19.53 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.411  16.178  24.366 1.00 20.19 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 6.890  17.445  22.012 1.00 20.06 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.256  17.660  22.680 1.00 21.17 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.332  16.785  22.016 1.00 21.63 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.660  19.142  22.594 1.00 21.86 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.113  14.739  24.027 1.00 19.16 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.267  14.352  25.429 1.00 19.60 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.565  14.944  25.973 1.00 20.37 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.596  15.567  27.047 1.00 21.85 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.247  12.801  25.547 1.00 21.71 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.582  12.338  26.967 1.00 22.85 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 5.877  12.264  25.127 1.00 23.01 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.646  14.818  25.189 1.00 18.70 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 10.965 15.287  25.620 1.00 19.37 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 11.878 15.351  24.412 1.00 18.35 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.768 14.526  23.498 1.00 18.12 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.550 14.273  26.653 1.00 19.88 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.016 14.429  26.992 1.00 20.92 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.569 15.268  27.915 1.00 22.44 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.104 13.679  26.431 1.00 20.43 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 14.944 15.109  27.940 1.00 23.08 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.293 14.130  27.047 1.00 21.54 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.188 12.681  25.466 1.00 20.31 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.548 13.592  26.739 1.00 22.16 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.430 12.169  25.147 1.00 21.03 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.592 12.614  25.791 1.00 21.29 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.789 16.317  24.413 1.00 18.17 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.808 16.363  23.350 1.00 18.00 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.105 16.942  23.892 1.00 17.47 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.100 17.696  24.865 1.00 17.80 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.317 17.101  22.092 1.00 18.80 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.764 18.513  22.334 1.00 19.74 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.765 19.621  22.632 1.00 21.58 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.431 20.523  23.439 1.00 24.66 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.889 19.591  22.091 1.00 19.09 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.232 16.583  23.269 1.00 17.82 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.526 17.099  23.703 1.00 17.24 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.411 17.253  22.468 1.00 17.09 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.853 16.240  21.902 1.00 17.00 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.144 16.174  24.747 1.00 19.44 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.400 16.724  25.405 1.00 23.96 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.075 17.593  24.785 1.00 24.36 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.711 16.290  26.517 1.00 25.33 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.639 18.503  22.009 1.00 17.06 ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 19.473 18.717  20.828 1.00 17.99 ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 20.900 18.234  21.059 1.00 17.09 ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 21.551 17.792  20.106 1.00 17.04 ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 19.481 20.198  20.407 1.00 21.96 ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 20.068 21.018  21.399 1.00 27.43 ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 21.401 18.278  22.316 1.00 15.96 ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 22.760 17.802  22.575 1.00 17.69 ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 22.884 16.288  22.402 1.00 16.74 ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 23.988 15.815  22.257 1.00 17.73 ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 23.285 18.234  23.944 1.00 22.01 ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 22.716 17.442  24.970 1.00 27.68 ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 21.766 15.531  22.432 1.00 15.04 ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 21.830 14.067  22.256 1.00 14.80 ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 21.282 13.620  20.874 1.00 14.30 ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 21.310 12.420  20.565 1.00 13.85 ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 20.971 13.385  23.352 1.00 15.20 ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 21.530 13.622  24.748 1.00 15.85 ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 20.718 12.947  25.856 1.00 16.68 ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 20.667 11.480  25.736 1.00 17.88 ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 20.449 10.655  26.758 1.00 17.60 ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 20.295 11.137  27.997 1.00 18.13 ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 20.459 9.339   26.570 1.00 17.48 ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 20.739 14.574  20.078 1.00 13.97 ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 20.036 14.264  18.824 1.00 12.58 ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 18.847 13.310  19.081 1.00 14.24 ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 18.568 12.469  18.226 1.00 13.96 ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 20.973 13.681  17.751 1.00 14.46 ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 20.300 13.450  16.405 1.00 16.11 ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 19.512 14.334  15.968 1.00 15.05 ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 20.595 12.397  15.761 1.00 15.03 ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 18.127 13.452  20.220 1.00 13.76 ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 16.965 12.592  20.473 1.00 13.88 ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 15.689 13.370  20.667 1.00 14.02 ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 15.705 14.470  21.213 1.00 15.08 ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.155 11.761  21.770 1.00 14.16 ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 18.192 10.627  21.721 1.00 15.53 ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 18.214 9.896   23.098 1.00 15.47 ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 17.857 9.627   20.615 1.00 14.66 ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 14.573 12.769  20.269 1.00 12.57 ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 13.252 13.327  20.520 1.00 13.42 ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 12.335 12.147  20.777 1.00 14.22 ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 12.442 11.108  20.110 1.00 15.13 ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 12.772 14.142  19.319 1.00 13.19 ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 11.374 14.814  19.506 1.00 14.97 ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 11.315 16.124  18.741 1.00 17.24 ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 10.223 13.892  19.022 1.00 15.73 ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 11.466 12.285  21.767 1.00 13.23 ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 10.471 11.251  22.105 1.00 13.86 ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 9.090  11.884  22.010 1.00 14.53 ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 8.860  12.972  22.560 1.00 16.48 ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 10.703 10.725  23.543 1.00 15.36 ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 9.594  9.719   23.935 1.00 16.22 ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 12.092 10.081  23.644 1.00 15.27 ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 8.180  11.226  21.292 1.00 14.90 ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 6.797  11.682  21.141 1.00 15.73 ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 5.828  10.611  21.674 1.00 18.16 ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 6.206  9.448   21.860 1.00 17.18 ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 6.484  12.013  19.678 1.00 16.53 ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 6.675  10.900  18.813 1.00 19.50 ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 4.570  11.016  21.927 1.00 18.60 ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 3.581  10.054  22.444 1.00 20.40 ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 2.794  9.380   21.317 1.00 21.66 ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 2.596  9.960   20.254 1.00 21.77 ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 2.661  10.736  23.444 1.00 23.42 ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 2.015  11.803  22.787 1.00 27.11 ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 2.412  8.113   21.522 1.00 22.95 ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 1.652  7.337   20.538 1.00 26.00 ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 0.351  6.816   21.171 1.00 29.13 ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 0.245  6.731   22.398 1.00 28.71 ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 2.485  6.135   20.025 1.00 27.28 ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 2.569  5.159   21.059 1.00 28.06 ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 3.862  6.518   19.576 1.00 26.90 ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? -0.613 6.429   20.340 1.00 32.14 ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? -1.869 5.858   20.834 1.00 35.15 ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? -1.783 4.322   20.905 1.00 36.36 ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? -2.479 3.699   21.715 1.00 37.76 ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? -3.048 6.286   19.945 1.00 38.59 ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? -2.698 6.029   18.580 1.00 40.70 ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? -3.404 7.750   20.114 1.00 39.57 ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? -0.967 3.705   20.048 1.00 35.56 ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? -0.837 2.253   20.021 1.00 34.82 ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 0.347  1.789   20.884 1.00 34.17 ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 1.307  2.532   21.079 1.00 33.83 ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? -0.665 1.776   18.584 1.00 34.85 ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 0.275  0.566   21.396 1.00 33.52 ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 1.350  0.018   22.226 1.00 33.40 ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 2.527  -0.382  21.350 1.00 31.66 ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 2.315  -1.002  20.311 1.00 32.58 ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 0.843  -1.201  23.006 1.00 36.80 ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 1.885  -1.802  23.948 1.00 43.42 ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 1.952  -1.096  25.292 1.00 51.86 ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 1.220  -0.134  25.587 1.00 53.67 ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 2.828  -1.582  26.157 1.00 54.17 ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 3.741  0.003   21.766 1.00 28.88 ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 4.987  -0.276  21.072 1.00 27.41 ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 5.379  -1.731  20.985 1.00 26.35 ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 4.874  -2.544  21.737 1.00 26.91 ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 6.305  -2.057  20.063 1.00 24.27 ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 6.783  -3.408  19.811 1.00 23.00 ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 8.139  -3.727  20.482 1.00 21.16 ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 8.476  -4.901  20.622 1.00 20.89 ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 6.856  -3.654  18.300 1.00 23.83 ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 7.913  -2.485  17.375 1.00 26.78 ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 8.869  -2.717  20.945 1.00 19.52 ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 10.256 -2.863  21.429 1.00 19.23 ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 10.427 -2.891  22.945 1.00 19.49 ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 9.549  -2.405  23.670 1.00 20.54 ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 11.083 -1.688  20.853 1.00 19.79 ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 11.262 -1.715  19.338 1.00 24.27 ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 11.713 -2.768  18.814 1.00 23.76 ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 11.005 -0.658  18.669 1.00 22.29 ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 11.556 -3.434  23.430 1.00 18.83 ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 11.958 -3.396  24.823 1.00 20.09 ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 13.407 -2.799  24.901 1.00 18.10 ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 14.190 -2.908  23.943 1.00 18.11 ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 11.797 -4.754  25.485 1.00 23.42 ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 12.736 -5.644  24.902 1.00 25.47 ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 10.371 -5.332  25.344 1.00 25.35 ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 13.721 -2.088  26.009 1.00 16.59 ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 14.982 -1.355  26.148 1.00 15.28 ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 15.946 -2.091  27.050 1.00 16.16 ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 15.561 -2.577  28.121 1.00 17.02 ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 14.716 0.070   26.764 1.00 15.50 ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 13.583 0.830   26.025 1.00 17.41 ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 16.005 0.921   26.768 1.00 16.41 ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 13.905 1.004   24.499 1.00 17.74 ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 17.196 -2.190  26.613 1.00 15.24 ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 18.255 -2.809  27.399 1.00 14.82 ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 18.574 -1.925  28.594 1.00 16.24 ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 18.583 -0.709  28.468 1.00 16.61 ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 19.523 -2.939  26.547 1.00 14.43 ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 18.887 -2.540  29.748 1.00 16.25 ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 19.289 -1.766  30.937 1.00 16.17 ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 20.571 -2.505  31.364 1.00 17.94 ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 20.520 -3.477  32.128 1.00 18.68 ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 18.212 -1.823  32.025 1.00 16.31 ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 16.869 -1.276  31.532 1.00 16.76 ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 16.895 0.226   31.212 1.00 17.92 ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 15.557 0.697   30.820 1.00 17.56 ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 15.317 1.849   30.195 1.00 19.26 ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 16.316 2.657   29.872 1.00 17.94 ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 14.077 2.179   29.852 1.00 19.88 ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 21.694 -2.130  30.754 1.00 17.96 ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 22.931 -2.897  30.887 1.00 19.03 ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 24.147 -2.036  30.539 1.00 19.50 ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 23.998 -0.877  30.140 1.00 19.44 ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 22.851 -4.076  29.927 1.00 18.70 ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 22.887 -3.587  28.181 1.00 17.56 ? 56  CYS   A SG  1 
ATOM   389  N  N   . ASP   A 1 51  ? 25.369 -2.658  30.630 1.00 20.58 ? 57  ASP   A N   1 
ATOM   390  C  CA  . ASP   A 1 51  ? 26.594 -1.983  30.224 1.00 21.06 ? 57  ASP   A CA  1 
ATOM   391  C  C   . ASP   A 1 51  ? 27.249 -2.705  29.053 1.00 20.88 ? 57  ASP   A C   1 
ATOM   392  O  O   . ASP   A 1 51  ? 28.467 -2.613  28.896 1.00 20.89 ? 57  ASP   A O   1 
ATOM   393  C  CB  . ASP   A 1 51  ? 27.603 -1.895  31.392 1.00 24.40 ? 57  ASP   A CB  1 
ATOM   394  C  CG  . ASP   A 1 51  ? 28.013 -3.225  31.997 1.00 30.51 ? 57  ASP   A CG  1 
ATOM   395  O  OD1 . ASP   A 1 51  ? 27.571 -4.272  31.498 1.00 29.66 ? 57  ASP   A OD1 1 
ATOM   396  O  OD2 . ASP   A 1 51  ? 28.796 -3.217  32.974 1.00 38.23 ? 57  ASP   A OD2 1 
ATOM   397  N  N   . CYS   A 1 52  ? 26.463 -3.383  28.173 1.00 19.12 ? 58  CYS   A N   1 
ATOM   398  C  CA  . CYS   A 1 52  ? 27.070 -4.046  26.997 1.00 17.65 ? 58  CYS   A CA  1 
ATOM   399  C  C   . CYS   A 1 52  ? 27.826 -3.060  26.136 1.00 17.22 ? 58  CYS   A C   1 
ATOM   400  O  O   . CYS   A 1 52  ? 27.390 -1.914  25.955 1.00 17.05 ? 58  CYS   A O   1 
ATOM   401  C  CB  . CYS   A 1 52  ? 25.999 -4.735  26.152 1.00 17.08 ? 58  CYS   A CB  1 
ATOM   402  S  SG  . CYS   A 1 52  ? 25.322 -6.254  26.882 1.00 19.53 ? 58  CYS   A SG  1 
ATOM   403  N  N   . GLN   A 1 53  ? 28.935 -3.500  25.563 1.00 16.16 ? 59  GLN   A N   1 
ATOM   404  C  CA  . GLN   A 1 53  ? 29.706 -2.714  24.601 1.00 16.14 ? 59  GLN   A CA  1 
ATOM   405  C  C   . GLN   A 1 53  ? 29.866 -3.498  23.275 1.00 15.25 ? 59  GLN   A C   1 
ATOM   406  O  O   . GLN   A 1 53  ? 30.737 -3.165  22.481 1.00 15.87 ? 59  GLN   A O   1 
ATOM   407  C  CB  . GLN   A 1 53  ? 31.099 -2.345  25.124 1.00 18.49 ? 59  GLN   A CB  1 
ATOM   408  C  CG  . GLN   A 1 53  ? 31.052 -1.173  26.064 1.00 23.56 ? 59  GLN   A CG  1 
ATOM   409  C  CD  . GLN   A 1 53  ? 32.470 -0.820  26.486 1.00 27.12 ? 59  GLN   A CD  1 
ATOM   410  O  OE1 . GLN   A 1 53  ? 32.854 -1.031  27.638 1.00 28.23 ? 59  GLN   A OE1 1 
ATOM   411  N  NE2 . GLN   A 1 53  ? 33.287 -0.273  25.552 1.00 25.65 ? 59  GLN   A NE2 1 
ATOM   412  N  N   . THR   A 1 54  ? 29.042 -4.556  23.049 1.00 14.61 ? 60  THR   A N   1 
ATOM   413  C  CA  . THR   A 1 54  ? 28.963 -5.264  21.785 1.00 15.35 ? 60  THR   A CA  1 
ATOM   414  C  C   . THR   A 1 54  ? 27.467 -5.438  21.468 1.00 14.48 ? 60  THR   A C   1 
ATOM   415  O  O   . THR   A 1 54  ? 26.608 -5.527  22.383 1.00 15.47 ? 60  THR   A O   1 
ATOM   416  C  CB  . THR   A 1 54  ? 29.709 -6.605  21.778 1.00 16.66 ? 60  THR   A CB  1 
ATOM   417  O  OG1 . THR   A 1 54  ? 29.027 -7.506  22.662 1.00 19.21 ? 60  THR   A OG1 1 
ATOM   418  C  CG2 . THR   A 1 54  ? 31.148 -6.469  22.179 1.00 17.13 ? 60  THR   A CG2 1 
ATOM   419  N  N   . GLY   A 1 55  ? 27.171 -5.506  20.187 1.00 13.36 ? 61  GLY   A N   1 
ATOM   420  C  CA  . GLY   A 1 55  ? 25.781 -5.671  19.759 1.00 12.95 ? 61  GLY   A CA  1 
ATOM   421  C  C   . GLY   A 1 55  ? 25.718 -5.744  18.252 1.00 12.92 ? 61  GLY   A C   1 
ATOM   422  O  O   . GLY   A 1 55  ? 26.731 -5.991  17.580 1.00 14.46 ? 61  GLY   A O   1 
ATOM   423  N  N   . VAL   A 1 56  ? 24.518 -5.588  17.733 1.00 12.90 ? 62  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 56  ? 24.264 -5.695  16.302 1.00 13.15 ? 62  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 56  ? 23.389 -4.514  15.891 1.00 13.44 ? 62  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 56  ? 22.386 -4.227  16.553 1.00 13.92 ? 62  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 56  ? 23.561 -7.032  15.959 1.00 15.50 ? 62  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 56  ? 23.227 -7.089  14.461 1.00 16.93 ? 62  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 56  ? 24.450 -8.223  16.335 1.00 17.36 ? 62  VAL   A CG2 1 
ATOM   430  N  N   . TYR   A 1 57  ? 23.753 -3.847  14.779 1.00 12.50 ? 63  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 57  ? 22.927 -2.731  14.303 1.00 12.26 ? 63  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 57  ? 22.415 -2.960  12.898 1.00 12.85 ? 63  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 57  ? 23.030 -3.696  12.122 1.00 13.72 ? 63  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 57  ? 23.654 -1.349  14.413 1.00 12.17 ? 63  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 57  ? 24.692 -1.081  13.325 1.00 12.74 ? 63  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 57  ? 25.947 -1.672  13.373 1.00 13.26 ? 63  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 57  ? 24.450 -0.164  12.309 1.00 13.39 ? 63  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 57  ? 26.900 -1.422  12.386 1.00 13.73 ? 63  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 57  ? 25.402 0.090   11.311 1.00 14.14 ? 63  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 57  ? 26.626 -0.539  11.363 1.00 15.25 ? 63  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 57  ? 27.624 -0.338  10.419 1.00 16.91 ? 63  TYR   A OH  1 
ATOM   442  N  N   . TYR   A 1 58  ? 21.296 -2.308  12.565 1.00 13.08 ? 64  TYR   A N   1 
ATOM   443  C  CA  . TYR   A 1 58  ? 20.756 -2.394  11.221 1.00 13.29 ? 64  TYR   A CA  1 
ATOM   444  C  C   . TYR   A 1 58  ? 21.295 -1.237  10.377 1.00 13.99 ? 64  TYR   A C   1 
ATOM   445  O  O   . TYR   A 1 58  ? 21.180 -0.066  10.786 1.00 13.80 ? 64  TYR   A O   1 
ATOM   446  C  CB  . TYR   A 1 58  ? 19.205 -2.364  11.254 1.00 13.94 ? 64  TYR   A CB  1 
ATOM   447  C  CG  . TYR   A 1 58  ? 18.652 -2.487  9.861  1.00 15.14 ? 64  TYR   A CG  1 
ATOM   448  C  CD1 . TYR   A 1 58  ? 18.845 -3.647  9.119  1.00 15.98 ? 64  TYR   A CD1 1 
ATOM   449  C  CD2 . TYR   A 1 58  ? 18.047 -1.402  9.235  1.00 15.85 ? 64  TYR   A CD2 1 
ATOM   450  C  CE1 . TYR   A 1 58  ? 18.392 -3.749  7.812  1.00 17.57 ? 64  TYR   A CE1 1 
ATOM   451  C  CE2 . TYR   A 1 58  ? 17.572 -1.499  7.933  1.00 17.00 ? 64  TYR   A CE2 1 
ATOM   452  C  CZ  . TYR   A 1 58  ? 17.766 -2.668  7.229  1.00 18.61 ? 64  TYR   A CZ  1 
ATOM   453  O  OH  . TYR   A 1 58  ? 17.300 -2.775  5.950  1.00 22.25 ? 64  TYR   A OH  1 
ATOM   454  N  N   . CYS   A 1 59  ? 21.853 -1.556  9.197  1.00 13.33 ? 65  CYS   A N   1 
ATOM   455  C  CA  . CYS   A 1 59  ? 22.442 -0.567  8.291  1.00 12.58 ? 65  CYS   A CA  1 
ATOM   456  C  C   . CYS   A 1 59  ? 21.561 -0.510  7.026  1.00 14.15 ? 65  CYS   A C   1 
ATOM   457  O  O   . CYS   A 1 59  ? 21.643 -1.391  6.164  1.00 14.93 ? 65  CYS   A O   1 
ATOM   458  C  CB  . CYS   A 1 59  ? 23.871 -0.976  7.956  1.00 13.65 ? 65  CYS   A CB  1 
ATOM   459  S  SG  . CYS   A 1 59  ? 24.655 0.093   6.708  1.00 16.97 ? 65  CYS   A SG  1 
ATOM   460  N  N   . SER   A 1 60  ? 20.697 0.508   6.935  1.00 13.83 ? 66  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 60  ? 19.746 0.579   5.818  1.00 14.77 ? 66  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 60  ? 20.418 0.745   4.448  1.00 15.36 ? 66  SER   A C   1 
ATOM   463  O  O   . SER   A 1 60  ? 19.917 0.193   3.448  1.00 16.49 ? 66  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 60  ? 18.716 1.679   6.040  1.00 19.64 ? 66  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 60  ? 19.327 2.941   6.167  1.00 25.81 ? 66  SER   A OG  1 
ATOM   466  N  N   . SER   A 1 61  ? 21.598 1.396   4.405  1.00 14.69 ? 67  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 61  ? 22.347 1.566   3.142  1.00 14.81 ? 67  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 61  ? 22.989 0.290   2.619  1.00 14.93 ? 67  SER   A C   1 
ATOM   469  O  O   . SER   A 1 61  ? 23.517 0.298   1.495  1.00 16.45 ? 67  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 61  ? 23.397 2.655   3.247  1.00 16.05 ? 67  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 61  ? 24.398 2.308   4.202  1.00 16.57 ? 67  SER   A OG  1 
ATOM   472  N  N   . ARG   A 1 62  ? 22.913 -0.813  3.386  1.00 14.03 ? 68  ARG   A N   1 
ATOM   473  C  CA  . ARG   A 1 62  ? 23.382 -2.110  2.944  1.00 15.13 ? 68  ARG   A CA  1 
ATOM   474  C  C   . ARG   A 1 62  ? 22.250 -3.166  3.097  1.00 16.86 ? 68  ARG   A C   1 
ATOM   475  O  O   . ARG   A 1 62  ? 22.498 -4.333  2.779  1.00 18.18 ? 68  ARG   A O   1 
ATOM   476  C  CB  . ARG   A 1 62  ? 24.605 -2.542  3.795  1.00 16.53 ? 68  ARG   A CB  1 
ATOM   477  C  CG  . ARG   A 1 62  ? 25.858 -1.702  3.549  1.00 17.37 ? 68  ARG   A CG  1 
ATOM   478  C  CD  . ARG   A 1 62  ? 26.433 -1.985  2.158  1.00 18.39 ? 68  ARG   A CD  1 
ATOM   479  N  NE  . ARG   A 1 62  ? 27.621 -1.169  1.859  1.00 19.30 ? 68  ARG   A NE  1 
ATOM   480  C  CZ  . ARG   A 1 62  ? 27.583 0.034   1.303  1.00 20.17 ? 68  ARG   A CZ  1 
ATOM   481  N  NH1 . ARG   A 1 62  ? 26.423 0.571   0.946  1.00 19.79 ? 68  ARG   A NH1 1 
ATOM   482  N  NH2 . ARG   A 1 62  ? 28.711 0.711   1.084  1.00 20.94 ? 68  ARG   A NH2 1 
ATOM   483  N  N   . ARG   A 1 63  ? 21.030 -2.773  3.599  1.00 17.03 ? 69  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 63  ? 19.943 -3.710  3.888  1.00 18.55 ? 69  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 63  ? 20.445 -4.912  4.713  1.00 18.90 ? 69  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 63  ? 20.145 -6.073  4.381  1.00 20.23 ? 69  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 63  ? 19.309 -4.207  2.568  1.00 21.70 ? 69  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 63  ? 18.232 -3.314  2.125  1.00 28.34 ? 69  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 63  ? 17.304 -4.069  1.168  1.00 30.68 ? 69  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 63  ? 16.694 -3.106  0.284  1.00 32.04 ? 69  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 63  ? 16.995 -2.972  -1.001 1.00 31.93 ? 69  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 63  ? 17.833 -3.830  -1.592 1.00 32.34 ? 69  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 63  ? 16.460 -1.992  -1.710 1.00 29.56 ? 69  ARG   A NH2 1 
ATOM   494  N  N   . LYS   A 1 64  ? 21.312 -4.647  5.692  1.00 16.99 ? 70  LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 64  ? 21.941 -5.744  6.437  1.00 17.27 ? 70  LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 64  ? 22.227 -5.333  7.872  1.00 15.58 ? 70  LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 64  ? 22.378 -4.142  8.173  1.00 15.84 ? 70  LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 64  ? 23.329 -6.071  5.804  1.00 21.09 ? 70  LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 64  ? 23.364 -7.154  4.749  1.00 30.88 ? 70  LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 64  ? 24.834 -7.344  4.345  1.00 37.99 ? 70  LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 64  ? 25.021 -8.268  3.165  1.00 45.04 ? 70  LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 64  ? 26.290 -7.958  2.458  1.00 49.44 ? 70  LYS   A NZ  1 
ATOM   503  N  N   . HIS   A 1 65  ? 22.346 -6.337  8.743  1.00 14.73 ? 71  HIS   A N   1 
ATOM   504  C  CA  . HIS   A 1 65  ? 22.760 -6.099  10.120 1.00 14.59 ? 71  HIS   A CA  1 
ATOM   505  C  C   . HIS   A 1 65  ? 24.255 -6.432  10.239 1.00 15.49 ? 71  HIS   A C   1 
ATOM   506  O  O   . HIS   A 1 65  ? 24.773 -7.373  9.578  1.00 16.95 ? 71  HIS   A O   1 
ATOM   507  C  CB  . HIS   A 1 65  ? 21.981 -7.028  11.069 1.00 14.90 ? 71  HIS   A CB  1 
ATOM   508  C  CG  . HIS   A 1 65  ? 20.492 -6.836  11.065 1.00 15.72 ? 71  HIS   A CG  1 
ATOM   509  N  ND1 . HIS   A 1 65  ? 19.847 -6.116  12.048 1.00 18.71 ? 71  HIS   A ND1 1 
ATOM   510  C  CD2 . HIS   A 1 65  ? 19.573 -7.331  10.220 1.00 16.24 ? 71  HIS   A CD2 1 
ATOM   511  C  CE1 . HIS   A 1 65  ? 18.558 -6.170  11.749 1.00 17.08 ? 71  HIS   A CE1 1 
ATOM   512  N  NE2 . HIS   A 1 65  ? 18.347 -6.883  10.658 1.00 19.68 ? 71  HIS   A NE2 1 
ATOM   513  N  N   . TYR   A 1 66  ? 24.967 -5.673  11.082 1.00 14.31 ? 72  TYR   A N   1 
ATOM   514  C  CA  . TYR   A 1 66  ? 26.398 -5.896  11.288 1.00 14.24 ? 72  TYR   A CA  1 
ATOM   515  C  C   . TYR   A 1 66  ? 26.706 -5.945  12.780 1.00 13.89 ? 72  TYR   A C   1 
ATOM   516  O  O   . TYR   A 1 66  ? 26.126 -5.182  13.568 1.00 14.24 ? 72  TYR   A O   1 
ATOM   517  C  CB  . TYR   A 1 66  ? 27.231 -4.711  10.701 1.00 15.06 ? 72  TYR   A CB  1 
ATOM   518  C  CG  . TYR   A 1 66  ? 27.242 -4.627  9.184  1.00 16.78 ? 72  TYR   A CG  1 
ATOM   519  C  CD1 . TYR   A 1 66  ? 28.005 -5.504  8.420  1.00 18.43 ? 72  TYR   A CD1 1 
ATOM   520  C  CD2 . TYR   A 1 66  ? 26.550 -3.629  8.521  1.00 17.83 ? 72  TYR   A CD2 1 
ATOM   521  C  CE1 . TYR   A 1 66  ? 28.055 -5.401  7.028  1.00 19.55 ? 72  TYR   A CE1 1 
ATOM   522  C  CE2 . TYR   A 1 66  ? 26.585 -3.522  7.133  1.00 19.42 ? 72  TYR   A CE2 1 
ATOM   523  C  CZ  . TYR   A 1 66  ? 27.328 -4.420  6.385  1.00 21.03 ? 72  TYR   A CZ  1 
ATOM   524  O  OH  . TYR   A 1 66  ? 27.388 -4.305  5.000  1.00 23.01 ? 72  TYR   A OH  1 
ATOM   525  N  N   . PRO   A 1 67  ? 27.623 -6.817  13.199 1.00 14.30 ? 73  PRO   A N   1 
ATOM   526  C  CA  . PRO   A 1 67  ? 28.046 -6.823  14.615 1.00 15.05 ? 73  PRO   A CA  1 
ATOM   527  C  C   . PRO   A 1 67  ? 29.025 -5.640  14.879 1.00 16.11 ? 73  PRO   A C   1 
ATOM   528  O  O   . PRO   A 1 67  ? 29.798 -5.262  13.975 1.00 18.09 ? 73  PRO   A O   1 
ATOM   529  C  CB  . PRO   A 1 67  ? 28.782 -8.167  14.756 1.00 15.41 ? 73  PRO   A CB  1 
ATOM   530  C  CG  . PRO   A 1 67  ? 29.397 -8.388  13.350 1.00 15.90 ? 73  PRO   A CG  1 
ATOM   531  C  CD  . PRO   A 1 67  ? 28.350 -7.832  12.386 1.00 14.49 ? 73  PRO   A CD  1 
ATOM   532  N  N   . VAL   A 1 68  ? 29.014 -5.066  16.107 1.00 14.01 ? 74  VAL   A N   1 
ATOM   533  C  CA  . VAL   A 1 68  ? 29.897 -3.929  16.436 1.00 14.98 ? 74  VAL   A CA  1 
ATOM   534  C  C   . VAL   A 1 68  ? 30.415 -4.033  17.847 1.00 14.79 ? 74  VAL   A C   1 
ATOM   535  O  O   . VAL   A 1 68  ? 29.762 -4.605  18.728 1.00 13.99 ? 74  VAL   A O   1 
ATOM   536  C  CB  . VAL   A 1 68  ? 29.188 -2.541  16.316 1.00 16.54 ? 74  VAL   A CB  1 
ATOM   537  C  CG1 . VAL   A 1 68  ? 29.163 -2.054  14.874 1.00 18.89 ? 74  VAL   A CG1 1 
ATOM   538  C  CG2 . VAL   A 1 68  ? 27.772 -2.595  16.892 1.00 17.04 ? 74  VAL   A CG2 1 
ATOM   539  N  N   . SER   A 1 69  ? 31.598 -3.435  18.077 1.00 15.23 ? 75  SER   A N   1 
ATOM   540  C  CA  . SER   A 1 69  ? 32.130 -3.180  19.414 1.00 16.08 ? 75  SER   A CA  1 
ATOM   541  C  C   . SER   A 1 69  ? 32.060 -1.665  19.499 1.00 14.97 ? 75  SER   A C   1 
ATOM   542  O  O   . SER   A 1 69  ? 32.562 -0.989  18.602 1.00 15.50 ? 75  SER   A O   1 
ATOM   543  C  CB  . SER   A 1 69  ? 33.584 -3.614  19.529 1.00 20.30 ? 75  SER   A CB  1 
ATOM   544  O  OG  . SER   A 1 69  ? 33.624 -5.032  19.459 1.00 26.95 ? 75  SER   A OG  1 
ATOM   545  N  N   . PHE   A 1 70  ? 31.411 -1.119  20.531 1.00 13.79 ? 76  PHE   A N   1 
ATOM   546  C  CA  . PHE   A 1 70  ? 31.217 0.311   20.611 1.00 14.28 ? 76  PHE   A CA  1 
ATOM   547  C  C   . PHE   A 1 70  ? 31.676 0.883   21.951 1.00 15.54 ? 76  PHE   A C   1 
ATOM   548  O  O   . PHE   A 1 70  ? 31.729 0.186   22.956 1.00 16.44 ? 76  PHE   A O   1 
ATOM   549  C  CB  . PHE   A 1 70  ? 29.735 0.666   20.318 1.00 13.97 ? 76  PHE   A CB  1 
ATOM   550  C  CG  . PHE   A 1 70  ? 28.684 -0.104  21.124 1.00 13.45 ? 76  PHE   A CG  1 
ATOM   551  C  CD1 . PHE   A 1 70  ? 28.161 -1.309  20.656 1.00 14.75 ? 76  PHE   A CD1 1 
ATOM   552  C  CD2 . PHE   A 1 70  ? 28.168 0.418   22.304 1.00 14.74 ? 76  PHE   A CD2 1 
ATOM   553  C  CE1 . PHE   A 1 70  ? 27.186 -2.009  21.392 1.00 14.18 ? 76  PHE   A CE1 1 
ATOM   554  C  CE2 . PHE   A 1 70  ? 27.188 -0.279  23.044 1.00 14.05 ? 76  PHE   A CE2 1 
ATOM   555  C  CZ  . PHE   A 1 70  ? 26.700 -1.486  22.578 1.00 14.40 ? 76  PHE   A CZ  1 
ATOM   556  N  N   . SER   A 1 71  ? 32.079 2.164   21.924 1.00 14.98 ? 77  SER   A N   1 
ATOM   557  C  CA  . SER   A 1 71  ? 32.539 2.839   23.122 1.00 16.27 ? 77  SER   A CA  1 
ATOM   558  C  C   . SER   A 1 71  ? 31.400 3.189   24.094 1.00 16.00 ? 77  SER   A C   1 
ATOM   559  O  O   . SER   A 1 71  ? 30.230 3.213   23.712 1.00 17.03 ? 77  SER   A O   1 
ATOM   560  C  CB  . SER   A 1 71  ? 33.355 4.074   22.745 1.00 18.18 ? 77  SER   A CB  1 
ATOM   561  O  OG  . SER   A 1 71  ? 32.502 5.048   22.157 1.00 21.07 ? 77  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 72  ? 31.742 3.433   25.382 1.00 15.95 ? 78  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 72  ? 30.712 3.810   26.373 1.00 16.80 ? 78  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 72  ? 30.134 5.178   25.973 1.00 17.74 ? 78  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 72  ? 30.825 5.992   25.355 1.00 18.26 ? 78  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 72  ? 31.356 3.882   27.778 1.00 19.87 ? 78  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 72  ? 31.802 2.518   28.302 1.00 25.71 ? 78  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 72  ? 32.305 2.661   29.745 1.00 32.30 ? 78  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 72  ? 33.014 1.403   30.169 1.00 38.60 ? 78  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 72  ? 33.503 1.503   31.566 1.00 43.41 ? 78  LYS   A NZ  1 
ATOM   571  N  N   . PRO   A 1 73  ? 28.897 5.493   26.398 1.00 17.57 ? 79  PRO   A N   1 
ATOM   572  C  CA  . PRO   A 1 73  ? 28.308 6.805   26.052 1.00 18.19 ? 79  PRO   A CA  1 
ATOM   573  C  C   . PRO   A 1 73  ? 29.181 7.956   26.519 1.00 18.52 ? 79  PRO   A C   1 
ATOM   574  O  O   . PRO   A 1 73  ? 29.635 7.954   27.665 1.00 18.63 ? 79  PRO   A O   1 
ATOM   575  C  CB  . PRO   A 1 73  ? 26.990 6.846   26.832 1.00 19.32 ? 79  PRO   A CB  1 
ATOM   576  C  CG  . PRO   A 1 73  ? 26.683 5.405   27.175 1.00 20.58 ? 79  PRO   A CG  1 
ATOM   577  C  CD  . PRO   A 1 73  ? 27.968 4.637   27.173 1.00 17.99 ? 79  PRO   A CD  1 
ATOM   578  N  N   . SER   A 1 74  ? 29.468 8.898   25.608 1.00 19.10 ? 80  SER   A N   1 
ATOM   579  C  CA  . SER   A 1 74  ? 30.367 9.988   25.959 1.00 19.98 ? 80  SER   A CA  1 
ATOM   580  C  C   . SER   A 1 74  ? 30.116 11.265  25.149 1.00 18.02 ? 80  SER   A C   1 
ATOM   581  O  O   . SER   A 1 74  ? 29.248 11.276  24.278 1.00 16.82 ? 80  SER   A O   1 
ATOM   582  C  CB  . SER   A 1 74  ? 31.816 9.516   25.817 1.00 25.10 ? 80  SER   A CB  1 
ATOM   583  O  OG  . SER   A 1 74  ? 32.095 9.309   24.452 1.00 29.99 ? 80  SER   A OG  1 
ATOM   584  N  N   . LEU   A 1 75  ? 30.856 12.356  25.472 1.00 18.18 ? 81  LEU   A N   1 
ATOM   585  C  CA  . LEU   A 1 75  ? 30.728 13.661  24.812 1.00 19.29 ? 81  LEU   A CA  1 
ATOM   586  C  C   . LEU   A 1 75  ? 31.711 13.653  23.648 1.00 19.89 ? 81  LEU   A C   1 
ATOM   587  O  O   . LEU   A 1 75  ? 32.923 13.523  23.867 1.00 20.72 ? 81  LEU   A O   1 
ATOM   588  C  CB  . LEU   A 1 75  ? 31.115 14.744  25.844 1.00 20.65 ? 81  LEU   A CB  1 
ATOM   589  C  CG  . LEU   A 1 75  ? 30.700 16.155  25.562 1.00 24.10 ? 81  LEU   A CG  1 
ATOM   590  C  CD1 . LEU   A 1 75  ? 29.182 16.290  25.327 1.00 24.43 ? 81  LEU   A CD1 1 
ATOM   591  C  CD2 . LEU   A 1 75  ? 31.174 17.127  26.661 1.00 26.76 ? 81  LEU   A CD2 1 
ATOM   592  N  N   . ILE   A 1 76  ? 31.200 13.732  22.411 1.00 19.13 ? 82  ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 76  ? 32.009 13.617  21.202 1.00 20.04 ? 82  ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 76  ? 31.777 14.783  20.271 1.00 19.73 ? 82  ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 76  ? 30.623 15.147  20.037 1.00 19.85 ? 82  ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 76  ? 31.632 12.281  20.515 1.00 22.15 ? 82  ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 76  ? 31.981 11.109  21.429 1.00 25.22 ? 82  ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 76  ? 32.264 12.138  19.114 1.00 22.71 ? 82  ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 76  ? 31.509 9.869   21.000 1.00 28.75 ? 82  ILE   A CD1 1 
ATOM   600  N  N   . PHE   A 1 77  ? 32.864 15.360  19.704 1.00 19.28 ? 83  PHE   A N   1 
ATOM   601  C  CA  . PHE   A 1 77  ? 32.710 16.463  18.768 1.00 19.98 ? 83  PHE   A CA  1 
ATOM   602  C  C   . PHE   A 1 77  ? 32.120 15.961  17.455 1.00 20.25 ? 83  PHE   A C   1 
ATOM   603  O  O   . PHE   A 1 77  ? 32.581 14.957  16.902 1.00 20.47 ? 83  PHE   A O   1 
ATOM   604  C  CB  . PHE   A 1 77  ? 34.087 17.126  18.498 1.00 20.46 ? 83  PHE   A CB  1 
ATOM   605  C  CG  . PHE   A 1 77  ? 34.028 18.247  17.490 1.00 22.81 ? 83  PHE   A CG  1 
ATOM   606  C  CD1 . PHE   A 1 77  ? 34.401 18.036  16.178 1.00 23.93 ? 83  PHE   A CD1 1 
ATOM   607  C  CD2 . PHE   A 1 77  ? 33.513 19.479  17.834 1.00 24.88 ? 83  PHE   A CD2 1 
ATOM   608  C  CE1 . PHE   A 1 77  ? 34.317 19.053  15.241 1.00 24.60 ? 83  PHE   A CE1 1 
ATOM   609  C  CE2 . PHE   A 1 77  ? 33.439 20.504  16.894 1.00 25.86 ? 83  PHE   A CE2 1 
ATOM   610  C  CZ  . PHE   A 1 77  ? 33.872 20.290  15.611 1.00 24.84 ? 83  PHE   A CZ  1 
ATOM   611  N  N   . VAL   A 1 78  ? 31.071 16.665  16.956 1.00 19.02 ? 84  VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 78  ? 30.432 16.334  15.690 1.00 18.72 ? 84  VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 78  ? 30.494 17.600  14.820 1.00 19.80 ? 84  VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 78  ? 30.047 18.687  15.251 1.00 20.19 ? 84  VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 78  ? 28.966 15.912  15.934 1.00 19.35 ? 84  VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 78  ? 28.264 15.592  14.609 1.00 20.86 ? 84  VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 78  ? 28.903 14.706  16.864 1.00 19.14 ? 84  VAL   A CG2 1 
ATOM   618  N  N   . GLU   A 1 79  ? 30.993 17.453  13.598 1.00 19.92 ? 85  GLU   A N   1 
ATOM   619  C  CA  . GLU   A 1 79  ? 31.146 18.565  12.662 1.00 20.88 ? 85  GLU   A CA  1 
ATOM   620  C  C   . GLU   A 1 79  ? 29.803 19.182  12.288 1.00 20.94 ? 85  GLU   A C   1 
ATOM   621  O  O   . GLU   A 1 79  ? 28.790 18.489  12.347 1.00 20.15 ? 85  GLU   A O   1 
ATOM   622  C  CB  . GLU   A 1 79  ? 31.821 18.046  11.373 1.00 24.52 ? 85  GLU   A CB  1 
ATOM   623  C  CG  . GLU   A 1 79  ? 32.169 19.175  10.423 1.00 33.55 ? 85  GLU   A CG  1 
ATOM   624  C  CD  . GLU   A 1 79  ? 33.068 20.201  11.072 1.00 43.05 ? 85  GLU   A CD  1 
ATOM   625  O  OE1 . GLU   A 1 79  ? 32.611 21.342  11.339 1.00 43.91 ? 85  GLU   A OE1 1 
ATOM   626  O  OE2 . GLU   A 1 79  ? 34.210 19.812  11.395 1.00 46.89 ? 85  GLU   A OE2 1 
ATOM   627  N  N   . ALA   A 1 80  ? 29.789 20.482  11.869 1.00 21.81 ? 86  ALA   A N   1 
ATOM   628  C  CA  . ALA   A 1 80  ? 28.569 21.135  11.417 1.00 21.94 ? 86  ALA   A CA  1 
ATOM   629  C  C   . ALA   A 1 80  ? 27.944 20.378  10.247 1.00 22.00 ? 86  ALA   A C   1 
ATOM   630  O  O   . ALA   A 1 80  ? 28.662 19.783  9.430  1.00 22.21 ? 86  ALA   A O   1 
ATOM   631  C  CB  . ALA   A 1 80  ? 28.857 22.569  10.981 1.00 22.37 ? 86  ALA   A CB  1 
ATOM   632  N  N   . SER   A 1 81  ? 26.615 20.355  10.214 1.00 21.87 ? 87  SER   A N   1 
ATOM   633  C  CA  . SER   A 1 81  ? 25.872 19.748  9.107  1.00 21.17 ? 87  SER   A CA  1 
ATOM   634  C  C   . SER   A 1 81  ? 24.729 20.701  8.784  1.00 22.87 ? 87  SER   A C   1 
ATOM   635  O  O   . SER   A 1 81  ? 24.624 21.770  9.416  1.00 24.62 ? 87  SER   A O   1 
ATOM   636  C  CB  . SER   A 1 81  ? 25.324 18.369  9.526  1.00 21.00 ? 87  SER   A CB  1 
ATOM   637  O  OG  . SER   A 1 81  ? 24.376 18.532  10.564 1.00 20.00 ? 87  SER   A OG  1 
ATOM   638  N  N   . GLU   A 1 82  ? 23.847 20.315  7.828  1.00 22.83 ? 88  GLU   A N   1 
ATOM   639  C  CA  . GLU   A 1 82  ? 22.674 21.143  7.574  1.00 23.88 ? 88  GLU   A CA  1 
ATOM   640  C  C   . GLU   A 1 82  ? 21.697 21.138  8.729  1.00 24.48 ? 88  GLU   A C   1 
ATOM   641  O  O   . GLU   A 1 82  ? 20.797 21.974  8.743  1.00 26.01 ? 88  GLU   A O   1 
ATOM   642  C  CB  . GLU   A 1 82  ? 21.970 20.818  6.245  1.00 28.69 ? 88  GLU   A CB  1 
ATOM   643  C  CG  . GLU   A 1 82  ? 21.817 19.353  5.900  1.00 38.15 ? 88  GLU   A CG  1 
ATOM   644  C  CD  . GLU   A 1 82  ? 22.066 19.051  4.428  1.00 49.50 ? 88  GLU   A CD  1 
ATOM   645  O  OE1 . GLU   A 1 82  ? 21.997 19.989  3.596  1.00 52.04 ? 88  GLU   A OE1 1 
ATOM   646  O  OE2 . GLU   A 1 82  ? 22.345 17.869  4.111  1.00 51.05 ? 88  GLU   A OE2 1 
ATOM   647  N  N   . TYR   A 1 83  ? 21.861 20.207  9.720  1.00 22.42 ? 89  TYR   A N   1 
ATOM   648  C  CA  . TYR   A 1 83  ? 20.949 20.079  10.837 1.00 21.25 ? 89  TYR   A CA  1 
ATOM   649  C  C   . TYR   A 1 83  ? 21.434 20.694  12.142 1.00 19.53 ? 89  TYR   A C   1 
ATOM   650  O  O   . TYR   A 1 83  ? 20.600 21.041  12.964 1.00 20.15 ? 89  TYR   A O   1 
ATOM   651  C  CB  . TYR   A 1 83  ? 20.644 18.607  11.077 1.00 20.58 ? 89  TYR   A CB  1 
ATOM   652  C  CG  . TYR   A 1 83  ? 20.060 17.928  9.863  1.00 20.96 ? 89  TYR   A CG  1 
ATOM   653  C  CD1 . TYR   A 1 83  ? 20.869 17.247  8.971  1.00 22.32 ? 89  TYR   A CD1 1 
ATOM   654  C  CD2 . TYR   A 1 83  ? 18.692 17.940  9.625  1.00 21.47 ? 89  TYR   A CD2 1 
ATOM   655  C  CE1 . TYR   A 1 83  ? 20.335 16.612  7.856  1.00 23.65 ? 89  TYR   A CE1 1 
ATOM   656  C  CE2 . TYR   A 1 83  ? 18.143 17.293  8.521  1.00 22.52 ? 89  TYR   A CE2 1 
ATOM   657  C  CZ  . TYR   A 1 83  ? 18.968 16.620  7.649  1.00 24.95 ? 89  TYR   A CZ  1 
ATOM   658  O  OH  . TYR   A 1 83  ? 18.418 15.986  6.560  1.00 28.62 ? 89  TYR   A OH  1 
ATOM   659  N  N   . TYR   A 1 84  ? 22.743 20.801  12.345 1.00 18.15 ? 90  TYR   A N   1 
ATOM   660  C  CA  . TYR   A 1 84  ? 23.275 21.338  13.598 1.00 18.91 ? 90  TYR   A CA  1 
ATOM   661  C  C   . TYR   A 1 84  ? 24.532 22.138  13.353 1.00 20.55 ? 90  TYR   A C   1 
ATOM   662  O  O   . TYR   A 1 84  ? 25.318 21.807  12.461 1.00 20.78 ? 90  TYR   A O   1 
ATOM   663  C  CB  . TYR   A 1 84  ? 23.681 20.187  14.570 1.00 18.38 ? 90  TYR   A CB  1 
ATOM   664  C  CG  . TYR   A 1 84  ? 22.550 19.313  15.085 1.00 16.97 ? 90  TYR   A CG  1 
ATOM   665  C  CD1 . TYR   A 1 84  ? 21.746 19.729  16.127 1.00 17.20 ? 90  TYR   A CD1 1 
ATOM   666  C  CD2 . TYR   A 1 84  ? 22.356 18.035  14.594 1.00 17.03 ? 90  TYR   A CD2 1 
ATOM   667  C  CE1 . TYR   A 1 84  ? 20.732 18.916  16.630 1.00 16.43 ? 90  TYR   A CE1 1 
ATOM   668  C  CE2 . TYR   A 1 84  ? 21.372 17.195  15.113 1.00 16.06 ? 90  TYR   A CE2 1 
ATOM   669  C  CZ  . TYR   A 1 84  ? 20.552 17.638  16.126 1.00 15.95 ? 90  TYR   A CZ  1 
ATOM   670  O  OH  . TYR   A 1 84  ? 19.524 16.862  16.614 1.00 15.56 ? 90  TYR   A OH  1 
ATOM   671  N  N   . PRO   A 1 85  ? 24.817 23.109  14.229 1.00 21.85 ? 91  PRO   A N   1 
ATOM   672  C  CA  . PRO   A 1 85  ? 26.147 23.748  14.163 1.00 21.81 ? 91  PRO   A CA  1 
ATOM   673  C  C   . PRO   A 1 85  ? 27.192 22.750  14.682 1.00 21.62 ? 91  PRO   A C   1 
ATOM   674  O  O   . PRO   A 1 85  ? 26.854 21.724  15.308 1.00 21.21 ? 91  PRO   A O   1 
ATOM   675  C  CB  . PRO   A 1 85  ? 26.014 24.925  15.132 1.00 23.70 ? 91  PRO   A CB  1 
ATOM   676  C  CG  . PRO   A 1 85  ? 25.030 24.412  16.189 1.00 24.52 ? 91  PRO   A CG  1 
ATOM   677  C  CD  . PRO   A 1 85  ? 24.033 23.553  15.409 1.00 22.22 ? 91  PRO   A CD  1 
ATOM   678  N  N   . ALA   A 1 86  ? 28.483 23.043  14.486 1.00 21.29 ? 92  ALA   A N   1 
ATOM   679  C  CA  . ALA   A 1 86  ? 29.565 22.221  15.042 1.00 22.29 ? 92  ALA   A CA  1 
ATOM   680  C  C   . ALA   A 1 86  ? 29.396 22.225  16.575 1.00 22.35 ? 92  ALA   A C   1 
ATOM   681  O  O   . ALA   A 1 86  ? 29.079 23.288  17.131 1.00 22.73 ? 92  ALA   A O   1 
ATOM   682  C  CB  . ALA   A 1 86  ? 30.914 22.838  14.666 1.00 23.17 ? 92  ALA   A CB  1 
ATOM   683  N  N   . ARG   A 1 87  ? 29.392 21.035  17.212 1.00 22.09 ? 93  ARG   A N   1 
ATOM   684  C  CA  . ARG   A 1 87  ? 29.091 20.985  18.656 1.00 21.17 ? 93  ARG   A CA  1 
ATOM   685  C  C   . ARG   A 1 87  ? 29.559 19.660  19.280 1.00 20.29 ? 93  ARG   A C   1 
ATOM   686  O  O   . ARG   A 1 87  ? 29.984 18.758  18.564 1.00 20.49 ? 93  ARG   A O   1 
ATOM   687  C  CB  . ARG   A 1 87  ? 27.554 21.141  18.850 1.00 20.67 ? 93  ARG   A CB  1 
ATOM   688  C  CG  . ARG   A 1 87  ? 26.771 19.824  18.549 1.00 19.96 ? 93  ARG   A CG  1 
ATOM   689  C  CD  . ARG   A 1 87  ? 25.363 20.027  18.039 1.00 19.07 ? 93  ARG   A CD  1 
ATOM   690  N  NE  . ARG   A 1 87  ? 24.469 18.915  18.407 1.00 19.92 ? 93  ARG   A NE  1 
ATOM   691  C  CZ  . ARG   A 1 87  ? 24.437 17.724  17.803 1.00 18.35 ? 93  ARG   A CZ  1 
ATOM   692  N  NH1 . ARG   A 1 87  ? 23.555 16.798  18.187 1.00 18.83 ? 93  ARG   A NH1 1 
ATOM   693  N  NH2 . ARG   A 1 87  ? 25.292 17.443  16.827 1.00 17.04 ? 93  ARG   A NH2 1 
ATOM   694  N  N   . TYR   A 1 88  ? 29.452 19.535  20.608 1.00 19.97 ? 94  TYR   A N   1 
ATOM   695  C  CA  . TYR   A 1 88  ? 29.710 18.243  21.259 1.00 20.43 ? 94  TYR   A CA  1 
ATOM   696  C  C   . TYR   A 1 88  ? 28.358 17.570  21.450 1.00 18.89 ? 94  TYR   A C   1 
ATOM   697  O  O   . TYR   A 1 88  ? 27.421 18.183  21.981 1.00 20.53 ? 94  TYR   A O   1 
ATOM   698  C  CB  . TYR   A 1 88  ? 30.363 18.422  22.629 1.00 21.63 ? 94  TYR   A CB  1 
ATOM   699  C  CG  . TYR   A 1 88  ? 31.777 18.910  22.470 1.00 24.12 ? 94  TYR   A CG  1 
ATOM   700  C  CD1 . TYR   A 1 88  ? 32.835 18.020  22.401 1.00 26.21 ? 94  TYR   A CD1 1 
ATOM   701  C  CD2 . TYR   A 1 88  ? 32.049 20.260  22.317 1.00 26.50 ? 94  TYR   A CD2 1 
ATOM   702  C  CE1 . TYR   A 1 88  ? 34.139 18.472  22.182 1.00 28.31 ? 94  TYR   A CE1 1 
ATOM   703  C  CE2 . TYR   A 1 88  ? 33.334 20.716  22.072 1.00 28.47 ? 94  TYR   A CE2 1 
ATOM   704  C  CZ  . TYR   A 1 88  ? 34.378 19.823  22.020 1.00 30.13 ? 94  TYR   A CZ  1 
ATOM   705  O  OH  . TYR   A 1 88  ? 35.646 20.323  21.806 1.00 33.33 ? 94  TYR   A OH  1 
ATOM   706  N  N   . GLN   A 1 89  ? 28.236 16.343  20.972 1.00 17.06 ? 95  GLN   A N   1 
ATOM   707  C  CA  . GLN   A 1 89  ? 27.005 15.568  21.170 1.00 15.74 ? 95  GLN   A CA  1 
ATOM   708  C  C   . GLN   A 1 89  ? 27.257 14.647  22.358 1.00 16.32 ? 95  GLN   A C   1 
ATOM   709  O  O   . GLN   A 1 89  ? 28.288 13.968  22.414 1.00 17.50 ? 95  GLN   A O   1 
ATOM   710  C  CB  . GLN   A 1 89  ? 26.622 14.751  19.915 1.00 15.60 ? 95  GLN   A CB  1 
ATOM   711  C  CG  . GLN   A 1 89  ? 25.381 13.857  20.128 1.00 15.18 ? 95  GLN   A CG  1 
ATOM   712  C  CD  . GLN   A 1 89  ? 24.777 13.404  18.823 1.00 15.58 ? 95  GLN   A CD  1 
ATOM   713  O  OE1 . GLN   A 1 89  ? 24.703 14.154  17.838 1.00 15.26 ? 95  GLN   A OE1 1 
ATOM   714  N  NE2 . GLN   A 1 89  ? 24.324 12.137  18.787 1.00 13.76 ? 95  GLN   A NE2 1 
ATOM   715  N  N   . SER   A 1 90  ? 26.345 14.628  23.328 1.00 15.56 ? 96  SER   A N   1 
ATOM   716  C  CA  . SER   A 1 90  ? 26.478 13.803  24.509 1.00 15.57 ? 96  SER   A CA  1 
ATOM   717  C  C   . SER   A 1 90  ? 25.790 12.435  24.358 1.00 16.42 ? 96  SER   A C   1 
ATOM   718  O  O   . SER   A 1 90  ? 24.937 12.253  23.453 1.00 15.97 ? 96  SER   A O   1 
ATOM   719  C  CB  . SER   A 1 90  ? 25.951 14.552  25.730 1.00 17.09 ? 96  SER   A CB  1 
ATOM   720  O  OG  . SER   A 1 90  ? 24.557 14.811  25.626 1.00 20.28 ? 96  SER   A OG  1 
ATOM   721  N  N   . HIS   A 1 91  ? 26.175 11.472  25.240 1.00 15.60 ? 97  HIS   A N   1 
ATOM   722  C  CA  . HIS   A 1 91  ? 25.597 10.124  25.297 1.00 14.69 ? 97  HIS   A CA  1 
ATOM   723  C  C   . HIS   A 1 91  ? 25.784 9.405   23.940 1.00 13.76 ? 97  HIS   A C   1 
ATOM   724  O  O   . HIS   A 1 91  ? 24.929 8.608   23.542 1.00 14.13 ? 97  HIS   A O   1 
ATOM   725  C  CB  . HIS   A 1 91  ? 24.100 10.182  25.702 1.00 16.84 ? 97  HIS   A CB  1 
ATOM   726  C  CG  . HIS   A 1 91  ? 23.893 10.780  27.077 1.00 18.98 ? 97  HIS   A CG  1 
ATOM   727  N  ND1 . HIS   A 1 91  ? 23.728 9.973   28.197 1.00 22.34 ? 97  HIS   A ND1 1 
ATOM   728  C  CD2 . HIS   A 1 91  ? 23.826 12.082  27.467 1.00 20.03 ? 97  HIS   A CD2 1 
ATOM   729  C  CE1 . HIS   A 1 91  ? 23.600 10.804  29.228 1.00 22.48 ? 97  HIS   A CE1 1 
ATOM   730  N  NE2 . HIS   A 1 91  ? 23.686 12.081  28.842 1.00 21.62 ? 97  HIS   A NE2 1 
ATOM   731  N  N   . LEU   A 1 92  ? 26.911 9.698   23.236 1.00 13.19 ? 98  LEU   A N   1 
ATOM   732  C  CA  . LEU   A 1 92  ? 27.133 9.099   21.917 1.00 13.90 ? 98  LEU   A CA  1 
ATOM   733  C  C   . LEU   A 1 92  ? 28.174 7.973   22.052 1.00 14.71 ? 98  LEU   A C   1 
ATOM   734  O  O   . LEU   A 1 92  ? 29.172 8.111   22.793 1.00 14.62 ? 98  LEU   A O   1 
ATOM   735  C  CB  . LEU   A 1 92  ? 27.675 10.193  20.960 1.00 14.36 ? 98  LEU   A CB  1 
ATOM   736  C  CG  . LEU   A 1 92  ? 27.904 9.807   19.466 1.00 16.42 ? 98  LEU   A CG  1 
ATOM   737  C  CD1 . LEU   A 1 92  ? 26.585 9.350   18.779 1.00 17.22 ? 98  LEU   A CD1 1 
ATOM   738  C  CD2 . LEU   A 1 92  ? 28.471 11.024  18.680 1.00 19.24 ? 98  LEU   A CD2 1 
ATOM   739  N  N   . MET   A 1 93  ? 27.953 6.874   21.307 1.00 14.73 ? 99  MET   A N   1 
ATOM   740  C  CA  . MET   A 1 93  ? 28.845 5.702   21.333 1.00 14.92 ? 99  MET   A CA  1 
ATOM   741  C  C   . MET   A 1 93  ? 29.366 5.463   19.944 1.00 15.35 ? 99  MET   A C   1 
ATOM   742  O  O   . MET   A 1 93  ? 28.579 5.407   18.996 1.00 15.46 ? 99  MET   A O   1 
ATOM   743  C  CB  . MET   A 1 93  ? 28.037 4.493   21.800 1.00 15.56 ? 99  MET   A CB  1 
ATOM   744  C  CG  . MET   A 1 93  ? 27.446 4.696   23.188 1.00 16.44 ? 99  MET   A CG  1 
ATOM   745  S  SD  . MET   A 1 93  ? 26.374 3.353   23.748 1.00 19.17 ? 99  MET   A SD  1 
ATOM   746  C  CE  . MET   A 1 93  ? 25.026 3.471   22.560 1.00 18.07 ? 99  MET   A CE  1 
ATOM   747  N  N   . LEU   A 1 94  ? 30.701 5.348   19.787 1.00 16.21 ? 100 LEU   A N   1 
ATOM   748  C  CA  . LEU   A 1 94  ? 31.261 5.143   18.457 1.00 16.56 ? 100 LEU   A CA  1 
ATOM   749  C  C   . LEU   A 1 94  ? 31.683 3.714   18.222 1.00 15.80 ? 100 LEU   A C   1 
ATOM   750  O  O   . LEU   A 1 94  ? 32.122 3.045   19.143 1.00 15.60 ? 100 LEU   A O   1 
ATOM   751  C  CB  . LEU   A 1 94  ? 32.485 6.041   18.220 1.00 17.67 ? 100 LEU   A CB  1 
ATOM   752  C  CG  . LEU   A 1 94  ? 32.234 7.533   18.259 1.00 20.93 ? 100 LEU   A CG  1 
ATOM   753  C  CD1 . LEU   A 1 94  ? 33.509 8.332   17.831 1.00 21.92 ? 100 LEU   A CD1 1 
ATOM   754  C  CD2 . LEU   A 1 94  ? 31.091 7.944   17.351 1.00 22.35 ? 100 LEU   A CD2 1 
ATOM   755  N  N   . ALA   A 1 95  ? 31.665 3.313   16.956 1.00 15.45 ? 101 ALA   A N   1 
ATOM   756  C  CA  . ALA   A 1 95  ? 32.126 1.983   16.561 1.00 15.52 ? 101 ALA   A CA  1 
ATOM   757  C  C   . ALA   A 1 95  ? 32.642 2.046   15.136 1.00 15.62 ? 101 ALA   A C   1 
ATOM   758  O  O   . ALA   A 1 95  ? 32.294 2.966   14.382 1.00 15.48 ? 101 ALA   A O   1 
ATOM   759  C  CB  . ALA   A 1 95  ? 30.956 0.981   16.641 1.00 16.65 ? 101 ALA   A CB  1 
ATOM   760  N  N   . VAL   A 1 96  ? 33.426 1.037   14.741 1.00 15.18 ? 102 VAL   A N   1 
ATOM   761  C  CA  . VAL   A 1 96  ? 33.873 0.896   13.359 1.00 15.89 ? 102 VAL   A CA  1 
ATOM   762  C  C   . VAL   A 1 96  ? 32.769 0.111   12.645 1.00 16.63 ? 102 VAL   A C   1 
ATOM   763  O  O   . VAL   A 1 96  ? 32.391 -0.994  13.048 1.00 16.88 ? 102 VAL   A O   1 
ATOM   764  C  CB  . VAL   A 1 96  ? 35.241 0.184   13.296 1.00 17.39 ? 102 VAL   A CB  1 
ATOM   765  C  CG1 . VAL   A 1 96  ? 35.658 -0.059  11.842 1.00 18.42 ? 102 VAL   A CG1 1 
ATOM   766  C  CG2 . VAL   A 1 96  ? 36.276 1.028   14.031 1.00 18.36 ? 102 VAL   A CG2 1 
ATOM   767  N  N   . GLY   A 1 97  ? 32.241 0.711   11.595 1.00 16.31 ? 103 GLY   A N   1 
ATOM   768  C  CA  . GLY   A 1 97  ? 31.197 0.104   10.803 1.00 16.79 ? 103 GLY   A CA  1 
ATOM   769  C  C   . GLY   A 1 97  ? 30.762 1.057   9.714  1.00 17.02 ? 103 GLY   A C   1 
ATOM   770  O  O   . GLY   A 1 97  ? 31.031 2.268   9.782  1.00 18.23 ? 103 GLY   A O   1 
ATOM   771  N  N   . HIS   A 1 98  ? 30.076 0.525   8.693  1.00 15.46 ? 104 HIS   A N   1 
ATOM   772  C  CA  . HIS   A 1 98  ? 29.584 1.372   7.617  1.00 14.39 ? 104 HIS   A CA  1 
ATOM   773  C  C   . HIS   A 1 98  ? 28.365 2.178   8.025  1.00 14.68 ? 104 HIS   A C   1 
ATOM   774  O  O   . HIS   A 1 98  ? 27.447 1.677   8.657  1.00 14.99 ? 104 HIS   A O   1 
ATOM   775  C  CB  . HIS   A 1 98  ? 29.228 0.541   6.350  1.00 15.81 ? 104 HIS   A CB  1 
ATOM   776  C  CG  . HIS   A 1 98  ? 28.725 1.388   5.225  1.00 17.12 ? 104 HIS   A CG  1 
ATOM   777  N  ND1 . HIS   A 1 98  ? 29.562 2.255   4.563  1.00 18.02 ? 104 HIS   A ND1 1 
ATOM   778  C  CD2 . HIS   A 1 98  ? 27.458 1.548   4.758  1.00 17.67 ? 104 HIS   A CD2 1 
ATOM   779  C  CE1 . HIS   A 1 98  ? 28.799 2.896   3.690  1.00 19.14 ? 104 HIS   A CE1 1 
ATOM   780  N  NE2 . HIS   A 1 98  ? 27.517 2.492   3.770  1.00 17.96 ? 104 HIS   A NE2 1 
ATOM   781  N  N   . SER   A 1 99  ? 28.325 3.385   7.539  1.00 14.62 ? 105 SER   A N   1 
ATOM   782  C  CA  . SER   A 1 99  ? 27.171 4.251   7.669  1.00 14.76 ? 105 SER   A CA  1 
ATOM   783  C  C   . SER   A 1 99  ? 27.293 5.388   6.677  1.00 16.83 ? 105 SER   A C   1 
ATOM   784  O  O   . SER   A 1 99  ? 28.398 5.821   6.313  1.00 18.54 ? 105 SER   A O   1 
ATOM   785  C  CB  . SER   A 1 99  ? 26.969 4.750   9.092  1.00 17.80 ? 105 SER   A CB  1 
ATOM   786  O  OG  . SER   A 1 99  ? 27.915 5.741   9.449  1.00 22.46 ? 105 SER   A OG  1 
ATOM   787  N  N   . GLU   A 1 100 ? 26.151 5.822   6.185  1.00 15.84 ? 106 GLU   A N   1 
ATOM   788  C  CA  . GLU   A 1 100 ? 26.098 6.957   5.305  1.00 17.57 ? 106 GLU   A CA  1 
ATOM   789  C  C   . GLU   A 1 100 ? 24.814 7.738   5.581  1.00 19.94 ? 106 GLU   A C   1 
ATOM   790  O  O   . GLU   A 1 100 ? 23.925 7.274   6.324  1.00 19.90 ? 106 GLU   A O   1 
ATOM   791  C  CB  . GLU   A 1 100 ? 26.293 6.525   3.816  1.00 21.55 ? 106 GLU   A CB  1 
ATOM   792  C  CG  . GLU   A 1 100 ? 25.235 5.581   3.335  1.00 25.56 ? 106 GLU   A CG  1 
ATOM   793  C  CD  . GLU   A 1 100 ? 25.521 5.086   1.914  1.00 24.02 ? 106 GLU   A CD  1 
ATOM   794  O  OE1 . GLU   A 1 100 ? 24.955 5.680   0.968  1.00 26.68 ? 106 GLU   A OE1 1 
ATOM   795  O  OE2 . GLU   A 1 100 ? 26.263 4.090   1.749  1.00 20.73 ? 106 GLU   A OE2 1 
ATOM   796  N  N   . PRO   A 1 101 ? 24.719 9.004   5.090  1.00 21.40 ? 107 PRO   A N   1 
ATOM   797  C  CA  . PRO   A 1 101 ? 23.481 9.747   5.272  1.00 23.33 ? 107 PRO   A CA  1 
ATOM   798  C  C   . PRO   A 1 101 ? 22.309 8.912   4.722  1.00 22.40 ? 107 PRO   A C   1 
ATOM   799  O  O   . PRO   A 1 101 ? 22.388 8.317   3.607  1.00 23.67 ? 107 PRO   A O   1 
ATOM   800  C  CB  . PRO   A 1 101 ? 23.717 11.018  4.452  1.00 25.24 ? 107 PRO   A CB  1 
ATOM   801  C  CG  . PRO   A 1 101 ? 25.170 11.175  4.434  1.00 24.42 ? 107 PRO   A CG  1 
ATOM   802  C  CD  . PRO   A 1 101 ? 25.676 9.764   4.266  1.00 21.54 ? 107 PRO   A CD  1 
ATOM   803  N  N   . GLY   A 1 102 ? 21.299 8.814   5.566  1.00 19.74 ? 108 GLY   A N   1 
ATOM   804  C  CA  . GLY   A 1 102 ? 20.127 7.965   5.367  1.00 18.58 ? 108 GLY   A CA  1 
ATOM   805  C  C   . GLY   A 1 102 ? 20.060 6.848   6.409  1.00 16.97 ? 108 GLY   A C   1 
ATOM   806  O  O   . GLY   A 1 102 ? 18.992 6.285   6.654  1.00 17.29 ? 108 GLY   A O   1 
ATOM   807  N  N   . ASP   A 1 103 ? 21.213 6.509   7.047  1.00 14.77 ? 109 ASP   A N   1 
ATOM   808  C  CA  . ASP   A 1 103 ? 21.229 5.399   8.014  1.00 13.49 ? 109 ASP   A CA  1 
ATOM   809  C  C   . ASP   A 1 103 ? 20.794 5.768   9.420  1.00 13.77 ? 109 ASP   A C   1 
ATOM   810  O  O   . ASP   A 1 103 ? 20.569 4.865   10.244 1.00 14.49 ? 109 ASP   A O   1 
ATOM   811  C  CB  . ASP   A 1 103 ? 22.632 4.774   8.077  1.00 15.07 ? 109 ASP   A CB  1 
ATOM   812  C  CG  . ASP   A 1 103 ? 22.920 3.858   6.907  1.00 16.69 ? 109 ASP   A CG  1 
ATOM   813  O  OD1 . ASP   A 1 103 ? 21.958 3.270   6.375  1.00 17.05 ? 109 ASP   A OD1 1 
ATOM   814  O  OD2 . ASP   A 1 103 ? 24.130 3.791   6.462  1.00 15.28 ? 109 ASP   A OD2 1 
ATOM   815  N  N   . CYS   A 1 104 ? 20.614 7.068   9.722  1.00 13.65 ? 110 CYS   A N   1 
ATOM   816  C  CA  . CYS   A 1 104 ? 20.161 7.443   11.078 1.00 13.24 ? 110 CYS   A CA  1 
ATOM   817  C  C   . CYS   A 1 104 ? 18.823 6.792   11.403 1.00 14.05 ? 110 CYS   A C   1 
ATOM   818  O  O   . CYS   A 1 104 ? 17.960 6.748   10.524 1.00 15.96 ? 110 CYS   A O   1 
ATOM   819  C  CB  . CYS   A 1 104 ? 20.083 8.959   11.220 1.00 14.71 ? 110 CYS   A CB  1 
ATOM   820  S  SG  . CYS   A 1 104 ? 21.703 9.771   11.202 1.00 16.43 ? 110 CYS   A SG  1 
ATOM   821  N  N   . GLY   A 1 105 ? 18.657 6.326   12.622 1.00 13.07 ? 111 GLY   A N   1 
ATOM   822  C  CA  . GLY   A 1 105 ? 17.388 5.682   12.998 1.00 13.93 ? 111 GLY   A CA  1 
ATOM   823  C  C   . GLY   A 1 105 ? 17.501 4.167   13.039 1.00 14.28 ? 111 GLY   A C   1 
ATOM   824  O  O   . GLY   A 1 105 ? 16.676 3.494   13.670 1.00 14.58 ? 111 GLY   A O   1 
ATOM   825  N  N   . GLY   A 1 106 ? 18.564 3.599   12.431 1.00 13.49 ? 112 GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 106 ? 18.787 2.141   12.512 1.00 13.28 ? 112 GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 106 ? 19.006 1.739   13.964 1.00 13.16 ? 112 GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 106 ? 19.721 2.431   14.707 1.00 14.39 ? 112 GLY   A O   1 
ATOM   829  N  N   . ILE   A 1 107 ? 18.383 0.642   14.389 1.00 12.75 ? 113 ILE   A N   1 
ATOM   830  C  CA  . ILE   A 1 107 ? 18.484 0.228   15.786 1.00 12.71 ? 113 ILE   A CA  1 
ATOM   831  C  C   . ILE   A 1 107 ? 19.756 -0.589  16.075 1.00 12.61 ? 113 ILE   A C   1 
ATOM   832  O  O   . ILE   A 1 107 ? 20.109 -1.511  15.307 1.00 13.58 ? 113 ILE   A O   1 
ATOM   833  C  CB  . ILE   A 1 107 ? 17.186 -0.535  16.198 1.00 13.94 ? 113 ILE   A CB  1 
ATOM   834  C  CG1 . ILE   A 1 107 ? 16.048 0.513   16.434 1.00 15.63 ? 113 ILE   A CG1 1 
ATOM   835  C  CG2 . ILE   A 1 107 ? 17.388 -1.394  17.453 1.00 15.34 ? 113 ILE   A CG2 1 
ATOM   836  C  CD1 . ILE   A 1 107 ? 14.644 -0.152  16.644 1.00 17.04 ? 113 ILE   A CD1 1 
ATOM   837  N  N   . LEU   A 1 108 ? 20.369 -0.325  17.227 1.00 12.28 ? 114 LEU   A N   1 
ATOM   838  C  CA  . LEU   A 1 108 ? 21.466 -1.101  17.829 1.00 12.17 ? 114 LEU   A CA  1 
ATOM   839  C  C   . LEU   A 1 108 ? 20.842 -1.928  18.977 1.00 13.03 ? 114 LEU   A C   1 
ATOM   840  O  O   . LEU   A 1 108 ? 20.178 -1.357  19.841 1.00 13.39 ? 114 LEU   A O   1 
ATOM   841  C  CB  . LEU   A 1 108 ? 22.556 -0.154  18.390 1.00 13.62 ? 114 LEU   A CB  1 
ATOM   842  C  CG  . LEU   A 1 108 ? 23.719 -0.829  19.174 1.00 14.38 ? 114 LEU   A CG  1 
ATOM   843  C  CD1 . LEU   A 1 108 ? 24.570 -1.744  18.272 1.00 14.58 ? 114 LEU   A CD1 1 
ATOM   844  C  CD2 . LEU   A 1 108 ? 24.619 0.242   19.823 1.00 15.74 ? 114 LEU   A CD2 1 
ATOM   845  N  N   . ARG   A 1 109 ? 21.062 -3.251  18.965 1.00 13.32 ? 115 ARG   A N   1 
ATOM   846  C  CA  . ARG   A 1 109 ? 20.541 -4.144  19.987 1.00 13.15 ? 115 ARG   A CA  1 
ATOM   847  C  C   . ARG   A 1 109 ? 21.662 -4.998  20.559 1.00 14.52 ? 115 ARG   A C   1 
ATOM   848  O  O   . ARG   A 1 109 ? 22.577 -5.427  19.840 1.00 14.69 ? 115 ARG   A O   1 
ATOM   849  C  CB  . ARG   A 1 109 ? 19.485 -5.099  19.359 1.00 16.36 ? 115 ARG   A CB  1 
ATOM   850  C  CG  . ARG   A 1 109 ? 18.088 -4.495  19.168 1.00 20.05 ? 115 ARG   A CG  1 
ATOM   851  C  CD  . ARG   A 1 109 ? 17.050 -5.520  18.607 1.00 23.12 ? 115 ARG   A CD  1 
ATOM   852  N  NE  . ARG   A 1 109 ? 15.640 -5.062  18.756 1.00 23.07 ? 115 ARG   A NE  1 
ATOM   853  C  CZ  . ARG   A 1 109 ? 14.833 -5.390  19.757 1.00 23.15 ? 115 ARG   A CZ  1 
ATOM   854  N  NH1 . ARG   A 1 109 ? 15.279 -6.132  20.764 1.00 19.11 ? 115 ARG   A NH1 1 
ATOM   855  N  NH2 . ARG   A 1 109 ? 13.589 -4.918  19.801 1.00 24.22 ? 115 ARG   A NH2 1 
ATOM   856  N  N   . CYS   A 1 110 ? 21.535 -5.336  21.834 1.00 15.22 ? 116 CYS   A N   1 
ATOM   857  C  CA  . CYS   A 1 110 ? 22.403 -6.341  22.452 1.00 15.52 ? 116 CYS   A CA  1 
ATOM   858  C  C   . CYS   A 1 110 ? 21.457 -7.502  22.878 1.00 15.75 ? 116 CYS   A C   1 
ATOM   859  O  O   . CYS   A 1 110 ? 20.246 -7.464  22.585 1.00 16.93 ? 116 CYS   A O   1 
ATOM   860  C  CB  . CYS   A 1 110 ? 23.140 -5.756  23.654 1.00 16.06 ? 116 CYS   A CB  1 
ATOM   861  S  SG  . CYS   A 1 110 ? 22.013 -5.295  24.991 1.00 15.23 ? 116 CYS   A SG  1 
ATOM   862  N  N   . GLN   A 1 111 ? 21.966 -8.488  23.630 1.00 16.53 ? 117 GLN   A N   1 
ATOM   863  C  CA  . GLN   A 1 111 ? 21.116 -9.600  24.100 1.00 17.60 ? 117 GLN   A CA  1 
ATOM   864  C  C   . GLN   A 1 111 ? 19.984 -9.171  25.059 1.00 17.55 ? 117 GLN   A C   1 
ATOM   865  O  O   . GLN   A 1 111 ? 19.070 -9.972  25.343 1.00 18.07 ? 117 GLN   A O   1 
ATOM   866  C  CB  . GLN   A 1 111 ? 21.981 -10.681 24.790 1.00 20.80 ? 117 GLN   A CB  1 
ATOM   867  C  CG  . GLN   A 1 111 ? 22.628 -10.159 26.072 1.00 27.15 ? 117 GLN   A CG  1 
ATOM   868  C  CD  . GLN   A 1 111 ? 23.623 -11.140 26.637 1.00 36.37 ? 117 GLN   A CD  1 
ATOM   869  O  OE1 . GLN   A 1 111 ? 24.845 -10.940 26.570 1.00 40.23 ? 117 GLN   A OE1 1 
ATOM   870  N  NE2 . GLN   A 1 111 ? 23.114 -12.208 27.216 1.00 34.66 ? 117 GLN   A NE2 1 
ATOM   871  N  N   . HIS   A 1 112 ? 20.050 -7.950  25.599 1.00 16.57 ? 118 HIS   A N   1 
ATOM   872  C  CA  . HIS   A 1 112 ? 19.089 -7.450  26.584 1.00 16.72 ? 118 HIS   A CA  1 
ATOM   873  C  C   . HIS   A 1 112 ? 17.982 -6.598  25.998 1.00 15.67 ? 118 HIS   A C   1 
ATOM   874  O  O   . HIS   A 1 112 ? 16.992 -6.320  26.710 1.00 16.68 ? 118 HIS   A O   1 
ATOM   875  C  CB  . HIS   A 1 112 ? 19.808 -6.656  27.707 1.00 18.22 ? 118 HIS   A CB  1 
ATOM   876  C  CG  . HIS   A 1 112 ? 20.923 -7.427  28.363 1.00 18.69 ? 118 HIS   A CG  1 
ATOM   877  N  ND1 . HIS   A 1 112 ? 22.255 -7.096  28.158 1.00 19.37 ? 118 HIS   A ND1 1 
ATOM   878  C  CD2 . HIS   A 1 112 ? 20.860 -8.486  29.218 1.00 20.10 ? 118 HIS   A CD2 1 
ATOM   879  C  CE1 . HIS   A 1 112 ? 22.962 -7.969  28.875 1.00 20.18 ? 118 HIS   A CE1 1 
ATOM   880  N  NE2 . HIS   A 1 112 ? 22.167 -8.836  29.510 1.00 20.64 ? 118 HIS   A NE2 1 
ATOM   881  N  N   . GLY   A 1 113 ? 18.156 -6.134  24.757 1.00 14.36 ? 119 GLY   A N   1 
ATOM   882  C  CA  . GLY   A 1 113 ? 17.129 -5.302  24.149 1.00 13.72 ? 119 GLY   A CA  1 
ATOM   883  C  C   . GLY   A 1 113 ? 17.756 -4.170  23.339 1.00 13.29 ? 119 GLY   A C   1 
ATOM   884  O  O   . GLY   A 1 113 ? 18.917 -4.233  22.908 1.00 14.91 ? 119 GLY   A O   1 
ATOM   885  N  N   . VAL   A 1 114 ? 16.961 -3.145  23.106 1.00 13.27 ? 120 VAL   A N   1 
ATOM   886  C  CA  . VAL   A 1 114 ? 17.410 -1.985  22.330 1.00 13.12 ? 120 VAL   A CA  1 
ATOM   887  C  C   . VAL   A 1 114 ? 18.398 -1.129  23.145 1.00 13.23 ? 120 VAL   A C   1 
ATOM   888  O  O   . VAL   A 1 114 ? 18.097 -0.736  24.287 1.00 14.31 ? 120 VAL   A O   1 
ATOM   889  C  CB  . VAL   A 1 114 ? 16.212 -1.115  21.898 1.00 14.63 ? 120 VAL   A CB  1 
ATOM   890  C  CG1 . VAL   A 1 114 ? 16.713 0.171   21.232 1.00 14.93 ? 120 VAL   A CG1 1 
ATOM   891  C  CG2 . VAL   A 1 114 ? 15.306 -1.906  20.942 1.00 15.13 ? 120 VAL   A CG2 1 
ATOM   892  N  N   . VAL   A 1 115 ? 19.551 -0.815  22.529 1.00 13.84 ? 121 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 115 ? 20.596 -0.006  23.163 1.00 13.80 ? 121 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 115 ? 20.502 1.461   22.713 1.00 14.78 ? 121 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 115 ? 20.729 2.386   23.501 1.00 14.29 ? 121 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 115 ? 21.986 -0.591  22.794 1.00 14.93 ? 121 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 115 ? 23.130 0.348   23.243 1.00 15.99 ? 121 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 115 ? 22.175 -2.009  23.364 1.00 15.09 ? 121 VAL   A CG2 1 
ATOM   899  N  N   . GLY   A 1 116 ? 20.266 1.669   21.420 1.00 13.81 ? 122 GLY   A N   1 
ATOM   900  C  CA  . GLY   A 1 116 ? 20.240 3.037   20.890 1.00 14.11 ? 122 GLY   A CA  1 
ATOM   901  C  C   . GLY   A 1 116 ? 19.962 3.086   19.408 1.00 13.84 ? 122 GLY   A C   1 
ATOM   902  O  O   . GLY   A 1 116 ? 19.576 2.064   18.832 1.00 13.98 ? 122 GLY   A O   1 
ATOM   903  N  N   . ILE   A 1 117 ? 20.122 4.286   18.795 1.00 13.25 ? 123 ILE   A N   1 
ATOM   904  C  CA  . ILE   A 1 117 ? 19.856 4.391   17.349 1.00 13.06 ? 123 ILE   A CA  1 
ATOM   905  C  C   . ILE   A 1 117 ? 21.024 5.053   16.649 1.00 13.60 ? 123 ILE   A C   1 
ATOM   906  O  O   . ILE   A 1 117 ? 21.654 5.915   17.240 1.00 12.97 ? 123 ILE   A O   1 
ATOM   907  C  CB  . ILE   A 1 117 ? 18.559 5.190   17.065 1.00 15.52 ? 123 ILE   A CB  1 
ATOM   908  C  CG1 . ILE   A 1 117 ? 18.516 6.514   17.868 1.00 17.08 ? 123 ILE   A CG1 1 
ATOM   909  C  CG2 . ILE   A 1 117 ? 17.332 4.315   17.271 1.00 17.20 ? 123 ILE   A CG2 1 
ATOM   910  C  CD1 . ILE   A 1 117 ? 17.248 7.394   17.411 1.00 18.96 ? 123 ILE   A CD1 1 
ATOM   911  N  N   . VAL   A 1 118 ? 21.261 4.724   15.357 1.00 12.58 ? 124 VAL   A N   1 
ATOM   912  C  CA  . VAL   A 1 118 ? 22.308 5.414   14.578 1.00 12.66 ? 124 VAL   A CA  1 
ATOM   913  C  C   . VAL   A 1 118 ? 22.036 6.940   14.561 1.00 12.91 ? 124 VAL   A C   1 
ATOM   914  O  O   . VAL   A 1 118 ? 20.896 7.357   14.335 1.00 13.19 ? 124 VAL   A O   1 
ATOM   915  C  CB  . VAL   A 1 118 ? 22.364 4.897   13.134 1.00 12.52 ? 124 VAL   A CB  1 
ATOM   916  C  CG1 . VAL   A 1 118 ? 23.401 5.691   12.311 1.00 13.36 ? 124 VAL   A CG1 1 
ATOM   917  C  CG2 . VAL   A 1 118 ? 22.694 3.393   13.080 1.00 13.93 ? 124 VAL   A CG2 1 
ATOM   918  N  N   . SER   A 1 119 ? 23.085 7.742   14.832 1.00 12.03 ? 125 SER   A N   1 
ATOM   919  C  CA  . SER   A 1 119 ? 22.924 9.200   14.900 1.00 12.40 ? 125 SER   A CA  1 
ATOM   920  C  C   . SER   A 1 119 ? 24.009 9.939   14.124 1.00 14.02 ? 125 SER   A C   1 
ATOM   921  O  O   . SER   A 1 119 ? 23.791 11.064  13.686 1.00 14.26 ? 125 SER   A O   1 
ATOM   922  C  CB  . SER   A 1 119 ? 22.912 9.641   16.370 1.00 13.47 ? 125 SER   A CB  1 
ATOM   923  O  OG  . SER   A 1 119 ? 22.822 11.055  16.523 1.00 14.75 ? 125 SER   A OG  1 
ATOM   924  N  N   . THR   A 1 120 ? 25.219 9.353   13.988 1.00 12.60 ? 126 THR   A N   1 
ATOM   925  C  CA  . THR   A 1 120 ? 26.323 10.019  13.266 1.00 14.32 ? 126 THR   A CA  1 
ATOM   926  C  C   . THR   A 1 120 ? 27.114 8.945   12.472 1.00 14.65 ? 126 THR   A C   1 
ATOM   927  O  O   . THR   A 1 120 ? 26.908 7.734   12.654 1.00 14.43 ? 126 THR   A O   1 
ATOM   928  C  CB  . THR   A 1 120 ? 27.302 10.730  14.273 1.00 15.84 ? 126 THR   A CB  1 
ATOM   929  O  OG1 . THR   A 1 120 ? 28.049 9.743   14.988 1.00 17.12 ? 126 THR   A OG1 1 
ATOM   930  C  CG2 . THR   A 1 120 ? 26.615 11.663  15.272 1.00 16.25 ? 126 THR   A CG2 1 
ATOM   931  N  N   . GLY   A 1 121 ? 28.006 9.382   11.595 1.00 15.16 ? 127 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 121 ? 28.874 8.462   10.900 1.00 16.72 ? 127 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 121 ? 29.906 9.163   10.070 1.00 18.23 ? 127 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 121 ? 29.899 10.394  9.959  1.00 18.91 ? 127 GLY   A O   1 
ATOM   935  N  N   . GLY   A 1 122 ? 30.714 8.356   9.422  1.00 18.50 ? 128 GLY   A N   1 
ATOM   936  C  CA  . GLY   A 1 122 ? 31.700 8.870   8.484  1.00 21.63 ? 128 GLY   A CA  1 
ATOM   937  C  C   . GLY   A 1 122 ? 32.962 8.052   8.426  1.00 23.65 ? 128 GLY   A C   1 
ATOM   938  O  O   . GLY   A 1 122 ? 33.479 7.641   9.461  1.00 24.92 ? 128 GLY   A O   1 
ATOM   939  N  N   . ASN   A 1 123 ? 33.502 7.886   7.217  1.00 23.36 ? 129 ASN   A N   1 
ATOM   940  C  CA  . ASN   A 1 123 ? 34.770 7.208   6.927  1.00 22.51 ? 129 ASN   A CA  1 
ATOM   941  C  C   . ASN   A 1 123 ? 35.029 5.916   7.688  1.00 21.26 ? 129 ASN   A C   1 
ATOM   942  O  O   . ASN   A 1 123 ? 36.124 5.730   8.257  1.00 21.48 ? 129 ASN   A O   1 
ATOM   943  C  CB  . ASN   A 1 123 ? 35.912 8.202   7.161  1.00 27.06 ? 129 ASN   A CB  1 
ATOM   944  C  CG  . ASN   A 1 123 ? 35.759 9.404   6.293  1.00 35.33 ? 129 ASN   A CG  1 
ATOM   945  O  OD1 . ASN   A 1 123 ? 35.618 9.270   5.086  1.00 38.49 ? 129 ASN   A OD1 1 
ATOM   946  N  ND2 . ASN   A 1 123 ? 35.724 10.599  6.887  1.00 37.31 ? 129 ASN   A ND2 1 
ATOM   947  N  N   . GLY   A 1 124 ? 34.046 5.015   7.683  1.00 19.39 ? 130 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 124 ? 34.187 3.726   8.351  1.00 18.15 ? 130 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 124 ? 33.843 3.747   9.827  1.00 17.44 ? 130 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 124 ? 34.087 2.758   10.519 1.00 18.69 ? 130 GLY   A O   1 
ATOM   951  N  N   . LEU   A 1 125 ? 33.276 4.850   10.327 1.00 15.42 ? 131 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 125 ? 32.743 4.940   11.699 1.00 15.09 ? 131 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 125 ? 31.210 5.041   11.673 1.00 15.00 ? 131 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 125 ? 30.628 5.496   10.692 1.00 15.83 ? 131 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 125 ? 33.263 6.187   12.429 1.00 16.62 ? 131 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 125 ? 34.779 6.198   12.700 1.00 19.40 ? 131 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 125 ? 35.243 7.595   13.109 1.00 20.88 ? 131 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 125 ? 35.152 5.164   13.793 1.00 19.87 ? 131 LEU   A CD2 1 
ATOM   959  N  N   . VAL   A 1 126 ? 30.585 4.651   12.774 1.00 12.52 ? 132 VAL   A N   1 
ATOM   960  C  CA  . VAL   A 1 126 ? 29.145 4.812   12.960 1.00 12.22 ? 132 VAL   A CA  1 
ATOM   961  C  C   . VAL   A 1 126 ? 28.933 5.168   14.429 1.00 13.99 ? 132 VAL   A C   1 
ATOM   962  O  O   . VAL   A 1 126 ? 29.636 4.614   15.287 1.00 15.83 ? 132 VAL   A O   1 
ATOM   963  C  CB  . VAL   A 1 126 ? 28.335 3.589   12.533 1.00 13.04 ? 132 VAL   A CB  1 
ATOM   964  C  CG1 . VAL   A 1 126 ? 28.797 2.309   13.220 1.00 14.82 ? 132 VAL   A CG1 1 
ATOM   965  C  CG2 . VAL   A 1 126 ? 26.834 3.833   12.741 1.00 12.92 ? 132 VAL   A CG2 1 
ATOM   966  N  N   . GLY   A 1 127 ? 28.089 6.167   14.697 1.00 12.84 ? 133 GLY   A N   1 
ATOM   967  C  CA  . GLY   A 1 127 ? 27.849 6.630   16.067 1.00 13.25 ? 133 GLY   A CA  1 
ATOM   968  C  C   . GLY   A 1 127 ? 26.398 6.403   16.444 1.00 13.57 ? 133 GLY   A C   1 
ATOM   969  O  O   . GLY   A 1 127 ? 25.498 6.575   15.608 1.00 14.13 ? 133 GLY   A O   1 
ATOM   970  N  N   . PHE   A 1 128 ? 26.173 5.933   17.672 1.00 13.28 ? 134 PHE   A N   1 
ATOM   971  C  CA  . PHE   A 1 128 ? 24.813 5.614   18.148 1.00 12.93 ? 134 PHE   A CA  1 
ATOM   972  C  C   . PHE   A 1 128 ? 24.442 6.477   19.349 1.00 13.44 ? 134 PHE   A C   1 
ATOM   973  O  O   . PHE   A 1 128 ? 25.215 6.582   20.310 1.00 12.98 ? 134 PHE   A O   1 
ATOM   974  C  CB  . PHE   A 1 128 ? 24.733 4.140   18.609 1.00 12.59 ? 134 PHE   A CB  1 
ATOM   975  C  CG  . PHE   A 1 128 ? 25.246 3.131   17.598 1.00 12.68 ? 134 PHE   A CG  1 
ATOM   976  C  CD1 . PHE   A 1 128 ? 24.419 2.653   16.599 1.00 12.91 ? 134 PHE   A CD1 1 
ATOM   977  C  CD2 . PHE   A 1 128 ? 26.558 2.678   17.647 1.00 13.16 ? 134 PHE   A CD2 1 
ATOM   978  C  CE1 . PHE   A 1 128 ? 24.888 1.756   15.649 1.00 13.42 ? 134 PHE   A CE1 1 
ATOM   979  C  CE2 . PHE   A 1 128 ? 27.030 1.738   16.704 1.00 13.45 ? 134 PHE   A CE2 1 
ATOM   980  C  CZ  . PHE   A 1 128 ? 26.187 1.306   15.691 1.00 13.37 ? 134 PHE   A CZ  1 
ATOM   981  N  N   . ALA   A 1 129 ? 23.226 7.011   19.335 1.00 12.50 ? 135 ALA   A N   1 
ATOM   982  C  CA  . ALA   A 1 129 ? 22.708 7.774   20.457 1.00 12.96 ? 135 ALA   A CA  1 
ATOM   983  C  C   . ALA   A 1 129 ? 22.188 6.735   21.475 1.00 12.76 ? 135 ALA   A C   1 
ATOM   984  O  O   . ALA   A 1 129 ? 21.271 5.959   21.140 1.00 13.77 ? 135 ALA   A O   1 
ATOM   985  C  CB  . ALA   A 1 129 ? 21.544 8.649   19.978 1.00 12.76 ? 135 ALA   A CB  1 
ATOM   986  N  N   . ASP   A 1 130 ? 22.749 6.721   22.688 1.00 12.23 ? 136 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 130 ? 22.313 5.765   23.722 1.00 13.37 ? 136 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 130 ? 20.949 6.118   24.251 1.00 14.44 ? 136 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 130 ? 20.627 7.309   24.419 1.00 15.17 ? 136 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 130 ? 23.332 5.775   24.882 1.00 15.53 ? 136 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 130 ? 23.052 4.741   25.955 1.00 21.75 ? 136 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 130 ? 22.861 3.586   25.613 1.00 22.97 ? 136 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 130 ? 22.966 5.122   27.141 1.00 25.48 ? 136 ASP   A OD2 1 
ATOM   994  N  N   . VAL   A 1 131 ? 20.123 5.092   24.592 1.00 12.84 ? 137 VAL   A N   1 
ATOM   995  C  CA  . VAL   A 1 131 ? 18.823 5.341   25.226 1.00 13.78 ? 137 VAL   A CA  1 
ATOM   996  C  C   . VAL   A 1 131 ? 18.677 4.560   26.541 1.00 15.14 ? 137 VAL   A C   1 
ATOM   997  O  O   . VAL   A 1 131 ? 17.619 4.634   27.184 1.00 15.95 ? 137 VAL   A O   1 
ATOM   998  C  CB  . VAL   A 1 131 ? 17.599 5.056   24.329 1.00 15.71 ? 137 VAL   A CB  1 
ATOM   999  C  CG1 . VAL   A 1 131 ? 17.649 5.929   23.072 1.00 15.96 ? 137 VAL   A CG1 1 
ATOM   1000 C  CG2 . VAL   A 1 131 ? 17.523 3.571   23.968 1.00 15.27 ? 137 VAL   A CG2 1 
ATOM   1001 N  N   . ARG   A 1 132 ? 19.718 3.805   26.956 1.00 15.51 ? 138 ARG   A N   1 
ATOM   1002 C  CA  . ARG   A 1 132 ? 19.626 2.952   28.132 1.00 14.09 ? 138 ARG   A CA  1 
ATOM   1003 C  C   . ARG   A 1 132 ? 19.475 3.682   29.443 1.00 16.11 ? 138 ARG   A C   1 
ATOM   1004 O  O   . ARG   A 1 132 ? 18.967 3.095   30.405 1.00 16.91 ? 138 ARG   A O   1 
ATOM   1005 C  CB  . ARG   A 1 132 ? 20.836 1.992   28.198 1.00 14.60 ? 138 ARG   A CB  1 
ATOM   1006 C  CG  . ARG   A 1 132 ? 20.928 1.038   27.004 1.00 14.54 ? 138 ARG   A CG  1 
ATOM   1007 C  CD  . ARG   A 1 132 ? 22.196 0.222   27.132 1.00 15.21 ? 138 ARG   A CD  1 
ATOM   1008 N  NE  . ARG   A 1 132 ? 23.338 1.038   26.800 1.00 15.43 ? 138 ARG   A NE  1 
ATOM   1009 C  CZ  . ARG   A 1 132 ? 24.593 0.591   26.718 1.00 16.44 ? 138 ARG   A CZ  1 
ATOM   1010 N  NH1 . ARG   A 1 132 ? 24.869 -0.697  26.943 1.00 15.57 ? 138 ARG   A NH1 1 
ATOM   1011 N  NH2 . ARG   A 1 132 ? 25.562 1.403   26.321 1.00 16.62 ? 138 ARG   A NH2 1 
ATOM   1012 N  N   . ASP   A 1 133 ? 19.853 4.972   29.486 1.00 15.94 ? 139 ASP   A N   1 
ATOM   1013 C  CA  . ASP   A 1 133 ? 19.670 5.749   30.729 1.00 16.85 ? 139 ASP   A CA  1 
ATOM   1014 C  C   . ASP   A 1 133 ? 18.282 6.365   30.863 1.00 17.35 ? 139 ASP   A C   1 
ATOM   1015 O  O   . ASP   A 1 133 ? 17.963 6.886   31.927 1.00 17.04 ? 139 ASP   A O   1 
ATOM   1016 C  CB  . ASP   A 1 133 ? 20.716 6.865   30.816 1.00 18.85 ? 139 ASP   A CB  1 
ATOM   1017 C  CG  . ASP   A 1 133 ? 20.581 7.880   29.708 1.00 22.53 ? 139 ASP   A CG  1 
ATOM   1018 O  OD1 . ASP   A 1 133 ? 20.429 7.463   28.531 1.00 23.27 ? 139 ASP   A OD1 1 
ATOM   1019 O  OD2 . ASP   A 1 133 ? 20.601 9.106   30.011 1.00 26.20 ? 139 ASP   A OD2 1 
ATOM   1020 N  N   . LEU   A 1 134 ? 17.445 6.295   29.820 1.00 16.96 ? 140 LEU   A N   1 
ATOM   1021 C  CA  . LEU   A 1 134 ? 16.098 6.883   29.873 1.00 15.82 ? 140 LEU   A CA  1 
ATOM   1022 C  C   . LEU   A 1 134 ? 15.126 5.896   30.524 1.00 15.95 ? 140 LEU   A C   1 
ATOM   1023 O  O   . LEU   A 1 134 ? 14.364 5.195   29.855 1.00 15.82 ? 140 LEU   A O   1 
ATOM   1024 C  CB  . LEU   A 1 134 ? 15.665 7.256   28.446 1.00 16.05 ? 140 LEU   A CB  1 
ATOM   1025 C  CG  . LEU   A 1 134 ? 16.650 8.199   27.709 1.00 19.12 ? 140 LEU   A CG  1 
ATOM   1026 C  CD1 . LEU   A 1 134 ? 16.188 8.421   26.247 1.00 19.73 ? 140 LEU   A CD1 1 
ATOM   1027 C  CD2 . LEU   A 1 134 ? 16.831 9.530   28.497 1.00 19.56 ? 140 LEU   A CD2 1 
ATOM   1028 N  N   . LEU   A 1 135 ? 15.185 5.812   31.864 1.00 16.59 ? 141 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 135 ? 14.430 4.788   32.583 1.00 17.14 ? 141 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 135 ? 12.924 4.942   32.478 1.00 17.95 ? 141 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 135 ? 12.188 3.948   32.529 1.00 19.44 ? 141 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 135 ? 14.860 4.754   34.044 1.00 17.43 ? 141 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 135 ? 16.370 4.690   34.298 1.00 18.43 ? 141 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 135 ? 16.635 4.474   35.821 1.00 19.46 ? 141 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 135 ? 17.070 3.585   33.457 1.00 19.54 ? 141 LEU   A CD2 1 
ATOM   1036 N  N   . TRP   A 1 136 ? 12.469 6.206   32.305 1.00 17.90 ? 142 TRP   A N   1 
ATOM   1037 C  CA  . TRP   A 1 136 ? 11.044 6.498   32.188 1.00 18.71 ? 142 TRP   A CA  1 
ATOM   1038 C  C   . TRP   A 1 136 ? 10.394 5.931   30.920 1.00 19.34 ? 142 TRP   A C   1 
ATOM   1039 O  O   . TRP   A 1 136 ? 9.146  5.905   30.836 1.00 20.57 ? 142 TRP   A O   1 
ATOM   1040 C  CB  . TRP   A 1 136 ? 10.814 8.021   32.298 1.00 18.78 ? 142 TRP   A CB  1 
ATOM   1041 C  CG  . TRP   A 1 136 ? 11.651 8.850   31.353 1.00 19.08 ? 142 TRP   A CG  1 
ATOM   1042 C  CD1 . TRP   A 1 136 ? 12.895 9.357   31.582 1.00 19.33 ? 142 TRP   A CD1 1 
ATOM   1043 C  CD2 . TRP   A 1 136 ? 11.328 9.190   30.000 1.00 19.30 ? 142 TRP   A CD2 1 
ATOM   1044 N  NE1 . TRP   A 1 136 ? 13.331 10.060  30.480 1.00 19.50 ? 142 TRP   A NE1 1 
ATOM   1045 C  CE2 . TRP   A 1 136 ? 12.367 10.008  29.511 1.00 19.42 ? 142 TRP   A CE2 1 
ATOM   1046 C  CE3 . TRP   A 1 136 ? 10.213 8.962   29.192 1.00 19.91 ? 142 TRP   A CE3 1 
ATOM   1047 C  CZ2 . TRP   A 1 136 ? 12.366 10.524  28.209 1.00 19.45 ? 142 TRP   A CZ2 1 
ATOM   1048 C  CZ3 . TRP   A 1 136 ? 10.171 9.541   27.937 1.00 20.06 ? 142 TRP   A CZ3 1 
ATOM   1049 C  CH2 . TRP   A 1 136 ? 11.230 10.331  27.469 1.00 19.72 ? 142 TRP   A CH2 1 
ATOM   1050 N  N   . LEU   A 1 137 ? 11.200 5.473   29.930 1.00 18.71 ? 143 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 137 ? 10.596 4.905   28.709 1.00 20.27 ? 143 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 137 ? 9.757  3.653   29.016 1.00 24.45 ? 143 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 137 ? 8.828  3.361   28.272 1.00 24.34 ? 143 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 137 ? 11.670 4.543   27.675 1.00 18.76 ? 143 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 137 ? 12.330 5.702   26.935 1.00 19.13 ? 143 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 137 ? 13.472 5.183   26.058 1.00 20.67 ? 143 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 137 ? 11.328 6.473   26.057 1.00 19.40 ? 143 LEU   A CD2 1 
ATOM   1058 N  N   . ASP   A 1 138 ? 10.119 2.926   30.107 1.00 28.00 ? 144 ASP   A N   1 
ATOM   1059 C  CA  . ASP   A 1 138 ? 9.575  1.669   30.624 1.00 32.90 ? 144 ASP   A CA  1 
ATOM   1060 C  C   . ASP   A 1 138 ? 8.322  1.791   31.431 1.00 37.14 ? 144 ASP   A C   1 
ATOM   1061 O  O   . ASP   A 1 138 ? 7.784  0.749   31.800 1.00 38.29 ? 144 ASP   A O   1 
ATOM   1062 C  CB  . ASP   A 1 138 ? 10.578 1.071   31.628 1.00 36.02 ? 144 ASP   A CB  1 
ATOM   1063 C  CG  . ASP   A 1 138 ? 11.760 0.389   31.043 1.00 43.11 ? 144 ASP   A CG  1 
ATOM   1064 O  OD1 . ASP   A 1 138 ? 11.712 0.062   29.839 1.00 44.19 ? 144 ASP   A OD1 1 
ATOM   1065 O  OD2 . ASP   A 1 138 ? 12.749 0.154   31.799 1.00 47.78 ? 144 ASP   A OD2 1 
ATOM   1066 N  N   . GLU   A 1 139 ? 7.952  2.988   31.866 1.00 39.35 ? 145 GLU   A N   1 
ATOM   1067 C  CA  . GLU   A 1 139 ? 6.753  3.155   32.685 1.00 43.00 ? 145 GLU   A CA  1 
ATOM   1068 C  C   . GLU   A 1 139 ? 5.840  4.206   32.081 1.00 44.90 ? 145 GLU   A C   1 
ATOM   1069 O  O   . GLU   A 1 139 ? 5.688  4.229   30.859 1.00 46.23 ? 145 GLU   A O   1 
ATOM   1070 C  CB  . GLU   A 1 139 ? 7.096  3.460   34.160 1.00 46.40 ? 145 GLU   A CB  1 
ATOM   1071 C  CG  . GLU   A 1 139 ? 8.256  4.417   34.362 1.00 53.00 ? 145 GLU   A CG  1 
ATOM   1072 C  CD  . GLU   A 1 139 ? 9.520  3.747   34.864 1.00 62.38 ? 145 GLU   A CD  1 
ATOM   1073 O  OE1 . GLU   A 1 139 ? 10.332 4.427   35.534 1.00 64.20 ? 145 GLU   A OE1 1 
ATOM   1074 O  OE2 . GLU   A 1 139 ? 9.696  2.536   34.593 1.00 64.91 ? 145 GLU   A OE2 1 
ATOM   1075 N  N   . SER   B 1 1   ? 19.696 -24.686 23.881 1.00 27.06 ? 7   SER   C N   1 
ATOM   1076 C  CA  . SER   B 1 1   ? 20.792 -24.494 22.918 1.00 27.39 ? 7   SER   C CA  1 
ATOM   1077 C  C   . SER   B 1 1   ? 20.844 -25.651 21.894 1.00 26.23 ? 7   SER   C C   1 
ATOM   1078 O  O   . SER   B 1 1   ? 20.197 -26.687 22.117 1.00 26.23 ? 7   SER   C O   1 
ATOM   1079 C  CB  . SER   B 1 1   ? 22.118 -24.399 23.677 1.00 30.73 ? 7   SER   C CB  1 
ATOM   1080 O  OG  . SER   B 1 1   ? 22.348 -25.606 24.383 1.00 35.32 ? 7   SER   C OG  1 
ATOM   1081 N  N   . GLY   B 1 2   ? 21.611 -25.481 20.805 1.00 23.39 ? 8   GLY   C N   1 
ATOM   1082 C  CA  . GLY   B 1 2   ? 21.778 -26.532 19.802 1.00 22.18 ? 8   GLY   C CA  1 
ATOM   1083 C  C   . GLY   B 1 2   ? 22.051 -25.986 18.413 1.00 21.21 ? 8   GLY   C C   1 
ATOM   1084 O  O   . GLY   B 1 2   ? 21.744 -24.823 18.135 1.00 22.44 ? 8   GLY   C O   1 
ATOM   1085 N  N   . ALA   B 1 3   ? 22.695 -26.771 17.549 1.00 19.24 ? 9   ALA   C N   1 
ATOM   1086 C  CA  . ALA   B 1 3   ? 23.014 -26.297 16.179 1.00 18.90 ? 9   ALA   C CA  1 
ATOM   1087 C  C   . ALA   B 1 3   ? 22.945 -27.451 15.190 1.00 18.78 ? 9   ALA   C C   1 
ATOM   1088 O  O   . ALA   B 1 3   ? 23.068 -28.626 15.582 1.00 20.02 ? 9   ALA   C O   1 
ATOM   1089 C  CB  . ALA   B 1 3   ? 24.425 -25.689 16.140 1.00 19.63 ? 9   ALA   C CB  1 
ATOM   1090 N  N   . ILE   B 1 4   ? 22.786 -27.121 13.895 1.00 17.86 ? 10  ILE   C N   1 
ATOM   1091 C  CA  . ILE   B 1 4   ? 22.880 -28.105 12.826 1.00 17.26 ? 10  ILE   C CA  1 
ATOM   1092 C  C   . ILE   B 1 4   ? 24.241 -27.893 12.144 1.00 18.42 ? 10  ILE   C C   1 
ATOM   1093 O  O   . ILE   B 1 4   ? 24.592 -26.758 11.820 1.00 18.34 ? 10  ILE   C O   1 
ATOM   1094 C  CB  . ILE   B 1 4   ? 21.755 -27.860 11.796 1.00 17.13 ? 10  ILE   C CB  1 
ATOM   1095 C  CG1 . ILE   B 1 4   ? 20.379 -27.895 12.478 1.00 17.96 ? 10  ILE   C CG1 1 
ATOM   1096 C  CG2 . ILE   B 1 4   ? 21.857 -28.871 10.637 1.00 17.70 ? 10  ILE   C CG2 1 
ATOM   1097 C  CD1 . ILE   B 1 4   ? 19.248 -27.282 11.574 1.00 18.43 ? 10  ILE   C CD1 1 
ATOM   1098 N  N   . TYR   B 1 5   ? 25.010 -28.986 11.896 1.00 18.86 ? 11  TYR   C N   1 
ATOM   1099 C  CA  . TYR   B 1 5   ? 26.301 -28.892 11.234 1.00 20.41 ? 11  TYR   C CA  1 
ATOM   1100 C  C   . TYR   B 1 5   ? 26.188 -29.617 9.913  1.00 22.20 ? 11  TYR   C C   1 
ATOM   1101 O  O   . TYR   B 1 5   ? 26.036 -30.841 9.905  1.00 22.94 ? 11  TYR   C O   1 
ATOM   1102 C  CB  . TYR   B 1 5   ? 27.392 -29.553 12.108 1.00 21.20 ? 11  TYR   C CB  1 
ATOM   1103 C  CG  . TYR   B 1 5   ? 27.635 -28.767 13.384 1.00 22.31 ? 11  TYR   C CG  1 
ATOM   1104 C  CD1 . TYR   B 1 5   ? 28.541 -27.716 13.414 1.00 23.49 ? 11  TYR   C CD1 1 
ATOM   1105 C  CD2 . TYR   B 1 5   ? 26.933 -29.053 14.546 1.00 24.31 ? 11  TYR   C CD2 1 
ATOM   1106 C  CE1 . TYR   B 1 5   ? 28.735 -26.959 14.573 1.00 25.24 ? 11  TYR   C CE1 1 
ATOM   1107 C  CE2 . TYR   B 1 5   ? 27.105 -28.289 15.705 1.00 25.81 ? 11  TYR   C CE2 1 
ATOM   1108 C  CZ  . TYR   B 1 5   ? 28.018 -27.254 15.717 1.00 26.62 ? 11  TYR   C CZ  1 
ATOM   1109 O  OH  . TYR   B 1 5   ? 28.158 -26.500 16.858 1.00 29.40 ? 11  TYR   C OH  1 
ATOM   1110 N  N   . VAL   B 1 6   ? 26.269 -28.891 8.794  1.00 21.90 ? 12  VAL   C N   1 
ATOM   1111 C  CA  . VAL   B 1 6   ? 26.159 -29.477 7.463  1.00 22.36 ? 12  VAL   C CA  1 
ATOM   1112 C  C   . VAL   B 1 6   ? 27.245 -28.889 6.564  1.00 23.87 ? 12  VAL   C C   1 
ATOM   1113 O  O   . VAL   B 1 6   ? 27.364 -27.676 6.447  1.00 23.43 ? 12  VAL   C O   1 
ATOM   1114 C  CB  . VAL   B 1 6   ? 24.721 -29.306 6.886  1.00 23.60 ? 12  VAL   C CB  1 
ATOM   1115 C  CG1 . VAL   B 1 6   ? 24.255 -27.865 6.986  1.00 23.25 ? 12  VAL   C CG1 1 
ATOM   1116 C  CG2 . VAL   B 1 6   ? 24.664 -29.828 5.458  1.00 24.62 ? 12  VAL   C CG2 1 
ATOM   1117 N  N   . GLY   B 1 7   ? 28.163 -29.736 6.071  1.00 25.14 ? 13  GLY   C N   1 
ATOM   1118 C  CA  . GLY   B 1 7   ? 29.283 -29.263 5.263  1.00 26.39 ? 13  GLY   C CA  1 
ATOM   1119 C  C   . GLY   B 1 7   ? 30.146 -28.290 6.041  1.00 26.77 ? 13  GLY   C C   1 
ATOM   1120 O  O   . GLY   B 1 7   ? 30.498 -28.566 7.198  1.00 26.92 ? 13  GLY   C O   1 
ATOM   1121 N  N   . ASN   B 1 8   ? 30.410 -27.108 5.461  1.00 26.15 ? 14  ASN   C N   1 
ATOM   1122 C  CA  . ASN   B 1 8   ? 31.181 -26.116 6.199  1.00 26.32 ? 14  ASN   C CA  1 
ATOM   1123 C  C   . ASN   B 1 8   ? 30.282 -25.039 6.796  1.00 24.22 ? 14  ASN   C C   1 
ATOM   1124 O  O   . ASN   B 1 8   ? 30.703 -23.889 6.923  1.00 24.81 ? 14  ASN   C O   1 
ATOM   1125 C  CB  . ASN   B 1 8   ? 32.294 -25.512 5.366  1.00 29.93 ? 14  ASN   C CB  1 
ATOM   1126 C  CG  . ASN   B 1 8   ? 33.361 -26.523 5.008  1.00 37.57 ? 14  ASN   C CG  1 
ATOM   1127 O  OD1 . ASN   B 1 8   ? 34.055 -27.072 5.874  1.00 39.52 ? 14  ASN   C OD1 1 
ATOM   1128 N  ND2 . ASN   B 1 8   ? 33.496 -26.799 3.719  1.00 39.17 ? 14  ASN   C ND2 1 
ATOM   1129 N  N   . TYR   B 1 9   ? 29.060 -25.417 7.176  1.00 21.95 ? 15  TYR   C N   1 
ATOM   1130 C  CA  . TYR   B 1 9   ? 28.100 -24.473 7.763  1.00 20.09 ? 15  TYR   C CA  1 
ATOM   1131 C  C   . TYR   B 1 9   ? 27.623 -24.946 9.125  1.00 19.89 ? 15  TYR   C C   1 
ATOM   1132 O  O   . TYR   B 1 9   ? 27.465 -26.149 9.354  1.00 20.54 ? 15  TYR   C O   1 
ATOM   1133 C  CB  . TYR   B 1 9   ? 26.849 -24.364 6.867  1.00 19.75 ? 15  TYR   C CB  1 
ATOM   1134 C  CG  . TYR   B 1 9   ? 27.097 -23.777 5.493  1.00 21.35 ? 15  TYR   C CG  1 
ATOM   1135 C  CD1 . TYR   B 1 9   ? 27.768 -22.571 5.342  1.00 23.56 ? 15  TYR   C CD1 1 
ATOM   1136 C  CD2 . TYR   B 1 9   ? 26.697 -24.454 4.343  1.00 23.03 ? 15  TYR   C CD2 1 
ATOM   1137 C  CE1 . TYR   B 1 9   ? 28.022 -22.043 4.082  1.00 24.78 ? 15  TYR   C CE1 1 
ATOM   1138 C  CE2 . TYR   B 1 9   ? 26.929 -23.927 3.080  1.00 24.18 ? 15  TYR   C CE2 1 
ATOM   1139 C  CZ  . TYR   B 1 9   ? 27.576 -22.714 2.954  1.00 25.77 ? 15  TYR   C CZ  1 
ATOM   1140 O  OH  . TYR   B 1 9   ? 27.760 -22.175 1.701  1.00 28.51 ? 15  TYR   C OH  1 
ATOM   1141 N  N   . ARG   B 1 10  ? 27.276 -23.963 10.002 1.00 17.97 ? 16  ARG   C N   1 
ATOM   1142 C  CA  . ARG   B 1 10  ? 26.686 -24.209 11.326 1.00 17.59 ? 16  ARG   C CA  1 
ATOM   1143 C  C   . ARG   B 1 10  ? 25.396 -23.375 11.350 1.00 17.12 ? 16  ARG   C C   1 
ATOM   1144 O  O   . ARG   B 1 10  ? 25.449 -22.182 11.063 1.00 18.00 ? 16  ARG   C O   1 
ATOM   1145 C  CB  . ARG   B 1 10  ? 27.651 -23.779 12.436 1.00 19.22 ? 16  ARG   C CB  1 
ATOM   1146 C  CG  . ARG   B 1 10  ? 27.028 -23.559 13.812 1.00 19.23 ? 16  ARG   C CG  1 
ATOM   1147 C  CD  . ARG   B 1 10  ? 28.102 -23.261 14.855 1.00 20.67 ? 16  ARG   C CD  1 
ATOM   1148 N  NE  . ARG   B 1 10  ? 27.686 -22.248 15.825 1.00 24.38 ? 16  ARG   C NE  1 
ATOM   1149 C  CZ  . ARG   B 1 10  ? 27.433 -22.493 17.103 1.00 28.02 ? 16  ARG   C CZ  1 
ATOM   1150 N  NH1 . ARG   B 1 10  ? 27.520 -23.735 17.579 1.00 27.08 ? 16  ARG   C NH1 1 
ATOM   1151 N  NH2 . ARG   B 1 10  ? 27.059 -21.503 17.917 1.00 27.26 ? 16  ARG   C NH2 1 
ATOM   1152 N  N   . VAL   B 1 11  ? 24.239 -24.008 11.627 1.00 16.58 ? 17  VAL   C N   1 
ATOM   1153 C  CA  . VAL   B 1 11  ? 22.936 -23.315 11.635 1.00 16.20 ? 17  VAL   C CA  1 
ATOM   1154 C  C   . VAL   B 1 11  ? 22.499 -23.190 13.084 1.00 15.72 ? 17  VAL   C C   1 
ATOM   1155 O  O   . VAL   B 1 11  ? 22.393 -24.208 13.772 1.00 16.23 ? 17  VAL   C O   1 
ATOM   1156 C  CB  . VAL   B 1 11  ? 21.849 -24.083 10.826 1.00 17.39 ? 17  VAL   C CB  1 
ATOM   1157 C  CG1 . VAL   B 1 11  ? 20.564 -23.250 10.736 1.00 18.05 ? 17  VAL   C CG1 1 
ATOM   1158 C  CG2 . VAL   B 1 11  ? 22.355 -24.451 9.438  1.00 18.03 ? 17  VAL   C CG2 1 
ATOM   1159 N  N   . VAL   B 1 12  ? 22.220 -21.968 13.561 1.00 14.12 ? 18  VAL   C N   1 
ATOM   1160 C  CA  . VAL   B 1 12  ? 21.823 -21.768 14.963 1.00 15.55 ? 18  VAL   C CA  1 
ATOM   1161 C  C   . VAL   B 1 12  ? 20.619 -20.832 15.023 1.00 14.54 ? 18  VAL   C C   1 
ATOM   1162 O  O   . VAL   B 1 12  ? 20.326 -20.109 14.055 1.00 14.45 ? 18  VAL   C O   1 
ATOM   1163 C  CB  . VAL   B 1 12  ? 23.008 -21.158 15.800 1.00 16.60 ? 18  VAL   C CB  1 
ATOM   1164 C  CG1 . VAL   B 1 12  ? 24.154 -22.155 15.890 1.00 18.99 ? 18  VAL   C CG1 1 
ATOM   1165 C  CG2 . VAL   B 1 12  ? 23.498 -19.841 15.196 1.00 16.11 ? 18  VAL   C CG2 1 
ATOM   1166 N  N   . ASN   B 1 13  ? 19.952 -20.753 16.193 1.00 14.00 ? 19  ASN   C N   1 
ATOM   1167 C  CA  . ASN   B 1 13  ? 18.932 -19.705 16.385 1.00 14.19 ? 19  ASN   C CA  1 
ATOM   1168 C  C   . ASN   B 1 13  ? 19.697 -18.348 16.340 1.00 14.57 ? 19  ASN   C C   1 
ATOM   1169 O  O   . ASN   B 1 13  ? 20.731 -18.195 17.017 1.00 14.89 ? 19  ASN   C O   1 
ATOM   1170 C  CB  . ASN   B 1 13  ? 18.321 -19.835 17.778 1.00 15.36 ? 19  ASN   C CB  1 
ATOM   1171 C  CG  . ASN   B 1 13  ? 17.490 -21.074 17.929 1.00 16.84 ? 19  ASN   C CG  1 
ATOM   1172 O  OD1 . ASN   B 1 13  ? 17.969 -22.126 18.396 1.00 16.82 ? 19  ASN   C OD1 1 
ATOM   1173 N  ND2 . ASN   B 1 13  ? 16.218 -20.966 17.549 1.00 14.92 ? 19  ASN   C ND2 1 
ATOM   1174 N  N   . ARG   B 1 14  ? 19.208 -17.406 15.543 1.00 14.35 ? 20  ARG   C N   1 
ATOM   1175 C  CA  . ARG   B 1 14  ? 19.869 -16.090 15.434 1.00 14.34 ? 20  ARG   C CA  1 
ATOM   1176 C  C   . ARG   B 1 14  ? 20.022 -15.400 16.814 1.00 13.75 ? 20  ARG   C C   1 
ATOM   1177 O  O   . ARG   B 1 14  ? 21.083 -14.866 17.091 1.00 14.81 ? 20  ARG   C O   1 
ATOM   1178 C  CB  . ARG   B 1 14  ? 19.107 -15.202 14.445 1.00 15.84 ? 20  ARG   C CB  1 
ATOM   1179 C  CG  . ARG   B 1 14  ? 19.833 -13.898 14.047 1.00 18.05 ? 20  ARG   C CG  1 
ATOM   1180 C  CD  . ARG   B 1 14  ? 18.844 -13.003 13.330 1.00 19.42 ? 20  ARG   C CD  1 
ATOM   1181 N  NE  . ARG   B 1 14  ? 19.394 -11.741 12.783 1.00 19.22 ? 20  ARG   C NE  1 
ATOM   1182 C  CZ  . ARG   B 1 14  ? 19.472 -10.605 13.460 1.00 19.41 ? 20  ARG   C CZ  1 
ATOM   1183 N  NH1 . ARG   B 1 14  ? 19.160 -10.570 14.750 1.00 18.88 ? 20  ARG   C NH1 1 
ATOM   1184 N  NH2 . ARG   B 1 14  ? 19.906 -9.493  12.862 1.00 19.33 ? 20  ARG   C NH2 1 
ATOM   1185 N  N   . HIS   B 1 15  ? 19.005 -15.531 17.688 1.00 14.10 ? 21  HIS   C N   1 
ATOM   1186 C  CA  . HIS   B 1 15  ? 19.074 -14.901 19.003 1.00 14.76 ? 21  HIS   C CA  1 
ATOM   1187 C  C   . HIS   B 1 15  ? 20.109 -15.526 19.945 1.00 15.26 ? 21  HIS   C C   1 
ATOM   1188 O  O   . HIS   B 1 15  ? 20.447 -14.902 20.970 1.00 16.52 ? 21  HIS   C O   1 
ATOM   1189 C  CB  . HIS   B 1 15  ? 17.691 -14.805 19.659 1.00 14.64 ? 21  HIS   C CB  1 
ATOM   1190 C  CG  . HIS   B 1 15  ? 17.120 -16.067 20.223 1.00 15.63 ? 21  HIS   C CG  1 
ATOM   1191 N  ND1 . HIS   B 1 15  ? 16.437 -16.970 19.420 1.00 16.09 ? 21  HIS   C ND1 1 
ATOM   1192 C  CD2 . HIS   B 1 15  ? 17.059 -16.478 21.508 1.00 17.06 ? 21  HIS   C CD2 1 
ATOM   1193 C  CE1 . HIS   B 1 15  ? 16.014 -17.937 20.239 1.00 17.11 ? 21  HIS   C CE1 1 
ATOM   1194 N  NE2 . HIS   B 1 15  ? 16.372 -17.684 21.508 1.00 18.35 ? 21  HIS   C NE2 1 
ATOM   1195 N  N   . LEU   B 1 16  ? 20.612 -16.741 19.607 1.00 15.39 ? 22  LEU   C N   1 
ATOM   1196 C  CA  . LEU   B 1 16  ? 21.630 -17.390 20.446 1.00 16.68 ? 22  LEU   C CA  1 
ATOM   1197 C  C   . LEU   B 1 16  ? 23.002 -17.421 19.754 1.00 17.93 ? 22  LEU   C C   1 
ATOM   1198 O  O   . LEU   B 1 16  ? 23.925 -18.029 20.298 1.00 19.34 ? 22  LEU   C O   1 
ATOM   1199 C  CB  . LEU   B 1 16  ? 21.193 -18.835 20.756 1.00 16.59 ? 22  LEU   C CB  1 
ATOM   1200 C  CG  . LEU   B 1 16  ? 19.850 -18.945 21.523 1.00 17.55 ? 22  LEU   C CG  1 
ATOM   1201 C  CD1 . LEU   B 1 16  ? 19.511 -20.420 21.767 1.00 18.07 ? 22  LEU   C CD1 1 
ATOM   1202 C  CD2 . LEU   B 1 16  ? 19.926 -18.205 22.903 1.00 18.53 ? 22  LEU   C CD2 1 
ATOM   1203 N  N   . ALA   B 1 17  ? 23.154 -16.742 18.588 1.00 16.39 ? 23  ALA   C N   1 
ATOM   1204 C  CA  . ALA   B 1 17  ? 24.458 -16.760 17.888 1.00 17.43 ? 23  ALA   C CA  1 
ATOM   1205 C  C   . ALA   B 1 17  ? 25.534 -16.112 18.744 1.00 18.07 ? 23  ALA   C C   1 
ATOM   1206 O  O   . ALA   B 1 17  ? 25.263 -15.153 19.469 1.00 18.55 ? 23  ALA   C O   1 
ATOM   1207 C  CB  . ALA   B 1 17  ? 24.343 -16.045 16.550 1.00 17.19 ? 23  ALA   C CB  1 
ATOM   1208 N  N   . THR   B 1 18  ? 26.746 -16.624 18.650 1.00 18.22 ? 24  THR   C N   1 
ATOM   1209 C  CA  . THR   B 1 18  ? 27.867 -16.123 19.437 1.00 18.75 ? 24  THR   C CA  1 
ATOM   1210 C  C   . THR   B 1 18  ? 28.610 -15.013 18.696 1.00 18.54 ? 24  THR   C C   1 
ATOM   1211 O  O   . THR   B 1 18  ? 28.382 -14.810 17.497 1.00 19.05 ? 24  THR   C O   1 
ATOM   1212 C  CB  . THR   B 1 18  ? 28.832 -17.305 19.761 1.00 19.89 ? 24  THR   C CB  1 
ATOM   1213 O  OG1 . THR   B 1 18  ? 29.436 -17.748 18.538 1.00 21.18 ? 24  THR   C OG1 1 
ATOM   1214 C  CG2 . THR   B 1 18  ? 28.141 -18.460 20.466 1.00 20.07 ? 24  THR   C CG2 1 
ATOM   1215 N  N   . HIS   B 1 19  ? 29.604 -14.351 19.365 1.00 19.27 ? 25  HIS   C N   1 
ATOM   1216 C  CA  . HIS   B 1 19  ? 30.411 -13.367 18.654 1.00 20.83 ? 25  HIS   C CA  1 
ATOM   1217 C  C   . HIS   B 1 19  ? 31.163 -14.063 17.463 1.00 20.27 ? 25  HIS   C C   1 
ATOM   1218 O  O   . HIS   B 1 19  ? 31.322 -13.465 16.388 1.00 20.29 ? 25  HIS   C O   1 
ATOM   1219 C  CB  . HIS   B 1 19  ? 31.395 -12.688 19.641 1.00 24.64 ? 25  HIS   C CB  1 
ATOM   1220 C  CG  . HIS   B 1 19  ? 32.622 -13.472 19.916 1.00 31.22 ? 25  HIS   C CG  1 
ATOM   1221 N  ND1 . HIS   B 1 19  ? 33.773 -13.300 19.154 1.00 34.80 ? 25  HIS   C ND1 1 
ATOM   1222 C  CD2 . HIS   B 1 19  ? 32.855 -14.426 20.843 1.00 34.05 ? 25  HIS   C CD2 1 
ATOM   1223 C  CE1 . HIS   B 1 19  ? 34.666 -14.153 19.636 1.00 35.02 ? 25  HIS   C CE1 1 
ATOM   1224 N  NE2 . HIS   B 1 19  ? 34.162 -14.878 20.632 1.00 35.13 ? 25  HIS   C NE2 1 
ATOM   1225 N  N   . ASN   B 1 20  ? 31.567 -15.344 17.649 1.00 19.72 ? 26  ASN   C N   1 
ATOM   1226 C  CA  . ASN   B 1 20  ? 32.256 -16.090 16.588 1.00 21.49 ? 26  ASN   C CA  1 
ATOM   1227 C  C   . ASN   B 1 20  ? 31.319 -16.380 15.413 1.00 20.37 ? 26  ASN   C C   1 
ATOM   1228 O  O   . ASN   B 1 20  ? 31.743 -16.289 14.260 1.00 20.68 ? 26  ASN   C O   1 
ATOM   1229 C  CB  . ASN   B 1 20  ? 32.884 -17.361 17.136 1.00 25.46 ? 26  ASN   C CB  1 
ATOM   1230 C  CG  . ASN   B 1 20  ? 33.759 -18.080 16.151 1.00 33.42 ? 26  ASN   C CG  1 
ATOM   1231 O  OD1 . ASN   B 1 20  ? 34.810 -17.572 15.739 1.00 36.25 ? 26  ASN   C OD1 1 
ATOM   1232 N  ND2 . ASN   B 1 20  ? 33.380 -19.310 15.803 1.00 35.52 ? 26  ASN   C ND2 1 
ATOM   1233 N  N   . ASP   B 1 21  ? 30.023 -16.676 15.676 1.00 20.09 ? 27  ASP   C N   1 
ATOM   1234 C  CA  . ASP   B 1 21  ? 29.072 -16.879 14.576 1.00 18.98 ? 27  ASP   C CA  1 
ATOM   1235 C  C   . ASP   B 1 21  ? 28.942 -15.587 13.750 1.00 19.51 ? 27  ASP   C C   1 
ATOM   1236 O  O   . ASP   B 1 21  ? 28.943 -15.631 12.525 1.00 20.49 ? 27  ASP   C O   1 
ATOM   1237 C  CB  . ASP   B 1 21  ? 27.686 -17.259 15.137 1.00 17.52 ? 27  ASP   C CB  1 
ATOM   1238 C  CG  . ASP   B 1 21  ? 27.585 -18.681 15.674 1.00 19.01 ? 27  ASP   C CG  1 
ATOM   1239 O  OD1 . ASP   B 1 21  ? 28.056 -19.618 14.981 1.00 21.58 ? 27  ASP   C OD1 1 
ATOM   1240 O  OD2 . ASP   B 1 21  ? 27.014 -18.857 16.784 1.00 18.94 ? 27  ASP   C OD2 1 
ATOM   1241 N  N   . TRP   B 1 22  ? 28.822 -14.436 14.424 1.00 19.19 ? 28  TRP   C N   1 
ATOM   1242 C  CA  . TRP   B 1 22  ? 28.693 -13.154 13.715 1.00 19.38 ? 28  TRP   C CA  1 
ATOM   1243 C  C   . TRP   B 1 22  ? 29.974 -12.748 12.974 1.00 20.03 ? 28  TRP   C C   1 
ATOM   1244 O  O   . TRP   B 1 22  ? 29.894 -12.163 11.889 1.00 21.21 ? 28  TRP   C O   1 
ATOM   1245 C  CB  . TRP   B 1 22  ? 28.265 -12.048 14.684 1.00 19.65 ? 28  TRP   C CB  1 
ATOM   1246 C  CG  . TRP   B 1 22  ? 26.779 -12.024 14.934 1.00 19.34 ? 28  TRP   C CG  1 
ATOM   1247 C  CD1 . TRP   B 1 22  ? 26.111 -12.508 16.022 1.00 19.52 ? 28  TRP   C CD1 1 
ATOM   1248 C  CD2 . TRP   B 1 22  ? 25.786 -11.469 14.058 1.00 18.75 ? 28  TRP   C CD2 1 
ATOM   1249 N  NE1 . TRP   B 1 22  ? 24.758 -12.275 15.880 1.00 19.59 ? 28  TRP   C NE1 1 
ATOM   1250 C  CE2 . TRP   B 1 22  ? 24.534 -11.645 14.677 1.00 19.19 ? 28  TRP   C CE2 1 
ATOM   1251 C  CE3 . TRP   B 1 22  ? 25.833 -10.871 12.795 1.00 19.59 ? 28  TRP   C CE3 1 
ATOM   1252 C  CZ2 . TRP   B 1 22  ? 23.342 -11.193 14.098 1.00 19.24 ? 28  TRP   C CZ2 1 
ATOM   1253 C  CZ3 . TRP   B 1 22  ? 24.654 -10.436 12.218 1.00 20.14 ? 28  TRP   C CZ3 1 
ATOM   1254 C  CH2 . TRP   B 1 22  ? 23.424 -10.626 12.856 1.00 19.80 ? 28  TRP   C CH2 1 
ATOM   1255 N  N   . ALA   B 1 23  ? 31.136 -13.127 13.505 1.00 19.83 ? 29  ALA   C N   1 
ATOM   1256 C  CA  . ALA   B 1 23  ? 32.406 -12.821 12.839 1.00 21.09 ? 29  ALA   C CA  1 
ATOM   1257 C  C   . ALA   B 1 23  ? 32.641 -13.714 11.589 1.00 21.93 ? 29  ALA   C C   1 
ATOM   1258 O  O   . ALA   B 1 23  ? 33.520 -13.422 10.767 1.00 23.72 ? 29  ALA   C O   1 
ATOM   1259 C  CB  . ALA   B 1 23  ? 33.547 -13.014 13.831 1.00 20.45 ? 29  ALA   C CB  1 
ATOM   1260 N  N   . ASN   B 1 24  ? 31.967 -14.876 11.526 1.00 20.39 ? 30  ASN   C N   1 
ATOM   1261 C  CA  . ASN   B 1 24  ? 32.070 -15.822 10.409 1.00 20.15 ? 30  ASN   C CA  1 
ATOM   1262 C  C   . ASN   B 1 24  ? 30.700 -15.960 9.712  1.00 19.73 ? 30  ASN   C C   1 
ATOM   1263 O  O   . ASN   B 1 24  ? 30.339 -17.024 9.237  1.00 19.78 ? 30  ASN   C O   1 
ATOM   1264 C  CB  . ASN   B 1 24  ? 32.583 -17.169 10.932 1.00 21.14 ? 30  ASN   C CB  1 
ATOM   1265 C  CG  . ASN   B 1 24  ? 34.010 -17.045 11.429 1.00 25.58 ? 30  ASN   C CG  1 
ATOM   1266 O  OD1 . ASN   B 1 24  ? 34.958 -16.980 10.636 1.00 26.11 ? 30  ASN   C OD1 1 
ATOM   1267 N  ND2 . ASN   B 1 24  ? 34.189 -16.927 12.743 1.00 24.96 ? 30  ASN   C ND2 1 
ATOM   1268 N  N   . LEU   B 1 25  ? 29.951 -14.864 9.652  1.00 19.86 ? 31  LEU   C N   1 
ATOM   1269 C  CA  . LEU   B 1 25  ? 28.601 -14.870 9.107  1.00 19.61 ? 31  LEU   C CA  1 
ATOM   1270 C  C   . LEU   B 1 25  ? 28.520 -15.240 7.622  1.00 20.84 ? 31  LEU   C C   1 
ATOM   1271 O  O   . LEU   B 1 25  ? 29.253 -14.685 6.792  1.00 22.31 ? 31  LEU   C O   1 
ATOM   1272 C  CB  . LEU   B 1 25  ? 28.020 -13.463 9.326  1.00 19.04 ? 31  LEU   C CB  1 
ATOM   1273 C  CG  . LEU   B 1 25  ? 26.613 -13.215 8.805  1.00 19.71 ? 31  LEU   C CG  1 
ATOM   1274 C  CD1 . LEU   B 1 25  ? 25.604 -14.092 9.583  1.00 20.30 ? 31  LEU   C CD1 1 
ATOM   1275 C  CD2 . LEU   B 1 25  ? 26.261 -11.772 9.026  1.00 20.38 ? 31  LEU   C CD2 1 
ATOM   1276 N  N   . VAL   B 1 26  ? 27.569 -16.134 7.276  1.00 20.44 ? 32  VAL   C N   1 
ATOM   1277 C  CA  . VAL   B 1 26  ? 27.253 -16.500 5.909  1.00 20.44 ? 32  VAL   C CA  1 
ATOM   1278 C  C   . VAL   B 1 26  ? 25.925 -15.855 5.510  1.00 21.07 ? 32  VAL   C C   1 
ATOM   1279 O  O   . VAL   B 1 26  ? 25.802 -15.243 4.433  1.00 22.59 ? 32  VAL   C O   1 
ATOM   1280 C  CB  . VAL   B 1 26  ? 27.227 -18.038 5.748  1.00 21.66 ? 32  VAL   C CB  1 
ATOM   1281 C  CG1 . VAL   B 1 26  ? 26.719 -18.455 4.355  1.00 22.68 ? 32  VAL   C CG1 1 
ATOM   1282 C  CG2 . VAL   B 1 26  ? 28.624 -18.616 6.039  1.00 22.05 ? 32  VAL   C CG2 1 
ATOM   1283 N  N   . TRP   B 1 27  ? 24.926 -15.981 6.393  1.00 18.94 ? 33  TRP   C N   1 
ATOM   1284 C  CA  . TRP   B 1 27  ? 23.583 -15.477 6.119  1.00 18.73 ? 33  TRP   C CA  1 
ATOM   1285 C  C   . TRP   B 1 27  ? 22.812 -15.425 7.418  1.00 18.12 ? 33  TRP   C C   1 
ATOM   1286 O  O   . TRP   B 1 27  ? 23.007 -16.268 8.297  1.00 18.23 ? 33  TRP   C O   1 
ATOM   1287 C  CB  . TRP   B 1 27  ? 22.866 -16.462 5.146  1.00 19.13 ? 33  TRP   C CB  1 
ATOM   1288 C  CG  . TRP   B 1 27  ? 21.377 -16.273 4.957  1.00 20.08 ? 33  TRP   C CG  1 
ATOM   1289 C  CD1 . TRP   B 1 27  ? 20.753 -15.407 4.104  1.00 21.73 ? 33  TRP   C CD1 1 
ATOM   1290 C  CD2 . TRP   B 1 27  ? 20.331 -17.008 5.618  1.00 19.50 ? 33  TRP   C CD2 1 
ATOM   1291 N  NE1 . TRP   B 1 27  ? 19.380 -15.534 4.222  1.00 22.02 ? 33  TRP   C NE1 1 
ATOM   1292 C  CE2 . TRP   B 1 27  ? 19.097 -16.509 5.145  1.00 20.64 ? 33  TRP   C CE2 1 
ATOM   1293 C  CE3 . TRP   B 1 27  ? 20.317 -18.011 6.592  1.00 20.05 ? 33  TRP   C CE3 1 
ATOM   1294 C  CZ2 . TRP   B 1 27  ? 17.862 -17.029 5.578  1.00 20.78 ? 33  TRP   C CZ2 1 
ATOM   1295 C  CZ3 . TRP   B 1 27  ? 19.095 -18.506 7.028  1.00 20.57 ? 33  TRP   C CZ3 1 
ATOM   1296 C  CH2 . TRP   B 1 27  ? 17.888 -18.027 6.515  1.00 19.99 ? 33  TRP   C CH2 1 
ATOM   1297 N  N   . GLU   B 1 28  ? 21.936 -14.451 7.544  1.00 16.97 ? 34  GLU   C N   1 
ATOM   1298 C  CA  . GLU   B 1 28  ? 21.039 -14.401 8.707  1.00 16.61 ? 34  GLU   C CA  1 
ATOM   1299 C  C   . GLU   B 1 28  ? 19.710 -13.774 8.308  1.00 17.48 ? 34  GLU   C C   1 
ATOM   1300 O  O   . GLU   B 1 28  ? 19.649 -12.983 7.352  1.00 18.27 ? 34  GLU   C O   1 
ATOM   1301 C  CB  . GLU   B 1 28  ? 21.657 -13.697 9.933  1.00 17.90 ? 34  GLU   C CB  1 
ATOM   1302 C  CG  . GLU   B 1 28  ? 22.207 -12.300 9.675  1.00 19.74 ? 34  GLU   C CG  1 
ATOM   1303 C  CD  . GLU   B 1 28  ? 21.226 -11.151 9.521  1.00 23.29 ? 34  GLU   C CD  1 
ATOM   1304 O  OE1 . GLU   B 1 28  ? 21.542 -10.228 8.733  1.00 28.29 ? 34  GLU   C OE1 1 
ATOM   1305 O  OE2 . GLU   B 1 28  ? 20.154 -11.154 10.171 1.00 19.61 ? 34  GLU   C OE2 1 
ATOM   1306 N  N   . ASP   B 1 29  ? 18.645 -14.134 9.034  1.00 16.49 ? 35  ASP   C N   1 
ATOM   1307 C  CA  . ASP   B 1 29  ? 17.331 -13.569 8.751  1.00 16.12 ? 35  ASP   C CA  1 
ATOM   1308 C  C   . ASP   B 1 29  ? 16.601 -13.416 10.081 1.00 15.57 ? 35  ASP   C C   1 
ATOM   1309 O  O   . ASP   B 1 29  ? 16.186 -14.397 10.689 1.00 15.85 ? 35  ASP   C O   1 
ATOM   1310 C  CB  . ASP   B 1 29  ? 16.572 -14.459 7.772  1.00 18.21 ? 35  ASP   C CB  1 
ATOM   1311 C  CG  . ASP   B 1 29  ? 15.267 -13.880 7.284  1.00 23.30 ? 35  ASP   C CG  1 
ATOM   1312 O  OD1 . ASP   B 1 29  ? 14.682 -13.039 8.001  1.00 24.58 ? 35  ASP   C OD1 1 
ATOM   1313 O  OD2 . ASP   B 1 29  ? 14.823 -14.269 6.188  1.00 23.80 ? 35  ASP   C OD2 1 
ATOM   1314 N  N   . SER   B 1 30  ? 16.448 -12.152 10.548 1.00 14.79 ? 36  SER   C N   1 
ATOM   1315 C  CA  A SER   B 1 30  ? 15.758 -11.863 11.792 0.50 16.17 ? 36  SER   C CA  1 
ATOM   1316 C  CA  B SER   B 1 30  ? 15.764 -11.892 11.805 0.50 15.99 ? 36  SER   C CA  1 
ATOM   1317 C  C   . SER   B 1 30  ? 14.310 -12.356 11.770 1.00 16.43 ? 36  SER   C C   1 
ATOM   1318 O  O   . SER   B 1 30  ? 13.787 -12.792 12.798 1.00 17.32 ? 36  SER   C O   1 
ATOM   1319 C  CB  A SER   B 1 30  ? 15.792 -10.362 12.057 0.50 19.12 ? 36  SER   C CB  1 
ATOM   1320 C  CB  B SER   B 1 30  ? 15.841 -10.408 12.151 0.50 18.40 ? 36  SER   C CB  1 
ATOM   1321 O  OG  A SER   B 1 30  ? 15.180 -10.069 13.299 0.50 21.69 ? 36  SER   C OG  1 
ATOM   1322 O  OG  B SER   B 1 30  ? 15.135 -9.634  11.197 0.50 19.60 ? 36  SER   C OG  1 
ATOM   1323 N  N   . SER   B 1 31  ? 13.659 -12.282 10.586 1.00 14.67 ? 37  SER   C N   1 
ATOM   1324 C  CA  . SER   B 1 31  ? 12.272 -12.709 10.488 1.00 15.88 ? 37  SER   C CA  1 
ATOM   1325 C  C   . SER   B 1 31  ? 12.130 -14.224 10.669 1.00 15.68 ? 37  SER   C C   1 
ATOM   1326 O  O   . SER   B 1 31  ? 11.019 -14.654 10.988 1.00 17.70 ? 37  SER   C O   1 
ATOM   1327 C  CB  . SER   B 1 31  ? 11.619 -12.256 9.187  1.00 18.79 ? 37  SER   C CB  1 
ATOM   1328 O  OG  . SER   B 1 31  ? 12.044 -13.085 8.115  1.00 23.19 ? 37  SER   C OG  1 
ATOM   1329 N  N   . ARG   B 1 32  ? 13.204 -15.008 10.499 1.00 14.40 ? 38  ARG   C N   1 
ATOM   1330 C  CA  . ARG   B 1 32  ? 13.116 -16.478 10.675 1.00 13.91 ? 38  ARG   C CA  1 
ATOM   1331 C  C   . ARG   B 1 32  ? 13.795 -16.962 11.973 1.00 14.53 ? 38  ARG   C C   1 
ATOM   1332 O  O   . ARG   B 1 32  ? 13.749 -18.167 12.267 1.00 14.00 ? 38  ARG   C O   1 
ATOM   1333 C  CB  . ARG   B 1 32  ? 13.798 -17.186 9.492  1.00 14.98 ? 38  ARG   C CB  1 
ATOM   1334 C  CG  . ARG   B 1 32  ? 13.097 -16.891 8.170  1.00 15.15 ? 38  ARG   C CG  1 
ATOM   1335 C  CD  . ARG   B 1 32  ? 13.787 -17.550 6.960  1.00 14.47 ? 38  ARG   C CD  1 
ATOM   1336 N  NE  . ARG   B 1 32  ? 13.781 -19.014 7.047  1.00 15.31 ? 38  ARG   C NE  1 
ATOM   1337 C  CZ  . ARG   B 1 32  ? 13.839 -19.817 5.984  1.00 17.01 ? 38  ARG   C CZ  1 
ATOM   1338 N  NH1 . ARG   B 1 32  ? 13.890 -19.304 4.749  1.00 16.49 ? 38  ARG   C NH1 1 
ATOM   1339 N  NH2 . ARG   B 1 32  ? 13.800 -21.135 6.142  1.00 18.11 ? 38  ARG   C NH2 1 
ATOM   1340 N  N   . ASP   B 1 33  ? 14.460 -16.061 12.696 1.00 15.09 ? 39  ASP   C N   1 
ATOM   1341 C  CA  . ASP   B 1 33  ? 15.285 -16.404 13.860 1.00 13.68 ? 39  ASP   C CA  1 
ATOM   1342 C  C   . ASP   B 1 33  ? 16.394 -17.411 13.463 1.00 14.08 ? 39  ASP   C C   1 
ATOM   1343 O  O   . ASP   B 1 33  ? 16.733 -18.298 14.261 1.00 14.12 ? 39  ASP   C O   1 
ATOM   1344 C  CB  . ASP   B 1 33  ? 14.450 -16.990 15.031 1.00 14.09 ? 39  ASP   C CB  1 
ATOM   1345 C  CG  . ASP   B 1 33  ? 15.269 -17.276 16.304 1.00 14.69 ? 39  ASP   C CG  1 
ATOM   1346 O  OD1 . ASP   B 1 33  ? 16.156 -16.438 16.661 1.00 15.61 ? 39  ASP   C OD1 1 
ATOM   1347 O  OD2 . ASP   B 1 33  ? 15.012 -18.325 16.976 1.00 14.91 ? 39  ASP   C OD2 1 
ATOM   1348 N  N   . LEU   B 1 34  ? 16.984 -17.275 12.256 1.00 13.59 ? 40  LEU   C N   1 
ATOM   1349 C  CA  . LEU   B 1 34  ? 18.081 -18.168 11.861 1.00 14.28 ? 40  LEU   C CA  1 
ATOM   1350 C  C   . LEU   B 1 34  ? 19.357 -17.406 11.533 1.00 14.64 ? 40  LEU   C C   1 
ATOM   1351 O  O   . LEU   B 1 34  ? 19.313 -16.309 10.990 1.00 15.69 ? 40  LEU   C O   1 
ATOM   1352 C  CB  . LEU   B 1 34  ? 17.729 -18.945 10.573 1.00 14.02 ? 40  LEU   C CB  1 
ATOM   1353 C  CG  . LEU   B 1 34  ? 16.660 -20.029 10.716 1.00 16.02 ? 40  LEU   C CG  1 
ATOM   1354 C  CD1 . LEU   B 1 34  ? 16.456 -20.723 9.320  1.00 16.05 ? 40  LEU   C CD1 1 
ATOM   1355 C  CD2 . LEU   B 1 34  ? 17.063 -21.075 11.758 1.00 17.70 ? 40  LEU   C CD2 1 
ATOM   1356 N  N   . LEU   B 1 35  ? 20.493 -18.054 11.787 1.00 13.21 ? 41  LEU   C N   1 
ATOM   1357 C  CA  . LEU   B 1 35  ? 21.797 -17.514 11.413 1.00 14.21 ? 41  LEU   C CA  1 
ATOM   1358 C  C   . LEU   B 1 35  ? 22.654 -18.705 11.014 1.00 14.49 ? 41  LEU   C C   1 
ATOM   1359 O  O   . LEU   B 1 35  ? 22.590 -19.757 11.664 1.00 15.28 ? 41  LEU   C O   1 
ATOM   1360 C  CB  . LEU   B 1 35  ? 22.426 -16.737 12.561 1.00 15.01 ? 41  LEU   C CB  1 
ATOM   1361 C  CG  . LEU   B 1 35  ? 23.797 -16.081 12.256 1.00 16.27 ? 41  LEU   C CG  1 
ATOM   1362 C  CD1 . LEU   B 1 35  ? 23.966 -14.771 13.033 1.00 17.83 ? 41  LEU   C CD1 1 
ATOM   1363 C  CD2 . LEU   B 1 35  ? 24.972 -17.034 12.605 1.00 16.87 ? 41  LEU   C CD2 1 
ATOM   1364 N  N   . VAL   B 1 36  ? 23.436 -18.544 9.962  1.00 14.72 ? 42  VAL   C N   1 
ATOM   1365 C  CA  . VAL   B 1 36  ? 24.357 -19.583 9.469  1.00 15.70 ? 42  VAL   C CA  1 
ATOM   1366 C  C   . VAL   B 1 36  ? 25.754 -18.980 9.444  1.00 16.84 ? 42  VAL   C C   1 
ATOM   1367 O  O   . VAL   B 1 36  ? 25.953 -17.881 8.888  1.00 16.61 ? 42  VAL   C O   1 
ATOM   1368 C  CB  . VAL   B 1 36  ? 23.950 -20.065 8.060  1.00 15.97 ? 42  VAL   C CB  1 
ATOM   1369 C  CG1 . VAL   B 1 36  ? 24.973 -21.074 7.521  1.00 17.18 ? 42  VAL   C CG1 1 
ATOM   1370 C  CG2 . VAL   B 1 36  ? 22.545 -20.685 8.094  1.00 16.16 ? 42  VAL   C CG2 1 
ATOM   1371 N  N   . SER   B 1 37  ? 26.705 -19.664 10.077 1.00 17.07 ? 43  SER   C N   1 
ATOM   1372 C  CA  . SER   B 1 37  ? 28.110 -19.239 10.088 1.00 18.20 ? 43  SER   C CA  1 
ATOM   1373 C  C   . SER   B 1 37  ? 28.997 -20.318 9.433  1.00 18.85 ? 43  SER   C C   1 
ATOM   1374 O  O   . SER   B 1 37  ? 28.570 -21.462 9.237  1.00 19.10 ? 43  SER   C O   1 
ATOM   1375 C  CB  . SER   B 1 37  ? 28.567 -18.940 11.511 1.00 19.02 ? 43  SER   C CB  1 
ATOM   1376 O  OG  . SER   B 1 37  ? 28.447 -20.088 12.344 1.00 21.59 ? 43  SER   C OG  1 
ATOM   1377 N  N   . SER   B 1 38  ? 30.237 -19.922 9.070  1.00 19.20 ? 44  SER   C N   1 
ATOM   1378 C  CA  . SER   B 1 38  ? 31.128 -20.878 8.418  1.00 22.78 ? 44  SER   C CA  1 
ATOM   1379 C  C   . SER   B 1 38  ? 32.010 -21.609 9.450  1.00 26.04 ? 44  SER   C C   1 
ATOM   1380 O  O   . SER   B 1 38  ? 32.370 -21.041 10.487 1.00 27.64 ? 44  SER   C O   1 
ATOM   1381 C  CB  . SER   B 1 38  ? 31.974 -20.177 7.370  1.00 26.70 ? 44  SER   C CB  1 
ATOM   1382 O  OG  . SER   B 1 38  ? 32.723 -19.167 8.005  1.00 31.25 ? 44  SER   C OG  1 
ATOM   1383 N  N   . THR   B 1 39  ? 32.312 -22.891 9.177  1.00 27.52 ? 45  THR   C N   1 
ATOM   1384 C  CA  . THR   B 1 39  ? 33.128 -23.726 10.064 1.00 31.15 ? 45  THR   C CA  1 
ATOM   1385 C  C   . THR   B 1 39  ? 34.345 -24.272 9.293  1.00 34.46 ? 45  THR   C C   1 
ATOM   1386 O  O   . THR   B 1 39  ? 34.348 -24.290 8.059  1.00 34.49 ? 45  THR   C O   1 
ATOM   1387 C  CB  . THR   B 1 39  ? 32.297 -24.932 10.579 1.00 33.44 ? 45  THR   C CB  1 
ATOM   1388 O  OG1 . THR   B 1 39  ? 32.079 -25.846 9.500  1.00 35.79 ? 45  THR   C OG1 1 
ATOM   1389 C  CG2 . THR   B 1 39  ? 30.982 -24.535 11.152 1.00 33.47 ? 45  THR   C CG2 1 
ATOM   1390 N  N   . THR   B 1 40  ? 35.361 -24.760 10.024 1.00 36.88 ? 46  THR   C N   1 
ATOM   1391 C  CA  . THR   B 1 40  ? 36.532 -25.380 9.407  1.00 39.88 ? 46  THR   C CA  1 
ATOM   1392 C  C   . THR   B 1 40  ? 36.348 -26.899 9.260  1.00 42.50 ? 46  THR   C C   1 
ATOM   1393 O  O   . THR   B 1 40  ? 36.951 -27.501 8.371  1.00 44.14 ? 46  THR   C O   1 
ATOM   1394 C  CB  . THR   B 1 40  ? 37.787 -25.075 10.236 1.00 41.51 ? 46  THR   C CB  1 
ATOM   1395 O  OG1 . THR   B 1 40  ? 37.516 -25.381 11.609 1.00 42.93 ? 46  THR   C OG1 1 
ATOM   1396 C  CG2 . THR   B 1 40  ? 38.223 -23.620 10.116 1.00 42.13 ? 46  THR   C CG2 1 
ATOM   1397 N  N   . ALA   B 1 41  ? 35.555 -27.528 10.145 1.00 42.73 ? 47  ALA   C N   1 
ATOM   1398 C  CA  . ALA   B 1 41  ? 35.345 -28.974 10.086 1.00 43.00 ? 47  ALA   C CA  1 
ATOM   1399 C  C   . ALA   B 1 41  ? 34.097 -29.334 9.283  1.00 43.12 ? 47  ALA   C C   1 
ATOM   1400 O  O   . ALA   B 1 41  ? 33.168 -28.544 9.195  1.00 43.84 ? 47  ALA   C O   1 
ATOM   1401 C  CB  . ALA   B 1 41  ? 35.241 -29.544 11.492 1.00 43.39 ? 47  ALA   C CB  1 
ATOM   1402 N  N   . GLN   B 1 42  ? 34.081 -30.530 8.697  1.00 42.27 ? 48  GLN   C N   1 
ATOM   1403 C  CA  . GLN   B 1 42  ? 32.956 -30.987 7.893  1.00 41.33 ? 48  GLN   C CA  1 
ATOM   1404 C  C   . GLN   B 1 42  ? 31.839 -31.480 8.799  1.00 38.64 ? 48  GLN   C C   1 
ATOM   1405 O  O   . GLN   B 1 42  ? 32.078 -32.273 9.699  1.00 39.67 ? 48  GLN   C O   1 
ATOM   1406 C  CB  . GLN   B 1 42  ? 33.406 -32.119 6.960  1.00 44.71 ? 48  GLN   C CB  1 
ATOM   1407 C  CG  . GLN   B 1 42  ? 32.302 -32.644 6.045  1.00 50.17 ? 48  GLN   C CG  1 
ATOM   1408 C  CD  . GLN   B 1 42  ? 32.126 -31.832 4.782  1.00 56.01 ? 48  GLN   C CD  1 
ATOM   1409 O  OE1 . GLN   B 1 42  ? 32.868 -30.878 4.502  1.00 57.58 ? 48  GLN   C OE1 1 
ATOM   1410 N  NE2 . GLN   B 1 42  ? 31.137 -32.213 3.981  1.00 56.99 ? 48  GLN   C NE2 1 
ATOM   1411 N  N   . GLY   B 1 43  ? 30.639 -30.981 8.577  1.00 34.55 ? 49  GLY   C N   1 
ATOM   1412 C  CA  . GLY   B 1 43  ? 29.457 -31.378 9.331  1.00 32.07 ? 49  GLY   C CA  1 
ATOM   1413 C  C   . GLY   B 1 43  ? 28.772 -32.506 8.590  1.00 29.30 ? 49  GLY   C C   1 
ATOM   1414 O  O   . GLY   B 1 43  ? 28.787 -32.534 7.350  1.00 29.23 ? 49  GLY   C O   1 
ATOM   1415 N  N   . CYS   B 1 44  ? 28.203 -33.445 9.322  1.00 27.33 ? 50  CYS   C N   1 
ATOM   1416 C  CA  . CYS   B 1 44  ? 27.593 -34.617 8.711  1.00 27.01 ? 50  CYS   C CA  1 
ATOM   1417 C  C   . CYS   B 1 44  ? 26.066 -34.681 8.821  1.00 25.34 ? 50  CYS   C C   1 
ATOM   1418 O  O   . CYS   B 1 44  ? 25.515 -35.742 8.514  1.00 25.24 ? 50  CYS   C O   1 
ATOM   1419 C  CB  . CYS   B 1 44  ? 28.236 -35.891 9.250  1.00 28.10 ? 50  CYS   C CB  1 
ATOM   1420 S  SG  . CYS   B 1 44  ? 29.994 -36.037 8.850  1.00 35.49 ? 50  CYS   C SG  1 
ATOM   1421 N  N   . ASP   B 1 45  ? 25.380 -33.602 9.273  1.00 22.49 ? 51  ASP   C N   1 
ATOM   1422 C  CA  . ASP   B 1 45  ? 23.918 -33.659 9.344  1.00 22.22 ? 51  ASP   C CA  1 
ATOM   1423 C  C   . ASP   B 1 45  ? 23.316 -33.656 7.928  1.00 22.71 ? 51  ASP   C C   1 
ATOM   1424 O  O   . ASP   B 1 45  ? 23.809 -32.982 7.023  1.00 24.09 ? 51  ASP   C O   1 
ATOM   1425 C  CB  . ASP   B 1 45  ? 23.330 -32.492 10.169 1.00 23.11 ? 51  ASP   C CB  1 
ATOM   1426 C  CG  . ASP   B 1 45  ? 23.454 -32.615 11.681 1.00 29.85 ? 51  ASP   C CG  1 
ATOM   1427 O  OD1 . ASP   B 1 45  ? 23.294 -33.747 12.208 1.00 33.89 ? 51  ASP   C OD1 1 
ATOM   1428 O  OD2 . ASP   B 1 45  ? 23.673 -31.572 12.348 1.00 27.76 ? 51  ASP   C OD2 1 
ATOM   1429 N  N   . THR   B 1 46  ? 22.291 -34.502 7.722  1.00 21.14 ? 52  THR   C N   1 
ATOM   1430 C  CA  . THR   B 1 46  ? 21.592 -34.582 6.441  1.00 22.27 ? 52  THR   C CA  1 
ATOM   1431 C  C   . THR   B 1 46  ? 20.324 -33.763 6.610  1.00 20.38 ? 52  THR   C C   1 
ATOM   1432 O  O   . THR   B 1 46  ? 19.585 -33.983 7.566  1.00 20.31 ? 52  THR   C O   1 
ATOM   1433 C  CB  . THR   B 1 46  ? 21.207 -36.034 6.086  1.00 27.19 ? 52  THR   C CB  1 
ATOM   1434 O  OG1 . THR   B 1 46  ? 22.397 -36.729 5.675  1.00 31.23 ? 52  THR   C OG1 1 
ATOM   1435 C  CG2 . THR   B 1 46  ? 20.183 -36.110 4.949  1.00 28.46 ? 52  THR   C CG2 1 
ATOM   1436 N  N   . ILE   B 1 47  ? 20.084 -32.820 5.692  1.00 19.12 ? 53  ILE   C N   1 
ATOM   1437 C  CA  . ILE   B 1 47  ? 18.887 -31.983 5.751  1.00 17.66 ? 53  ILE   C CA  1 
ATOM   1438 C  C   . ILE   B 1 47  ? 17.779 -32.650 4.952  1.00 16.94 ? 53  ILE   C C   1 
ATOM   1439 O  O   . ILE   B 1 47  ? 18.009 -33.142 3.840  1.00 17.75 ? 53  ILE   C O   1 
ATOM   1440 C  CB  . ILE   B 1 47  ? 19.172 -30.579 5.149  1.00 18.97 ? 53  ILE   C CB  1 
ATOM   1441 C  CG1 . ILE   B 1 47  ? 20.449 -29.927 5.759  1.00 21.40 ? 53  ILE   C CG1 1 
ATOM   1442 C  CG2 . ILE   B 1 47  ? 17.942 -29.649 5.302  1.00 19.07 ? 53  ILE   C CG2 1 
ATOM   1443 C  CD1 . ILE   B 1 47  ? 20.308 -29.734 7.263  1.00 23.46 ? 53  ILE   C CD1 1 
ATOM   1444 N  N   . ALA   B 1 48  ? 16.568 -32.696 5.532  1.00 15.36 ? 54  ALA   C N   1 
ATOM   1445 C  CA  . ALA   B 1 48  ? 15.419 -33.245 4.844  1.00 15.12 ? 54  ALA   C CA  1 
ATOM   1446 C  C   . ALA   B 1 48  ? 15.022 -32.323 3.700  1.00 14.47 ? 54  ALA   C C   1 
ATOM   1447 O  O   . ALA   B 1 48  ? 15.084 -31.108 3.851  1.00 15.15 ? 54  ALA   C O   1 
ATOM   1448 C  CB  . ALA   B 1 48  ? 14.259 -33.325 5.827  1.00 14.98 ? 54  ALA   C CB  1 
ATOM   1449 N  N   . ARG   B 1 49  ? 14.568 -32.883 2.573  1.00 14.26 ? 55  ARG   C N   1 
ATOM   1450 C  CA  . ARG   B 1 49  ? 14.095 -32.083 1.425  1.00 13.87 ? 55  ARG   C CA  1 
ATOM   1451 C  C   . ARG   B 1 49  ? 12.729 -32.734 1.126  1.00 14.01 ? 55  ARG   C C   1 
ATOM   1452 O  O   . ARG   B 1 49  ? 12.638 -33.709 0.365  1.00 15.25 ? 55  ARG   C O   1 
ATOM   1453 C  CB  . ARG   B 1 49  ? 15.061 -32.189 0.244  1.00 14.49 ? 55  ARG   C CB  1 
ATOM   1454 C  CG  . ARG   B 1 49  ? 16.472 -31.715 0.613  1.00 15.18 ? 55  ARG   C CG  1 
ATOM   1455 C  CD  . ARG   B 1 49  ? 16.527 -30.208 0.959  1.00 16.41 ? 55  ARG   C CD  1 
ATOM   1456 N  NE  . ARG   B 1 49  ? 17.920 -29.792 1.221  1.00 18.45 ? 55  ARG   C NE  1 
ATOM   1457 C  CZ  . ARG   B 1 49  ? 18.270 -28.681 1.867  1.00 19.74 ? 55  ARG   C CZ  1 
ATOM   1458 N  NH1 . ARG   B 1 49  ? 17.347 -27.851 2.315  1.00 19.44 ? 55  ARG   C NH1 1 
ATOM   1459 N  NH2 . ARG   B 1 49  ? 19.559 -28.393 2.065  1.00 19.41 ? 55  ARG   C NH2 1 
ATOM   1460 N  N   . CYS   B 1 50  ? 11.681 -32.230 1.794  1.00 13.37 ? 56  CYS   C N   1 
ATOM   1461 C  CA  . CYS   B 1 50  ? 10.383 -32.900 1.808  1.00 14.84 ? 56  CYS   C CA  1 
ATOM   1462 C  C   . CYS   B 1 50  ? 9.265  -31.983 2.318  1.00 15.63 ? 56  CYS   C C   1 
ATOM   1463 O  O   . CYS   B 1 50  ? 9.534  -30.869 2.738  1.00 14.83 ? 56  CYS   C O   1 
ATOM   1464 C  CB  . CYS   B 1 50  ? 10.505 -34.111 2.733  1.00 16.39 ? 56  CYS   C CB  1 
ATOM   1465 S  SG  . CYS   B 1 50  ? 10.667 -33.663 4.499  1.00 15.25 ? 56  CYS   C SG  1 
ATOM   1466 N  N   . ASP   B 1 51  ? 8.009  -32.499 2.347  1.00 15.82 ? 57  ASP   C N   1 
ATOM   1467 C  CA  . ASP   B 1 51  ? 6.871  -31.801 2.912  1.00 16.18 ? 57  ASP   C CA  1 
ATOM   1468 C  C   . ASP   B 1 51  ? 6.300  -32.573 4.107  1.00 16.48 ? 57  ASP   C C   1 
ATOM   1469 O  O   . ASP   B 1 51  ? 5.106  -32.446 4.406  1.00 16.83 ? 57  ASP   C O   1 
ATOM   1470 C  CB  . ASP   B 1 51  ? 5.776  -31.548 1.873  1.00 17.94 ? 57  ASP   C CB  1 
ATOM   1471 C  CG  . ASP   B 1 51  ? 5.153  -32.770 1.260  1.00 23.59 ? 57  ASP   C CG  1 
ATOM   1472 O  OD1 . ASP   B 1 51  ? 5.530  -33.899 1.645  1.00 23.51 ? 57  ASP   C OD1 1 
ATOM   1473 O  OD2 . ASP   B 1 51  ? 4.251  -32.605 0.401  1.00 29.23 ? 57  ASP   C OD2 1 
ATOM   1474 N  N   . CYS   B 1 52  ? 7.125  -33.353 4.843  1.00 14.65 ? 58  CYS   C N   1 
ATOM   1475 C  CA  . CYS   B 1 52  ? 6.628  -34.084 6.038  1.00 13.95 ? 58  CYS   C CA  1 
ATOM   1476 C  C   . CYS   B 1 52  ? 5.965  -33.152 7.009  1.00 14.09 ? 58  CYS   C C   1 
ATOM   1477 O  O   . CYS   B 1 52  ? 6.414  -32.008 7.199  1.00 14.23 ? 58  CYS   C O   1 
ATOM   1478 C  CB  . CYS   B 1 52  ? 7.772  -34.812 6.747  1.00 15.63 ? 58  CYS   C CB  1 
ATOM   1479 S  SG  . CYS   B 1 52  ? 8.330  -36.288 5.891  1.00 16.43 ? 58  CYS   C SG  1 
ATOM   1480 N  N   . GLN   B 1 53  ? 4.972  -33.691 7.699  1.00 12.97 ? 59  GLN   C N   1 
ATOM   1481 C  CA  . GLN   B 1 53  ? 4.333  -33.002 8.807  1.00 13.31 ? 59  GLN   C CA  1 
ATOM   1482 C  C   . GLN   B 1 53  ? 4.339  -33.857 10.080 1.00 14.27 ? 59  GLN   C C   1 
ATOM   1483 O  O   . GLN   B 1 53  ? 3.555  -33.587 10.997 1.00 14.44 ? 59  GLN   C O   1 
ATOM   1484 C  CB  . GLN   B 1 53  ? 2.882  -32.577 8.460  1.00 14.15 ? 59  GLN   C CB  1 
ATOM   1485 C  CG  . GLN   B 1 53  ? 2.839  -31.290 7.600  1.00 14.11 ? 59  GLN   C CG  1 
ATOM   1486 C  CD  . GLN   B 1 53  ? 1.411  -30.903 7.333  1.00 17.97 ? 59  GLN   C CD  1 
ATOM   1487 O  OE1 . GLN   B 1 53  ? 0.904  -31.100 6.216  1.00 19.88 ? 59  GLN   C OE1 1 
ATOM   1488 N  NE2 . GLN   B 1 53  ? 0.732  -30.402 8.367  1.00 15.66 ? 59  GLN   C NE2 1 
ATOM   1489 N  N   . THR   B 1 54  ? 5.155  -34.918 10.134 1.00 14.37 ? 60  THR   C N   1 
ATOM   1490 C  CA  . THR   B 1 54  ? 5.332  -35.716 11.353 1.00 14.56 ? 60  THR   C CA  1 
ATOM   1491 C  C   . THR   B 1 54  ? 6.831  -35.915 11.533 1.00 14.12 ? 60  THR   C C   1 
ATOM   1492 O  O   . THR   B 1 54  ? 7.584  -35.998 10.541 1.00 14.79 ? 60  THR   C O   1 
ATOM   1493 C  CB  . THR   B 1 54  ? 4.599  -37.054 11.325 1.00 19.87 ? 60  THR   C CB  1 
ATOM   1494 O  OG1 . THR   B 1 54  ? 5.161  -37.893 10.324 1.00 22.86 ? 60  THR   C OG1 1 
ATOM   1495 C  CG2 . THR   B 1 54  ? 3.138  -36.925 11.044 1.00 21.57 ? 60  THR   C CG2 1 
ATOM   1496 N  N   . GLY   B 1 55  ? 7.262  -35.976 12.787 1.00 13.10 ? 61  GLY   C N   1 
ATOM   1497 C  CA  . GLY   B 1 55  ? 8.691  -36.106 13.066 1.00 13.52 ? 61  GLY   C CA  1 
ATOM   1498 C  C   . GLY   B 1 55  ? 8.942  -36.223 14.546 1.00 12.99 ? 61  GLY   C C   1 
ATOM   1499 O  O   . GLY   B 1 55  ? 8.019  -36.529 15.292 1.00 14.77 ? 61  GLY   C O   1 
ATOM   1500 N  N   . VAL   B 1 56  ? 10.192 -36.105 14.953 1.00 12.30 ? 62  VAL   C N   1 
ATOM   1501 C  CA  . VAL   B 1 56  ? 10.590 -36.270 16.345 1.00 13.33 ? 62  VAL   C CA  1 
ATOM   1502 C  C   . VAL   B 1 56  ? 11.510 -35.126 16.712 1.00 14.21 ? 62  VAL   C C   1 
ATOM   1503 O  O   . VAL   B 1 56  ? 12.453 -34.836 15.972 1.00 14.44 ? 62  VAL   C O   1 
ATOM   1504 C  CB  . VAL   B 1 56  ? 11.345 -37.608 16.556 1.00 13.76 ? 62  VAL   C CB  1 
ATOM   1505 C  CG1 . VAL   B 1 56  ? 11.847 -37.742 18.010 1.00 14.85 ? 62  VAL   C CG1 1 
ATOM   1506 C  CG2 . VAL   B 1 56  ? 10.476 -38.793 16.165 1.00 13.93 ? 62  VAL   C CG2 1 
ATOM   1507 N  N   . TYR   B 1 57  ? 11.256 -34.477 17.883 1.00 13.61 ? 63  TYR   C N   1 
ATOM   1508 C  CA  . TYR   B 1 57  ? 12.155 -33.391 18.313 1.00 14.05 ? 63  TYR   C CA  1 
ATOM   1509 C  C   . TYR   B 1 57  ? 12.779 -33.651 19.658 1.00 14.12 ? 63  TYR   C C   1 
ATOM   1510 O  O   . TYR   B 1 57  ? 12.216 -34.395 20.464 1.00 14.54 ? 63  TYR   C O   1 
ATOM   1511 C  CB  . TYR   B 1 57  ? 11.461 -31.987 18.300 1.00 14.36 ? 63  TYR   C CB  1 
ATOM   1512 C  CG  . TYR   B 1 57  ? 10.531 -31.714 19.469 1.00 15.53 ? 63  TYR   C CG  1 
ATOM   1513 C  CD1 . TYR   B 1 57  ? 9.277  -32.307 19.541 1.00 17.00 ? 63  TYR   C CD1 1 
ATOM   1514 C  CD2 . TYR   B 1 57  ? 10.888 -30.826 20.479 1.00 16.83 ? 63  TYR   C CD2 1 
ATOM   1515 C  CE1 . TYR   B 1 57  ? 8.404  -32.034 20.590 1.00 18.68 ? 63  TYR   C CE1 1 
ATOM   1516 C  CE2 . TYR   B 1 57  ? 10.034 -30.583 21.564 1.00 17.43 ? 63  TYR   C CE2 1 
ATOM   1517 C  CZ  . TYR   B 1 57  ? 8.786  -31.171 21.603 1.00 19.23 ? 63  TYR   C CZ  1 
ATOM   1518 O  OH  . TYR   B 1 57  ? 7.902  -30.885 22.631 1.00 21.68 ? 63  TYR   C OH  1 
ATOM   1519 N  N   . TYR   B 1 58  ? 13.955 -33.053 19.892 1.00 13.41 ? 64  TYR   C N   1 
ATOM   1520 C  CA  . TYR   B 1 58  ? 14.608 -33.161 21.177 1.00 13.27 ? 64  TYR   C CA  1 
ATOM   1521 C  C   . TYR   B 1 58  ? 14.174 -32.032 22.088 1.00 13.67 ? 64  TYR   C C   1 
ATOM   1522 O  O   . TYR   B 1 58  ? 14.307 -30.864 21.727 1.00 14.29 ? 64  TYR   C O   1 
ATOM   1523 C  CB  . TYR   B 1 58  ? 16.141 -33.150 21.034 1.00 14.01 ? 64  TYR   C CB  1 
ATOM   1524 C  CG  . TYR   B 1 58  ? 16.816 -33.320 22.383 1.00 15.97 ? 64  TYR   C CG  1 
ATOM   1525 C  CD1 . TYR   B 1 58  ? 16.684 -34.507 23.104 1.00 16.70 ? 64  TYR   C CD1 1 
ATOM   1526 C  CD2 . TYR   B 1 58  ? 17.484 -32.259 22.991 1.00 18.22 ? 64  TYR   C CD2 1 
ATOM   1527 C  CE1 . TYR   B 1 58  ? 17.239 -34.654 24.379 1.00 17.83 ? 64  TYR   C CE1 1 
ATOM   1528 C  CE2 . TYR   B 1 58  ? 18.055 -32.400 24.254 1.00 18.40 ? 64  TYR   C CE2 1 
ATOM   1529 C  CZ  . TYR   B 1 58  ? 17.908 -33.591 24.950 1.00 19.19 ? 64  TYR   C CZ  1 
ATOM   1530 O  OH  . TYR   B 1 58  ? 18.474 -33.720 26.204 1.00 22.01 ? 64  TYR   C OH  1 
ATOM   1531 N  N   . CYS   B 1 59  ? 13.688 -32.390 23.304 1.00 14.20 ? 65  CYS   C N   1 
ATOM   1532 C  CA  . CYS   B 1 59  ? 13.200 -31.414 24.285 1.00 14.15 ? 65  CYS   C CA  1 
ATOM   1533 C  C   . CYS   B 1 59  ? 14.169 -31.409 25.493 1.00 15.30 ? 65  CYS   C C   1 
ATOM   1534 O  O   . CYS   B 1 59  ? 14.112 -32.318 26.336 1.00 16.18 ? 65  CYS   C O   1 
ATOM   1535 C  CB  . CYS   B 1 59  ? 11.780 -31.791 24.708 1.00 14.68 ? 65  CYS   C CB  1 
ATOM   1536 S  SG  . CYS   B 1 59  ? 11.116 -30.733 26.023 1.00 18.52 ? 65  CYS   C SG  1 
ATOM   1537 N  N   . SER   B 1 60  ? 15.065 -30.426 25.545 1.00 15.08 ? 66  SER   C N   1 
ATOM   1538 C  CA  . SER   B 1 60  ? 16.089 -30.415 26.599 1.00 17.50 ? 66  SER   C CA  1 
ATOM   1539 C  C   . SER   B 1 60  ? 15.516 -30.291 27.997 1.00 17.35 ? 66  SER   C C   1 
ATOM   1540 O  O   . SER   B 1 60  ? 16.067 -30.876 28.926 1.00 18.80 ? 66  SER   C O   1 
ATOM   1541 C  CB  . SER   B 1 60  ? 17.159 -29.347 26.377 1.00 23.84 ? 66  SER   C CB  1 
ATOM   1542 O  OG  . SER   B 1 60  ? 16.607 -28.056 26.325 1.00 31.70 ? 66  SER   C OG  1 
ATOM   1543 N  N   . SER   B 1 61  ? 14.365 -29.609 28.153 1.00 16.94 ? 67  SER   C N   1 
ATOM   1544 C  CA  . SER   B 1 61  ? 13.743 -29.481 29.488 1.00 17.43 ? 67  SER   C CA  1 
ATOM   1545 C  C   . SER   B 1 61  ? 13.079 -30.763 30.001 1.00 17.85 ? 67  SER   C C   1 
ATOM   1546 O  O   . SER   B 1 61  ? 12.636 -30.824 31.165 1.00 17.50 ? 67  SER   C O   1 
ATOM   1547 C  CB  . SER   B 1 61  ? 12.752 -28.332 29.501 1.00 17.22 ? 67  SER   C CB  1 
ATOM   1548 O  OG  . SER   B 1 61  ? 11.686 -28.596 28.602 1.00 19.40 ? 67  SER   C OG  1 
ATOM   1549 N  N   . ARG   B 1 62  ? 13.057 -31.818 29.176 1.00 16.66 ? 68  ARG   C N   1 
ATOM   1550 C  CA  . ARG   B 1 62  ? 12.565 -33.112 29.604 1.00 16.28 ? 68  ARG   C CA  1 
ATOM   1551 C  C   . ARG   B 1 62  ? 13.654 -34.197 29.362 1.00 17.89 ? 68  ARG   C C   1 
ATOM   1552 O  O   . ARG   B 1 62  ? 13.405 -35.359 29.690 1.00 18.87 ? 68  ARG   C O   1 
ATOM   1553 C  CB  . ARG   B 1 62  ? 11.281 -33.476 28.828 1.00 17.71 ? 68  ARG   C CB  1 
ATOM   1554 C  CG  . ARG   B 1 62  ? 10.090 -32.574 29.148 1.00 17.64 ? 68  ARG   C CG  1 
ATOM   1555 C  CD  . ARG   B 1 62  ? 9.554  -32.898 30.540 1.00 18.91 ? 68  ARG   C CD  1 
ATOM   1556 N  NE  . ARG   B 1 62  ? 8.427  -32.030 30.916 1.00 20.91 ? 68  ARG   C NE  1 
ATOM   1557 C  CZ  . ARG   B 1 62  ? 8.558  -30.873 31.556 1.00 26.12 ? 68  ARG   C CZ  1 
ATOM   1558 N  NH1 . ARG   B 1 62  ? 9.763  -30.434 31.916 1.00 26.31 ? 68  ARG   C NH1 1 
ATOM   1559 N  NH2 . ARG   B 1 62  ? 7.484  -30.147 31.856 1.00 27.34 ? 68  ARG   C NH2 1 
ATOM   1560 N  N   . ARG   B 1 63  ? 14.864 -33.816 28.804 1.00 17.61 ? 69  ARG   C N   1 
ATOM   1561 C  CA  . ARG   B 1 63  ? 15.951 -34.748 28.439 1.00 19.36 ? 69  ARG   C CA  1 
ATOM   1562 C  C   . ARG   B 1 63  ? 15.389 -35.895 27.612 1.00 20.81 ? 69  ARG   C C   1 
ATOM   1563 O  O   . ARG   B 1 63  ? 15.687 -37.070 27.872 1.00 23.50 ? 69  ARG   C O   1 
ATOM   1564 C  CB  . ARG   B 1 63  ? 16.653 -35.294 29.712 1.00 22.40 ? 69  ARG   C CB  1 
ATOM   1565 C  CG  . ARG   B 1 63  ? 17.629 -34.334 30.319 1.00 27.58 ? 69  ARG   C CG  1 
ATOM   1566 C  CD  . ARG   B 1 63  ? 18.509 -35.068 31.297 1.00 35.09 ? 69  ARG   C CD  1 
ATOM   1567 N  NE  . ARG   B 1 63  ? 19.031 -34.144 32.294 1.00 40.86 ? 69  ARG   C NE  1 
ATOM   1568 C  CZ  . ARG   B 1 63  ? 18.748 -34.199 33.590 1.00 45.25 ? 69  ARG   C CZ  1 
ATOM   1569 N  NH1 . ARG   B 1 63  ? 17.944 -35.146 34.063 1.00 45.53 ? 69  ARG   C NH1 1 
ATOM   1570 N  NH2 . ARG   B 1 63  ? 19.249 -33.293 34.425 1.00 45.53 ? 69  ARG   C NH2 1 
ATOM   1571 N  N   . LYS   B 1 64  ? 14.445 -35.581 26.690 1.00 19.10 ? 70  LYS   C N   1 
ATOM   1572 C  CA  . LYS   B 1 64  ? 13.747 -36.642 25.965 1.00 19.05 ? 70  LYS   C CA  1 
ATOM   1573 C  C   . LYS   B 1 64  ? 13.367 -36.173 24.565 1.00 17.04 ? 70  LYS   C C   1 
ATOM   1574 O  O   . LYS   B 1 64  ? 13.207 -34.971 24.320 1.00 17.14 ? 70  LYS   C O   1 
ATOM   1575 C  CB  . LYS   B 1 64  ? 12.388 -36.966 26.678 1.00 22.73 ? 70  LYS   C CB  1 
ATOM   1576 C  CG  . LYS   B 1 64  ? 12.394 -38.086 27.690 1.00 33.68 ? 70  LYS   C CG  1 
ATOM   1577 C  CD  . LYS   B 1 64  ? 10.945 -38.275 28.151 1.00 41.82 ? 70  LYS   C CD  1 
ATOM   1578 C  CE  . LYS   B 1 64  ? 10.811 -39.239 29.306 1.00 47.38 ? 70  LYS   C CE  1 
ATOM   1579 N  NZ  . LYS   B 1 64  ? 9.592  -38.944 30.107 1.00 50.61 ? 70  LYS   C NZ  1 
ATOM   1580 N  N   . HIS   B 1 65  ? 13.201 -37.129 23.679 1.00 15.91 ? 71  HIS   C N   1 
ATOM   1581 C  CA  . HIS   B 1 65  ? 12.666 -36.882 22.343 1.00 16.27 ? 71  HIS   C CA  1 
ATOM   1582 C  C   . HIS   B 1 65  ? 11.173 -37.179 22.352 1.00 18.06 ? 71  HIS   C C   1 
ATOM   1583 O  O   . HIS   B 1 65  ? 10.713 -38.137 23.024 1.00 20.01 ? 71  HIS   C O   1 
ATOM   1584 C  CB  . HIS   B 1 65  ? 13.359 -37.805 21.323 1.00 17.15 ? 71  HIS   C CB  1 
ATOM   1585 C  CG  . HIS   B 1 65  ? 14.835 -37.592 21.195 1.00 17.90 ? 71  HIS   C CG  1 
ATOM   1586 N  ND1 . HIS   B 1 65  ? 15.378 -36.846 20.165 1.00 20.64 ? 71  HIS   C ND1 1 
ATOM   1587 C  CD2 . HIS   B 1 65  ? 15.835 -38.097 21.940 1.00 18.71 ? 71  HIS   C CD2 1 
ATOM   1588 C  CE1 . HIS   B 1 65  ? 16.695 -36.881 20.350 1.00 19.22 ? 71  HIS   C CE1 1 
ATOM   1589 N  NE2 . HIS   B 1 65  ? 17.008 -37.644 21.391 1.00 21.00 ? 71  HIS   C NE2 1 
ATOM   1590 N  N   . TYR   B 1 66  ? 10.393 -36.401 21.574 1.00 16.09 ? 72  TYR   C N   1 
ATOM   1591 C  CA  . TYR   B 1 66  ? 8.949  -36.616 21.462 1.00 16.09 ? 72  TYR   C CA  1 
ATOM   1592 C  C   . TYR   B 1 66  ? 8.526  -36.676 20.014 1.00 15.59 ? 72  TYR   C C   1 
ATOM   1593 O  O   . TYR   B 1 66  ? 8.962  -35.840 19.203 1.00 15.18 ? 72  TYR   C O   1 
ATOM   1594 C  CB  . TYR   B 1 66  ? 8.169  -35.442 22.104 1.00 16.43 ? 72  TYR   C CB  1 
ATOM   1595 C  CG  . TYR   B 1 66  ? 8.255  -35.372 23.619 1.00 19.65 ? 72  TYR   C CG  1 
ATOM   1596 C  CD1 . TYR   B 1 66  ? 7.509  -36.232 24.415 1.00 21.72 ? 72  TYR   C CD1 1 
ATOM   1597 C  CD2 . TYR   B 1 66  ? 9.002  -34.385 24.247 1.00 21.91 ? 72  TYR   C CD2 1 
ATOM   1598 C  CE1 . TYR   B 1 66  ? 7.545  -36.142 25.797 1.00 23.85 ? 72  TYR   C CE1 1 
ATOM   1599 C  CE2 . TYR   B 1 66  ? 9.080  -34.316 25.629 1.00 23.91 ? 72  TYR   C CE2 1 
ATOM   1600 C  CZ  . TYR   B 1 66  ? 8.341  -35.195 26.401 1.00 25.91 ? 72  TYR   C CZ  1 
ATOM   1601 O  OH  . TYR   B 1 66  ? 8.363  -35.146 27.783 1.00 28.39 ? 72  TYR   C OH  1 
ATOM   1602 N  N   . PRO   B 1 67  ? 7.676  -37.672 19.664 1.00 15.73 ? 73  PRO   C N   1 
ATOM   1603 C  CA  . PRO   B 1 67  ? 7.115  -37.706 18.307 1.00 15.66 ? 73  PRO   C CA  1 
ATOM   1604 C  C   . PRO   B 1 67  ? 6.008  -36.627 18.222 1.00 16.80 ? 73  PRO   C C   1 
ATOM   1605 O  O   . PRO   B 1 67  ? 5.215  -36.516 19.160 1.00 17.51 ? 73  PRO   C O   1 
ATOM   1606 C  CB  . PRO   B 1 67  ? 6.528  -39.123 18.200 1.00 16.28 ? 73  PRO   C CB  1 
ATOM   1607 C  CG  . PRO   B 1 67  ? 6.169  -39.468 19.591 1.00 16.46 ? 73  PRO   C CG  1 
ATOM   1608 C  CD  . PRO   B 1 67  ? 7.153  -38.775 20.509 1.00 15.13 ? 73  PRO   C CD  1 
ATOM   1609 N  N   . VAL   B 1 68  ? 5.969  -35.845 17.137 1.00 15.05 ? 74  VAL   C N   1 
ATOM   1610 C  CA  . VAL   B 1 68  ? 4.938  -34.795 16.968 1.00 16.90 ? 74  VAL   C CA  1 
ATOM   1611 C  C   . VAL   B 1 68  ? 4.439  -34.683 15.530 1.00 16.11 ? 74  VAL   C C   1 
ATOM   1612 O  O   . VAL   B 1 68  ? 5.175  -35.013 14.598 1.00 16.78 ? 74  VAL   C O   1 
ATOM   1613 C  CB  . VAL   B 1 68  ? 5.454  -33.390 17.378 1.00 19.86 ? 74  VAL   C CB  1 
ATOM   1614 C  CG1 . VAL   B 1 68  ? 5.620  -33.267 18.905 1.00 21.96 ? 74  VAL   C CG1 1 
ATOM   1615 C  CG2 . VAL   B 1 68  ? 6.717  -33.011 16.620 1.00 20.27 ? 74  VAL   C CG2 1 
ATOM   1616 N  N   . SER   B 1 69  ? 3.189  -34.175 15.347 1.00 16.06 ? 75  SER   C N   1 
ATOM   1617 C  CA  . SER   B 1 69  ? 2.683  -33.691 14.082 1.00 16.10 ? 75  SER   C CA  1 
ATOM   1618 C  C   . SER   B 1 69  ? 2.932  -32.149 14.156 1.00 14.42 ? 75  SER   C C   1 
ATOM   1619 O  O   . SER   B 1 69  ? 2.834  -31.504 15.210 1.00 15.11 ? 75  SER   C O   1 
ATOM   1620 C  CB  . SER   B 1 69  ? 1.170  -33.931 13.947 1.00 20.12 ? 75  SER   C CB  1 
ATOM   1621 O  OG  . SER   B 1 69  ? 0.839  -35.314 13.916 1.00 25.02 ? 75  SER   C OG  1 
ATOM   1622 N  N   . PHE   B 1 70  ? 3.253  -31.533 13.009 1.00 13.91 ? 76  PHE   C N   1 
ATOM   1623 C  CA  . PHE   B 1 70  ? 3.516  -30.085 12.975 1.00 13.32 ? 76  PHE   C CA  1 
ATOM   1624 C  C   . PHE   B 1 70  ? 2.942  -29.461 11.710 1.00 13.71 ? 76  PHE   C C   1 
ATOM   1625 O  O   . PHE   B 1 70  ? 2.717  -30.163 10.730 1.00 13.74 ? 76  PHE   C O   1 
ATOM   1626 C  CB  . PHE   B 1 70  ? 5.023  -29.774 13.131 1.00 12.78 ? 76  PHE   C CB  1 
ATOM   1627 C  CG  . PHE   B 1 70  ? 5.924  -30.546 12.177 1.00 12.81 ? 76  PHE   C CG  1 
ATOM   1628 C  CD1 . PHE   B 1 70  ? 6.447  -31.783 12.534 1.00 13.84 ? 76  PHE   C CD1 1 
ATOM   1629 C  CD2 . PHE   B 1 70  ? 6.350  -29.972 10.991 1.00 13.64 ? 76  PHE   C CD2 1 
ATOM   1630 C  CE1 . PHE   B 1 70  ? 7.296  -32.493 11.646 1.00 14.64 ? 76  PHE   C CE1 1 
ATOM   1631 C  CE2 . PHE   B 1 70  ? 7.206  -30.652 10.124 1.00 14.14 ? 76  PHE   C CE2 1 
ATOM   1632 C  CZ  . PHE   B 1 70  ? 7.678  -31.911 10.449 1.00 14.10 ? 76  PHE   C CZ  1 
ATOM   1633 N  N   . SER   B 1 71  ? 2.703  -28.161 11.744 1.00 13.25 ? 77  SER   C N   1 
ATOM   1634 C  CA  . SER   B 1 71  ? 2.065  -27.466 10.641 1.00 14.74 ? 77  SER   C CA  1 
ATOM   1635 C  C   . SER   B 1 71  ? 3.026  -27.193 9.495  1.00 15.54 ? 77  SER   C C   1 
ATOM   1636 O  O   . SER   B 1 71  ? 4.209  -27.562 9.539  1.00 16.03 ? 77  SER   C O   1 
ATOM   1637 C  CB  . SER   B 1 71  ? 1.464  -26.154 11.151 1.00 16.03 ? 77  SER   C CB  1 
ATOM   1638 O  OG  . SER   B 1 71  ? 2.483  -25.244 11.548 1.00 17.61 ? 77  SER   C OG  1 
ATOM   1639 N  N   . LYS   B 1 72  ? 2.478  -26.644 8.404  1.00 14.52 ? 78  LYS   C N   1 
ATOM   1640 C  CA  . LYS   B 1 72  ? 3.336  -26.247 7.294  1.00 14.93 ? 78  LYS   C CA  1 
ATOM   1641 C  C   . LYS   B 1 72  ? 4.023  -24.899 7.649  1.00 16.12 ? 78  LYS   C C   1 
ATOM   1642 O  O   . LYS   B 1 72  ? 3.470  -24.101 8.418  1.00 18.70 ? 78  LYS   C O   1 
ATOM   1643 C  CB  . LYS   B 1 72  ? 2.470  -26.078 6.034  1.00 17.54 ? 78  LYS   C CB  1 
ATOM   1644 C  CG  . LYS   B 1 72  ? 1.831  -27.412 5.599  1.00 21.63 ? 78  LYS   C CG  1 
ATOM   1645 C  CD  . LYS   B 1 72  ? 1.030  -27.203 4.310  1.00 30.22 ? 78  LYS   C CD  1 
ATOM   1646 C  CE  . LYS   B 1 72  ? 0.195  -28.397 3.966  1.00 36.94 ? 78  LYS   C CE  1 
ATOM   1647 N  NZ  . LYS   B 1 72  ? -1.065 -27.981 3.277  1.00 42.75 ? 78  LYS   C NZ  1 
ATOM   1648 N  N   . PRO   B 1 73  ? 5.217  -24.608 7.086  1.00 15.72 ? 79  PRO   C N   1 
ATOM   1649 C  CA  . PRO   B 1 73  ? 5.902  -23.338 7.400  1.00 16.29 ? 79  PRO   C CA  1 
ATOM   1650 C  C   . PRO   B 1 73  ? 5.046  -22.124 7.082  1.00 17.89 ? 79  PRO   C C   1 
ATOM   1651 O  O   . PRO   B 1 73  ? 4.403  -22.066 6.009  1.00 18.76 ? 79  PRO   C O   1 
ATOM   1652 C  CB  . PRO   B 1 73  ? 7.170  -23.355 6.519  1.00 16.92 ? 79  PRO   C CB  1 
ATOM   1653 C  CG  . PRO   B 1 73  ? 7.336  -24.747 6.103  1.00 18.76 ? 79  PRO   C CG  1 
ATOM   1654 C  CD  . PRO   B 1 73  ? 6.008  -25.454 6.167  1.00 15.89 ? 79  PRO   C CD  1 
ATOM   1655 N  N   . SER   B 1 74  ? 4.926  -21.223 8.052  1.00 18.55 ? 80  SER   C N   1 
ATOM   1656 C  CA  . SER   B 1 74  ? 4.040  -20.074 7.869  1.00 20.37 ? 80  SER   C CA  1 
ATOM   1657 C  C   . SER   B 1 74  ? 4.432  -18.863 8.703  1.00 18.75 ? 80  SER   C C   1 
ATOM   1658 O  O   . SER   B 1 74  ? 5.400  -18.925 9.468  1.00 16.32 ? 80  SER   C O   1 
ATOM   1659 C  CB  . SER   B 1 74  ? 2.601  -20.495 8.154  1.00 25.21 ? 80  SER   C CB  1 
ATOM   1660 O  OG  . SER   B 1 74  ? 2.446  -20.750 9.539  1.00 29.49 ? 80  SER   C OG  1 
ATOM   1661 N  N   . LEU   B 1 75  ? 3.714  -17.733 8.497  1.00 18.62 ? 81  LEU   C N   1 
ATOM   1662 C  CA  . LEU   B 1 75  ? 3.949  -16.466 9.189  1.00 19.51 ? 81  LEU   C CA  1 
ATOM   1663 C  C   . LEU   B 1 75  ? 3.097  -16.496 10.465 1.00 19.58 ? 81  LEU   C C   1 
ATOM   1664 O  O   . LEU   B 1 75  ? 1.853  -16.594 10.390 1.00 20.72 ? 81  LEU   C O   1 
ATOM   1665 C  CB  . LEU   B 1 75  ? 3.443  -15.321 8.274  1.00 22.00 ? 81  LEU   C CB  1 
ATOM   1666 C  CG  . LEU   B 1 75  ? 4.351  -14.218 7.703  1.00 27.14 ? 81  LEU   C CG  1 
ATOM   1667 C  CD1 . LEU   B 1 75  ? 3.542  -12.970 7.412  1.00 29.37 ? 81  LEU   C CD1 1 
ATOM   1668 C  CD2 . LEU   B 1 75  ? 5.540  -13.909 8.518  1.00 27.56 ? 81  LEU   C CD2 1 
ATOM   1669 N  N   . ILE   B 1 76  ? 3.746  -16.458 11.639 1.00 17.06 ? 82  ILE   C N   1 
ATOM   1670 C  CA  . ILE   B 1 76  ? 3.088  -16.563 12.934 1.00 17.90 ? 82  ILE   C CA  1 
ATOM   1671 C  C   . ILE   B 1 76  ? 3.485  -15.425 13.860 1.00 18.73 ? 82  ILE   C C   1 
ATOM   1672 O  O   . ILE   B 1 76  ? 4.669  -15.133 13.970 1.00 18.53 ? 82  ILE   C O   1 
ATOM   1673 C  CB  . ILE   B 1 76  ? 3.467  -17.938 13.542 1.00 20.65 ? 82  ILE   C CB  1 
ATOM   1674 C  CG1 . ILE   B 1 76  ? 2.986  -19.083 12.613 1.00 23.91 ? 82  ILE   C CG1 1 
ATOM   1675 C  CG2 . ILE   B 1 76  ? 3.002  -18.092 15.003 1.00 21.46 ? 82  ILE   C CG2 1 
ATOM   1676 C  CD1 . ILE   B 1 76  ? 3.451  -20.351 12.929 1.00 28.41 ? 82  ILE   C CD1 1 
ATOM   1677 N  N   . PHE   B 1 77  ? 2.513  -14.786 14.536 1.00 19.57 ? 83  PHE   C N   1 
ATOM   1678 C  CA  . PHE   B 1 77  ? 2.800  -13.689 15.452 1.00 20.83 ? 83  PHE   C CA  1 
ATOM   1679 C  C   . PHE   B 1 77  ? 3.508  -14.204 16.702 1.00 20.23 ? 83  PHE   C C   1 
ATOM   1680 O  O   . PHE   B 1 77  ? 3.097  -15.204 17.298 1.00 20.36 ? 83  PHE   C O   1 
ATOM   1681 C  CB  . PHE   B 1 77  ? 1.507  -12.946 15.857 1.00 22.10 ? 83  PHE   C CB  1 
ATOM   1682 C  CG  . PHE   B 1 77  ? 1.725  -11.811 16.847 1.00 23.75 ? 83  PHE   C CG  1 
ATOM   1683 C  CD1 . PHE   B 1 77  ? 1.474  -11.989 18.197 1.00 25.89 ? 83  PHE   C CD1 1 
ATOM   1684 C  CD2 . PHE   B 1 77  ? 2.284  -10.614 16.438 1.00 26.08 ? 83  PHE   C CD2 1 
ATOM   1685 C  CE1 . PHE   B 1 77  ? 1.712  -10.967 19.111 1.00 27.53 ? 83  PHE   C CE1 1 
ATOM   1686 C  CE2 . PHE   B 1 77  ? 2.519  -9.579  17.358 1.00 27.13 ? 83  PHE   C CE2 1 
ATOM   1687 C  CZ  . PHE   B 1 77  ? 2.218  -9.767  18.684 1.00 27.21 ? 83  PHE   C CZ  1 
ATOM   1688 N  N   . VAL   B 1 78  ? 4.606  -13.540 17.074 1.00 19.88 ? 84  VAL   C N   1 
ATOM   1689 C  CA  . VAL   B 1 78  ? 5.395  -13.900 18.257 1.00 19.29 ? 84  VAL   C CA  1 
ATOM   1690 C  C   . VAL   B 1 78  ? 5.521  -12.631 19.104 1.00 19.73 ? 84  VAL   C C   1 
ATOM   1691 O  O   . VAL   B 1 78  ? 5.953  -11.588 18.609 1.00 18.79 ? 84  VAL   C O   1 
ATOM   1692 C  CB  . VAL   B 1 78  ? 6.804  -14.394 17.838 1.00 19.07 ? 84  VAL   C CB  1 
ATOM   1693 C  CG1 . VAL   B 1 78  ? 7.645  -14.765 19.068 1.00 18.84 ? 84  VAL   C CG1 1 
ATOM   1694 C  CG2 . VAL   B 1 78  ? 6.710  -15.586 16.879 1.00 18.61 ? 84  VAL   C CG2 1 
ATOM   1695 N  N   . GLU   B 1 79  ? 5.172  -12.732 20.392 1.00 20.49 ? 85  GLU   C N   1 
ATOM   1696 C  CA  . GLU   B 1 79  ? 5.238  -11.613 21.322 1.00 21.51 ? 85  GLU   C CA  1 
ATOM   1697 C  C   . GLU   B 1 79  ? 6.677  -11.110 21.505 1.00 19.93 ? 85  GLU   C C   1 
ATOM   1698 O  O   . GLU   B 1 79  ? 7.632  -11.869 21.317 1.00 19.58 ? 85  GLU   C O   1 
ATOM   1699 C  CB  . GLU   B 1 79  ? 4.727  -12.036 22.707 1.00 24.81 ? 85  GLU   C CB  1 
ATOM   1700 C  CG  . GLU   B 1 79  ? 3.371  -12.695 22.762 1.00 32.47 ? 85  GLU   C CG  1 
ATOM   1701 C  CD  . GLU   B 1 79  ? 2.216  -11.727 22.764 1.00 42.09 ? 85  GLU   C CD  1 
ATOM   1702 O  OE1 . GLU   B 1 79  ? 1.089  -12.206 22.512 1.00 45.71 ? 85  GLU   C OE1 1 
ATOM   1703 O  OE2 . GLU   B 1 79  ? 2.417  -10.509 22.987 1.00 43.02 ? 85  GLU   C OE2 1 
ATOM   1704 N  N   . ALA   B 1 80  ? 6.832  -9.820  21.922 1.00 20.02 ? 86  ALA   C N   1 
ATOM   1705 C  CA  . ALA   B 1 80  ? 8.162  -9.240  22.162 1.00 19.21 ? 86  ALA   C CA  1 
ATOM   1706 C  C   . ALA   B 1 80  ? 8.907  -10.028 23.224 1.00 19.14 ? 86  ALA   C C   1 
ATOM   1707 O  O   . ALA   B 1 80  ? 8.307  -10.582 24.151 1.00 19.72 ? 86  ALA   C O   1 
ATOM   1708 C  CB  . ALA   B 1 80  ? 8.029  -7.784  22.641 1.00 18.91 ? 86  ALA   C CB  1 
ATOM   1709 N  N   . SER   B 1 81  ? 10.219 -10.081 23.093 1.00 17.00 ? 87  SER   C N   1 
ATOM   1710 C  CA  . SER   B 1 81  ? 11.087 -10.686 24.100 1.00 17.36 ? 87  SER   C CA  1 
ATOM   1711 C  C   . SER   B 1 81  ? 12.316 -9.742  24.201 1.00 18.48 ? 87  SER   C C   1 
ATOM   1712 O  O   . SER   B 1 81  ? 12.351 -8.690  23.520 1.00 19.94 ? 87  SER   C O   1 
ATOM   1713 C  CB  . SER   B 1 81  ? 11.521 -12.091 23.650 1.00 17.70 ? 87  SER   C CB  1 
ATOM   1714 O  OG  . SER   B 1 81  ? 12.299 -11.988 22.477 1.00 18.50 ? 87  SER   C OG  1 
ATOM   1715 N  N   . GLU   B 1 82  ? 13.284 -10.061 25.049 1.00 18.66 ? 88  GLU   C N   1 
ATOM   1716 C  CA  . GLU   B 1 82  ? 14.520 -9.253  25.101 1.00 20.34 ? 88  GLU   C CA  1 
ATOM   1717 C  C   . GLU   B 1 82  ? 15.275 -9.296  23.764 1.00 20.07 ? 88  GLU   C C   1 
ATOM   1718 O  O   . GLU   B 1 82  ? 16.047 -8.370  23.457 1.00 20.39 ? 88  GLU   C O   1 
ATOM   1719 C  CB  . GLU   B 1 82  ? 15.454 -9.728  26.225 1.00 25.77 ? 88  GLU   C CB  1 
ATOM   1720 C  CG  . GLU   B 1 82  ? 15.526 -11.224 26.422 1.00 35.22 ? 88  GLU   C CG  1 
ATOM   1721 C  CD  . GLU   B 1 82  ? 14.455 -11.768 27.351 1.00 45.97 ? 88  GLU   C CD  1 
ATOM   1722 O  OE1 . GLU   B 1 82  ? 14.653 -11.704 28.588 1.00 50.37 ? 88  GLU   C OE1 1 
ATOM   1723 O  OE2 . GLU   B 1 82  ? 13.404 -12.225 26.843 1.00 44.46 ? 88  GLU   C OE2 1 
ATOM   1724 N  N   . TYR   B 1 83  ? 15.039 -10.343 22.954 1.00 18.86 ? 89  TYR   C N   1 
ATOM   1725 C  CA  . TYR   B 1 83  ? 15.762 -10.558 21.716 1.00 18.95 ? 89  TYR   C CA  1 
ATOM   1726 C  C   . TYR   B 1 83  ? 15.136 -9.932  20.486 1.00 19.05 ? 89  TYR   C C   1 
ATOM   1727 O  O   . TYR   B 1 83  ? 15.855 -9.690  19.509 1.00 20.93 ? 89  TYR   C O   1 
ATOM   1728 C  CB  . TYR   B 1 83  ? 15.885 -12.067 21.490 1.00 18.64 ? 89  TYR   C CB  1 
ATOM   1729 C  CG  . TYR   B 1 83  ? 16.529 -12.786 22.642 1.00 20.25 ? 89  TYR   C CG  1 
ATOM   1730 C  CD1 . TYR   B 1 83  ? 17.902 -12.729 22.841 1.00 22.06 ? 89  TYR   C CD1 1 
ATOM   1731 C  CD2 . TYR   B 1 83  ? 15.768 -13.509 23.542 1.00 21.28 ? 89  TYR   C CD2 1 
ATOM   1732 C  CE1 . TYR   B 1 83  ? 18.511 -13.438 23.870 1.00 23.55 ? 89  TYR   C CE1 1 
ATOM   1733 C  CE2 . TYR   B 1 83  ? 16.361 -14.205 24.586 1.00 23.34 ? 89  TYR   C CE2 1 
ATOM   1734 C  CZ  . TYR   B 1 83  ? 17.737 -14.168 24.748 1.00 24.80 ? 89  TYR   C CZ  1 
ATOM   1735 O  OH  . TYR   B 1 83  ? 18.345 -14.866 25.768 1.00 28.39 ? 89  TYR   C OH  1 
ATOM   1736 N  N   . TYR   B 1 84  ? 13.815 -9.723  20.479 1.00 17.11 ? 90  TYR   C N   1 
ATOM   1737 C  CA  . TYR   B 1 84  ? 13.107 -9.248  19.290 1.00 17.01 ? 90  TYR   C CA  1 
ATOM   1738 C  C   . TYR   B 1 84  ? 11.949 -8.378  19.677 1.00 18.71 ? 90  TYR   C C   1 
ATOM   1739 O  O   . TYR   B 1 84  ? 11.276 -8.639  20.686 1.00 18.26 ? 90  TYR   C O   1 
ATOM   1740 C  CB  . TYR   B 1 84  ? 12.468 -10.432 18.474 1.00 16.59 ? 90  TYR   C CB  1 
ATOM   1741 C  CG  . TYR   B 1 84  ? 13.468 -11.357 17.843 1.00 16.54 ? 90  TYR   C CG  1 
ATOM   1742 C  CD1 . TYR   B 1 84  ? 13.650 -12.651 18.326 1.00 17.14 ? 90  TYR   C CD1 1 
ATOM   1743 C  CD2 . TYR   B 1 84  ? 14.176 -10.975 16.709 1.00 16.60 ? 90  TYR   C CD2 1 
ATOM   1744 C  CE1 . TYR   B 1 84  ? 14.539 -13.523 17.721 1.00 16.70 ? 90  TYR   C CE1 1 
ATOM   1745 C  CE2 . TYR   B 1 84  ? 15.080 -11.833 16.110 1.00 16.73 ? 90  TYR   C CE2 1 
ATOM   1746 C  CZ  . TYR   B 1 84  ? 15.229 -13.114 16.596 1.00 16.88 ? 90  TYR   C CZ  1 
ATOM   1747 O  OH  . TYR   B 1 84  ? 16.165 -13.924 16.020 1.00 16.64 ? 90  TYR   C OH  1 
ATOM   1748 N  N   . PRO   B 1 85  ? 11.584 -7.428  18.806 1.00 19.80 ? 91  PRO   C N   1 
ATOM   1749 C  CA  . PRO   B 1 85  ? 10.320 -6.738  19.019 1.00 19.62 ? 91  PRO   C CA  1 
ATOM   1750 C  C   . PRO   B 1 85  ? 9.146  -7.708  18.740 1.00 20.24 ? 91  PRO   C C   1 
ATOM   1751 O  O   . PRO   B 1 85  ? 9.332  -8.728  18.085 1.00 19.57 ? 91  PRO   C O   1 
ATOM   1752 C  CB  . PRO   B 1 85  ? 10.358 -5.627  17.938 1.00 20.87 ? 91  PRO   C CB  1 
ATOM   1753 C  CG  . PRO   B 1 85  ? 11.172 -6.222  16.831 1.00 21.24 ? 91  PRO   C CG  1 
ATOM   1754 C  CD  . PRO   B 1 85  ? 12.223 -7.052  17.515 1.00 18.80 ? 91  PRO   C CD  1 
ATOM   1755 N  N   . ALA   B 1 86  ? 7.926  -7.360  19.113 1.00 20.14 ? 92  ALA   C N   1 
ATOM   1756 C  CA  . ALA   B 1 86  ? 6.712  -8.108  18.741 1.00 20.87 ? 92  ALA   C CA  1 
ATOM   1757 C  C   . ALA   B 1 86  ? 6.661  -8.100  17.188 1.00 21.01 ? 92  ALA   C C   1 
ATOM   1758 O  O   . ALA   B 1 86  ? 6.963  -7.051  16.587 1.00 21.20 ? 92  ALA   C O   1 
ATOM   1759 C  CB  . ALA   B 1 86  ? 5.471  -7.397  19.293 1.00 20.74 ? 92  ALA   C CB  1 
ATOM   1760 N  N   . ARG   B 1 87  ? 6.494  -9.279  16.559 1.00 20.54 ? 93  ARG   C N   1 
ATOM   1761 C  CA  . ARG   B 1 87  ? 6.593  -9.324  15.091 1.00 20.06 ? 93  ARG   C CA  1 
ATOM   1762 C  C   . ARG   B 1 87  ? 5.994  -10.636 14.548 1.00 20.34 ? 93  ARG   C C   1 
ATOM   1763 O  O   . ARG   B 1 87  ? 5.651  -11.532 15.326 1.00 20.52 ? 93  ARG   C O   1 
ATOM   1764 C  CB  . ARG   B 1 87  ? 8.101  -9.250  14.684 1.00 19.51 ? 93  ARG   C CB  1 
ATOM   1765 C  CG  . ARG   B 1 87  ? 8.846  -10.622 14.932 1.00 18.33 ? 93  ARG   C CG  1 
ATOM   1766 C  CD  . ARG   B 1 87  ? 10.317 -10.497 15.254 1.00 18.64 ? 93  ARG   C CD  1 
ATOM   1767 N  NE  . ARG   B 1 87  ? 11.108 -11.628 14.784 1.00 17.96 ? 93  ARG   C NE  1 
ATOM   1768 C  CZ  . ARG   B 1 87  ? 11.171 -12.803 15.394 1.00 18.79 ? 93  ARG   C CZ  1 
ATOM   1769 N  NH1 . ARG   B 1 87  ? 11.945 -13.764 14.907 1.00 17.34 ? 93  ARG   C NH1 1 
ATOM   1770 N  NH2 . ARG   B 1 87  ? 10.437 -13.039 16.486 1.00 18.36 ? 93  ARG   C NH2 1 
ATOM   1771 N  N   . TYR   B 1 88  ? 5.921  -10.758 13.226 1.00 20.55 ? 94  TYR   C N   1 
ATOM   1772 C  CA  . TYR   B 1 88  ? 5.527  -12.024 12.620 1.00 20.90 ? 94  TYR   C CA  1 
ATOM   1773 C  C   . TYR   B 1 88  ? 6.821  -12.746 12.257 1.00 18.37 ? 94  TYR   C C   1 
ATOM   1774 O  O   . TYR   B 1 88  ? 7.689  -12.165 11.594 1.00 18.29 ? 94  TYR   C O   1 
ATOM   1775 C  CB  . TYR   B 1 88  ? 4.739  -11.796 11.334 1.00 22.97 ? 94  TYR   C CB  1 
ATOM   1776 C  CG  . TYR   B 1 88  ? 3.372  -11.259 11.641 1.00 26.02 ? 94  TYR   C CG  1 
ATOM   1777 C  CD1 . TYR   B 1 88  ? 2.306  -12.114 11.859 1.00 28.06 ? 94  TYR   C CD1 1 
ATOM   1778 C  CD2 . TYR   B 1 88  ? 3.172  -9.903  11.840 1.00 28.90 ? 94  TYR   C CD2 1 
ATOM   1779 C  CE1 . TYR   B 1 88  ? 1.053  -11.623 12.203 1.00 30.16 ? 94  TYR   C CE1 1 
ATOM   1780 C  CE2 . TYR   B 1 88  ? 1.934  -9.402  12.204 1.00 30.84 ? 94  TYR   C CE2 1 
ATOM   1781 C  CZ  . TYR   B 1 88  ? 0.875  -10.266 12.375 1.00 32.31 ? 94  TYR   C CZ  1 
ATOM   1782 O  OH  . TYR   B 1 88  ? -0.343 -9.746  12.740 1.00 37.26 ? 94  TYR   C OH  1 
ATOM   1783 N  N   . GLN   B 1 89  ? 6.974  -13.975 12.745 1.00 15.70 ? 95  GLN   C N   1 
ATOM   1784 C  CA  . GLN   B 1 89  ? 8.130  -14.803 12.380 1.00 15.06 ? 95  GLN   C CA  1 
ATOM   1785 C  C   . GLN   B 1 89  ? 7.705  -15.684 11.212 1.00 16.29 ? 95  GLN   C C   1 
ATOM   1786 O  O   . GLN   B 1 89  ? 6.644  -16.315 11.262 1.00 17.41 ? 95  GLN   C O   1 
ATOM   1787 C  CB  . GLN   B 1 89  ? 8.616  -15.649 13.570 1.00 15.57 ? 95  GLN   C CB  1 
ATOM   1788 C  CG  . GLN   B 1 89  ? 9.802  -16.580 13.182 1.00 16.03 ? 95  GLN   C CG  1 
ATOM   1789 C  CD  . GLN   B 1 89  ? 10.550 -17.085 14.400 1.00 15.82 ? 95  GLN   C CD  1 
ATOM   1790 O  OE1 . GLN   B 1 89  ? 10.754 -16.353 15.396 1.00 16.47 ? 95  GLN   C OE1 1 
ATOM   1791 N  NE2 . GLN   B 1 89  ? 10.953 -18.357 14.356 1.00 14.80 ? 95  GLN   C NE2 1 
ATOM   1792 N  N   . SER   B 1 90  ? 8.521  -15.710 10.150 1.00 15.93 ? 96  SER   C N   1 
ATOM   1793 C  CA  . SER   B 1 90  ? 8.214  -16.502 8.962  1.00 15.86 ? 96  SER   C CA  1 
ATOM   1794 C  C   . SER   B 1 90  ? 8.863  -17.890 9.009  1.00 14.90 ? 96  SER   C C   1 
ATOM   1795 O  O   . SER   B 1 90  ? 9.803  -18.133 9.823  1.00 15.11 ? 96  SER   C O   1 
ATOM   1796 C  CB  . SER   B 1 90  ? 8.635  -15.743 7.698  1.00 16.69 ? 96  SER   C CB  1 
ATOM   1797 O  OG  . SER   B 1 90  ? 10.042 -15.559 7.654  1.00 19.34 ? 96  SER   C OG  1 
ATOM   1798 N  N   . HIS   B 1 91  ? 8.354  -18.805 8.148  1.00 14.84 ? 97  HIS   C N   1 
ATOM   1799 C  CA  . HIS   B 1 91  ? 8.853  -20.169 7.960  1.00 13.59 ? 97  HIS   C CA  1 
ATOM   1800 C  C   . HIS   B 1 91  ? 8.793  -20.931 9.309  1.00 15.17 ? 97  HIS   C C   1 
ATOM   1801 O  O   . HIS   B 1 91  ? 9.677  -21.748 9.592  1.00 16.48 ? 97  HIS   C O   1 
ATOM   1802 C  CB  . HIS   B 1 91  ? 10.305 -20.141 7.396  1.00 14.53 ? 97  HIS   C CB  1 
ATOM   1803 C  CG  . HIS   B 1 91  ? 10.402 -19.514 6.028  1.00 16.33 ? 97  HIS   C CG  1 
ATOM   1804 N  ND1 . HIS   B 1 91  ? 10.391 -20.284 4.877  1.00 19.66 ? 97  HIS   C ND1 1 
ATOM   1805 C  CD2 . HIS   B 1 91  ? 10.482 -18.207 5.671  1.00 18.75 ? 97  HIS   C CD2 1 
ATOM   1806 C  CE1 . HIS   B 1 91  ? 10.488 -19.429 3.861  1.00 19.69 ? 97  HIS   C CE1 1 
ATOM   1807 N  NE2 . HIS   B 1 91  ? 10.500 -18.170 4.283  1.00 20.16 ? 97  HIS   C NE2 1 
ATOM   1808 N  N   . LEU   B 1 92  ? 7.769  -20.619 10.145 1.00 14.55 ? 98  LEU   C N   1 
ATOM   1809 C  CA  . LEU   B 1 92  ? 7.644  -21.245 11.471 1.00 14.67 ? 98  LEU   C CA  1 
ATOM   1810 C  C   . LEU   B 1 92  ? 6.555  -22.335 11.418 1.00 15.06 ? 98  LEU   C C   1 
ATOM   1811 O  O   . LEU   B 1 92  ? 5.507  -22.138 10.776 1.00 15.39 ? 98  LEU   C O   1 
ATOM   1812 C  CB  . LEU   B 1 92  ? 7.272  -20.167 12.513 1.00 15.21 ? 98  LEU   C CB  1 
ATOM   1813 C  CG  . LEU   B 1 92  ? 7.217  -20.588 13.994 1.00 16.90 ? 98  LEU   C CG  1 
ATOM   1814 C  CD1 . LEU   B 1 92  ? 8.603  -21.043 14.496 1.00 17.08 ? 98  LEU   C CD1 1 
ATOM   1815 C  CD2 . LEU   B 1 92  ? 6.759  -19.400 14.870 1.00 19.41 ? 98  LEU   C CD2 1 
ATOM   1816 N  N   . MET   B 1 93  ? 6.822  -23.468 12.081 1.00 14.35 ? 99  MET   C N   1 
ATOM   1817 C  CA  . MET   B 1 93  ? 5.880  -24.610 12.126 1.00 14.35 ? 99  MET   C CA  1 
ATOM   1818 C  C   . MET   B 1 93  ? 5.503  -24.888 13.567 1.00 15.60 ? 99  MET   C C   1 
ATOM   1819 O  O   . MET   B 1 93  ? 6.388  -24.937 14.406 1.00 15.86 ? 99  MET   C O   1 
ATOM   1820 C  CB  . MET   B 1 93  ? 6.552  -25.847 11.534 1.00 14.94 ? 99  MET   C CB  1 
ATOM   1821 C  CG  . MET   B 1 93  ? 6.974  -25.606 10.116 1.00 16.09 ? 99  MET   C CG  1 
ATOM   1822 S  SD  . MET   B 1 93  ? 7.967  -26.934 9.442  1.00 19.01 ? 99  MET   C SD  1 
ATOM   1823 C  CE  . MET   B 1 93  ? 9.454  -26.863 10.474 1.00 16.36 ? 99  MET   C CE  1 
ATOM   1824 N  N   . LEU   B 1 94  ? 4.222  -25.032 13.873 1.00 14.19 ? 100 LEU   C N   1 
ATOM   1825 C  CA  . LEU   B 1 94  ? 3.799  -25.283 15.254 1.00 14.73 ? 100 LEU   C CA  1 
ATOM   1826 C  C   . LEU   B 1 94  ? 3.373  -26.727 15.484 1.00 15.36 ? 100 LEU   C C   1 
ATOM   1827 O  O   . LEU   B 1 94  ? 2.852  -27.374 14.589 1.00 15.47 ? 100 LEU   C O   1 
ATOM   1828 C  CB  . LEU   B 1 94  ? 2.614  -24.365 15.643 1.00 16.00 ? 100 LEU   C CB  1 
ATOM   1829 C  CG  . LEU   B 1 94  ? 2.879  -22.857 15.537 1.00 17.58 ? 100 LEU   C CG  1 
ATOM   1830 C  CD1 . LEU   B 1 94  ? 1.652  -22.030 16.077 1.00 18.35 ? 100 LEU   C CD1 1 
ATOM   1831 C  CD2 . LEU   B 1 94  ? 4.108  -22.450 16.371 1.00 18.52 ? 100 LEU   C CD2 1 
ATOM   1832 N  N   . ALA   B 1 95  ? 3.624  -27.229 16.712 1.00 15.37 ? 101 ALA   C N   1 
ATOM   1833 C  CA  . ALA   B 1 95  ? 3.133  -28.534 17.177 1.00 15.55 ? 101 ALA   C CA  1 
ATOM   1834 C  C   . ALA   B 1 95  ? 2.582  -28.368 18.590 1.00 16.29 ? 101 ALA   C C   1 
ATOM   1835 O  O   . ALA   B 1 95  ? 2.919  -27.408 19.295 1.00 16.34 ? 101 ALA   C O   1 
ATOM   1836 C  CB  . ALA   B 1 95  ? 4.281  -29.559 17.201 1.00 15.52 ? 101 ALA   C CB  1 
ATOM   1837 N  N   . VAL   B 1 96  ? 1.709  -29.295 19.002 1.00 16.07 ? 102 VAL   C N   1 
ATOM   1838 C  CA  . VAL   B 1 96  ? 1.236  -29.361 20.366 1.00 16.96 ? 102 VAL   C CA  1 
ATOM   1839 C  C   . VAL   B 1 96  ? 2.349  -30.122 21.120 1.00 19.30 ? 102 VAL   C C   1 
ATOM   1840 O  O   . VAL   B 1 96  ? 2.645  -31.280 20.810 1.00 19.80 ? 102 VAL   C O   1 
ATOM   1841 C  CB  . VAL   B 1 96  ? -0.110 -30.121 20.429 1.00 18.83 ? 102 VAL   C CB  1 
ATOM   1842 C  CG1 . VAL   B 1 96  ? -0.550 -30.277 21.890 1.00 19.30 ? 102 VAL   C CG1 1 
ATOM   1843 C  CG2 . VAL   B 1 96  ? -1.170 -29.385 19.596 1.00 19.62 ? 102 VAL   C CG2 1 
ATOM   1844 N  N   . GLY   B 1 97  ? 2.960  -29.454 22.072 1.00 21.89 ? 103 GLY   C N   1 
ATOM   1845 C  CA  . GLY   B 1 97  ? 4.040  -30.093 22.812 1.00 24.15 ? 103 GLY   C CA  1 
ATOM   1846 C  C   . GLY   B 1 97  ? 4.733  -29.169 23.743 1.00 25.60 ? 103 GLY   C C   1 
ATOM   1847 O  O   . GLY   B 1 97  ? 4.559  -27.941 23.684 1.00 26.50 ? 103 GLY   C O   1 
ATOM   1848 N  N   . HIS   B 1 98  ? 5.576  -29.779 24.566 1.00 24.16 ? 104 HIS   C N   1 
ATOM   1849 C  CA  . HIS   B 1 98  ? 6.249  -29.043 25.591 1.00 23.70 ? 104 HIS   C CA  1 
ATOM   1850 C  C   . HIS   B 1 98  ? 7.480  -28.334 25.127 1.00 23.11 ? 104 HIS   C C   1 
ATOM   1851 O  O   . HIS   B 1 98  ? 8.286  -28.876 24.349 1.00 23.01 ? 104 HIS   C O   1 
ATOM   1852 C  CB  . HIS   B 1 98  ? 6.611  -29.963 26.776 1.00 23.07 ? 104 HIS   C CB  1 
ATOM   1853 C  CG  . HIS   B 1 98  ? 7.257  -29.197 27.895 1.00 23.45 ? 104 HIS   C CG  1 
ATOM   1854 N  ND1 . HIS   B 1 98  ? 6.537  -28.266 28.659 1.00 25.68 ? 104 HIS   C ND1 1 
ATOM   1855 C  CD2 . HIS   B 1 98  ? 8.562  -29.152 28.269 1.00 22.82 ? 104 HIS   C CD2 1 
ATOM   1856 C  CE1 . HIS   B 1 98  ? 7.419  -27.732 29.489 1.00 25.72 ? 104 HIS   C CE1 1 
ATOM   1857 N  NE2 . HIS   B 1 98  ? 8.651  -28.246 29.289 1.00 24.98 ? 104 HIS   C NE2 1 
ATOM   1858 N  N   . SER   B 1 99  ? 7.645  -27.111 25.677 1.00 23.14 ? 105 SER   C N   1 
ATOM   1859 C  CA  . SER   B 1 99  ? 8.845  -26.302 25.555 1.00 23.58 ? 105 SER   C CA  1 
ATOM   1860 C  C   . SER   B 1 99  ? 8.966  -25.210 26.642 1.00 23.40 ? 105 SER   C C   1 
ATOM   1861 O  O   . SER   B 1 99  ? 7.985  -24.695 27.163 1.00 24.54 ? 105 SER   C O   1 
ATOM   1862 C  CB  . SER   B 1 99  ? 9.011  -25.714 24.158 1.00 25.36 ? 105 SER   C CB  1 
ATOM   1863 O  OG  . SER   B 1 99  ? 8.045  -24.711 23.910 1.00 28.01 ? 105 SER   C OG  1 
ATOM   1864 N  N   . GLU   B 1 100 ? 10.192 -24.945 27.037 1.00 23.07 ? 106 GLU   C N   1 
ATOM   1865 C  CA  . GLU   B 1 100 ? 10.631 -23.904 27.987 1.00 23.40 ? 106 GLU   C CA  1 
ATOM   1866 C  C   . GLU   B 1 100 ? 11.713 -23.072 27.259 1.00 22.25 ? 106 GLU   C C   1 
ATOM   1867 O  O   . GLU   B 1 100 ? 12.303 -23.559 26.309 1.00 21.33 ? 106 GLU   C O   1 
ATOM   1868 C  CB  . GLU   B 1 100 ? 11.250 -24.493 29.269 1.00 27.40 ? 106 GLU   C CB  1 
ATOM   1869 C  CG  . GLU   B 1 100 ? 10.548 -25.732 29.722 1.00 35.28 ? 106 GLU   C CG  1 
ATOM   1870 C  CD  . GLU   B 1 100 ? 9.988  -25.861 31.111 1.00 42.58 ? 106 GLU   C CD  1 
ATOM   1871 O  OE1 . GLU   B 1 100 ? 9.635  -24.842 31.747 1.00 44.59 ? 106 GLU   C OE1 1 
ATOM   1872 O  OE2 . GLU   B 1 100 ? 9.831  -27.027 31.529 1.00 44.48 ? 106 GLU   C OE2 1 
ATOM   1873 N  N   . PRO   B 1 101 ? 12.017 -21.825 27.687 1.00 23.91 ? 107 PRO   C N   1 
ATOM   1874 C  CA  . PRO   B 1 101 ? 12.993 -20.993 26.930 1.00 25.11 ? 107 PRO   C CA  1 
ATOM   1875 C  C   . PRO   B 1 101 ? 14.320 -21.650 26.486 1.00 25.10 ? 107 PRO   C C   1 
ATOM   1876 O  O   . PRO   B 1 101 ? 14.792 -21.481 25.344 1.00 27.20 ? 107 PRO   C O   1 
ATOM   1877 C  CB  . PRO   B 1 101 ? 13.255 -19.813 27.872 1.00 26.64 ? 107 PRO   C CB  1 
ATOM   1878 C  CG  . PRO   B 1 101 ? 11.985 -19.687 28.666 1.00 26.89 ? 107 PRO   C CG  1 
ATOM   1879 C  CD  . PRO   B 1 101 ? 11.397 -21.087 28.806 1.00 24.39 ? 107 PRO   C CD  1 
ATOM   1880 N  N   . GLY   B 1 102 ? 14.906 -22.415 27.387 1.00 22.99 ? 108 GLY   C N   1 
ATOM   1881 C  CA  . GLY   B 1 102 ? 16.159 -23.123 27.155 1.00 21.11 ? 108 GLY   C CA  1 
ATOM   1882 C  C   . GLY   B 1 102 ? 16.087 -24.248 26.131 1.00 19.52 ? 108 GLY   C C   1 
ATOM   1883 O  O   . GLY   B 1 102 ? 17.104 -24.873 25.800 1.00 19.40 ? 108 GLY   C O   1 
ATOM   1884 N  N   . ASP   B 1 103 ? 14.875 -24.495 25.591 1.00 17.39 ? 109 ASP   C N   1 
ATOM   1885 C  CA  . ASP   B 1 103 ? 14.696 -25.548 24.599 1.00 16.95 ? 109 ASP   C CA  1 
ATOM   1886 C  C   . ASP   B 1 103 ? 15.071 -25.134 23.186 1.00 15.81 ? 109 ASP   C C   1 
ATOM   1887 O  O   . ASP   B 1 103 ? 15.199 -26.010 22.317 1.00 15.83 ? 109 ASP   C O   1 
ATOM   1888 C  CB  . ASP   B 1 103 ? 13.252 -26.105 24.627 1.00 17.88 ? 109 ASP   C CB  1 
ATOM   1889 C  CG  . ASP   B 1 103 ? 13.007 -26.994 25.841 1.00 19.93 ? 109 ASP   C CG  1 
ATOM   1890 O  OD1 . ASP   B 1 103 ? 13.955 -27.626 26.309 1.00 19.59 ? 109 ASP   C OD1 1 
ATOM   1891 O  OD2 . ASP   B 1 103 ? 11.857 -27.046 26.316 1.00 20.64 ? 109 ASP   C OD2 1 
ATOM   1892 N  N   . CYS   B 1 104 ? 15.250 -23.825 22.915 1.00 14.70 ? 110 CYS   C N   1 
ATOM   1893 C  CA  . CYS   B 1 104 ? 15.675 -23.384 21.571 1.00 15.26 ? 110 CYS   C CA  1 
ATOM   1894 C  C   . CYS   B 1 104 ? 16.924 -24.081 21.127 1.00 16.06 ? 110 CYS   C C   1 
ATOM   1895 O  O   . CYS   B 1 104 ? 17.803 -24.294 21.959 1.00 16.47 ? 110 CYS   C O   1 
ATOM   1896 C  CB  . CYS   B 1 104 ? 15.832 -21.863 21.510 1.00 16.14 ? 110 CYS   C CB  1 
ATOM   1897 S  SG  . CYS   B 1 104 ? 14.247 -20.994 21.651 1.00 18.85 ? 110 CYS   C SG  1 
ATOM   1898 N  N   . GLY   B 1 105 ? 16.929 -24.533 19.883 1.00 14.89 ? 111 GLY   C N   1 
ATOM   1899 C  CA  . GLY   B 1 105 ? 18.100 -25.214 19.351 1.00 15.80 ? 111 GLY   C CA  1 
ATOM   1900 C  C   . GLY   B 1 105 ? 17.940 -26.718 19.263 1.00 16.00 ? 111 GLY   C C   1 
ATOM   1901 O  O   . GLY   B 1 105 ? 18.709 -27.390 18.565 1.00 16.37 ? 111 GLY   C O   1 
ATOM   1902 N  N   . GLY   B 1 106 ? 16.898 -27.254 19.903 1.00 14.11 ? 112 GLY   C N   1 
ATOM   1903 C  CA  . GLY   B 1 106 ? 16.635 -28.699 19.815 1.00 13.70 ? 112 GLY   C CA  1 
ATOM   1904 C  C   . GLY   B 1 106 ? 16.244 -29.047 18.383 1.00 14.77 ? 112 GLY   C C   1 
ATOM   1905 O  O   . GLY   B 1 106 ? 15.505 -28.289 17.742 1.00 15.65 ? 112 GLY   C O   1 
ATOM   1906 N  N   . ILE   B 1 107 ? 16.775 -30.176 17.861 1.00 14.63 ? 113 ILE   C N   1 
ATOM   1907 C  CA  . ILE   B 1 107 ? 16.510 -30.501 16.466 1.00 14.76 ? 113 ILE   C CA  1 
ATOM   1908 C  C   . ILE   B 1 107 ? 15.204 -31.287 16.285 1.00 14.16 ? 113 ILE   C C   1 
ATOM   1909 O  O   . ILE   B 1 107 ? 14.914 -32.232 17.055 1.00 15.61 ? 113 ILE   C O   1 
ATOM   1910 C  CB  . ILE   B 1 107 ? 17.747 -31.245 15.857 1.00 17.22 ? 113 ILE   C CB  1 
ATOM   1911 C  CG1 . ILE   B 1 107 ? 18.931 -30.247 15.618 1.00 18.83 ? 113 ILE   C CG1 1 
ATOM   1912 C  CG2 . ILE   B 1 107 ? 17.395 -32.001 14.554 1.00 19.09 ? 113 ILE   C CG2 1 
ATOM   1913 C  CD1 . ILE   B 1 107 ? 20.252 -30.987 15.160 1.00 23.00 ? 113 ILE   C CD1 1 
ATOM   1914 N  N   . LEU   B 1 108 ? 14.466 -30.956 15.208 1.00 12.69 ? 114 LEU   C N   1 
ATOM   1915 C  CA  . LEU   B 1 108 ? 13.289 -31.683 14.724 1.00 13.64 ? 114 LEU   C CA  1 
ATOM   1916 C  C   . LEU   B 1 108 ? 13.756 -32.486 13.479 1.00 14.05 ? 114 LEU   C C   1 
ATOM   1917 O  O   . LEU   B 1 108 ? 14.335 -31.906 12.547 1.00 14.42 ? 114 LEU   C O   1 
ATOM   1918 C  CB  . LEU   B 1 108 ? 12.178 -30.688 14.304 1.00 13.54 ? 114 LEU   C CB  1 
ATOM   1919 C  CG  . LEU   B 1 108 ? 10.946 -31.304 13.626 1.00 14.36 ? 114 LEU   C CG  1 
ATOM   1920 C  CD1 . LEU   B 1 108 ? 10.148 -32.239 14.592 1.00 15.72 ? 114 LEU   C CD1 1 
ATOM   1921 C  CD2 . LEU   B 1 108 ? 10.028 -30.178 13.097 1.00 14.39 ? 114 LEU   C CD2 1 
ATOM   1922 N  N   . ARG   B 1 109 ? 13.490 -33.794 13.467 1.00 12.73 ? 115 ARG   C N   1 
ATOM   1923 C  CA  . ARG   B 1 109 ? 13.866 -34.682 12.368 1.00 14.06 ? 115 ARG   C CA  1 
ATOM   1924 C  C   . ARG   B 1 109 ? 12.667 -35.454 11.876 1.00 14.65 ? 115 ARG   C C   1 
ATOM   1925 O  O   . ARG   B 1 109 ? 11.834 -35.880 12.671 1.00 14.60 ? 115 ARG   C O   1 
ATOM   1926 C  CB  . ARG   B 1 109 ? 14.938 -35.701 12.856 1.00 17.78 ? 115 ARG   C CB  1 
ATOM   1927 C  CG  . ARG   B 1 109 ? 16.341 -35.141 13.008 1.00 25.38 ? 115 ARG   C CG  1 
ATOM   1928 C  CD  . ARG   B 1 109 ? 17.345 -36.204 13.512 1.00 33.12 ? 115 ARG   C CD  1 
ATOM   1929 N  NE  . ARG   B 1 109 ? 18.720 -35.837 13.132 1.00 41.55 ? 115 ARG   C NE  1 
ATOM   1930 C  CZ  . ARG   B 1 109 ? 19.544 -35.129 13.895 1.00 44.53 ? 115 ARG   C CZ  1 
ATOM   1931 N  NH1 . ARG   B 1 109 ? 19.209 -34.832 15.148 1.00 42.44 ? 115 ARG   C NH1 1 
ATOM   1932 N  NH2 . ARG   B 1 109 ? 20.748 -34.801 13.450 1.00 46.61 ? 115 ARG   C NH2 1 
ATOM   1933 N  N   . CYS   B 1 110 ? 12.647 -35.756 10.590 1.00 14.81 ? 116 CYS   C N   1 
ATOM   1934 C  CA  . CYS   B 1 110 ? 11.647 -36.683 10.039 1.00 16.33 ? 116 CYS   C CA  1 
ATOM   1935 C  C   . CYS   B 1 110 ? 12.432 -37.893 9.481  1.00 17.65 ? 116 CYS   C C   1 
ATOM   1936 O  O   . CYS   B 1 110 ? 13.651 -37.989 9.655  1.00 17.83 ? 116 CYS   C O   1 
ATOM   1937 C  CB  . CYS   B 1 110 ? 10.832 -36.002 8.940  1.00 15.52 ? 116 CYS   C CB  1 
ATOM   1938 S  SG  . CYS   B 1 110 ? 11.840 -35.515 7.508  1.00 15.02 ? 116 CYS   C SG  1 
ATOM   1939 N  N   . GLN   B 1 111 ? 11.743 -38.791 8.736  1.00 18.52 ? 117 GLN   C N   1 
ATOM   1940 C  CA  . GLN   B 1 111 ? 12.416 -39.939 8.133  1.00 19.87 ? 117 GLN   C CA  1 
ATOM   1941 C  C   . GLN   B 1 111 ? 13.488 -39.552 7.101  1.00 20.02 ? 117 GLN   C C   1 
ATOM   1942 O  O   . GLN   B 1 111 ? 14.308 -40.390 6.726  1.00 21.77 ? 117 GLN   C O   1 
ATOM   1943 C  CB  . GLN   B 1 111 ? 11.384 -40.874 7.491  1.00 22.80 ? 117 GLN   C CB  1 
ATOM   1944 C  CG  . GLN   B 1 111 ? 10.693 -40.257 6.280  1.00 25.30 ? 117 GLN   C CG  1 
ATOM   1945 C  CD  . GLN   B 1 111 ? 9.640  -41.183 5.722  1.00 33.34 ? 117 GLN   C CD  1 
ATOM   1946 O  OE1 . GLN   B 1 111 ? 8.442  -40.945 5.893  1.00 35.70 ? 117 GLN   C OE1 1 
ATOM   1947 N  NE2 . GLN   B 1 111 ? 10.071 -42.254 5.061  1.00 35.15 ? 117 GLN   C NE2 1 
ATOM   1948 N  N   . HIS   B 1 112 ? 13.498 -38.283 6.625  1.00 18.12 ? 118 HIS   C N   1 
ATOM   1949 C  CA  . HIS   B 1 112 ? 14.412 -37.827 5.581  1.00 17.50 ? 118 HIS   C CA  1 
ATOM   1950 C  C   . HIS   B 1 112 ? 15.627 -37.064 6.110  1.00 18.88 ? 118 HIS   C C   1 
ATOM   1951 O  O   . HIS   B 1 112 ? 16.547 -36.790 5.335  1.00 20.23 ? 118 HIS   C O   1 
ATOM   1952 C  CB  . HIS   B 1 112 ? 13.662 -36.949 4.561  1.00 17.24 ? 118 HIS   C CB  1 
ATOM   1953 C  CG  . HIS   B 1 112 ? 12.461 -37.609 3.958  1.00 17.76 ? 118 HIS   C CG  1 
ATOM   1954 N  ND1 . HIS   B 1 112 ? 11.170 -37.206 4.276  1.00 16.93 ? 118 HIS   C ND1 1 
ATOM   1955 C  CD2 . HIS   B 1 112 ? 12.393 -38.602 3.039  1.00 18.94 ? 118 HIS   C CD2 1 
ATOM   1956 C  CE1 . HIS   B 1 112 ? 10.352 -37.983 3.579  1.00 18.58 ? 118 HIS   C CE1 1 
ATOM   1957 N  NE2 . HIS   B 1 112 ? 11.029 -38.853 2.817  1.00 19.91 ? 118 HIS   C NE2 1 
ATOM   1958 N  N   . GLY   B 1 113 ? 15.630 -36.701 7.397  1.00 17.84 ? 119 GLY   C N   1 
ATOM   1959 C  CA  . GLY   B 1 113 ? 16.744 -35.936 7.952  1.00 16.26 ? 119 GLY   C CA  1 
ATOM   1960 C  C   . GLY   B 1 113 ? 16.286 -34.771 8.812  1.00 15.34 ? 119 GLY   C C   1 
ATOM   1961 O  O   . GLY   B 1 113 ? 15.173 -34.788 9.350  1.00 15.06 ? 119 GLY   C O   1 
ATOM   1962 N  N   . VAL   B 1 114 ? 17.163 -33.784 8.969  1.00 14.71 ? 120 VAL   C N   1 
ATOM   1963 C  CA  . VAL   B 1 114 ? 16.854 -32.603 9.785  1.00 14.33 ? 120 VAL   C CA  1 
ATOM   1964 C  C   . VAL   B 1 114 ? 15.825 -31.690 9.113  1.00 13.72 ? 120 VAL   C C   1 
ATOM   1965 O  O   . VAL   B 1 114 ? 16.009 -31.280 7.951  1.00 15.21 ? 120 VAL   C O   1 
ATOM   1966 C  CB  . VAL   B 1 114 ? 18.139 -31.825 10.105 1.00 15.42 ? 120 VAL   C CB  1 
ATOM   1967 C  CG1 . VAL   B 1 114 ? 17.788 -30.529 10.827 1.00 15.91 ? 120 VAL   C CG1 1 
ATOM   1968 C  CG2 . VAL   B 1 114 ? 19.112 -32.693 10.950 1.00 16.11 ? 120 VAL   C CG2 1 
ATOM   1969 N  N   . VAL   B 1 115 ? 14.751 -31.326 9.851  1.00 13.12 ? 121 VAL   C N   1 
ATOM   1970 C  CA  . VAL   B 1 115 ? 13.689 -30.482 9.342  1.00 13.00 ? 121 VAL   C CA  1 
ATOM   1971 C  C   . VAL   B 1 115 ? 13.894 -29.037 9.812  1.00 14.31 ? 121 VAL   C C   1 
ATOM   1972 O  O   . VAL   B 1 115 ? 13.621 -28.105 9.064  1.00 13.66 ? 121 VAL   C O   1 
ATOM   1973 C  CB  . VAL   B 1 115 ? 12.308 -31.008 9.849  1.00 14.42 ? 121 VAL   C CB  1 
ATOM   1974 C  CG1 . VAL   B 1 115 ? 11.176 -30.015 9.534  1.00 14.92 ? 121 VAL   C CG1 1 
ATOM   1975 C  CG2 . VAL   B 1 115 ? 12.018 -32.377 9.256  1.00 15.18 ? 121 VAL   C CG2 1 
ATOM   1976 N  N   . GLY   B 1 116 ? 14.269 -28.873 11.091 1.00 13.57 ? 122 GLY   C N   1 
ATOM   1977 C  CA  . GLY   B 1 116 ? 14.378 -27.518 11.641 1.00 14.53 ? 122 GLY   C CA  1 
ATOM   1978 C  C   . GLY   B 1 116 ? 14.798 -27.519 13.088 1.00 13.97 ? 122 GLY   C C   1 
ATOM   1979 O  O   . GLY   B 1 116 ? 15.233 -28.552 13.587 1.00 15.01 ? 122 GLY   C O   1 
ATOM   1980 N  N   . ILE   B 1 117 ? 14.742 -26.344 13.742 1.00 12.69 ? 123 ILE   C N   1 
ATOM   1981 C  CA  . ILE   B 1 117 ? 15.181 -26.277 15.138 1.00 13.71 ? 123 ILE   C CA  1 
ATOM   1982 C  C   . ILE   B 1 117 ? 14.137 -25.570 15.972 1.00 13.08 ? 123 ILE   C C   1 
ATOM   1983 O  O   . ILE   B 1 117 ? 13.508 -24.648 15.496 1.00 13.20 ? 123 ILE   C O   1 
ATOM   1984 C  CB  . ILE   B 1 117 ? 16.529 -25.549 15.282 1.00 16.53 ? 123 ILE   C CB  1 
ATOM   1985 C  CG1 . ILE   B 1 117 ? 16.547 -24.213 14.518 1.00 17.75 ? 123 ILE   C CG1 1 
ATOM   1986 C  CG2 . ILE   B 1 117 ? 17.707 -26.460 14.910 1.00 18.53 ? 123 ILE   C CG2 1 
ATOM   1987 C  CD1 . ILE   B 1 117 ? 17.906 -23.397 14.812 1.00 21.59 ? 123 ILE   C CD1 1 
ATOM   1988 N  N   . VAL   B 1 118 ? 14.014 -25.940 17.277 1.00 12.24 ? 124 VAL   C N   1 
ATOM   1989 C  CA  . VAL   B 1 118 ? 13.071 -25.227 18.160 1.00 12.00 ? 124 VAL   C CA  1 
ATOM   1990 C  C   . VAL   B 1 118 ? 13.412 -23.714 18.185 1.00 13.57 ? 124 VAL   C C   1 
ATOM   1991 O  O   . VAL   B 1 118 ? 14.586 -23.356 18.331 1.00 13.47 ? 124 VAL   C O   1 
ATOM   1992 C  CB  . VAL   B 1 118 ? 13.135 -25.794 19.609 1.00 13.01 ? 124 VAL   C CB  1 
ATOM   1993 C  CG1 . VAL   B 1 118 ? 12.214 -24.982 20.538 1.00 13.62 ? 124 VAL   C CG1 1 
ATOM   1994 C  CG2 . VAL   B 1 118 ? 12.738 -27.282 19.642 1.00 14.40 ? 124 VAL   C CG2 1 
ATOM   1995 N  N   . SER   B 1 119 ? 12.393 -22.865 18.053 1.00 13.37 ? 125 SER   C N   1 
ATOM   1996 C  CA  . SER   B 1 119 ? 12.608 -21.418 18.000 1.00 13.18 ? 125 SER   C CA  1 
ATOM   1997 C  C   . SER   B 1 119 ? 11.661 -20.640 18.889 1.00 14.47 ? 125 SER   C C   1 
ATOM   1998 O  O   . SER   B 1 119 ? 12.030 -19.565 19.374 1.00 15.10 ? 125 SER   C O   1 
ATOM   1999 C  CB  . SER   B 1 119 ? 12.511 -20.938 16.545 1.00 14.43 ? 125 SER   C CB  1 
ATOM   2000 O  OG  . SER   B 1 119 ? 12.675 -19.521 16.443 1.00 16.47 ? 125 SER   C OG  1 
ATOM   2001 N  N   . THR   B 1 120 ? 10.442 -21.151 19.123 1.00 13.89 ? 126 THR   C N   1 
ATOM   2002 C  CA  . THR   B 1 120 ? 9.436  -20.458 19.957 1.00 15.39 ? 126 THR   C CA  1 
ATOM   2003 C  C   . THR   B 1 120 ? 8.654  -21.492 20.807 1.00 15.88 ? 126 THR   C C   1 
ATOM   2004 O  O   . THR   B 1 120 ? 8.744  -22.711 20.572 1.00 13.70 ? 126 THR   C O   1 
ATOM   2005 C  CB  . THR   B 1 120 ? 8.408  -19.679 19.076 1.00 17.57 ? 126 THR   C CB  1 
ATOM   2006 O  OG1 . THR   B 1 120 ? 7.564  -20.632 18.395 1.00 18.01 ? 126 THR   C OG1 1 
ATOM   2007 C  CG2 . THR   B 1 120 ? 9.047  -18.760 18.066 1.00 17.80 ? 126 THR   C CG2 1 
ATOM   2008 N  N   . GLY   B 1 121 ? 7.903  -21.016 21.794 1.00 16.93 ? 127 GLY   C N   1 
ATOM   2009 C  CA  . GLY   B 1 121 ? 7.055  -21.911 22.578 1.00 19.75 ? 127 GLY   C CA  1 
ATOM   2010 C  C   . GLY   B 1 121 ? 6.152  -21.151 23.519 1.00 21.39 ? 127 GLY   C C   1 
ATOM   2011 O  O   . GLY   B 1 121 ? 6.295  -19.946 23.683 1.00 20.24 ? 127 GLY   C O   1 
ATOM   2012 N  N   . GLY   B 1 122 ? 5.219  -21.868 24.130 1.00 24.29 ? 128 GLY   C N   1 
ATOM   2013 C  CA  . GLY   B 1 122 ? 4.270  -21.302 25.085 1.00 25.95 ? 128 GLY   C CA  1 
ATOM   2014 C  C   . GLY   B 1 122 ? 2.857  -21.783 24.815 1.00 27.22 ? 128 GLY   C C   1 
ATOM   2015 O  O   . GLY   B 1 122 ? 2.568  -22.230 23.708 1.00 26.77 ? 128 GLY   C O   1 
ATOM   2016 N  N   . ASN   B 1 123 ? 1.948  -21.712 25.828 1.00 28.66 ? 129 ASN   C N   1 
ATOM   2017 C  CA  . ASN   B 1 123 ? 0.554  -22.176 25.676 1.00 29.81 ? 129 ASN   C CA  1 
ATOM   2018 C  C   . ASN   B 1 123 ? 0.434  -23.632 25.246 1.00 28.94 ? 129 ASN   C C   1 
ATOM   2019 O  O   . ASN   B 1 123 ? -0.544 -24.011 24.575 1.00 31.28 ? 129 ASN   C O   1 
ATOM   2020 C  CB  . ASN   B 1 123 ? -0.224 -21.294 24.712 1.00 32.73 ? 129 ASN   C CB  1 
ATOM   2021 C  CG  . ASN   B 1 123 ? -0.807 -20.075 25.357 1.00 36.69 ? 129 ASN   C CG  1 
ATOM   2022 O  OD1 . ASN   B 1 123 ? -1.099 -20.054 26.552 1.00 38.59 ? 129 ASN   C OD1 1 
ATOM   2023 N  ND2 . ASN   B 1 123 ? -1.037 -19.060 24.560 1.00 37.97 ? 129 ASN   C ND2 1 
ATOM   2024 N  N   . GLY   B 1 124 ? 1.405  -24.447 25.626 1.00 25.87 ? 130 GLY   C N   1 
ATOM   2025 C  CA  . GLY   B 1 124 ? 1.389  -25.847 25.234 1.00 24.47 ? 130 GLY   C CA  1 
ATOM   2026 C  C   . GLY   B 1 124 ? 1.654  -26.052 23.753 1.00 22.30 ? 130 GLY   C C   1 
ATOM   2027 O  O   . GLY   B 1 124 ? 1.259  -27.068 23.196 1.00 23.49 ? 130 GLY   C O   1 
ATOM   2028 N  N   . LEU   B 1 125 ? 2.327  -25.084 23.097 1.00 19.87 ? 131 LEU   C N   1 
ATOM   2029 C  CA  . LEU   B 1 125 ? 2.696  -25.222 21.710 1.00 19.76 ? 131 LEU   C CA  1 
ATOM   2030 C  C   . LEU   B 1 125 ? 4.223  -25.096 21.634 1.00 19.24 ? 131 LEU   C C   1 
ATOM   2031 O  O   . LEU   B 1 125 ? 4.852  -24.517 22.524 1.00 21.42 ? 131 LEU   C O   1 
ATOM   2032 C  CB  . LEU   B 1 125 ? 2.079  -24.110 20.858 1.00 21.82 ? 131 LEU   C CB  1 
ATOM   2033 C  CG  . LEU   B 1 125 ? 0.552  -23.973 20.919 1.00 25.42 ? 131 LEU   C CG  1 
ATOM   2034 C  CD1 . LEU   B 1 125 ? 0.102  -22.648 20.253 1.00 27.91 ? 131 LEU   C CD1 1 
ATOM   2035 C  CD2 . LEU   B 1 125 ? -0.120 -25.155 20.214 1.00 25.25 ? 131 LEU   C CD2 1 
ATOM   2036 N  N   . VAL   B 1 126 ? 4.808  -25.719 20.625 1.00 15.51 ? 132 VAL   C N   1 
ATOM   2037 C  CA  . VAL   B 1 126 ? 6.239  -25.574 20.352 1.00 15.21 ? 132 VAL   C CA  1 
ATOM   2038 C  C   . VAL   B 1 126 ? 6.374  -25.139 18.896 1.00 15.59 ? 132 VAL   C C   1 
ATOM   2039 O  O   . VAL   B 1 126 ? 5.631  -25.624 18.019 1.00 16.07 ? 132 VAL   C O   1 
ATOM   2040 C  CB  . VAL   B 1 126 ? 7.062  -26.833 20.691 1.00 16.75 ? 132 VAL   C CB  1 
ATOM   2041 C  CG1 . VAL   B 1 126 ? 6.562  -28.063 19.966 1.00 18.27 ? 132 VAL   C CG1 1 
ATOM   2042 C  CG2 . VAL   B 1 126 ? 8.574  -26.605 20.450 1.00 17.00 ? 132 VAL   C CG2 1 
ATOM   2043 N  N   . GLY   B 1 127 ? 7.304  -24.191 18.633 1.00 14.09 ? 133 GLY   C N   1 
ATOM   2044 C  CA  . GLY   B 1 127 ? 7.479  -23.718 17.261 1.00 13.87 ? 133 GLY   C CA  1 
ATOM   2045 C  C   . GLY   B 1 127 ? 8.869  -24.029 16.751 1.00 13.73 ? 133 GLY   C C   1 
ATOM   2046 O  O   . GLY   B 1 127 ? 9.862  -23.921 17.484 1.00 14.16 ? 133 GLY   C O   1 
ATOM   2047 N  N   . PHE   B 1 128 ? 8.932  -24.499 15.501 1.00 13.04 ? 134 PHE   C N   1 
ATOM   2048 C  CA  . PHE   B 1 128 ? 10.225 -24.868 14.883 1.00 12.91 ? 134 PHE   C CA  1 
ATOM   2049 C  C   . PHE   B 1 128 ? 10.506 -24.007 13.667 1.00 12.85 ? 134 PHE   C C   1 
ATOM   2050 O  O   . PHE   B 1 128 ? 9.645  -23.860 12.796 1.00 12.84 ? 134 PHE   C O   1 
ATOM   2051 C  CB  . PHE   B 1 128 ? 10.178 -26.337 14.386 1.00 12.63 ? 134 PHE   C CB  1 
ATOM   2052 C  CG  . PHE   B 1 128 ? 9.738  -27.332 15.436 1.00 12.82 ? 134 PHE   C CG  1 
ATOM   2053 C  CD1 . PHE   B 1 128 ? 10.643 -27.863 16.322 1.00 12.92 ? 134 PHE   C CD1 1 
ATOM   2054 C  CD2 . PHE   B 1 128 ? 8.412  -27.749 15.511 1.00 13.80 ? 134 PHE   C CD2 1 
ATOM   2055 C  CE1 . PHE   B 1 128 ? 10.242 -28.765 17.293 1.00 13.69 ? 134 PHE   C CE1 1 
ATOM   2056 C  CE2 . PHE   B 1 128 ? 8.006  -28.663 16.484 1.00 14.79 ? 134 PHE   C CE2 1 
ATOM   2057 C  CZ  . PHE   B 1 128 ? 8.931  -29.152 17.383 1.00 14.57 ? 134 PHE   C CZ  1 
ATOM   2058 N  N   . ALA   B 1 129 ? 11.734 -23.495 13.586 1.00 12.40 ? 135 ALA   C N   1 
ATOM   2059 C  CA  . ALA   B 1 129 ? 12.175 -22.741 12.411 1.00 12.37 ? 135 ALA   C CA  1 
ATOM   2060 C  C   . ALA   B 1 129 ? 12.545 -23.750 11.325 1.00 13.37 ? 135 ALA   C C   1 
ATOM   2061 O  O   . ALA   B 1 129 ? 13.462 -24.560 11.523 1.00 13.00 ? 135 ALA   C O   1 
ATOM   2062 C  CB  . ALA   B 1 129 ? 13.413 -21.910 12.767 1.00 13.07 ? 135 ALA   C CB  1 
ATOM   2063 N  N   . ASP   B 1 130 ? 11.839 -23.722 10.183 1.00 13.49 ? 136 ASP   C N   1 
ATOM   2064 C  CA  . ASP   B 1 130 ? 12.134 -24.670 9.094  1.00 13.81 ? 136 ASP   C CA  1 
ATOM   2065 C  C   . ASP   B 1 130 ? 13.470 -24.366 8.434  1.00 14.35 ? 136 ASP   C C   1 
ATOM   2066 O  O   . ASP   B 1 130 ? 13.823 -23.191 8.265  1.00 14.35 ? 136 ASP   C O   1 
ATOM   2067 C  CB  . ASP   B 1 130 ? 11.000 -24.552 8.037  1.00 14.99 ? 136 ASP   C CB  1 
ATOM   2068 C  CG  . ASP   B 1 130 ? 11.107 -25.573 6.924  1.00 21.25 ? 136 ASP   C CG  1 
ATOM   2069 O  OD1 . ASP   B 1 130 ? 11.296 -26.747 7.227  1.00 20.35 ? 136 ASP   C OD1 1 
ATOM   2070 O  OD2 . ASP   B 1 130 ? 11.078 -25.172 5.753  1.00 25.31 ? 136 ASP   C OD2 1 
ATOM   2071 N  N   . VAL   B 1 131 ? 14.198 -25.417 7.991  1.00 13.23 ? 137 VAL   C N   1 
ATOM   2072 C  CA  . VAL   B 1 131 ? 15.438 -25.193 7.209  1.00 13.33 ? 137 VAL   C CA  1 
ATOM   2073 C  C   . VAL   B 1 131 ? 15.406 -25.969 5.876  1.00 14.74 ? 137 VAL   C C   1 
ATOM   2074 O  O   . VAL   B 1 131 ? 16.390 -25.919 5.111  1.00 15.48 ? 137 VAL   C O   1 
ATOM   2075 C  CB  . VAL   B 1 131 ? 16.744 -25.540 7.963  1.00 14.99 ? 137 VAL   C CB  1 
ATOM   2076 C  CG1 . VAL   B 1 131 ? 16.871 -24.696 9.238  1.00 15.50 ? 137 VAL   C CG1 1 
ATOM   2077 C  CG2 . VAL   B 1 131 ? 16.834 -27.040 8.273  1.00 15.12 ? 137 VAL   C CG2 1 
ATOM   2078 N  N   . ARG   B 1 132 ? 14.273 -26.639 5.560  1.00 13.92 ? 138 ARG   C N   1 
ATOM   2079 C  CA  . ARG   B 1 132 ? 14.211 -27.480 4.372  1.00 12.60 ? 138 ARG   C CA  1 
ATOM   2080 C  C   . ARG   B 1 132 ? 14.244 -26.726 3.071  1.00 15.14 ? 138 ARG   C C   1 
ATOM   2081 O  O   . ARG   B 1 132 ? 14.630 -27.325 2.062  1.00 16.95 ? 138 ARG   C O   1 
ATOM   2082 C  CB  . ARG   B 1 132 ? 12.961 -28.362 4.426  1.00 12.70 ? 138 ARG   C CB  1 
ATOM   2083 C  CG  . ARG   B 1 132 ? 12.952 -29.325 5.591  1.00 12.67 ? 138 ARG   C CG  1 
ATOM   2084 C  CD  . ARG   B 1 132 ? 11.632 -30.065 5.580  1.00 12.79 ? 138 ARG   C CD  1 
ATOM   2085 N  NE  . ARG   B 1 132 ? 10.555 -29.181 6.037  1.00 12.46 ? 138 ARG   C NE  1 
ATOM   2086 C  CZ  . ARG   B 1 132 ? 9.307  -29.572 6.269  1.00 15.90 ? 138 ARG   C CZ  1 
ATOM   2087 N  NH1 . ARG   B 1 132 ? 8.939  -30.821 6.033  1.00 13.94 ? 138 ARG   C NH1 1 
ATOM   2088 N  NH2 . ARG   B 1 132 ? 8.417  -28.715 6.749  1.00 14.98 ? 138 ARG   C NH2 1 
ATOM   2089 N  N   . ASP   B 1 133 ? 13.907 -25.446 3.071  1.00 14.97 ? 139 ASP   C N   1 
ATOM   2090 C  CA  . ASP   B 1 133 ? 13.989 -24.630 1.849  1.00 16.15 ? 139 ASP   C CA  1 
ATOM   2091 C  C   . ASP   B 1 133 ? 15.371 -24.081 1.582  1.00 16.86 ? 139 ASP   C C   1 
ATOM   2092 O  O   . ASP   B 1 133 ? 15.593 -23.547 0.495  1.00 17.13 ? 139 ASP   C O   1 
ATOM   2093 C  CB  . ASP   B 1 133 ? 12.980 -23.483 1.893  1.00 18.39 ? 139 ASP   C CB  1 
ATOM   2094 C  CG  . ASP   B 1 133 ? 13.281 -22.489 2.994  1.00 22.52 ? 139 ASP   C CG  1 
ATOM   2095 O  OD1 . ASP   B 1 133 ? 13.518 -22.936 4.139  1.00 23.24 ? 139 ASP   C OD1 1 
ATOM   2096 O  OD2 . ASP   B 1 133 ? 13.303 -21.246 2.700  1.00 22.97 ? 139 ASP   C OD2 1 
ATOM   2097 N  N   . LEU   B 1 134 ? 16.314 -24.201 2.530  1.00 15.75 ? 140 LEU   C N   1 
ATOM   2098 C  CA  . LEU   B 1 134 ? 17.668 -23.655 2.340  1.00 16.22 ? 140 LEU   C CA  1 
ATOM   2099 C  C   . LEU   B 1 134 ? 18.526 -24.651 1.562  1.00 17.12 ? 140 LEU   C C   1 
ATOM   2100 O  O   . LEU   B 1 134 ? 19.389 -25.368 2.113  1.00 17.18 ? 140 LEU   C O   1 
ATOM   2101 C  CB  . LEU   B 1 134 ? 18.275 -23.324 3.719  1.00 16.68 ? 140 LEU   C CB  1 
ATOM   2102 C  CG  . LEU   B 1 134 ? 17.420 -22.384 4.579  1.00 18.35 ? 140 LEU   C CG  1 
ATOM   2103 C  CD1 . LEU   B 1 134 ? 18.087 -22.198 5.981  1.00 19.44 ? 140 LEU   C CD1 1 
ATOM   2104 C  CD2 . LEU   B 1 134 ? 17.200 -21.034 3.881  1.00 19.80 ? 140 LEU   C CD2 1 
ATOM   2105 N  N   . LEU   B 1 135 ? 18.288 -24.700 0.240  1.00 16.69 ? 141 LEU   C N   1 
ATOM   2106 C  CA  . LEU   B 1 135 ? 18.940 -25.728 -0.586 1.00 17.56 ? 141 LEU   C CA  1 
ATOM   2107 C  C   . LEU   B 1 135 ? 20.432 -25.585 -0.665 1.00 19.27 ? 141 LEU   C C   1 
ATOM   2108 O  O   . LEU   B 1 135 ? 21.133 -26.589 -0.844 1.00 21.40 ? 141 LEU   C O   1 
ATOM   2109 C  CB  . LEU   B 1 135 ? 18.325 -25.787 -1.987 1.00 17.08 ? 141 LEU   C CB  1 
ATOM   2110 C  CG  . LEU   B 1 135 ? 16.806 -25.789 -2.059 1.00 17.86 ? 141 LEU   C CG  1 
ATOM   2111 C  CD1 . LEU   B 1 135 ? 16.327 -26.056 -3.460 1.00 19.03 ? 141 LEU   C CD1 1 
ATOM   2112 C  CD2 . LEU   B 1 135 ? 16.182 -26.861 -1.154 1.00 18.13 ? 141 LEU   C CD2 1 
ATOM   2113 N  N   . TRP   B 1 136 ? 20.926 -24.337 -0.548 1.00 19.13 ? 142 TRP   C N   1 
ATOM   2114 C  CA  . TRP   B 1 136 ? 22.360 -24.049 -0.627 1.00 20.62 ? 142 TRP   C CA  1 
ATOM   2115 C  C   . TRP   B 1 136 ? 23.171 -24.645 0.543  1.00 21.98 ? 142 TRP   C C   1 
ATOM   2116 O  O   . TRP   B 1 136 ? 24.405 -24.703 0.451  1.00 22.61 ? 142 TRP   C O   1 
ATOM   2117 C  CB  . TRP   B 1 136 ? 22.581 -22.527 -0.715 1.00 20.45 ? 142 TRP   C CB  1 
ATOM   2118 C  CG  . TRP   B 1 136 ? 21.904 -21.735 0.364  1.00 20.76 ? 142 TRP   C CG  1 
ATOM   2119 C  CD1 . TRP   B 1 136 ? 20.657 -21.180 0.323  1.00 21.08 ? 142 TRP   C CD1 1 
ATOM   2120 C  CD2 . TRP   B 1 136 ? 22.442 -21.426 1.667  1.00 20.68 ? 142 TRP   C CD2 1 
ATOM   2121 N  NE1 . TRP   B 1 136 ? 20.394 -20.527 1.511  1.00 21.53 ? 142 TRP   C NE1 1 
ATOM   2122 C  CE2 . TRP   B 1 136 ? 21.504 -20.612 2.323  1.00 21.25 ? 142 TRP   C CE2 1 
ATOM   2123 C  CE3 . TRP   B 1 136 ? 23.666 -21.699 2.309  1.00 21.20 ? 142 TRP   C CE3 1 
ATOM   2124 C  CZ2 . TRP   B 1 136 ? 21.709 -20.148 3.627  1.00 22.00 ? 142 TRP   C CZ2 1 
ATOM   2125 C  CZ3 . TRP   B 1 136 ? 23.902 -21.151 3.568  1.00 22.92 ? 142 TRP   C CZ3 1 
ATOM   2126 C  CH2 . TRP   B 1 136 ? 22.937 -20.375 4.204  1.00 22.87 ? 142 TRP   C CH2 1 
ATOM   2127 N  N   . LEU   B 1 137 ? 22.495 -25.130 1.615  1.00 21.97 ? 143 LEU   C N   1 
ATOM   2128 C  CA  . LEU   B 1 137 ? 23.243 -25.738 2.731  1.00 23.62 ? 143 LEU   C CA  1 
ATOM   2129 C  C   . LEU   B 1 137 ? 24.003 -26.996 2.270  1.00 27.57 ? 143 LEU   C C   1 
ATOM   2130 O  O   . LEU   B 1 137 ? 25.036 -27.315 2.855  1.00 29.05 ? 143 LEU   C O   1 
ATOM   2131 C  CB  . LEU   B 1 137 ? 22.303 -26.110 3.894  1.00 21.61 ? 143 LEU   C CB  1 
ATOM   2132 C  CG  . LEU   B 1 137 ? 21.755 -24.978 4.748  1.00 20.83 ? 143 LEU   C CG  1 
ATOM   2133 C  CD1 . LEU   B 1 137 ? 20.712 -25.508 5.757  1.00 20.88 ? 143 LEU   C CD1 1 
ATOM   2134 C  CD2 . LEU   B 1 137 ? 22.893 -24.233 5.512  1.00 20.94 ? 143 LEU   C CD2 1 
ATOM   2135 N  N   . ASP   B 1 138 ? 23.464 -27.691 1.242  1.00 30.66 ? 144 ASP   C N   1 
ATOM   2136 C  CA  . ASP   B 1 138 ? 23.915 -28.940 0.609  1.00 34.92 ? 144 ASP   C CA  1 
ATOM   2137 C  C   . ASP   B 1 138 ? 25.016 -28.786 -0.397 1.00 38.35 ? 144 ASP   C C   1 
ATOM   2138 O  O   . ASP   B 1 138 ? 25.506 -29.806 -0.876 1.00 39.18 ? 144 ASP   C O   1 
ATOM   2139 C  CB  . ASP   B 1 138 ? 22.761 -29.520 -0.224 1.00 37.23 ? 144 ASP   C CB  1 
ATOM   2140 C  CG  . ASP   B 1 138 ? 21.652 -30.199 0.527  1.00 41.24 ? 144 ASP   C CG  1 
ATOM   2141 O  OD1 . ASP   B 1 138 ? 21.852 -30.523 1.712  1.00 42.30 ? 144 ASP   C OD1 1 
ATOM   2142 O  OD2 . ASP   B 1 138 ? 20.569 -30.420 -0.084 1.00 43.95 ? 144 ASP   C OD2 1 
ATOM   2143 N  N   . GLU   B 1 139 ? 25.269 -27.561 -0.874 1.00 40.25 ? 145 GLU   C N   1 
ATOM   2144 C  CA  . GLU   B 1 139 ? 26.255 -27.338 -1.923 1.00 43.06 ? 145 GLU   C CA  1 
ATOM   2145 C  C   . GLU   B 1 139 ? 27.424 -26.478 -1.467 1.00 44.97 ? 145 GLU   C C   1 
ATOM   2146 O  O   . GLU   B 1 139 ? 28.267 -26.123 -2.297 1.00 46.55 ? 145 GLU   C O   1 
ATOM   2147 C  CB  . GLU   B 1 139 ? 25.583 -26.729 -3.164 1.00 46.96 ? 145 GLU   C CB  1 
ATOM   2148 C  CG  . GLU   B 1 139 ? 25.045 -25.323 -2.957 1.00 53.70 ? 145 GLU   C CG  1 
ATOM   2149 C  CD  . GLU   B 1 139 ? 23.971 -24.924 -3.954 1.00 62.36 ? 145 GLU   C CD  1 
ATOM   2150 O  OE1 . GLU   B 1 139 ? 23.916 -23.730 -4.334 1.00 63.49 ? 145 GLU   C OE1 1 
ATOM   2151 O  OE2 . GLU   B 1 139 ? 23.176 -25.808 -4.349 1.00 65.00 ? 145 GLU   C OE2 1 
HETATM 2152 N  N1  . A1B5A C 2 .   ? 28.462 10.181  6.949  1.00 18.11 ? 201 A1B5A A N1  1 
HETATM 2153 N  N3  . A1B5A C 2 .   ? 23.836 13.714  15.071 1.00 16.13 ? 201 A1B5A A N3  1 
HETATM 2154 C  C4  . A1B5A C 2 .   ? 26.699 11.198  8.228  1.00 16.88 ? 201 A1B5A A C4  1 
HETATM 2155 C  C5  . A1B5A C 2 .   ? 25.959 12.453  8.635  1.00 16.81 ? 201 A1B5A A C5  1 
HETATM 2156 C  C6  . A1B5A C 2 .   ? 26.134 12.785  10.106 1.00 16.42 ? 201 A1B5A A C6  1 
HETATM 2157 C  C7  . A1B5A C 2 .   ? 24.382 14.534  9.807  1.00 16.31 ? 201 A1B5A A C7  1 
HETATM 2158 C  C8  . A1B5A C 2 .   ? 23.017 14.497  10.456 1.00 16.91 ? 201 A1B5A A C8  1 
HETATM 2159 C  C10 . A1B5A C 2 .   ? 24.122 14.091  12.702 1.00 16.27 ? 201 A1B5A A C10 1 
HETATM 2160 O  O1  . A1B5A C 2 .   ? 24.712 15.672  14.409 1.00 17.05 ? 201 A1B5A A O1  1 
HETATM 2161 C  C11 . A1B5A C 2 .   ? 24.240 14.566  14.140 1.00 16.42 ? 201 A1B5A A C11 1 
HETATM 2162 C  C9  . A1B5A C 2 .   ? 23.115 14.953  11.917 1.00 16.81 ? 201 A1B5A A C9  1 
HETATM 2163 C  C12 . A1B5A C 2 .   ? 25.486 14.183  12.006 1.00 16.24 ? 201 A1B5A A C12 1 
HETATM 2164 N  N2  . A1B5A C 2 .   ? 25.369 13.784  10.601 1.00 16.43 ? 201 A1B5A A N2  1 
HETATM 2165 O  O   . A1B5A C 2 .   ? 26.971 12.216  10.787 1.00 16.69 ? 201 A1B5A A O   1 
HETATM 2166 C  C1  . A1B5A C 2 .   ? 26.325 9.885   8.598  1.00 17.06 ? 201 A1B5A A C1  1 
HETATM 2167 S  S   . A1B5A C 2 .   ? 24.898 9.704   9.600  1.00 17.72 ? 201 A1B5A A S   1 
HETATM 2168 C  C   . A1B5A C 2 .   ? 24.760 7.911   9.753  1.00 17.74 ? 201 A1B5A A C   1 
HETATM 2169 C  C3  . A1B5A C 2 .   ? 27.793 11.251  7.380  1.00 18.31 ? 201 A1B5A A C3  1 
HETATM 2170 C  C2  . A1B5A C 2 .   ? 28.020 9.018   7.397  1.00 16.81 ? 201 A1B5A A C2  1 
HETATM 2171 N  N   . A1B5A C 2 .   ? 26.981 8.799   8.205  1.00 17.15 ? 201 A1B5A A N   1 
HETATM 2172 C  C1  . GOL   D 3 .   ? 19.783 23.216  17.564 1.00 46.24 ? 202 GOL   A C1  1 
HETATM 2173 O  O1  . GOL   D 3 .   ? 21.185 23.463  17.570 1.00 46.18 ? 202 GOL   A O1  1 
HETATM 2174 C  C2  . GOL   D 3 .   ? 19.347 22.582  16.263 1.00 46.36 ? 202 GOL   A C2  1 
HETATM 2175 O  O2  . GOL   D 3 .   ? 20.044 23.167  15.156 1.00 46.65 ? 202 GOL   A O2  1 
HETATM 2176 C  C3  . GOL   D 3 .   ? 17.860 22.709  16.042 1.00 46.21 ? 202 GOL   A C3  1 
HETATM 2177 O  O3  . GOL   D 3 .   ? 17.399 21.834  15.021 1.00 46.13 ? 202 GOL   A O3  1 
HETATM 2178 ZN ZN  . ZN    E 4 .   ? 23.080 -5.609  27.020 1.00 17.82 2 203 ZN    A ZN  1 
HETATM 2179 S  S   . DMS   F 5 .   ? 15.084 -0.337  12.215 1.00 38.47 ? 204 DMS   A S   1 
HETATM 2180 O  O   . DMS   F 5 .   ? 16.455 -0.642  12.740 1.00 35.79 ? 204 DMS   A O   1 
HETATM 2181 C  C1  . DMS   F 5 .   ? 15.036 0.330   10.534 1.00 39.08 ? 204 DMS   A C1  1 
HETATM 2182 C  C2  . DMS   F 5 .   ? 14.392 1.123   13.066 1.00 37.90 ? 204 DMS   A C2  1 
HETATM 2183 S  S   . DMS   G 5 .   ? 31.734 9.988   14.133 1.00 38.33 ? 205 DMS   A S   1 
HETATM 2184 O  O   . DMS   G 5 .   ? 31.043 11.191  14.779 1.00 39.00 ? 205 DMS   A O   1 
HETATM 2185 C  C1  . DMS   G 5 .   ? 32.234 10.392  12.452 1.00 38.24 ? 205 DMS   A C1  1 
HETATM 2186 C  C2  . DMS   G 5 .   ? 30.602 8.654   13.830 1.00 37.80 ? 205 DMS   A C2  1 
HETATM 2187 N  N1  . A1B5A H 2 .   ? 8.020  -20.338 26.520 1.00 20.87 ? 201 A1B5A C N1  1 
HETATM 2188 N  N3  . A1B5A H 2 .   ? 11.961 -16.843 18.028 1.00 14.38 ? 201 A1B5A C N3  1 
HETATM 2189 C  C4  . A1B5A H 2 .   ? 9.702  -19.425 25.060 1.00 19.01 ? 201 A1B5A C C4  1 
HETATM 2190 C  C5  . A1B5A H 2 .   ? 10.494 -18.222 24.594 1.00 18.15 ? 201 A1B5A C C5  1 
HETATM 2191 C  C6  . A1B5A H 2 .   ? 10.152 -17.807 23.174 1.00 16.71 ? 201 A1B5A C C6  1 
HETATM 2192 C  C7  . A1B5A H 2 .   ? 11.988 -16.097 23.334 1.00 15.36 ? 201 A1B5A C C7  1 
HETATM 2193 C  C8  . A1B5A H 2 .   ? 13.288 -16.186 22.537 1.00 15.18 ? 201 A1B5A C C8  1 
HETATM 2194 C  C10 . A1B5A H 2 .   ? 11.931 -16.512 20.419 1.00 14.09 ? 201 A1B5A C C10 1 
HETATM 2195 O  O1  . A1B5A H 2 .   ? 11.233 -14.858 18.821 1.00 14.04 ? 201 A1B5A C O1  1 
HETATM 2196 C  C11 . A1B5A H 2 .   ? 11.683 -15.997 19.012 1.00 14.36 ? 201 A1B5A C C11 1 
HETATM 2197 C  C9  . A1B5A H 2 .   ? 13.071 -15.722 21.090 1.00 15.15 ? 201 A1B5A C C9  1 
HETATM 2198 C  C12 . A1B5A H 2 .   ? 10.651 -16.366 21.260 1.00 14.62 ? 201 A1B5A C C12 1 
HETATM 2199 N  N2  . A1B5A H 2 .   ? 10.903 -16.811 22.634 1.00 15.58 ? 201 A1B5A C N2  1 
HETATM 2200 O  O   . A1B5A H 2 .   ? 9.193  -18.298 22.576 1.00 16.92 ? 201 A1B5A C O   1 
HETATM 2201 C  C1  . A1B5A H 2 .   ? 9.910  -20.751 24.613 1.00 19.18 ? 201 A1B5A C C1  1 
HETATM 2202 S  S   . A1B5A H 2 .   ? 11.172 -20.987 23.420 1.00 18.57 ? 201 A1B5A C S   1 
HETATM 2203 C  C   . A1B5A H 2 .   ? 11.179 -22.773 23.224 1.00 18.33 ? 201 A1B5A C C   1 
HETATM 2204 C  C3  . A1B5A H 2 .   ? 8.724  -19.311 26.033 1.00 20.21 ? 201 A1B5A C C3  1 
HETATM 2205 C  C2  . A1B5A H 2 .   ? 8.307  -21.524 25.999 1.00 20.30 ? 201 A1B5A C C2  1 
HETATM 2206 N  N   . A1B5A H 2 .   ? 9.211  -21.801 25.054 1.00 19.94 ? 201 A1B5A C N   1 
HETATM 2207 S  S   . DMS   I 5 .   ? 3.993  -20.383 19.566 1.00 32.02 ? 202 DMS   C S   1 
HETATM 2208 O  O   . DMS   I 5 .   ? 4.593  -19.177 18.828 1.00 32.58 ? 202 DMS   C O   1 
HETATM 2209 C  C1  . DMS   I 5 .   ? 3.757  -19.955 21.328 1.00 32.73 ? 202 DMS   C C1  1 
HETATM 2210 C  C2  . DMS   I 5 .   ? 5.222  -21.612 19.784 1.00 31.54 ? 202 DMS   C C2  1 
HETATM 2211 S  S   . DMS   J 5 .   ? 8.618  -14.461 24.778 1.00 48.41 ? 203 DMS   C S   1 
HETATM 2212 O  O   . DMS   J 5 .   ? 8.053  -14.479 23.359 1.00 47.33 ? 203 DMS   C O   1 
HETATM 2213 C  C1  . DMS   J 5 .   ? 8.041  -15.909 25.680 1.00 47.99 ? 203 DMS   C C1  1 
HETATM 2214 C  C2  . DMS   J 5 .   ? 7.626  -13.325 25.786 1.00 48.35 ? 203 DMS   C C2  1 
HETATM 2215 ZN ZN  . ZN    K 4 .   ? 10.548 -35.710 5.590  1.00 15.86 2 204 ZN    C ZN  1 
HETATM 2216 S  S   . DMS   L 5 .   ? 19.831 -30.951 19.913 1.00 42.86 ? 205 DMS   C S   1 
HETATM 2217 O  O   . DMS   L 5 .   ? 18.816 -31.736 19.134 1.00 39.61 ? 205 DMS   C O   1 
HETATM 2218 C  C1  . DMS   L 5 .   ? 20.956 -30.077 18.796 1.00 42.69 ? 205 DMS   C C1  1 
HETATM 2219 C  C2  . DMS   L 5 .   ? 21.019 -32.107 20.650 1.00 43.17 ? 205 DMS   C C2  1 
HETATM 2220 O  O   . HOH   M 6 .   ? 15.028 22.162  24.449 1.00 25.31 ? 301 HOH   A O   1 
HETATM 2221 O  O   . HOH   M 6 .   ? 23.701 7.206   28.327 1.00 26.14 ? 302 HOH   A O   1 
HETATM 2222 O  O   . HOH   M 6 .   ? -0.405 15.883  15.288 1.00 45.38 ? 303 HOH   A O   1 
HETATM 2223 O  O   . HOH   M 6 .   ? 18.753 -11.455 27.417 1.00 35.27 ? 304 HOH   A O   1 
HETATM 2224 O  O   . HOH   M 6 .   ? 22.536 6.788   1.531  1.00 35.03 ? 305 HOH   A O   1 
HETATM 2225 O  O   . HOH   M 6 .   ? 24.708 24.099  10.534 1.00 39.63 ? 306 HOH   A O   1 
HETATM 2226 O  O   . HOH   M 6 .   ? 5.301  -2.357  25.776 1.00 52.01 ? 307 HOH   A O   1 
HETATM 2227 O  O   . HOH   M 6 .   ? 17.085 20.652  23.049 1.00 24.87 ? 308 HOH   A O   1 
HETATM 2228 O  O   . HOH   M 6 .   ? 11.127 21.279  24.444 1.00 33.35 ? 309 HOH   A O   1 
HETATM 2229 O  O   . HOH   M 6 .   ? 15.040 8.636   13.382 1.00 15.67 ? 310 HOH   A O   1 
HETATM 2230 O  O   . HOH   M 6 .   ? 17.999 19.775  13.469 1.00 26.14 ? 311 HOH   A O   1 
HETATM 2231 O  O   . HOH   M 6 .   ? 35.527 10.712  9.528  1.00 42.95 ? 312 HOH   A O   1 
HETATM 2232 O  O   . HOH   M 6 .   ? 14.403 -5.632  26.967 1.00 34.02 ? 313 HOH   A O   1 
HETATM 2233 O  O   . HOH   M 6 .   ? 23.382 22.882  18.949 1.00 37.28 ? 314 HOH   A O   1 
HETATM 2234 O  O   . HOH   M 6 .   ? 28.438 -6.308  3.594  1.00 29.22 ? 315 HOH   A O   1 
HETATM 2235 O  O   . HOH   M 6 .   ? 11.456 -1.814  27.941 1.00 27.69 ? 316 HOH   A O   1 
HETATM 2236 O  O   . HOH   M 6 .   ? 30.987 12.695  9.106  1.00 40.87 ? 317 HOH   A O   1 
HETATM 2237 O  O   . HOH   M 6 .   ? 25.669 17.758  12.786 1.00 17.20 ? 318 HOH   A O   1 
HETATM 2238 O  O   . HOH   M 6 .   ? 17.786 -7.623  21.517 1.00 21.13 ? 319 HOH   A O   1 
HETATM 2239 O  O   . HOH   M 6 .   ? 6.824  15.522  29.094 1.00 36.05 ? 320 HOH   A O   1 
HETATM 2240 O  O   . HOH   M 6 .   ? 23.719 16.707  27.388 1.00 44.07 ? 321 HOH   A O   1 
HETATM 2241 O  O   . HOH   M 6 .   ? 27.130 19.027  15.061 1.00 16.75 ? 322 HOH   A O   1 
HETATM 2242 O  O   . HOH   M 6 .   ? 6.967  7.404   31.614 1.00 34.03 ? 323 HOH   A O   1 
HETATM 2243 O  O   . HOH   M 6 .   ? 18.153 16.242  28.759 1.00 48.63 ? 324 HOH   A O   1 
HETATM 2244 O  O   . HOH   M 6 .   ? 34.527 -0.820  16.709 1.00 16.29 ? 325 HOH   A O   1 
HETATM 2245 O  O   . HOH   M 6 .   ? 29.882 7.126   4.423  1.00 38.17 ? 326 HOH   A O   1 
HETATM 2246 O  O   . HOH   M 6 .   ? 23.578 1.805   -0.795 1.00 18.44 ? 327 HOH   A O   1 
HETATM 2247 O  O   . HOH   M 6 .   ? 17.319 0.513   2.618  1.00 37.93 ? 328 HOH   A O   1 
HETATM 2248 O  O   . HOH   M 6 .   ? 29.308 13.290  11.752 1.00 31.86 ? 329 HOH   A O   1 
HETATM 2249 O  O   . HOH   M 6 .   ? 20.230 11.944  8.670  1.00 21.61 ? 330 HOH   A O   1 
HETATM 2250 O  O   . HOH   M 6 .   ? 23.506 10.887  21.514 1.00 14.29 ? 331 HOH   A O   1 
HETATM 2251 O  O   . HOH   M 6 .   ? 3.589  18.161  23.714 1.00 41.50 ? 332 HOH   A O   1 
HETATM 2252 O  O   . HOH   M 6 .   ? 4.906  11.078  12.383 1.00 38.51 ? 333 HOH   A O   1 
HETATM 2253 O  O   . HOH   M 6 .   ? 11.122 -0.189  15.851 1.00 25.37 ? 334 HOH   A O   1 
HETATM 2254 O  O   . HOH   M 6 .   ? 29.622 25.835  16.137 1.00 40.58 ? 335 HOH   A O   1 
HETATM 2255 O  O   . HOH   M 6 .   ? 4.056  19.951  21.506 1.00 33.91 ? 336 HOH   A O   1 
HETATM 2256 O  O   . HOH   M 6 .   ? 22.445 -6.132  0.647  1.00 42.72 ? 337 HOH   A O   1 
HETATM 2257 O  O   . HOH   M 6 .   ? 12.762 17.663  13.068 1.00 35.95 ? 338 HOH   A O   1 
HETATM 2258 O  O   . HOH   M 6 .   ? 16.859 4.631   5.932  1.00 29.50 ? 339 HOH   A O   1 
HETATM 2259 O  O   . HOH   M 6 .   ? 32.284 2.605   5.105  1.00 32.78 ? 340 HOH   A O   1 
HETATM 2260 O  O   . HOH   M 6 .   ? 16.057 -0.489  4.906  1.00 35.26 ? 341 HOH   A O   1 
HETATM 2261 O  O   . HOH   M 6 .   ? 24.295 14.172  30.610 1.00 69.64 ? 342 HOH   A O   1 
HETATM 2262 O  O   . HOH   M 6 .   ? 25.145 4.081   -1.329 1.00 28.29 ? 343 HOH   A O   1 
HETATM 2263 O  O   . HOH   M 6 .   ? 30.665 10.882  5.360  1.00 39.74 ? 344 HOH   A O   1 
HETATM 2264 O  O   . HOH   M 6 .   ? 20.347 2.210   9.364  1.00 15.60 ? 345 HOH   A O   1 
HETATM 2265 O  O   . HOH   M 6 .   ? 12.544 -6.197  22.154 1.00 19.97 ? 346 HOH   A O   1 
HETATM 2266 O  O   . HOH   M 6 .   ? 24.237 8.373   1.372  1.00 29.02 ? 347 HOH   A O   1 
HETATM 2267 O  O   . HOH   M 6 .   ? 23.990 3.719   29.372 1.00 38.79 ? 348 HOH   A O   1 
HETATM 2268 O  O   . HOH   M 6 .   ? 34.788 -6.366  21.665 1.00 43.21 ? 349 HOH   A O   1 
HETATM 2269 O  O   . HOH   M 6 .   ? 12.218 -2.710  16.031 1.00 32.84 ? 350 HOH   A O   1 
HETATM 2270 O  O   . HOH   M 6 .   ? 20.837 10.233  32.614 1.00 37.72 ? 351 HOH   A O   1 
HETATM 2271 O  O   . HOH   M 6 .   ? 4.919  3.113   20.895 1.00 22.49 ? 352 HOH   A O   1 
HETATM 2272 O  O   . HOH   M 6 .   ? 17.429 2.260   9.430  1.00 23.24 ? 353 HOH   A O   1 
HETATM 2273 O  O   . HOH   M 6 .   ? 17.293 18.447  15.645 1.00 16.39 ? 354 HOH   A O   1 
HETATM 2274 O  O   . HOH   M 6 .   ? 30.964 5.267   7.863  1.00 28.32 ? 355 HOH   A O   1 
HETATM 2275 O  O   . HOH   M 6 .   ? 31.364 -0.059  1.830  1.00 34.33 ? 356 HOH   A O   1 
HETATM 2276 O  O   . HOH   M 6 .   ? 29.878 -2.328  8.474  1.00 28.70 ? 357 HOH   A O   1 
HETATM 2277 O  O   . HOH   M 6 .   ? 4.133  4.075   28.034 1.00 42.51 ? 358 HOH   A O   1 
HETATM 2278 O  O   . HOH   M 6 .   ? 34.486 3.663   26.247 1.00 27.79 ? 359 HOH   A O   1 
HETATM 2279 O  O   . HOH   M 6 .   ? 2.595  8.570   25.940 1.00 31.32 ? 360 HOH   A O   1 
HETATM 2280 O  O   . HOH   M 6 .   ? 14.647 -4.040  16.241 1.00 30.79 ? 361 HOH   A O   1 
HETATM 2281 O  O   . HOH   M 6 .   ? 28.118 3.156   -0.345 1.00 27.49 ? 362 HOH   A O   1 
HETATM 2282 O  O   . HOH   M 6 .   ? 21.544 9.870   23.427 1.00 14.38 ? 363 HOH   A O   1 
HETATM 2283 O  O   . HOH   M 6 .   ? 16.551 -7.143  29.458 1.00 41.46 ? 364 HOH   A O   1 
HETATM 2284 O  O   . HOH   M 6 .   ? 21.696 -5.627  33.686 1.00 31.29 ? 365 HOH   A O   1 
HETATM 2285 O  O   . HOH   M 6 .   ? 25.573 1.554   29.930 1.00 27.49 ? 366 HOH   A O   1 
HETATM 2286 O  O   . HOH   M 6 .   ? 16.386 -3.281  13.952 1.00 35.12 ? 367 HOH   A O   1 
HETATM 2287 O  O   . HOH   M 6 .   ? 3.999  10.497  17.755 1.00 42.47 ? 368 HOH   A O   1 
HETATM 2288 O  O   . HOH   M 6 .   ? 25.515 20.378  22.142 1.00 44.17 ? 369 HOH   A O   1 
HETATM 2289 O  O   . HOH   M 6 .   ? 28.372 0.773   26.751 1.00 25.72 ? 370 HOH   A O   1 
HETATM 2290 O  O   . HOH   M 6 .   ? 29.858 6.303   30.056 1.00 36.56 ? 371 HOH   A O   1 
HETATM 2291 O  O   . HOH   M 6 .   ? 19.813 -5.159  15.549 1.00 32.26 ? 372 HOH   A O   1 
HETATM 2292 O  O   . HOH   M 6 .   ? 32.936 -2.739  15.319 1.00 21.97 ? 373 HOH   A O   1 
HETATM 2293 O  O   . HOH   M 6 .   ? 29.960 -10.170 21.930 1.00 40.63 ? 374 HOH   A O   1 
HETATM 2294 O  O   . HOH   M 6 .   ? 9.000  4.147   11.816 1.00 38.87 ? 375 HOH   A O   1 
HETATM 2295 O  O   . HOH   M 6 .   ? 16.824 9.067   6.803  1.00 23.50 ? 376 HOH   A O   1 
HETATM 2296 O  O   . HOH   M 6 .   ? 30.597 -3.101  12.051 1.00 29.04 ? 377 HOH   A O   1 
HETATM 2297 O  O   . HOH   M 6 .   ? 28.262 16.094  10.719 1.00 29.98 ? 378 HOH   A O   1 
HETATM 2298 O  O   . HOH   M 6 .   ? 15.472 16.071  6.491  1.00 43.68 ? 379 HOH   A O   1 
HETATM 2299 O  O   . HOH   M 6 .   ? 30.101 -6.156  26.165 1.00 36.96 ? 380 HOH   A O   1 
HETATM 2300 O  O   . HOH   M 6 .   ? 35.594 14.515  20.495 1.00 31.30 ? 381 HOH   A O   1 
HETATM 2301 O  O   . HOH   M 6 .   ? 19.743 9.397   8.030  1.00 24.59 ? 382 HOH   A O   1 
HETATM 2302 O  O   . HOH   M 6 .   ? 29.332 25.625  13.277 1.00 29.96 ? 383 HOH   A O   1 
HETATM 2303 O  O   . HOH   M 6 .   ? 18.199 -5.320  30.562 1.00 26.34 ? 384 HOH   A O   1 
HETATM 2304 O  O   . HOH   M 6 .   ? 4.442  20.510  15.242 1.00 40.08 ? 385 HOH   A O   1 
HETATM 2305 O  O   . HOH   M 6 .   ? 24.378 17.565  6.276  1.00 39.05 ? 386 HOH   A O   1 
HETATM 2306 O  O   . HOH   M 6 .   ? 32.171 8.656   4.648  1.00 40.90 ? 387 HOH   A O   1 
HETATM 2307 O  O   . HOH   M 6 .   ? 28.796 21.968  22.235 1.00 32.19 ? 388 HOH   A O   1 
HETATM 2308 O  O   . HOH   M 6 .   ? 31.663 14.672  12.687 1.00 28.66 ? 389 HOH   A O   1 
HETATM 2309 O  O   . HOH   M 6 .   ? 26.341 -6.542  29.942 1.00 38.43 ? 390 HOH   A O   1 
HETATM 2310 O  O   . HOH   M 6 .   ? 19.918 13.984  28.934 1.00 35.19 ? 391 HOH   A O   1 
HETATM 2311 O  O   . HOH   M 6 .   ? 3.979  14.772  10.426 1.00 28.42 ? 392 HOH   A O   1 
HETATM 2312 O  O   . HOH   M 6 .   ? 3.315  2.525   18.799 1.00 41.13 ? 393 HOH   A O   1 
HETATM 2313 O  O   . HOH   M 6 .   ? 6.804  16.324  8.851  1.00 35.69 ? 394 HOH   A O   1 
HETATM 2314 O  O   . HOH   M 6 .   ? 23.003 20.914  20.521 1.00 23.69 ? 395 HOH   A O   1 
HETATM 2315 O  O   . HOH   M 6 .   ? 12.377 18.513  26.528 1.00 34.41 ? 396 HOH   A O   1 
HETATM 2316 O  O   . HOH   M 6 .   ? 2.121  14.275  24.636 1.00 53.87 ? 397 HOH   A O   1 
HETATM 2317 O  O   . HOH   M 6 .   ? 35.045 15.305  25.244 1.00 47.94 ? 398 HOH   A O   1 
HETATM 2318 O  O   . HOH   M 6 .   ? 25.725 -8.499  22.603 1.00 43.98 ? 399 HOH   A O   1 
HETATM 2319 O  O   . HOH   M 6 .   ? 11.148 2.219   12.317 1.00 28.94 ? 400 HOH   A O   1 
HETATM 2320 O  O   . HOH   M 6 .   ? 13.364 8.707   11.081 1.00 22.82 ? 401 HOH   A O   1 
HETATM 2321 O  O   . HOH   M 6 .   ? 11.497 10.387  9.947  1.00 54.79 ? 402 HOH   A O   1 
HETATM 2322 O  O   . HOH   M 6 .   ? 15.282 23.194  16.910 1.00 25.98 ? 403 HOH   A O   1 
HETATM 2323 O  O   . HOH   M 6 .   ? 11.748 15.778  9.206  1.00 50.96 ? 404 HOH   A O   1 
HETATM 2324 O  O   . HOH   M 6 .   ? 15.709 12.171  30.704 1.00 39.05 ? 405 HOH   A O   1 
HETATM 2325 O  O   . HOH   M 6 .   ? 16.952 18.541  27.520 1.00 61.73 ? 406 HOH   A O   1 
HETATM 2326 O  O   . HOH   M 6 .   ? 24.651 -5.294  32.776 1.00 36.68 ? 407 HOH   A O   1 
HETATM 2327 O  O   . HOH   M 6 .   ? 32.834 5.287   4.532  1.00 48.91 ? 408 HOH   A O   1 
HETATM 2328 O  O   . HOH   M 6 .   ? 30.327 -1.983  3.754  1.00 47.02 ? 409 HOH   A O   1 
HETATM 2329 O  O   . HOH   M 6 .   ? 15.324 8.339   34.159 1.00 33.10 ? 410 HOH   A O   1 
HETATM 2330 O  O   . HOH   M 6 .   ? 13.944 21.639  14.688 1.00 28.14 ? 411 HOH   A O   1 
HETATM 2331 O  O   . HOH   M 6 .   ? 2.339  20.998  12.306 1.00 44.29 ? 412 HOH   A O   1 
HETATM 2332 O  O   . HOH   M 6 .   ? 5.158  2.515   12.129 1.00 68.13 ? 413 HOH   A O   1 
HETATM 2333 O  O   . HOH   M 6 .   ? 6.549  -4.765  24.163 1.00 51.87 ? 414 HOH   A O   1 
HETATM 2334 O  O   . HOH   M 6 .   ? 2.072  21.277  8.962  1.00 55.44 ? 415 HOH   A O   1 
HETATM 2335 O  O   . HOH   M 6 .   ? 33.076 0.542   6.173  1.00 36.92 ? 416 HOH   A O   1 
HETATM 2336 O  O   . HOH   M 6 .   ? 9.653  17.401  8.654  1.00 69.35 ? 417 HOH   A O   1 
HETATM 2337 O  O   . HOH   M 6 .   ? 33.828 -2.314  9.332  1.00 29.93 ? 418 HOH   A O   1 
HETATM 2338 O  O   . HOH   M 6 .   ? 27.897 -9.888  18.425 1.00 53.81 ? 419 HOH   A O   1 
HETATM 2339 O  O   . HOH   M 6 .   ? 18.409 11.710  6.369  1.00 58.40 ? 420 HOH   A O   1 
HETATM 2340 O  O   . HOH   M 6 .   ? 8.806  -2.526  27.771 1.00 41.16 ? 421 HOH   A O   1 
HETATM 2341 O  O   . HOH   M 6 .   ? 28.049 15.851  8.162  1.00 49.37 ? 422 HOH   A O   1 
HETATM 2342 O  O   . HOH   M 6 .   ? 4.309  0.069   16.651 1.00 71.92 ? 423 HOH   A O   1 
HETATM 2343 O  O   . HOH   M 6 .   ? 2.661  4.074   16.856 1.00 44.87 ? 424 HOH   A O   1 
HETATM 2344 O  O   . HOH   M 6 .   ? 31.725 25.581  12.076 1.00 37.40 ? 425 HOH   A O   1 
HETATM 2345 O  O   . HOH   M 6 .   ? 30.872 -8.845  18.129 1.00 42.41 ? 426 HOH   A O   1 
HETATM 2346 O  O   . HOH   M 6 .   ? 31.465 -3.960  9.803  1.00 36.87 ? 427 HOH   A O   1 
HETATM 2347 O  O   . HOH   M 6 .   ? 25.992 14.906  6.027  1.00 60.31 ? 428 HOH   A O   1 
HETATM 2348 O  O   . HOH   M 6 .   ? 29.662 21.331  25.210 1.00 52.23 ? 429 HOH   A O   1 
HETATM 2349 O  O   . HOH   M 6 .   ? 0.029  16.137  31.145 1.00 77.29 ? 430 HOH   A O   1 
HETATM 2350 O  O   . HOH   N 6 .   ? 10.721 -27.639 33.688 1.00 50.85 ? 301 HOH   C O   1 
HETATM 2351 O  O   . HOH   N 6 .   ? 2.618  -22.971 10.644 1.00 32.39 ? 302 HOH   C O   1 
HETATM 2352 O  O   . HOH   N 6 .   ? 10.241 -23.023 4.786  1.00 24.47 ? 303 HOH   C O   1 
HETATM 2353 O  O   . HOH   N 6 .   ? 20.136 -8.467  7.642  1.00 29.76 ? 304 HOH   C O   1 
HETATM 2354 O  O   . HOH   N 6 .   ? 27.486 -27.546 2.128  1.00 38.88 ? 305 HOH   C O   1 
HETATM 2355 O  O   . HOH   N 6 .   ? 23.794 -9.298  7.844  1.00 24.31 ? 306 HOH   C O   1 
HETATM 2356 O  O   . HOH   N 6 .   ? 19.126 -34.239 18.505 1.00 39.57 ? 307 HOH   C O   1 
HETATM 2357 O  O   . HOH   N 6 .   ? 12.282 -29.494 33.378 1.00 24.01 ? 308 HOH   C O   1 
HETATM 2358 O  O   . HOH   N 6 .   ? 5.576  -17.888 25.126 1.00 37.79 ? 309 HOH   C O   1 
HETATM 2359 O  O   . HOH   N 6 .   ? 20.665 -22.464 18.522 1.00 16.58 ? 310 HOH   C O   1 
HETATM 2360 O  O   . HOH   N 6 .   ? 23.709 -31.366 14.967 1.00 31.37 ? 311 HOH   C O   1 
HETATM 2361 O  O   . HOH   N 6 .   ? 16.947 -37.778 2.928  1.00 36.56 ? 312 HOH   C O   1 
HETATM 2362 O  O   . HOH   N 6 .   ? 12.448 -14.102 5.042  1.00 47.47 ? 313 HOH   C O   1 
HETATM 2363 O  O   . HOH   N 6 .   ? 3.834  -23.415 3.804  1.00 30.04 ? 314 HOH   C O   1 
HETATM 2364 O  O   . HOH   N 6 .   ? 9.883  -26.215 3.628  1.00 22.70 ? 315 HOH   C O   1 
HETATM 2365 O  O   . HOH   N 6 .   ? 29.642 -27.895 9.617  1.00 30.58 ? 316 HOH   C O   1 
HETATM 2366 O  O   . HOH   N 6 .   ? 26.612 -23.247 -0.437 1.00 37.79 ? 317 HOH   C O   1 
HETATM 2367 O  O   . HOH   N 6 .   ? 6.856  -36.816 29.211 1.00 39.34 ? 318 HOH   C O   1 
HETATM 2368 O  O   . HOH   N 6 .   ? 10.602 -12.797 20.558 1.00 17.50 ? 319 HOH   C O   1 
HETATM 2369 O  O   . HOH   N 6 .   ? 24.780 -20.583 20.409 1.00 45.96 ? 320 HOH   C O   1 
HETATM 2370 O  O   . HOH   N 6 .   ? 32.218 -16.778 20.567 1.00 28.76 ? 321 HOH   C O   1 
HETATM 2371 O  O   . HOH   N 6 .   ? 6.059  -23.451 28.632 1.00 46.96 ? 322 HOH   C O   1 
HETATM 2372 O  O   . HOH   N 6 .   ? 16.242 -18.849 23.988 1.00 25.59 ? 323 HOH   C O   1 
HETATM 2373 O  O   . HOH   N 6 .   ? 0.188  -18.689 22.132 1.00 42.55 ? 324 HOH   C O   1 
HETATM 2374 O  O   . HOH   N 6 .   ? 8.292  -28.425 2.954  1.00 25.01 ? 325 HOH   C O   1 
HETATM 2375 O  O   . HOH   N 6 .   ? 22.144 -32.504 3.601  1.00 30.09 ? 326 HOH   C O   1 
HETATM 2376 O  O   . HOH   N 6 .   ? 11.390 -19.558 11.569 1.00 15.65 ? 327 HOH   C O   1 
HETATM 2377 O  O   . HOH   N 6 .   ? 8.893  -11.442 18.398 1.00 17.25 ? 328 HOH   C O   1 
HETATM 2378 O  O   . HOH   N 6 .   ? 15.458 -28.748 23.094 1.00 17.45 ? 329 HOH   C O   1 
HETATM 2379 O  O   . HOH   N 6 .   ? 0.951  -31.485 17.247 1.00 15.31 ? 330 HOH   C O   1 
HETATM 2380 O  O   . HOH   N 6 .   ? 18.392 -28.666 22.846 1.00 27.03 ? 331 HOH   C O   1 
HETATM 2381 O  O   . HOH   N 6 .   ? 27.460 -15.273 2.205  1.00 45.28 ? 332 HOH   C O   1 
HETATM 2382 O  O   . HOH   N 6 .   ? 22.247 -12.349 17.294 1.00 28.32 ? 333 HOH   C O   1 
HETATM 2383 O  O   . HOH   N 6 .   ? 6.738  -17.326 21.693 1.00 36.66 ? 334 HOH   C O   1 
HETATM 2384 O  O   . HOH   N 6 .   ? 17.823 -9.983  9.178  1.00 21.28 ? 335 HOH   C O   1 
HETATM 2385 O  O   . HOH   N 6 .   ? 19.979 -31.523 27.042 1.00 31.48 ? 336 HOH   C O   1 
HETATM 2386 O  O   . HOH   N 6 .   ? 4.257  -8.415  22.781 1.00 30.50 ? 337 HOH   C O   1 
HETATM 2387 O  O   . HOH   N 6 .   ? 31.309 -10.675 16.193 1.00 29.14 ? 338 HOH   C O   1 
HETATM 2388 O  O   . HOH   N 6 .   ? 30.974 -21.116 13.003 1.00 43.26 ? 339 HOH   C O   1 
HETATM 2389 O  O   . HOH   N 6 .   ? 18.029 -12.019 5.269  1.00 46.81 ? 340 HOH   C O   1 
HETATM 2390 O  O   . HOH   N 6 .   ? 9.922  -40.782 1.063  1.00 47.04 ? 341 HOH   C O   1 
HETATM 2391 O  O   . HOH   N 6 .   ? 13.092 -20.688 9.390  1.00 16.44 ? 342 HOH   C O   1 
HETATM 2392 O  O   . HOH   N 6 .   ? 2.693  -31.028 3.912  1.00 34.18 ? 343 HOH   C O   1 
HETATM 2393 O  O   . HOH   N 6 .   ? 30.921 -20.166 18.827 1.00 35.55 ? 344 HOH   C O   1 
HETATM 2394 O  O   . HOH   N 6 .   ? 29.793 -26.613 2.720  1.00 40.86 ? 345 HOH   C O   1 
HETATM 2395 O  O   . HOH   N 6 .   ? 18.358 -10.967 19.002 1.00 27.62 ? 346 HOH   C O   1 
HETATM 2396 O  O   . HOH   N 6 .   ? 18.495 -12.414 16.834 1.00 18.16 ? 347 HOH   C O   1 
HETATM 2397 O  O   . HOH   N 6 .   ? 13.758 -36.816 32.130 1.00 46.01 ? 348 HOH   C O   1 
HETATM 2398 O  O   . HOH   N 6 .   ? 14.994 -35.806 16.918 1.00 25.11 ? 349 HOH   C O   1 
HETATM 2399 O  O   . HOH   N 6 .   ? 22.929 -33.950 15.140 1.00 41.54 ? 350 HOH   C O   1 
HETATM 2400 O  O   . HOH   N 6 .   ? 19.738 -22.122 25.212 1.00 35.46 ? 351 HOH   C O   1 
HETATM 2401 O  O   . HOH   N 6 .   ? -3.487 -18.804 27.621 1.00 34.24 ? 352 HOH   C O   1 
HETATM 2402 O  O   . HOH   N 6 .   ? 14.367 -9.878  8.409  1.00 44.21 ? 353 HOH   C O   1 
HETATM 2403 O  O   . HOH   N 6 .   ? 14.290 -16.586 3.792  1.00 32.37 ? 354 HOH   C O   1 
HETATM 2404 O  O   . HOH   N 6 .   ? 8.025  -5.271  14.544 1.00 36.03 ? 355 HOH   C O   1 
HETATM 2405 O  O   . HOH   N 6 .   ? 14.336 -22.540 30.243 1.00 39.65 ? 356 HOH   C O   1 
HETATM 2406 O  O   . HOH   N 6 .   ? 9.751  -10.128 11.209 1.00 39.34 ? 357 HOH   C O   1 
HETATM 2407 O  O   . HOH   N 6 .   ? 5.603  -29.177 7.399  1.00 16.71 ? 358 HOH   C O   1 
HETATM 2408 O  O   . HOH   N 6 .   ? -2.195 -30.404 8.494  1.00 20.96 ? 359 HOH   C O   1 
HETATM 2409 O  O   . HOH   N 6 .   ? 16.407 -38.504 10.520 1.00 42.70 ? 360 HOH   C O   1 
HETATM 2410 O  O   . HOH   N 6 .   ? 5.746  -32.713 24.581 1.00 31.39 ? 361 HOH   C O   1 
HETATM 2411 O  O   . HOH   N 6 .   ? -0.251 -15.689 14.107 1.00 30.00 ? 362 HOH   C O   1 
HETATM 2412 O  O   . HOH   N 6 .   ? 21.343 -12.145 21.495 1.00 41.16 ? 363 HOH   C O   1 
HETATM 2413 O  O   . HOH   N 6 .   ? 1.892  -17.725 6.171  1.00 36.31 ? 364 HOH   C O   1 
HETATM 2414 O  O   . HOH   N 6 .   ? 3.774  -36.280 6.922  1.00 28.42 ? 365 HOH   C O   1 
HETATM 2415 O  O   . HOH   N 6 .   ? 26.345 -32.980 5.484  1.00 56.47 ? 366 HOH   C O   1 
HETATM 2416 O  O   . HOH   N 6 .   ? 15.105 -35.681 1.671  1.00 22.71 ? 367 HOH   C O   1 
HETATM 2417 O  O   . HOH   N 6 .   ? 29.375 -14.678 22.328 1.00 40.45 ? 368 HOH   C O   1 
HETATM 2418 O  O   . HOH   N 6 .   ? 8.029  -35.026 0.438  1.00 26.58 ? 369 HOH   C O   1 
HETATM 2419 O  O   . HOH   N 6 .   ? 16.132 -7.541  14.606 1.00 51.95 ? 370 HOH   C O   1 
HETATM 2420 O  O   . HOH   N 6 .   ? 6.447  -18.304 5.885  1.00 23.72 ? 371 HOH   C O   1 
HETATM 2421 O  O   . HOH   N 6 .   ? 19.442 -7.616  15.216 1.00 28.35 ? 372 HOH   C O   1 
HETATM 2422 O  O   . HOH   N 6 .   ? 28.767 -33.114 12.254 1.00 53.64 ? 373 HOH   C O   1 
HETATM 2423 O  O   . HOH   N 6 .   ? 8.668  -38.596 9.478  1.00 33.44 ? 374 HOH   C O   1 
HETATM 2424 O  O   . HOH   N 6 .   ? 22.495 -12.235 5.572  1.00 31.62 ? 375 HOH   C O   1 
HETATM 2425 O  O   . HOH   N 6 .   ? -1.825 -35.520 15.328 1.00 53.52 ? 376 HOH   C O   1 
HETATM 2426 O  O   . HOH   N 6 .   ? 24.808 -17.039 23.016 1.00 54.24 ? 377 HOH   C O   1 
HETATM 2427 O  O   . HOH   N 6 .   ? 21.757 -36.670 9.764  1.00 32.57 ? 378 HOH   C O   1 
HETATM 2428 O  O   . HOH   N 6 .   ? 6.434  -8.282  11.546 1.00 32.67 ? 379 HOH   C O   1 
HETATM 2429 O  O   . HOH   N 6 .   ? 1.198  -29.433 25.100 1.00 42.08 ? 380 HOH   C O   1 
HETATM 2430 O  O   . HOH   N 6 .   ? 5.767  -32.664 29.551 1.00 59.66 ? 381 HOH   C O   1 
HETATM 2431 O  O   . HOH   N 6 .   ? 16.993 -34.429 17.493 1.00 38.84 ? 382 HOH   C O   1 
HETATM 2432 O  O   . HOH   N 6 .   ? 24.244 -29.094 18.839 1.00 37.86 ? 383 HOH   C O   1 
HETATM 2433 O  O   . HOH   N 6 .   ? 0.522  -16.752 17.968 1.00 42.00 ? 384 HOH   C O   1 
HETATM 2434 O  O   . HOH   N 6 .   ? 14.151 -41.940 4.069  1.00 53.09 ? 385 HOH   C O   1 
HETATM 2435 O  O   . HOH   N 6 .   ? 32.566 -16.713 6.149  1.00 53.59 ? 386 HOH   C O   1 
HETATM 2436 O  O   . HOH   N 6 .   ? 4.691  -15.547 21.567 1.00 28.52 ? 387 HOH   C O   1 
HETATM 2437 O  O   . HOH   N 6 .   ? 1.719  -34.025 18.066 1.00 25.49 ? 388 HOH   C O   1 
HETATM 2438 O  O   . HOH   N 6 .   ? 31.558 -22.099 4.516  1.00 48.73 ? 389 HOH   C O   1 
HETATM 2439 O  O   . HOH   N 6 .   ? 12.171 -9.772  12.452 1.00 33.62 ? 390 HOH   C O   1 
HETATM 2440 O  O   . HOH   N 6 .   ? 4.530  -24.707 25.872 1.00 41.35 ? 391 HOH   C O   1 
HETATM 2441 O  O   . HOH   N 6 .   ? 6.967  -36.368 3.014  1.00 30.69 ? 392 HOH   C O   1 
HETATM 2442 O  O   . HOH   N 6 .   ? 17.232 -9.938  29.104 1.00 42.92 ? 393 HOH   C O   1 
HETATM 2443 O  O   . HOH   N 6 .   ? 22.534 -22.441 20.556 1.00 27.99 ? 394 HOH   C O   1 
HETATM 2444 O  O   . HOH   N 6 .   ? 17.882 -18.527 1.283  1.00 38.85 ? 395 HOH   C O   1 
HETATM 2445 O  O   . HOH   N 6 .   ? 4.343  -30.340 31.102 1.00 52.65 ? 396 HOH   C O   1 
HETATM 2446 O  O   . HOH   N 6 .   ? 12.173 -39.229 12.830 1.00 43.32 ? 397 HOH   C O   1 
HETATM 2447 O  O   . HOH   N 6 .   ? 25.063 -24.228 19.889 1.00 45.13 ? 398 HOH   C O   1 
HETATM 2448 O  O   . HOH   N 6 .   ? 20.775 -9.619  17.668 1.00 41.84 ? 399 HOH   C O   1 
HETATM 2449 O  O   . HOH   N 6 .   ? 17.555 -39.069 24.616 1.00 59.35 ? 400 HOH   C O   1 
HETATM 2450 O  O   . HOH   N 6 .   ? 26.591 -32.980 13.847 1.00 47.88 ? 401 HOH   C O   1 
HETATM 2451 O  O   . HOH   N 6 .   ? 5.375  -28.840 4.720  1.00 39.00 ? 402 HOH   C O   1 
HETATM 2452 O  O   . HOH   N 6 .   ? 1.901  -34.261 4.683  1.00 56.39 ? 403 HOH   C O   1 
HETATM 2453 O  O   . HOH   N 6 .   ? 10.312 -10.281 27.574 1.00 61.84 ? 404 HOH   C O   1 
HETATM 2454 O  O   . HOH   N 6 .   ? -0.284 -34.458 10.286 1.00 54.69 ? 405 HOH   C O   1 
HETATM 2455 O  O   . HOH   N 6 .   ? 2.562  -29.256 27.218 1.00 42.60 ? 406 HOH   C O   1 
HETATM 2456 O  O   . HOH   N 6 .   ? 8.618  -23.785 2.706  1.00 44.29 ? 407 HOH   C O   1 
HETATM 2457 O  O   . HOH   N 6 .   ? 32.879 -9.087  11.999 1.00 50.46 ? 408 HOH   C O   1 
HETATM 2458 O  O   . HOH   N 6 .   ? 9.306  -39.779 12.337 1.00 36.65 ? 409 HOH   C O   1 
HETATM 2459 O  O   . HOH   N 6 .   ? 5.377  -39.568 23.428 1.00 44.98 ? 410 HOH   C O   1 
HETATM 2460 O  O   . HOH   N 6 .   ? 35.538 -10.200 15.435 1.00 34.58 ? 411 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   ? 0.2434 0.2460 0.2431 0.0014  -0.0007 0.0106  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2455 0.2494 0.2541 -0.0002 -0.0020 0.0105  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2468 0.2500 0.2566 -0.0014 -0.0020 0.0076  7   SER   A C   
4    O O   . SER   A 1   ? 0.2564 0.2575 0.2596 -0.0010 -0.0024 0.0057  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2912 0.2951 0.3008 0.0000  -0.0068 0.0123  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3561 0.3575 0.3586 0.0002  -0.0107 0.0104  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2266 0.2313 0.2447 -0.0027 -0.0010 0.0076  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2182 0.2219 0.2377 -0.0037 -0.0004 0.0056  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2013 0.2064 0.2279 -0.0044 0.0031  0.0057  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2083 0.2147 0.2373 -0.0039 0.0056  0.0063  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1845 0.1889 0.2146 -0.0054 0.0037  0.0051  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1932 0.1984 0.2287 -0.0056 0.0078  0.0052  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1935 0.1965 0.2272 -0.0060 0.0096  0.0043  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1946 0.1958 0.2263 -0.0067 0.0071  0.0039  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2000 0.2076 0.2459 -0.0062 0.0075  0.0072  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1710 0.1737 0.2053 -0.0055 0.0139  0.0040  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1606 0.1610 0.1937 -0.0056 0.0164  0.0039  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1761 0.1778 0.2189 -0.0064 0.0189  0.0057  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1831 0.1866 0.2301 -0.0057 0.0212  0.0060  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1686 0.1676 0.1947 -0.0039 0.0196  0.0026  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1725 0.1714 0.1912 -0.0031 0.0172  0.0010  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1907 0.1867 0.2143 -0.0036 0.0225  0.0032  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2103 0.2091 0.2239 -0.0016 0.0192  -0.0007 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1709 0.1717 0.2180 -0.0077 0.0190  0.0068  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1853 0.1878 0.2432 -0.0085 0.0222  0.0089  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1879 0.1872 0.2431 -0.0080 0.0274  0.0097  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2038 0.2005 0.2574 -0.0090 0.0266  0.0100  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1995 0.2038 0.2669 -0.0108 0.0178  0.0100  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2225 0.2299 0.2925 -0.0109 0.0127  0.0098  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2514 0.2626 0.3310 -0.0105 0.0134  0.0114  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2519 0.2579 0.3140 -0.0109 0.0076  0.0083  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2685 0.2822 0.3497 -0.0101 0.0087  0.0118  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2734 0.2816 0.3361 -0.0105 0.0033  0.0086  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2870 0.2990 0.3592 -0.0101 0.0037  0.0105  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3166 0.3303 0.3886 -0.0094 -0.0005 0.0113  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1894 0.1884 0.2433 -0.0062 0.0330  0.0100  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2099 0.2054 0.2593 -0.0051 0.0386  0.0111  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2209 0.2177 0.2778 -0.0044 0.0448  0.0129  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2260 0.2245 0.2846 -0.0032 0.0461  0.0119  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2420 0.2344 0.2770 -0.0028 0.0392  0.0090  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2481 0.2422 0.2808 -0.0015 0.0388  0.0066  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2791 0.2677 0.3082 -0.0010 0.0452  0.0104  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2320 0.2279 0.2949 -0.0052 0.0489  0.0157  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2302 0.2276 0.3020 -0.0045 0.0557  0.0180  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2268 0.2298 0.3118 -0.0054 0.0533  0.0181  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2277 0.2334 0.3197 -0.0078 0.0471  0.0181  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2268 0.2309 0.3137 -0.0032 0.0574  0.0177  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2349 0.2439 0.3339 -0.0035 0.0551  0.0180  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2133 0.2218 0.3047 -0.0023 0.0512  0.0150  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2130 0.2233 0.3101 -0.0010 0.0523  0.0149  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2599 0.2710 0.3697 -0.0019 0.0626  0.0202  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3592 0.3723 0.4809 -0.0036 0.0661  0.0238  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3987 0.4161 0.5331 -0.0064 0.0612  0.0253  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3893 0.3991 0.5071 -0.0019 0.0746  0.0253  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1963 0.2021 0.2755 -0.0028 0.0469  0.0128  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1882 0.1935 0.2606 -0.0020 0.0434  0.0102  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1764 0.1830 0.2472 -0.0038 0.0360  0.0098  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1792 0.1849 0.2478 -0.0052 0.0337  0.0103  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2014 0.2022 0.2594 -0.0003 0.0457  0.0074  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2163 0.2146 0.2721 0.0021  0.0528  0.0068  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2338 0.2329 0.2964 0.0034  0.0557  0.0065  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2399 0.2343 0.2860 0.0035  0.0568  0.0066  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2504 0.2464 0.3099 0.0059  0.0626  0.0056  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2514 0.2428 0.2937 0.0061  0.0637  0.0060  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2675 0.2596 0.3163 0.0073  0.0667  0.0052  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2901 0.2784 0.3339 0.0103  0.0737  0.0041  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1621 0.1699 0.2326 -0.0035 0.0326  0.0090  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1617 0.1701 0.2285 -0.0045 0.0264  0.0086  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1747 0.1812 0.2326 -0.0034 0.0265  0.0062  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1891 0.1955 0.2494 -0.0024 0.0287  0.0057  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1776 0.1897 0.2542 -0.0051 0.0225  0.0107  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2043 0.2166 0.2759 -0.0053 0.0171  0.0104  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2187 0.2342 0.2988 -0.0055 0.0128  0.0128  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2494 0.2649 0.3266 -0.0045 0.0105  0.0135  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2866 0.3020 0.3588 -0.0046 0.0054  0.0141  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2879 0.3031 0.3574 -0.0059 0.0015  0.0134  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2625 0.2776 0.3321 -0.0034 0.0044  0.0153  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1622 0.1673 0.2110 -0.0037 0.0242  0.0047  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1650 0.1690 0.2068 -0.0030 0.0240  0.0026  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1633 0.1687 0.2044 -0.0035 0.0198  0.0032  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1674 0.1728 0.2056 -0.0041 0.0169  0.0037  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1860 0.1877 0.2184 -0.0024 0.0248  0.0006  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1941 0.1955 0.2216 -0.0018 0.0244  -0.0019 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1814 0.1811 0.2128 -0.0015 0.0292  0.0007  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1427 0.1487 0.1858 -0.0033 0.0197  0.0033  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1593 0.1662 0.2011 -0.0035 0.0165  0.0045  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1625 0.1690 0.2020 -0.0033 0.0175  0.0032  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1615 0.1669 0.2019 -0.0031 0.0200  0.0012  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1804 0.1888 0.2293 -0.0033 0.0148  0.0074  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2061 0.2157 0.2587 -0.0039 0.0128  0.0086  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1947 0.2029 0.2506 -0.0027 0.0179  0.0077  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1465 0.1537 0.1835 -0.0033 0.0156  0.0044  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1460 0.1532 0.1836 -0.0035 0.0168  0.0039  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1558 0.1622 0.2006 -0.0034 0.0183  0.0052  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1599 0.1667 0.2081 -0.0029 0.0172  0.0081  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1494 0.1575 0.1838 -0.0032 0.0154  0.0058  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1784 0.1870 0.2060 -0.0029 0.0143  0.0045  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1929 0.2010 0.2169 -0.0025 0.0123  0.0051  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2006 0.2101 0.2269 -0.0030 0.0153  0.0026  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1487 0.1537 0.1959 -0.0038 0.0206  0.0030  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1443 0.1476 0.1985 -0.0036 0.0224  0.0039  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1541 0.1576 0.2113 -0.0033 0.0216  0.0080  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1677 0.1708 0.2301 -0.0024 0.0217  0.0106  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1630 0.1640 0.2182 -0.0042 0.0245  0.0000  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1698 0.1678 0.2318 -0.0037 0.0270  0.0000  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1746 0.1697 0.2371 -0.0047 0.0281  -0.0041 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1901 0.1811 0.2582 -0.0041 0.0308  -0.0053 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2046 0.1936 0.2796 -0.0043 0.0318  -0.0030 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.1985 0.1894 0.2751 -0.0049 0.0305  0.0012  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1916 0.1761 0.2715 -0.0036 0.0344  -0.0047 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1540 0.1584 0.2077 -0.0038 0.0208  0.0090  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1645 0.1686 0.2196 -0.0033 0.0207  0.0133  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1829 0.1879 0.2354 -0.0019 0.0178  0.0167  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2128 0.2172 0.2662 -0.0009 0.0174  0.0207  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1732 0.1780 0.2258 -0.0040 0.0216  0.0137  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1814 0.1883 0.2262 -0.0036 0.0201  0.0135  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1860 0.1943 0.2278 -0.0041 0.0195  0.0097  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2027 0.2100 0.2422 -0.0024 0.0192  0.0166  21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1977 0.2071 0.2331 -0.0032 0.0185  0.0106  21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2077 0.2165 0.2412 -0.0022 0.0183  0.0145  21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1794 0.1859 0.2288 -0.0018 0.0156  0.0152  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1930 0.2004 0.2406 -0.0008 0.0120  0.0176  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2045 0.2128 0.2591 -0.0007 0.0113  0.0176  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2171 0.2268 0.2720 -0.0002 0.0077  0.0192  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1888 0.1967 0.2281 -0.0011 0.0099  0.0160  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2106 0.2182 0.2432 -0.0008 0.0109  0.0162  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2080 0.2155 0.2328 -0.0006 0.0090  0.0143  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2157 0.2224 0.2466 0.0006  0.0106  0.0205  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1873 0.1949 0.2479 -0.0009 0.0147  0.0159  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1817 0.1904 0.2498 -0.0004 0.0150  0.0161  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1853 0.1951 0.2598 0.0010  0.0128  0.0203  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1844 0.1928 0.2591 0.0018  0.0129  0.0228  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1812 0.1881 0.2529 -0.0004 0.0196  0.0134  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2008 0.2133 0.2808 0.0012  0.0106  0.0213  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2171 0.2315 0.3039 0.0027  0.0074  0.0254  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2255 0.2400 0.3234 0.0041  0.0110  0.0263  24  THR   A C   
137  O O   . THR   A 18  ? 0.2223 0.2353 0.3220 0.0038  0.0159  0.0234  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2355 0.2534 0.3243 0.0021  0.0024  0.0258  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2483 0.2679 0.3444 0.0013  0.0051  0.0240  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2392 0.2562 0.3167 0.0009  -0.0011 0.0243  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2277 0.2439 0.3333 0.0061  0.0084  0.0304  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2530 0.2695 0.3706 0.0079  0.0119  0.0316  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2287 0.2480 0.3530 0.0072  0.0144  0.0293  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2388 0.2565 0.3682 0.0081  0.0202  0.0277  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3078 0.3268 0.4331 0.0103  0.0076  0.0369  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4159 0.4318 0.5355 0.0116  0.0060  0.0402  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4698 0.4816 0.5932 0.0132  0.0103  0.0417  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4566 0.4725 0.5675 0.0118  0.0009  0.0427  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4867 0.4963 0.6037 0.0140  0.0080  0.0452  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4872 0.4992 0.5960 0.0134  0.0025  0.0460  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2259 0.2488 0.3497 0.0056  0.0105  0.0290  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2210 0.2464 0.3515 0.0047  0.0132  0.0275  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2053 0.2270 0.3281 0.0037  0.0190  0.0233  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2145 0.2361 0.3427 0.0044  0.0245  0.0222  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2521 0.2814 0.3845 0.0030  0.0075  0.0281  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3230 0.3577 0.4688 0.0040  0.0028  0.0317  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3247 0.3617 0.4829 0.0059  0.0060  0.0336  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3448 0.3814 0.4879 0.0032  -0.0049 0.0328  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1791 0.1975 0.2892 0.0025  0.0182  0.0211  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1751 0.1901 0.2775 0.0019  0.0229  0.0172  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1845 0.1964 0.2898 0.0035  0.0283  0.0159  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1973 0.2075 0.3020 0.0040  0.0332  0.0135  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1676 0.1804 0.2579 0.0006  0.0206  0.0155  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2161 0.2304 0.3011 -0.0009 0.0165  0.0154  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2213 0.2366 0.3083 -0.0017 0.0175  0.0146  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2291 0.2431 0.3079 -0.0012 0.0126  0.0161  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1836 0.1940 0.2911 0.0046  0.0276  0.0175  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1872 0.1937 0.2977 0.0061  0.0325  0.0160  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2132 0.2209 0.3347 0.0082  0.0365  0.0170  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2309 0.2351 0.3524 0.0094  0.0419  0.0141  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1900 0.1941 0.3011 0.0066  0.0310  0.0179  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2067 0.2080 0.3077 0.0047  0.0302  0.0156  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2285 0.2312 0.3237 0.0036  0.0262  0.0173  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2119 0.2089 0.3086 0.0040  0.0334  0.0111  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2353 0.2352 0.3240 0.0021  0.0272  0.0146  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2283 0.2249 0.3180 0.0022  0.0311  0.0106  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2220 0.2153 0.3196 0.0048  0.0380  0.0072  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2247 0.2180 0.3101 0.0009  0.0327  0.0065  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2288 0.2180 0.3204 0.0036  0.0391  0.0028  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2282 0.2179 0.3144 0.0015  0.0362  0.0024  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2169 0.2298 0.3479 0.0088  0.0337  0.0208  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2331 0.2485 0.3769 0.0109  0.0375  0.0223  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2387 0.2548 0.3818 0.0104  0.0422  0.0200  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2514 0.2682 0.4033 0.0124  0.0476  0.0204  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2377 0.2592 0.3925 0.0115  0.0321  0.0271  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2132 0.2290 0.3463 0.0080  0.0403  0.0182  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2126 0.2283 0.3431 0.0074  0.0446  0.0164  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2033 0.2133 0.3184 0.0068  0.0467  0.0120  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1875 0.1971 0.2957 0.0057  0.0473  0.0108  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2323 0.2526 0.3659 0.0052  0.0403  0.0185  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2610 0.2874 0.4110 0.0057  0.0381  0.0225  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2874 0.3161 0.4481 0.0069  0.0431  0.0238  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2665 0.2955 0.4188 0.0051  0.0308  0.0246  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2005 0.2062 0.3109 0.0077  0.0475  0.0097  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2104 0.2114 0.3075 0.0070  0.0481  0.0054  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2180 0.2159 0.3084 0.0081  0.0537  0.0024  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2253 0.2216 0.3202 0.0103  0.0594  0.0020  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2228 0.2199 0.3197 0.0077  0.0483  0.0036  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2423 0.2347 0.3275 0.0068  0.0482  -0.0012 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2496 0.2442 0.3278 0.0043  0.0429  -0.0009 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2515 0.2396 0.3394 0.0073  0.0490  -0.0028 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2173 0.2140 0.2965 0.0068  0.0523  0.0004  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2274 0.2203 0.2971 0.0081  0.0570  -0.0025 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2423 0.2305 0.3010 0.0081  0.0557  -0.0073 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2644 0.2478 0.3179 0.0100  0.0598  -0.0109 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2547 0.2497 0.3204 0.0070  0.0561  -0.0007 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2747 0.2653 0.3283 0.0085  0.0604  -0.0032 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2655 0.2651 0.3438 0.0067  0.0577  0.0037  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2217 0.2112 0.2775 0.0060  0.0500  -0.0077 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2342 0.2204 0.2813 0.0055  0.0479  -0.0121 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2196 0.2086 0.2688 0.0032  0.0424  -0.0109 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2147 0.2076 0.2662 0.0022  0.0397  -0.0075 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2454 0.2300 0.2802 0.0060  0.0481  -0.0143 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2620 0.2448 0.2882 0.0051  0.0443  -0.0184 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2847 0.2629 0.3050 0.0059  0.0448  -0.0234 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2558 0.2417 0.2788 0.0035  0.0393  -0.0179 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2944 0.2733 0.3093 0.0045  0.0399  -0.0259 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2726 0.2563 0.2893 0.0032  0.0368  -0.0224 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2522 0.2422 0.2774 0.0023  0.0367  -0.0143 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2807 0.2671 0.2943 0.0019  0.0321  -0.0230 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2621 0.2539 0.2831 0.0012  0.0325  -0.0150 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2676 0.2580 0.2833 0.0011  0.0304  -0.0191 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2185 0.2050 0.2668 0.0025  0.0410  -0.0138 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2150 0.2041 0.2647 0.0004  0.0366  -0.0126 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2107 0.1972 0.2560 -0.0006 0.0350  -0.0172 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2170 0.1991 0.2603 0.0001  0.0369  -0.0212 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2214 0.2119 0.2809 0.0001  0.0361  -0.0087 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2324 0.2191 0.2985 0.0012  0.0392  -0.0095 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2572 0.2397 0.3230 0.0001  0.0389  -0.0133 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2975 0.2751 0.3645 0.0012  0.0420  -0.0164 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2255 0.2095 0.2902 -0.0019 0.0359  -0.0133 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2145 0.2039 0.2586 -0.0023 0.0313  -0.0167 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2083 0.1964 0.2504 -0.0037 0.0291  -0.0208 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2034 0.1950 0.2508 -0.0056 0.0268  -0.0181 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2019 0.1973 0.2466 -0.0058 0.0248  -0.0160 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2393 0.2277 0.2717 -0.0030 0.0274  -0.0240 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2977 0.2848 0.3280 -0.0042 0.0246  -0.0290 35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3000 0.2877 0.3378 -0.0063 0.0233  -0.0292 35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3184 0.3040 0.3401 -0.0031 0.0234  -0.0325 35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2013 0.1909 0.2561 -0.0068 0.0274  -0.0180 36  SER   A N   
241  C CA  . SER   A 30  ? 0.2105 0.2029 0.2703 -0.0084 0.0261  -0.0149 36  SER   A CA  
242  C C   . SER   A 30  ? 0.1988 0.1942 0.2562 -0.0098 0.0233  -0.0173 36  SER   A C   
243  O O   . SER   A 30  ? 0.1965 0.1957 0.2551 -0.0104 0.0224  -0.0142 36  SER   A O   
244  C CB  . SER   A 30  ? 0.2589 0.2479 0.3274 -0.0095 0.0278  -0.0141 36  SER   A CB  
245  O OG  . SER   A 30  ? 0.3290 0.3144 0.3990 -0.0108 0.0275  -0.0196 36  SER   A OG  
246  N N   . SER   A 31  ? 0.1863 0.1801 0.2400 -0.0101 0.0218  -0.0227 37  SER   A N   
247  C CA  . SER   A 31  ? 0.2075 0.2049 0.2598 -0.0112 0.0184  -0.0249 37  SER   A CA  
248  C C   . SER   A 31  ? 0.1963 0.1977 0.2419 -0.0097 0.0171  -0.0228 37  SER   A C   
249  O O   . SER   A 31  ? 0.2074 0.2128 0.2536 -0.0103 0.0148  -0.0231 37  SER   A O   
250  C CB  . SER   A 31  ? 0.2641 0.2587 0.3136 -0.0117 0.0161  -0.0314 37  SER   A CB  
251  O OG  . SER   A 31  ? 0.3399 0.3329 0.3789 -0.0093 0.0160  -0.0335 37  SER   A OG  
252  N N   . ARG   A 32  ? 0.1770 0.1774 0.2172 -0.0078 0.0187  -0.0208 38  ARG   A N   
253  C CA  . ARG   A 32  ? 0.1750 0.1783 0.2091 -0.0064 0.0177  -0.0189 38  ARG   A CA  
254  C C   . ARG   A 32  ? 0.1674 0.1724 0.2036 -0.0062 0.0187  -0.0138 38  ARG   A C   
255  O O   . ARG   A 32  ? 0.1625 0.1694 0.1943 -0.0052 0.0179  -0.0122 38  ARG   A O   
256  C CB  . ARG   A 32  ? 0.1836 0.1842 0.2098 -0.0045 0.0186  -0.0203 38  ARG   A CB  
257  C CG  . ARG   A 32  ? 0.1943 0.1928 0.2152 -0.0041 0.0171  -0.0253 38  ARG   A CG  
258  C CD  . ARG   A 32  ? 0.2089 0.2042 0.2206 -0.0018 0.0188  -0.0262 38  ARG   A CD  
259  N NE  . ARG   A 32  ? 0.2251 0.2224 0.2318 -0.0005 0.0184  -0.0234 38  ARG   A NE  
260  C CZ  . ARG   A 32  ? 0.2253 0.2205 0.2230 0.0016  0.0189  -0.0240 38  ARG   A CZ  
261  N NH1 . ARG   A 32  ? 0.2354 0.2266 0.2268 0.0028  0.0198  -0.0276 38  ARG   A NH1 
262  N NH2 . ARG   A 32  ? 0.2245 0.2210 0.2186 0.0026  0.0186  -0.0212 38  ARG   A NH2 
263  N N   . ASP   A 33  ? 0.1615 0.1655 0.2039 -0.0069 0.0204  -0.0114 39  ASP   A N   
264  C CA  . ASP   A 33  ? 0.1431 0.1481 0.1866 -0.0063 0.0209  -0.0068 39  ASP   A CA  
265  C C   . ASP   A 33  ? 0.1658 0.1701 0.2053 -0.0050 0.0211  -0.0060 39  ASP   A C   
266  O O   . ASP   A 33  ? 0.1624 0.1682 0.2000 -0.0045 0.0200  -0.0034 39  ASP   A O   
267  C CB  . ASP   A 33  ? 0.1663 0.1744 0.2086 -0.0064 0.0197  -0.0045 39  ASP   A CB  
268  C CG  . ASP   A 33  ? 0.1873 0.1957 0.2293 -0.0057 0.0198  -0.0002 39  ASP   A CG  
269  O OD1 . ASP   A 33  ? 0.1729 0.1797 0.2192 -0.0057 0.0208  0.0020  39  ASP   A OD1 
270  O OD2 . ASP   A 33  ? 0.1747 0.1846 0.2118 -0.0049 0.0186  0.0010  39  ASP   A OD2 
271  N N   . LEU   A 34  ? 0.1608 0.1627 0.1994 -0.0044 0.0226  -0.0083 40  LEU   A N   
272  C CA  . LEU   A 34  ? 0.1631 0.1647 0.1997 -0.0033 0.0235  -0.0070 40  LEU   A CA  
273  C C   . LEU   A 34  ? 0.1635 0.1634 0.2058 -0.0027 0.0261  -0.0061 40  LEU   A C   
274  O O   . LEU   A 34  ? 0.1769 0.1743 0.2217 -0.0026 0.0279  -0.0082 40  LEU   A O   
275  C CB  . LEU   A 34  ? 0.1695 0.1698 0.1988 -0.0024 0.0240  -0.0097 40  LEU   A CB  
276  C CG  . LEU   A 34  ? 0.1882 0.1903 0.2116 -0.0023 0.0215  -0.0101 40  LEU   A CG  
277  C CD1 . LEU   A 34  ? 0.1906 0.1907 0.2064 -0.0009 0.0223  -0.0122 40  LEU   A CD1 
278  C CD2 . LEU   A 34  ? 0.1766 0.1804 0.2002 -0.0024 0.0203  -0.0068 40  LEU   A CD2 
279  N N   . LEU   A 35  ? 0.1439 0.1449 0.1886 -0.0022 0.0264  -0.0034 41  LEU   A N   
280  C CA  . LEU   A 35  ? 0.1529 0.1531 0.2040 -0.0013 0.0291  -0.0022 41  LEU   A CA  
281  C C   . LEU   A 35  ? 0.1627 0.1640 0.2135 -0.0010 0.0297  -0.0008 41  LEU   A C   
282  O O   . LEU   A 35  ? 0.1742 0.1774 0.2230 -0.0017 0.0269  0.0006  41  LEU   A O   
283  C CB  . LEU   A 35  ? 0.1469 0.1484 0.2057 -0.0014 0.0279  0.0011  41  LEU   A CB  
284  C CG  . LEU   A 35  ? 0.1667 0.1679 0.2341 -0.0001 0.0305  0.0027  41  LEU   A CG  
285  C CD1 . LEU   A 35  ? 0.1937 0.1941 0.2674 0.0003  0.0303  0.0046  41  LEU   A CD1 
286  C CD2 . LEU   A 35  ? 0.1738 0.1783 0.2456 0.0000  0.0292  0.0058  41  LEU   A CD2 
287  N N   . VAL   A 36  ? 0.1499 0.1499 0.2028 0.0001  0.0337  -0.0014 42  VAL   A N   
288  C CA  . VAL   A 36  ? 0.1570 0.1580 0.2116 0.0004  0.0355  0.0003  42  VAL   A CA  
289  C C   . VAL   A 36  ? 0.1613 0.1637 0.2270 0.0012  0.0381  0.0026  42  VAL   A C   
290  O O   . VAL   A 36  ? 0.1860 0.1863 0.2540 0.0026  0.0415  0.0013  42  VAL   A O   
291  C CB  . VAL   A 36  ? 0.1797 0.1777 0.2261 0.0014  0.0390  -0.0020 42  VAL   A CB  
292  C CG1 . VAL   A 36  ? 0.1893 0.1880 0.2388 0.0017  0.0420  0.0005  42  VAL   A CG1 
293  C CG2 . VAL   A 36  ? 0.1822 0.1794 0.2185 0.0009  0.0359  -0.0040 42  VAL   A CG2 
294  N N   . SER   A 37  ? 0.1624 0.1682 0.2354 0.0004  0.0363  0.0057  43  SER   A N   
295  C CA  . SER   A 37  ? 0.1680 0.1763 0.2534 0.0012  0.0382  0.0083  43  SER   A CA  
296  C C   . SER   A 37  ? 0.1967 0.2067 0.2867 0.0009  0.0409  0.0099  43  SER   A C   
297  O O   . SER   A 37  ? 0.1866 0.1957 0.2703 -0.0003 0.0400  0.0095  43  SER   A O   
298  C CB  . SER   A 37  ? 0.1747 0.1864 0.2671 0.0006  0.0328  0.0111  43  SER   A CB  
299  O OG  . SER   A 37  ? 0.2126 0.2260 0.3023 -0.0012 0.0277  0.0120  43  SER   A OG  
300  N N   . SER   A 38  ? 0.1976 0.2098 0.2993 0.0020  0.0445  0.0120  44  SER   A N   
301  C CA  . SER   A 38  ? 0.2176 0.2317 0.3259 0.0015  0.0478  0.0140  44  SER   A CA  
302  C C   . SER   A 38  ? 0.2280 0.2474 0.3474 -0.0006 0.0424  0.0169  44  SER   A C   
303  O O   . SER   A 38  ? 0.2266 0.2488 0.3518 -0.0007 0.0374  0.0181  44  SER   A O   
304  C CB  . SER   A 38  ? 0.2535 0.2674 0.3688 0.0039  0.0556  0.0146  44  SER   A CB  
305  O OG  . SER   A 38  ? 0.2955 0.3124 0.4220 0.0051  0.0544  0.0161  44  SER   A OG  
306  N N   . THR   A 39  ? 0.2435 0.2636 0.3649 -0.0024 0.0428  0.0180  45  THR   A N   
307  C CA  . THR   A 39  ? 0.2772 0.3016 0.4092 -0.0049 0.0372  0.0201  45  THR   A CA  
308  C C   . THR   A 39  ? 0.3110 0.3385 0.4571 -0.0054 0.0422  0.0228  45  THR   A C   
309  O O   . THR   A 39  ? 0.3074 0.3325 0.4511 -0.0041 0.0502  0.0230  45  THR   A O   
310  C CB  . THR   A 39  ? 0.2974 0.3194 0.4196 -0.0071 0.0321  0.0187  45  THR   A CB  
311  O OG1 . THR   A 39  ? 0.3098 0.3287 0.4278 -0.0076 0.0372  0.0186  45  THR   A OG1 
312  C CG2 . THR   A 39  ? 0.2984 0.3172 0.4064 -0.0064 0.0288  0.0162  45  THR   A CG2 
313  N N   . THR   A 40  ? 0.3427 0.3755 0.5032 -0.0074 0.0376  0.0250  46  THR   A N   
314  C CA  . THR   A 40  ? 0.3741 0.4108 0.5506 -0.0085 0.0418  0.0278  46  THR   A CA  
315  C C   . THR   A 40  ? 0.3907 0.4253 0.5655 -0.0117 0.0407  0.0278  46  THR   A C   
316  O O   . THR   A 40  ? 0.4056 0.4407 0.5885 -0.0124 0.0469  0.0300  46  THR   A O   
317  C CB  . THR   A 40  ? 0.4087 0.4530 0.6044 -0.0090 0.0371  0.0303  46  THR   A CB  
318  O OG1 . THR   A 40  ? 0.4363 0.4814 0.6288 -0.0108 0.0264  0.0291  46  THR   A OG1 
319  C CG2 . THR   A 40  ? 0.4186 0.4650 0.6197 -0.0054 0.0405  0.0313  46  THR   A CG2 
320  N N   . ALA   A 41  ? 0.3847 0.4168 0.5497 -0.0135 0.0331  0.0256  47  ALA   A N   
321  C CA  . ALA   A 41  ? 0.3769 0.4062 0.5401 -0.0165 0.0315  0.0253  47  ALA   A CA  
322  C C   . ALA   A 41  ? 0.3771 0.3992 0.5221 -0.0153 0.0359  0.0237  47  ALA   A C   
323  O O   . ALA   A 41  ? 0.3778 0.3974 0.5100 -0.0128 0.0367  0.0218  47  ALA   A O   
324  C CB  . ALA   A 41  ? 0.3773 0.4072 0.5398 -0.0188 0.0208  0.0235  47  ALA   A CB  
325  N N   . GLN   A 42  ? 0.3699 0.3888 0.5148 -0.0170 0.0385  0.0246  48  GLN   A N   
326  C CA  . GLN   A 42  ? 0.3762 0.3885 0.5045 -0.0156 0.0423  0.0236  48  GLN   A CA  
327  C C   . GLN   A 42  ? 0.3594 0.3685 0.4749 -0.0161 0.0349  0.0204  48  GLN   A C   
328  O O   . GLN   A 42  ? 0.3693 0.3792 0.4895 -0.0186 0.0282  0.0196  48  GLN   A O   
329  C CB  . GLN   A 42  ? 0.4187 0.4281 0.5513 -0.0171 0.0477  0.0263  48  GLN   A CB  
330  C CG  . GLN   A 42  ? 0.5102 0.5131 0.6265 -0.0146 0.0537  0.0264  48  GLN   A CG  
331  C CD  . GLN   A 42  ? 0.6177 0.6208 0.7318 -0.0113 0.0625  0.0277  48  GLN   A CD  
332  O OE1 . GLN   A 42  ? 0.6349 0.6426 0.7618 -0.0110 0.0658  0.0294  48  GLN   A OE1 
333  N NE2 . GLN   A 42  ? 0.6542 0.6520 0.7518 -0.0084 0.0664  0.0270  48  GLN   A NE2 
334  N N   . GLY   A 43  ? 0.3306 0.3362 0.4304 -0.0135 0.0362  0.0185  49  GLY   A N   
335  C CA  . GLY   A 43  ? 0.3172 0.3199 0.4044 -0.0133 0.0307  0.0157  49  GLY   A CA  
336  C C   . GLY   A 43  ? 0.3069 0.3049 0.3894 -0.0147 0.0292  0.0155  49  GLY   A C   
337  O O   . GLY   A 43  ? 0.3134 0.3093 0.3998 -0.0154 0.0337  0.0176  49  GLY   A O   
338  N N   . CYS   A 44  ? 0.2840 0.2801 0.3582 -0.0148 0.0233  0.0129  50  CYS   A N   
339  C CA  . CYS   A 44  ? 0.2712 0.2623 0.3402 -0.0157 0.0211  0.0120  50  CYS   A CA  
340  C C   . CYS   A 44  ? 0.2542 0.2410 0.3086 -0.0131 0.0234  0.0112  50  CYS   A C   
341  O O   . CYS   A 44  ? 0.2537 0.2357 0.3042 -0.0133 0.0235  0.0113  50  CYS   A O   
342  C CB  . CYS   A 44  ? 0.2816 0.2730 0.3509 -0.0173 0.0131  0.0096  50  CYS   A CB  
343  S SG  . CYS   A 44  ? 0.3214 0.3151 0.3809 -0.0150 0.0090  0.0073  50  CYS   A SG  
344  N N   . ASP   A 45  ? 0.2353 0.2237 0.2826 -0.0106 0.0252  0.0105  51  ASP   A N   
345  C CA  . ASP   A 45  ? 0.2370 0.2225 0.2711 -0.0080 0.0258  0.0092  51  ASP   A CA  
346  C C   . ASP   A 45  ? 0.2428 0.2261 0.2715 -0.0058 0.0318  0.0107  51  ASP   A C   
347  O O   . ASP   A 45  ? 0.2539 0.2385 0.2879 -0.0058 0.0363  0.0125  51  ASP   A O   
348  C CB  . ASP   A 45  ? 0.2444 0.2333 0.2743 -0.0068 0.0229  0.0070  51  ASP   A CB  
349  C CG  . ASP   A 45  ? 0.3005 0.2905 0.3312 -0.0079 0.0171  0.0054  51  ASP   A CG  
350  O OD1 . ASP   A 45  ? 0.2965 0.2832 0.3231 -0.0081 0.0145  0.0045  51  ASP   A OD1 
351  O OD2 . ASP   A 45  ? 0.2729 0.2666 0.3075 -0.0082 0.0151  0.0052  51  ASP   A OD2 
352  N N   . THR   A 46  ? 0.2392 0.2192 0.2570 -0.0036 0.0318  0.0102  52  THR   A N   
353  C CA  . THR   A 46  ? 0.2586 0.2363 0.2682 -0.0009 0.0363  0.0112  52  THR   A CA  
354  C C   . THR   A 46  ? 0.2363 0.2152 0.2361 0.0014  0.0334  0.0085  52  THR   A C   
355  O O   . THR   A 46  ? 0.2364 0.2165 0.2352 0.0012  0.0289  0.0066  52  THR   A O   
356  C CB  . THR   A 46  ? 0.3035 0.2758 0.3106 -0.0004 0.0393  0.0141  52  THR   A CB  
357  O OG1 . THR   A 46  ? 0.3319 0.3017 0.3342 0.0001  0.0353  0.0131  52  THR   A OG1 
358  C CG2 . THR   A 46  ? 0.3242 0.2958 0.3433 -0.0033 0.0420  0.0168  52  THR   A CG2 
359  N N   . ILE   A 47  ? 0.2192 0.1981 0.2128 0.0036  0.0360  0.0079  53  ILE   A N   
360  C CA  . ILE   A 47  ? 0.2045 0.1852 0.1910 0.0053  0.0331  0.0051  53  ILE   A CA  
361  C C   . ILE   A 47  ? 0.2201 0.1978 0.1961 0.0083  0.0330  0.0054  53  ILE   A C   
362  O O   . ILE   A 47  ? 0.2339 0.2078 0.2049 0.0099  0.0369  0.0077  53  ILE   A O   
363  C CB  . ILE   A 47  ? 0.2066 0.1891 0.1933 0.0058  0.0352  0.0034  53  ILE   A CB  
364  C CG1 . ILE   A 47  ? 0.2261 0.2114 0.2240 0.0034  0.0361  0.0037  53  ILE   A CG1 
365  C CG2 . ILE   A 47  ? 0.2190 0.2038 0.2008 0.0068  0.0315  0.0000  53  ILE   A CG2 
366  C CD1 . ILE   A 47  ? 0.2273 0.2160 0.2309 0.0015  0.0311  0.0027  53  ILE   A CD1 
367  N N   . ALA   A 48  ? 0.2091 0.1884 0.1817 0.0092  0.0287  0.0037  54  ALA   A N   
368  C CA  . ALA   A 48  ? 0.2074 0.1848 0.1707 0.0123  0.0275  0.0039  54  ALA   A CA  
369  C C   . ALA   A 48  ? 0.2276 0.2054 0.1840 0.0142  0.0281  0.0022  54  ALA   A C   
370  O O   . ALA   A 48  ? 0.2303 0.2111 0.1895 0.0131  0.0273  -0.0004 54  ALA   A O   
371  C CB  . ALA   A 48  ? 0.2013 0.1818 0.1651 0.0127  0.0227  0.0021  54  ALA   A CB  
372  N N   . ARG   A 49  ? 0.2322 0.2064 0.1788 0.0173  0.0292  0.0037  55  ARG   A N   
373  C CA  . ARG   A 49  ? 0.2343 0.2081 0.1720 0.0196  0.0289  0.0017  55  ARG   A CA  
374  C C   . ARG   A 49  ? 0.2594 0.2328 0.1893 0.0228  0.0248  0.0020  55  ARG   A C   
375  O O   . ARG   A 49  ? 0.2729 0.2418 0.1951 0.0255  0.0267  0.0052  55  ARG   A O   
376  C CB  . ARG   A 49  ? 0.2397 0.2085 0.1716 0.0209  0.0351  0.0039  55  ARG   A CB  
377  C CG  . ARG   A 49  ? 0.2417 0.2113 0.1836 0.0180  0.0394  0.0044  55  ARG   A CG  
378  C CD  . ARG   A 49  ? 0.2537 0.2270 0.2002 0.0164  0.0378  0.0003  55  ARG   A CD  
379  N NE  . ARG   A 49  ? 0.2457 0.2197 0.2018 0.0142  0.0422  0.0014  55  ARG   A NE  
380  C CZ  . ARG   A 49  ? 0.2636 0.2409 0.2274 0.0123  0.0413  -0.0010 55  ARG   A CZ  
381  N NH1 . ARG   A 49  ? 0.2461 0.2261 0.2094 0.0119  0.0366  -0.0046 55  ARG   A NH1 
382  N NH2 . ARG   A 49  ? 0.2681 0.2462 0.2412 0.0107  0.0450  0.0005  55  ARG   A NH2 
383  N N   . CYS   A 50  ? 0.2568 0.2352 0.1903 0.0224  0.0196  -0.0008 56  CYS   A N   
384  C CA  . CYS   A 50  ? 0.2714 0.2508 0.2010 0.0252  0.0154  -0.0003 56  CYS   A CA  
385  C C   . CYS   A 50  ? 0.2738 0.2596 0.2075 0.0247  0.0100  -0.0042 56  CYS   A C   
386  O O   . CYS   A 50  ? 0.2702 0.2590 0.2095 0.0220  0.0097  -0.0071 56  CYS   A O   
387  C CB  . CYS   A 50  ? 0.2659 0.2440 0.2006 0.0247  0.0163  0.0025  56  CYS   A CB  
388  S SG  . CYS   A 50  ? 0.2457 0.2286 0.1929 0.0209  0.0150  0.0004  56  CYS   A SG  
389  N N   . ASP   A 51  ? 0.2872 0.2753 0.2193 0.0274  0.0058  -0.0039 57  ASP   A N   
390  C CA  . ASP   A 51  ? 0.2891 0.2840 0.2272 0.0269  0.0008  -0.0070 57  ASP   A CA  
391  C C   . ASP   A 51  ? 0.2834 0.2812 0.2290 0.0270  0.0001  -0.0057 57  ASP   A C   
392  O O   . ASP   A 51  ? 0.2803 0.2835 0.2299 0.0281  -0.0039 -0.0069 57  ASP   A O   
393  C CB  . ASP   A 51  ? 0.3332 0.3296 0.2642 0.0301  -0.0043 -0.0085 57  ASP   A CB  
394  C CG  . ASP   A 51  ? 0.4141 0.4077 0.3376 0.0345  -0.0053 -0.0050 57  ASP   A CG  
395  O OD1 . ASP   A 51  ? 0.4043 0.3943 0.3285 0.0351  -0.0019 -0.0014 57  ASP   A OD1 
396  O OD2 . ASP   A 51  ? 0.5136 0.5083 0.4305 0.0376  -0.0099 -0.0058 57  ASP   A OD2 
397  N N   . CYS   A 52  ? 0.2612 0.2558 0.2096 0.0257  0.0038  -0.0034 58  CYS   A N   
398  C CA  . CYS   A 52  ? 0.2400 0.2365 0.1943 0.0260  0.0034  -0.0027 58  CYS   A CA  
399  C C   . CYS   A 52  ? 0.2294 0.2327 0.1923 0.0241  0.0015  -0.0053 58  CYS   A C   
400  O O   . CYS   A 52  ? 0.2255 0.2305 0.1917 0.0211  0.0021  -0.0072 58  CYS   A O   
401  C CB  . CYS   A 52  ? 0.2339 0.2254 0.1896 0.0243  0.0071  -0.0009 58  CYS   A CB  
402  S SG  . CYS   A 52  ? 0.2701 0.2533 0.2185 0.0266  0.0097  0.0030  58  CYS   A SG  
403  N N   . GLN   A 53  ? 0.2133 0.2203 0.1803 0.0259  -0.0002 -0.0051 59  GLN   A N   
404  C CA  . GLN   A 53  ? 0.2080 0.2214 0.1840 0.0243  -0.0009 -0.0068 59  GLN   A CA  
405  C C   . GLN   A 53  ? 0.1960 0.2085 0.1748 0.0250  0.0014  -0.0055 59  GLN   A C   
406  O O   . GLN   A 53  ? 0.2000 0.2176 0.1854 0.0250  0.0013  -0.0061 59  GLN   A O   
407  C CB  . GLN   A 53  ? 0.2341 0.2542 0.2143 0.0260  -0.0051 -0.0082 59  GLN   A CB  
408  C CG  . GLN   A 53  ? 0.2979 0.3199 0.2775 0.0242  -0.0077 -0.0108 59  GLN   A CG  
409  C CD  . GLN   A 53  ? 0.3387 0.3679 0.3240 0.0255  -0.0126 -0.0125 59  GLN   A CD  
410  O OE1 . GLN   A 53  ? 0.3544 0.3838 0.3345 0.0278  -0.0166 -0.0131 59  GLN   A OE1 
411  N NE2 . GLN   A 53  ? 0.3142 0.3498 0.3108 0.0240  -0.0125 -0.0131 59  GLN   A NE2 
412  N N   . THR   A 54  ? 0.1918 0.1975 0.1656 0.0256  0.0036  -0.0038 60  THR   A N   
413  C CA  . THR   A 54  ? 0.2017 0.2049 0.1766 0.0258  0.0057  -0.0033 60  THR   A CA  
414  C C   . THR   A 54  ? 0.1937 0.1908 0.1657 0.0231  0.0077  -0.0029 60  THR   A C   
415  O O   . THR   A 54  ? 0.2086 0.2022 0.1771 0.0224  0.0082  -0.0020 60  THR   A O   
416  C CB  . THR   A 54  ? 0.2197 0.2207 0.1925 0.0299  0.0056  -0.0020 60  THR   A CB  
417  O OG1 . THR   A 54  ? 0.2563 0.2507 0.2229 0.0311  0.0059  -0.0002 60  THR   A OG1 
418  C CG2 . THR   A 54  ? 0.2221 0.2297 0.1990 0.0329  0.0032  -0.0021 60  THR   A CG2 
419  N N   . GLY   A 55  ? 0.1794 0.1752 0.1529 0.0219  0.0089  -0.0034 61  GLY   A N   
420  C CA  . GLY   A 55  ? 0.1764 0.1672 0.1486 0.0192  0.0100  -0.0032 61  GLY   A CA  
421  C C   . GLY   A 55  ? 0.1761 0.1660 0.1490 0.0185  0.0104  -0.0042 61  GLY   A C   
422  O O   . GLY   A 55  ? 0.1949 0.1865 0.1680 0.0207  0.0108  -0.0047 61  GLY   A O   
423  N N   . VAL   A 56  ? 0.1766 0.1637 0.1498 0.0157  0.0105  -0.0044 62  VAL   A N   
424  C CA  . VAL   A 56  ? 0.1807 0.1659 0.1529 0.0150  0.0102  -0.0054 62  VAL   A CA  
425  C C   . VAL   A 56  ? 0.1825 0.1702 0.1578 0.0119  0.0097  -0.0054 62  VAL   A C   
426  O O   . VAL   A 56  ? 0.1880 0.1752 0.1657 0.0098  0.0096  -0.0047 62  VAL   A O   
427  C CB  . VAL   A 56  ? 0.2142 0.1918 0.1831 0.0149  0.0097  -0.0059 62  VAL   A CB  
428  C CG1 . VAL   A 56  ? 0.2338 0.2091 0.2004 0.0142  0.0086  -0.0076 62  VAL   A CG1 
429  C CG2 . VAL   A 56  ? 0.2397 0.2141 0.2057 0.0184  0.0105  -0.0058 62  VAL   A CG2 
430  N N   . TYR   A 57  ? 0.1699 0.1601 0.1452 0.0119  0.0098  -0.0058 63  TYR   A N   
431  C CA  . TYR   A 57  ? 0.1652 0.1573 0.1433 0.0094  0.0091  -0.0053 63  TYR   A CA  
432  C C   . TYR   A 57  ? 0.1749 0.1639 0.1494 0.0091  0.0078  -0.0058 63  TYR   A C   
433  O O   . TYR   A 57  ? 0.1885 0.1749 0.1579 0.0112  0.0081  -0.0068 63  TYR   A O   
434  C CB  . TYR   A 57  ? 0.1606 0.1589 0.1429 0.0092  0.0103  -0.0046 63  TYR   A CB  
435  C CG  . TYR   A 57  ? 0.1675 0.1679 0.1485 0.0108  0.0117  -0.0043 63  TYR   A CG  
436  C CD1 . TYR   A 57  ? 0.1740 0.1756 0.1541 0.0135  0.0130  -0.0047 63  TYR   A CD1 
437  C CD2 . TYR   A 57  ? 0.1754 0.1768 0.1567 0.0099  0.0120  -0.0033 63  TYR   A CD2 
438  C CE1 . TYR   A 57  ? 0.1794 0.1833 0.1591 0.0153  0.0151  -0.0042 63  TYR   A CE1 
439  C CE2 . TYR   A 57  ? 0.1848 0.1879 0.1645 0.0117  0.0142  -0.0026 63  TYR   A CE2 
440  C CZ  . TYR   A 57  ? 0.1986 0.2030 0.1777 0.0143  0.0160  -0.0030 63  TYR   A CZ  
441  O OH  . TYR   A 57  ? 0.2193 0.2257 0.1976 0.0163  0.0190  -0.0021 63  TYR   A OH  
442  N N   . TYR   A 58  ? 0.1770 0.1662 0.1539 0.0067  0.0062  -0.0052 64  TYR   A N   
443  C CA  . TYR   A 58  ? 0.1817 0.1684 0.1548 0.0065  0.0040  -0.0057 64  TYR   A CA  
444  C C   . TYR   A 58  ? 0.1897 0.1798 0.1619 0.0072  0.0051  -0.0044 64  TYR   A C   
445  O O   . TYR   A 58  ? 0.1841 0.1783 0.1619 0.0060  0.0061  -0.0028 64  TYR   A O   
446  C CB  . TYR   A 58  ? 0.1891 0.1744 0.1662 0.0037  0.0012  -0.0055 64  TYR   A CB  
447  C CG  . TYR   A 58  ? 0.2067 0.1893 0.1793 0.0036  -0.0022 -0.0063 64  TYR   A CG  
448  C CD1 . TYR   A 58  ? 0.2215 0.1987 0.1869 0.0048  -0.0038 -0.0087 64  TYR   A CD1 
449  C CD2 . TYR   A 58  ? 0.2141 0.1994 0.1887 0.0027  -0.0038 -0.0047 64  TYR   A CD2 
450  C CE1 . TYR   A 58  ? 0.2446 0.2188 0.2041 0.0050  -0.0074 -0.0099 64  TYR   A CE1 
451  C CE2 . TYR   A 58  ? 0.2313 0.2141 0.2004 0.0030  -0.0075 -0.0054 64  TYR   A CE2 
452  C CZ  . TYR   A 58  ? 0.2563 0.2335 0.2174 0.0042  -0.0094 -0.0081 64  TYR   A CZ  
453  O OH  . TYR   A 58  ? 0.3057 0.2799 0.2599 0.0047  -0.0136 -0.0092 64  TYR   A OH  
454  N N   . CYS   A 59  ? 0.1845 0.1724 0.1495 0.0093  0.0054  -0.0049 65  CYS   A N   
455  C CA  . CYS   A 59  ? 0.1748 0.1653 0.1379 0.0105  0.0073  -0.0032 65  CYS   A CA  
456  C C   . CYS   A 59  ? 0.1979 0.1849 0.1547 0.0105  0.0041  -0.0031 65  CYS   A C   
457  O O   . CYS   A 59  ? 0.2123 0.1946 0.1604 0.0122  0.0030  -0.0050 65  CYS   A O   
458  C CB  . CYS   A 59  ? 0.1895 0.1803 0.1488 0.0136  0.0108  -0.0035 65  CYS   A CB  
459  S SG  . CYS   A 59  ? 0.2318 0.2250 0.1880 0.0154  0.0143  -0.0008 65  CYS   A SG  
460  N N   . SER   A 60  ? 0.1918 0.1810 0.1528 0.0087  0.0024  -0.0011 66  SER   A N   
461  C CA  . SER   A 60  ? 0.2063 0.1927 0.1621 0.0086  -0.0016 -0.0009 66  SER   A CA  
462  C C   . SER   A 60  ? 0.2180 0.2023 0.1632 0.0116  -0.0003 -0.0001 66  SER   A C   
463  O O   . SER   A 60  ? 0.2369 0.2165 0.1731 0.0126  -0.0040 -0.0015 66  SER   A O   
464  C CB  . SER   A 60  ? 0.2644 0.2539 0.2279 0.0066  -0.0035 0.0015  66  SER   A CB  
465  O OG  . SER   A 60  ? 0.3400 0.3333 0.3074 0.0069  0.0002  0.0044  66  SER   A OG  
466  N N   . SER   A 61  ? 0.2084 0.1956 0.1541 0.0132  0.0049  0.0021  67  SER   A N   
467  C CA  . SER   A 61  ? 0.2140 0.1992 0.1497 0.0164  0.0077  0.0035  67  SER   A CA  
468  C C   . SER   A 61  ? 0.2203 0.2008 0.1461 0.0191  0.0087  0.0004  67  SER   A C   
469  O O   . SER   A 61  ? 0.2439 0.2217 0.1595 0.0222  0.0110  0.0012  67  SER   A O   
470  C CB  . SER   A 61  ? 0.2262 0.2162 0.1673 0.0169  0.0135  0.0070  67  SER   A CB  
471  O OG  . SER   A 61  ? 0.2296 0.2227 0.1772 0.0168  0.0168  0.0058  67  SER   A OG  
472  N N   . ARG   A 62  ? 0.2087 0.1875 0.1368 0.0183  0.0071  -0.0029 68  ARG   A N   
473  C CA  . ARG   A 62  ? 0.2275 0.2008 0.1468 0.0209  0.0076  -0.0063 68  ARG   A CA  
474  C C   . ARG   A 62  ? 0.2517 0.2197 0.1694 0.0190  0.0016  -0.0100 68  ARG   A C   
475  O O   . ARG   A 62  ? 0.2727 0.2348 0.1833 0.0208  0.0012  -0.0133 68  ARG   A O   
476  C CB  . ARG   A 62  ? 0.2425 0.2185 0.1672 0.0222  0.0123  -0.0066 68  ARG   A CB  
477  C CG  . ARG   A 62  ? 0.2506 0.2317 0.1775 0.0243  0.0184  -0.0034 68  ARG   A CG  
478  C CD  . ARG   A 62  ? 0.2692 0.2460 0.1835 0.0283  0.0215  -0.0036 68  ARG   A CD  
479  N NE  . ARG   A 62  ? 0.2781 0.2599 0.1954 0.0303  0.0281  0.0000  68  ARG   A NE  
480  C CZ  . ARG   A 62  ? 0.2882 0.2724 0.2057 0.0299  0.0300  0.0038  68  ARG   A CZ  
481  N NH1 . ARG   A 62  ? 0.2852 0.2673 0.1994 0.0281  0.0255  0.0046  68  ARG   A NH1 
482  N NH2 . ARG   A 62  ? 0.2950 0.2837 0.2168 0.0314  0.0365  0.0072  68  ARG   A NH2 
483  N N   . ARG   A 63  ? 0.2507 0.2206 0.1759 0.0154  -0.0028 -0.0093 69  ARG   A N   
484  C CA  . ARG   A 63  ? 0.2706 0.2365 0.1977 0.0130  -0.0080 -0.0122 69  ARG   A CA  
485  C C   . ARG   A 63  ? 0.2753 0.2384 0.2042 0.0134  -0.0061 -0.0146 69  ARG   A C   
486  O O   . ARG   A 63  ? 0.2961 0.2526 0.2200 0.0135  -0.0088 -0.0181 69  ARG   A O   
487  C CB  . ARG   A 63  ? 0.3163 0.2759 0.2324 0.0138  -0.0132 -0.0150 69  ARG   A CB  
488  C CG  . ARG   A 63  ? 0.3988 0.3609 0.3169 0.0121  -0.0177 -0.0131 69  ARG   A CG  
489  C CD  . ARG   A 63  ? 0.4331 0.3890 0.3436 0.0117  -0.0250 -0.0167 69  ARG   A CD  
490  N NE  . ARG   A 63  ? 0.4509 0.4085 0.3579 0.0121  -0.0287 -0.0144 69  ARG   A NE  
491  C CZ  . ARG   A 63  ? 0.4557 0.4094 0.3480 0.0154  -0.0297 -0.0148 69  ARG   A CZ  
492  N NH1 . ARG   A 63  ? 0.4672 0.4146 0.3469 0.0184  -0.0275 -0.0180 69  ARG   A NH1 
493  N NH2 . ARG   A 63  ? 0.4259 0.3817 0.3156 0.0160  -0.0328 -0.0117 69  ARG   A NH2 
494  N N   . LYS   A 64  ? 0.2476 0.2152 0.1826 0.0139  -0.0015 -0.0127 70  LYS   A N   
495  C CA  . LYS   A 64  ? 0.2516 0.2168 0.1876 0.0151  0.0005  -0.0143 70  LYS   A CA  
496  C C   . LYS   A 64  ? 0.2252 0.1960 0.1710 0.0139  0.0028  -0.0121 70  LYS   A C   
497  O O   . LYS   A 64  ? 0.2248 0.2016 0.1756 0.0131  0.0043  -0.0096 70  LYS   A O   
498  C CB  . LYS   A 64  ? 0.3029 0.2668 0.2315 0.0194  0.0047  -0.0150 70  LYS   A CB  
499  C CG  . LYS   A 64  ? 0.4335 0.3889 0.3509 0.0217  0.0034  -0.0186 70  LYS   A CG  
500  C CD  . LYS   A 64  ? 0.5251 0.4808 0.4376 0.0263  0.0090  -0.0185 70  LYS   A CD  
501  C CE  . LYS   A 64  ? 0.6215 0.5687 0.5210 0.0295  0.0089  -0.0221 70  LYS   A CE  
502  N NZ  . LYS   A 64  ? 0.6786 0.6274 0.5724 0.0339  0.0149  -0.0209 70  LYS   A NZ  
503  N N   . HIS   A 65  ? 0.2146 0.1828 0.1624 0.0141  0.0033  -0.0130 71  HIS   A N   
504  C CA  . HIS   A 65  ? 0.2089 0.1816 0.1638 0.0138  0.0054  -0.0112 71  HIS   A CA  
505  C C   . HIS   A 65  ? 0.2204 0.1945 0.1736 0.0175  0.0088  -0.0111 71  HIS   A C   
506  O O   . HIS   A 65  ? 0.2426 0.2118 0.1897 0.0203  0.0096  -0.0129 71  HIS   A O   
507  C CB  . HIS   A 65  ? 0.2132 0.1819 0.1711 0.0122  0.0041  -0.0116 71  HIS   A CB  
508  C CG  . HIS   A 65  ? 0.2226 0.1903 0.1844 0.0085  0.0011  -0.0115 71  HIS   A CG  
509  N ND1 . HIS   A 65  ? 0.2567 0.2285 0.2257 0.0063  0.0015  -0.0094 71  HIS   A ND1 
510  C CD2 . HIS   A 65  ? 0.2314 0.1944 0.1912 0.0069  -0.0025 -0.0133 71  HIS   A CD2 
511  C CE1 . HIS   A 65  ? 0.2355 0.2056 0.2078 0.0035  -0.0013 -0.0097 71  HIS   A CE1 
512  N NE2 . HIS   A 65  ? 0.2717 0.2369 0.2390 0.0036  -0.0042 -0.0121 71  HIS   A NE2 
513  N N   . TYR   A 66  ? 0.2015 0.1820 0.1604 0.0178  0.0107  -0.0093 72  TYR   A N   
514  C CA  . TYR   A 66  ? 0.1993 0.1828 0.1590 0.0211  0.0135  -0.0089 72  TYR   A CA  
515  C C   . TYR   A 66  ? 0.1920 0.1786 0.1571 0.0211  0.0133  -0.0079 72  TYR   A C   
516  O O   . TYR   A 66  ? 0.1942 0.1836 0.1634 0.0185  0.0122  -0.0070 72  TYR   A O   
517  C CB  . TYR   A 66  ? 0.2066 0.1965 0.1689 0.0217  0.0159  -0.0075 72  TYR   A CB  
518  C CG  . TYR   A 66  ? 0.2317 0.2189 0.1871 0.0229  0.0171  -0.0080 72  TYR   A CG  
519  C CD1 . TYR   A 66  ? 0.2557 0.2395 0.2052 0.0267  0.0194  -0.0092 72  TYR   A CD1 
520  C CD2 . TYR   A 66  ? 0.2450 0.2331 0.1995 0.0208  0.0163  -0.0070 72  TYR   A CD2 
521  C CE1 . TYR   A 66  ? 0.2735 0.2544 0.2150 0.0283  0.0210  -0.0097 72  TYR   A CE1 
522  C CE2 . TYR   A 66  ? 0.2685 0.2539 0.2153 0.0224  0.0173  -0.0070 72  TYR   A CE2 
523  C CZ  . TYR   A 66  ? 0.2926 0.2741 0.2322 0.0261  0.0197  -0.0085 72  TYR   A CZ  
524  O OH  . TYR   A 66  ? 0.3219 0.3002 0.2521 0.0281  0.0212  -0.0086 72  TYR   A OH  
525  N N   . PRO   A 67  ? 0.1975 0.1835 0.1623 0.0243  0.0143  -0.0079 73  PRO   A N   
526  C CA  . PRO   A 67  ? 0.2045 0.1939 0.1735 0.0249  0.0137  -0.0067 73  PRO   A CA  
527  C C   . PRO   A 67  ? 0.2128 0.2110 0.1881 0.0249  0.0143  -0.0059 73  PRO   A C   
528  O O   . PRO   A 67  ? 0.2363 0.2377 0.2132 0.0261  0.0163  -0.0059 73  PRO   A O   
529  C CB  . PRO   A 67  ? 0.2111 0.1967 0.1777 0.0289  0.0145  -0.0069 73  PRO   A CB  
530  C CG  . PRO   A 67  ? 0.2187 0.2032 0.1824 0.0311  0.0168  -0.0081 73  PRO   A CG  
531  C CD  . PRO   A 67  ? 0.2027 0.1848 0.1630 0.0280  0.0161  -0.0091 73  PRO   A CD  
532  N N   . VAL   A 68  ? 0.1838 0.1856 0.1628 0.0237  0.0127  -0.0054 74  VAL   A N   
533  C CA  . VAL   A 68  ? 0.1912 0.2010 0.1770 0.0232  0.0126  -0.0051 74  VAL   A CA  
534  C C   . VAL   A 68  ? 0.1872 0.1997 0.1749 0.0244  0.0103  -0.0050 74  VAL   A C   
535  O O   . VAL   A 68  ? 0.1799 0.1882 0.1633 0.0245  0.0091  -0.0047 74  VAL   A O   
536  C CB  . VAL   A 68  ? 0.2094 0.2212 0.1980 0.0194  0.0124  -0.0052 74  VAL   A CB  
537  C CG1 . VAL   A 68  ? 0.2391 0.2511 0.2276 0.0188  0.0146  -0.0048 74  VAL   A CG1 
538  C CG2 . VAL   A 68  ? 0.2184 0.2255 0.2035 0.0171  0.0112  -0.0054 74  VAL   A CG2 
539  N N   . SER   A 69  ? 0.1881 0.2079 0.1827 0.0253  0.0097  -0.0051 75  SER   A N   
540  C CA  . SER   A 69  ? 0.1968 0.2205 0.1939 0.0258  0.0065  -0.0055 75  SER   A CA  
541  C C   . SER   A 69  ? 0.1794 0.2074 0.1819 0.0222  0.0059  -0.0066 75  SER   A C   
542  O O   . SER   A 69  ? 0.1828 0.2148 0.1915 0.0212  0.0078  -0.0064 75  SER   A O   
543  C CB  . SER   A 69  ? 0.2464 0.2757 0.2490 0.0293  0.0056  -0.0050 75  SER   A CB  
544  O OG  . SER   A 69  ? 0.3341 0.3585 0.3315 0.0329  0.0063  -0.0040 75  SER   A OG  
545  N N   . PHE   A 70  ? 0.1656 0.1924 0.1659 0.0204  0.0038  -0.0076 76  PHE   A N   
546  C CA  . PHE   A 70  ? 0.1694 0.1989 0.1744 0.0170  0.0035  -0.0089 76  PHE   A CA  
547  C C   . PHE   A 70  ? 0.1839 0.2163 0.1902 0.0168  -0.0004 -0.0109 76  PHE   A C   
548  O O   . PHE   A 70  ? 0.1977 0.2285 0.1985 0.0190  -0.0027 -0.0110 76  PHE   A O   
549  C CB  . PHE   A 70  ? 0.1686 0.1927 0.1694 0.0145  0.0054  -0.0087 76  PHE   A CB  
550  C CG  . PHE   A 70  ? 0.1668 0.1848 0.1595 0.0151  0.0052  -0.0083 76  PHE   A CG  
551  C CD1 . PHE   A 70  ? 0.1865 0.1996 0.1744 0.0164  0.0066  -0.0069 76  PHE   A CD1 
552  C CD2 . PHE   A 70  ? 0.1844 0.2011 0.1744 0.0142  0.0040  -0.0095 76  PHE   A CD2 
553  C CE1 . PHE   A 70  ? 0.1831 0.1906 0.1650 0.0167  0.0069  -0.0061 76  PHE   A CE1 
554  C CE2 . PHE   A 70  ? 0.1799 0.1910 0.1628 0.0149  0.0048  -0.0086 76  PHE   A CE2 
555  C CZ  . PHE   A 70  ? 0.1869 0.1937 0.1665 0.0160  0.0063  -0.0067 76  PHE   A CZ  
556  N N   . SER   A 71  ? 0.1728 0.2096 0.1868 0.0141  -0.0012 -0.0125 77  SER   A N   
557  C CA  . SER   A 71  ? 0.1877 0.2271 0.2034 0.0135  -0.0054 -0.0152 77  SER   A CA  
558  C C   . SER   A 71  ? 0.1890 0.2226 0.1964 0.0125  -0.0059 -0.0167 77  SER   A C   
559  O O   . SER   A 71  ? 0.2049 0.2337 0.2084 0.0114  -0.0027 -0.0157 77  SER   A O   
560  C CB  . SER   A 71  ? 0.2059 0.2513 0.2336 0.0107  -0.0059 -0.0165 77  SER   A CB  
561  O OG  . SER   A 71  ? 0.2430 0.2855 0.2720 0.0076  -0.0029 -0.0165 77  SER   A OG  
562  N N   . LYS   A 72  ? 0.1892 0.2234 0.1936 0.0132  -0.0101 -0.0193 78  LYS   A N   
563  C CA  . LYS   A 72  ? 0.2047 0.2332 0.2004 0.0127  -0.0100 -0.0209 78  LYS   A CA  
564  C C   . LYS   A 72  ? 0.2152 0.2428 0.2160 0.0090  -0.0080 -0.0226 78  LYS   A C   
565  O O   . LYS   A 72  ? 0.2169 0.2490 0.2279 0.0068  -0.0085 -0.0234 78  LYS   A O   
566  C CB  . LYS   A 72  ? 0.2449 0.2743 0.2357 0.0145  -0.0155 -0.0238 78  LYS   A CB  
567  C CG  . LYS   A 72  ? 0.3212 0.3503 0.3053 0.0187  -0.0175 -0.0216 78  LYS   A CG  
568  C CD  . LYS   A 72  ? 0.4069 0.4362 0.3842 0.0207  -0.0232 -0.0245 78  LYS   A CD  
569  C CE  . LYS   A 72  ? 0.4879 0.5183 0.4606 0.0252  -0.0261 -0.0221 78  LYS   A CE  
570  N NZ  . LYS   A 72  ? 0.5511 0.5819 0.5165 0.0274  -0.0325 -0.0246 78  LYS   A NZ  
571  N N   . PRO   A 73  ? 0.2170 0.2389 0.2116 0.0084  -0.0056 -0.0230 79  PRO   A N   
572  C CA  . PRO   A 73  ? 0.2236 0.2442 0.2234 0.0052  -0.0035 -0.0245 79  PRO   A CA  
573  C C   . PRO   A 73  ? 0.2249 0.2483 0.2306 0.0034  -0.0071 -0.0285 79  PRO   A C   
574  O O   . PRO   A 73  ? 0.2280 0.2512 0.2287 0.0046  -0.0112 -0.0315 79  PRO   A O   
575  C CB  . PRO   A 73  ? 0.2429 0.2571 0.2339 0.0059  -0.0011 -0.0248 79  PRO   A CB  
576  C CG  . PRO   A 73  ? 0.2625 0.2745 0.2450 0.0088  -0.0003 -0.0222 79  PRO   A CG  
577  C CD  . PRO   A 73  ? 0.2280 0.2443 0.2114 0.0107  -0.0040 -0.0218 79  PRO   A CD  
578  N N   . SER   A 74  ? 0.2277 0.2538 0.2442 0.0005  -0.0060 -0.0284 80  SER   A N   
579  C CA  . SER   A 74  ? 0.2353 0.2642 0.2596 -0.0017 -0.0094 -0.0321 80  SER   A CA  
580  C C   . SER   A 74  ? 0.2075 0.2357 0.2414 -0.0051 -0.0064 -0.0319 80  SER   A C   
581  O O   . SER   A 74  ? 0.1932 0.2191 0.2269 -0.0053 -0.0020 -0.0286 80  SER   A O   
582  C CB  . SER   A 74  ? 0.2955 0.3317 0.3267 -0.0011 -0.0129 -0.0319 80  SER   A CB  
583  O OG  . SER   A 74  ? 0.3537 0.3933 0.3925 -0.0016 -0.0094 -0.0279 80  SER   A OG  
584  N N   . LEU   A 75  ? 0.2063 0.2361 0.2484 -0.0077 -0.0092 -0.0355 81  LEU   A N   
585  C CA  . LEU   A 75  ? 0.2174 0.2460 0.2694 -0.0110 -0.0067 -0.0355 81  LEU   A CA  
586  C C   . LEU   A 75  ? 0.2189 0.2539 0.2827 -0.0123 -0.0053 -0.0321 81  LEU   A C   
587  O O   . LEU   A 75  ? 0.2253 0.2661 0.2959 -0.0127 -0.0089 -0.0334 81  LEU   A O   
588  C CB  . LEU   A 75  ? 0.2344 0.2611 0.2892 -0.0132 -0.0108 -0.0416 81  LEU   A CB  
589  C CG  . LEU   A 75  ? 0.2771 0.2995 0.3390 -0.0162 -0.0083 -0.0428 81  LEU   A CG  
590  C CD1 . LEU   A 75  ? 0.2858 0.3018 0.3407 -0.0149 -0.0032 -0.0406 81  LEU   A CD1 
591  C CD2 . LEU   A 75  ? 0.3108 0.3308 0.3749 -0.0182 -0.0131 -0.0497 81  LEU   A CD2 
592  N N   . ILE   A 76  ? 0.2088 0.2430 0.2748 -0.0125 -0.0002 -0.0274 82  ILE   A N   
593  C CA  . ILE   A 76  ? 0.2158 0.2552 0.2906 -0.0130 0.0024  -0.0234 82  ILE   A CA  
594  C C   . ILE   A 76  ? 0.2097 0.2473 0.2926 -0.0155 0.0065  -0.0209 82  ILE   A C   
595  O O   . ILE   A 76  ? 0.2146 0.2467 0.2927 -0.0154 0.0089  -0.0197 82  ILE   A O   
596  C CB  . ILE   A 76  ? 0.2452 0.2849 0.3116 -0.0097 0.0046  -0.0195 82  ILE   A CB  
597  C CG1 . ILE   A 76  ? 0.2858 0.3272 0.3452 -0.0071 0.0008  -0.0215 82  ILE   A CG1 
598  C CG2 . ILE   A 76  ? 0.2488 0.2924 0.3215 -0.0095 0.0085  -0.0150 82  ILE   A CG2 
599  C CD1 . ILE   A 76  ? 0.3337 0.3739 0.3846 -0.0042 0.0025  -0.0187 82  ILE   A CD1 
600  N N   . PHE   A 77  ? 0.1983 0.2404 0.2940 -0.0177 0.0075  -0.0196 83  PHE   A N   
601  C CA  . PHE   A 77  ? 0.2052 0.2453 0.3088 -0.0199 0.0120  -0.0164 83  PHE   A CA  
602  C C   . PHE   A 77  ? 0.2110 0.2499 0.3086 -0.0176 0.0169  -0.0105 83  PHE   A C   
603  O O   . PHE   A 77  ? 0.2134 0.2561 0.3083 -0.0154 0.0180  -0.0082 83  PHE   A O   
604  C CB  . PHE   A 77  ? 0.2041 0.2498 0.3237 -0.0228 0.0124  -0.0160 83  PHE   A CB  
605  C CG  . PHE   A 77  ? 0.2317 0.2751 0.3600 -0.0250 0.0177  -0.0119 83  PHE   A CG  
606  C CD1 . PHE   A 77  ? 0.2440 0.2901 0.3750 -0.0240 0.0231  -0.0058 83  PHE   A CD1 
607  C CD2 . PHE   A 77  ? 0.2586 0.2962 0.3907 -0.0276 0.0176  -0.0139 83  PHE   A CD2 
608  C CE1 . PHE   A 77  ? 0.2512 0.2946 0.3889 -0.0256 0.0283  -0.0013 83  PHE   A CE1 
609  C CE2 . PHE   A 77  ? 0.2693 0.3042 0.4092 -0.0294 0.0227  -0.0095 83  PHE   A CE2 
610  C CZ  . PHE   A 77  ? 0.2543 0.2923 0.3971 -0.0284 0.0280  -0.0031 83  PHE   A CZ  
611  N N   . VAL   A 78  ? 0.1980 0.2313 0.2933 -0.0179 0.0197  -0.0083 84  VAL   A N   
612  C CA  . VAL   A 78  ? 0.1967 0.2283 0.2861 -0.0159 0.0236  -0.0029 84  VAL   A CA  
613  C C   . VAL   A 78  ? 0.2083 0.2378 0.3060 -0.0178 0.0277  0.0010  84  VAL   A C   
614  O O   . VAL   A 78  ? 0.2131 0.2386 0.3154 -0.0198 0.0275  -0.0005 84  VAL   A O   
615  C CB  . VAL   A 78  ? 0.2101 0.2368 0.2883 -0.0141 0.0225  -0.0034 84  VAL   A CB  
616  C CG1 . VAL   A 78  ? 0.2319 0.2568 0.3040 -0.0120 0.0254  0.0018  84  VAL   A CG1 
617  C CG2 . VAL   A 78  ? 0.2097 0.2376 0.2800 -0.0123 0.0189  -0.0069 84  VAL   A CG2 
618  N N   . GLU   A 79  ? 0.2086 0.2404 0.3077 -0.0168 0.0318  0.0061  85  GLU   A N   
619  C CA  . GLU   A 79  ? 0.2190 0.2489 0.3254 -0.0181 0.0365  0.0109  85  GLU   A CA  
620  C C   . GLU   A 79  ? 0.2238 0.2471 0.3248 -0.0174 0.0374  0.0132  85  GLU   A C   
621  O O   . GLU   A 79  ? 0.2180 0.2393 0.3084 -0.0151 0.0353  0.0126  85  GLU   A O   
622  C CB  . GLU   A 79  ? 0.2645 0.2975 0.3695 -0.0161 0.0412  0.0163  85  GLU   A CB  
623  C CG  . GLU   A 79  ? 0.3768 0.4081 0.4898 -0.0174 0.0468  0.0218  85  GLU   A CG  
624  C CD  . GLU   A 79  ? 0.4908 0.5241 0.6206 -0.0217 0.0470  0.0199  85  GLU   A CD  
625  O OE1 . GLU   A 79  ? 0.5015 0.5300 0.6368 -0.0240 0.0469  0.0194  85  GLU   A OE1 
626  O OE2 . GLU   A 79  ? 0.5347 0.5744 0.6723 -0.0226 0.0466  0.0182  85  GLU   A OE2 
627  N N   . ALA   A 80  ? 0.2332 0.2532 0.3424 -0.0192 0.0406  0.0163  86  ALA   A N   
628  C CA  . ALA   A 80  ? 0.2382 0.2521 0.3434 -0.0181 0.0416  0.0193  86  ALA   A CA  
629  C C   . ALA   A 80  ? 0.2431 0.2565 0.3364 -0.0144 0.0429  0.0242  86  ALA   A C   
630  O O   . ALA   A 80  ? 0.2456 0.2621 0.3361 -0.0131 0.0453  0.0271  86  ALA   A O   
631  C CB  . ALA   A 80  ? 0.2411 0.2517 0.3573 -0.0202 0.0456  0.0230  86  ALA   A CB  
632  N N   . SER   A 81  ? 0.2450 0.2547 0.3314 -0.0127 0.0409  0.0246  87  SER   A N   
633  C CA  . SER   A 81  ? 0.2401 0.2487 0.3155 -0.0094 0.0410  0.0289  87  SER   A CA  
634  C C   . SER   A 81  ? 0.2631 0.2667 0.3392 -0.0086 0.0411  0.0320  87  SER   A C   
635  O O   . SER   A 81  ? 0.2832 0.2840 0.3684 -0.0106 0.0418  0.0308  87  SER   A O   
636  C CB  . SER   A 81  ? 0.2405 0.2509 0.3064 -0.0078 0.0368  0.0251  87  SER   A CB  
637  O OG  . SER   A 81  ? 0.2281 0.2366 0.2953 -0.0085 0.0338  0.0213  87  SER   A OG  
638  N N   . GLU   A 82  ? 0.2662 0.2682 0.3329 -0.0056 0.0401  0.0359  88  GLU   A N   
639  C CA  . GLU   A 82  ? 0.2806 0.2785 0.3484 -0.0044 0.0394  0.0388  88  GLU   A CA  
640  C C   . GLU   A 82  ? 0.2874 0.2846 0.3580 -0.0051 0.0361  0.0341  88  GLU   A C   
641  O O   . GLU   A 82  ? 0.3066 0.3006 0.3812 -0.0044 0.0360  0.0359  88  GLU   A O   
642  C CB  . GLU   A 82  ? 0.3453 0.3419 0.4029 -0.0010 0.0383  0.0442  88  GLU   A CB  
643  C CG  . GLU   A 82  ? 0.4681 0.4673 0.5142 0.0007  0.0352  0.0424  88  GLU   A CG  
644  C CD  . GLU   A 82  ? 0.6157 0.6138 0.6513 0.0036  0.0365  0.0476  88  GLU   A CD  
645  O OE1 . GLU   A 82  ? 0.6488 0.6438 0.6846 0.0049  0.0390  0.0535  88  GLU   A OE1 
646  O OE2 . GLU   A 82  ? 0.6378 0.6376 0.6644 0.0047  0.0352  0.0458  88  GLU   A OE2 
647  N N   . TYR   A 83  ? 0.2609 0.2611 0.3297 -0.0061 0.0337  0.0282  89  TYR   A N   
648  C CA  . TYR   A 83  ? 0.2460 0.2455 0.3161 -0.0064 0.0313  0.0238  89  TYR   A CA  
649  C C   . TYR   A 83  ? 0.2220 0.2205 0.2994 -0.0089 0.0320  0.0187  89  TYR   A C   
650  O O   . TYR   A 83  ? 0.2299 0.2262 0.3096 -0.0088 0.0314  0.0161  89  TYR   A O   
651  C CB  . TYR   A 83  ? 0.2391 0.2416 0.3011 -0.0055 0.0282  0.0211  89  TYR   A CB  
652  C CG  . TYR   A 83  ? 0.2464 0.2493 0.3005 -0.0031 0.0265  0.0250  89  TYR   A CG  
653  C CD1 . TYR   A 83  ? 0.2654 0.2698 0.3128 -0.0023 0.0270  0.0268  89  TYR   A CD1 
654  C CD2 . TYR   A 83  ? 0.2535 0.2553 0.3069 -0.0016 0.0241  0.0267  89  TYR   A CD2 
655  C CE1 . TYR   A 83  ? 0.2852 0.2892 0.3240 0.0000  0.0250  0.0297  89  TYR   A CE1 
656  C CE2 . TYR   A 83  ? 0.2692 0.2714 0.3152 0.0004  0.0215  0.0297  89  TYR   A CE2 
657  C CZ  . TYR   A 83  ? 0.3025 0.3053 0.3403 0.0012  0.0218  0.0309  89  TYR   A CZ  
658  O OH  . TYR   A 83  ? 0.3519 0.3544 0.3812 0.0033  0.0188  0.0333  89  TYR   A OH  
659  N N   . TYR   A 84  ? 0.2028 0.2031 0.2838 -0.0109 0.0332  0.0171  90  TYR   A N   
660  C CA  . TYR   A 84  ? 0.2105 0.2099 0.2980 -0.0134 0.0329  0.0116  90  TYR   A CA  
661  C C   . TYR   A 84  ? 0.2282 0.2280 0.3245 -0.0159 0.0352  0.0125  90  TYR   A C   
662  O O   . TYR   A 84  ? 0.2302 0.2331 0.3261 -0.0157 0.0369  0.0161  90  TYR   A O   
663  C CB  . TYR   A 84  ? 0.2044 0.2074 0.2867 -0.0136 0.0299  0.0063  90  TYR   A CB  
664  C CG  . TYR   A 84  ? 0.1891 0.1919 0.2637 -0.0116 0.0278  0.0045  90  TYR   A CG  
665  C CD1 . TYR   A 84  ? 0.1929 0.1924 0.2682 -0.0116 0.0275  0.0010  90  TYR   A CD1 
666  C CD2 . TYR   A 84  ? 0.1917 0.1972 0.2584 -0.0100 0.0264  0.0060  90  TYR   A CD2 
667  C CE1 . TYR   A 84  ? 0.1852 0.1847 0.2545 -0.0099 0.0263  -0.0002 90  TYR   A CE1 
668  C CE2 . TYR   A 84  ? 0.1812 0.1866 0.2422 -0.0086 0.0247  0.0044  90  TYR   A CE2 
669  C CZ  . TYR   A 84  ? 0.1803 0.1829 0.2430 -0.0086 0.0248  0.0016  90  TYR   A CZ  
670  O OH  . TYR   A 84  ? 0.1768 0.1792 0.2351 -0.0073 0.0240  0.0006  90  TYR   A OH  
671  N N   . PRO   A 85  ? 0.2429 0.2399 0.3474 -0.0183 0.0352  0.0086  91  PRO   A N   
672  C CA  . PRO   A 85  ? 0.2387 0.2368 0.3532 -0.0214 0.0368  0.0084  91  PRO   A CA  
673  C C   . PRO   A 85  ? 0.2347 0.2390 0.3478 -0.0223 0.0341  0.0047  91  PRO   A C   
674  O O   . PRO   A 85  ? 0.2316 0.2380 0.3362 -0.0207 0.0311  0.0014  91  PRO   A O   
675  C CB  . PRO   A 85  ? 0.2619 0.2546 0.3842 -0.0237 0.0363  0.0038  91  PRO   A CB  
676  C CG  . PRO   A 85  ? 0.2755 0.2667 0.3893 -0.0219 0.0333  -0.0012 91  PRO   A CG  
677  C CD  . PRO   A 85  ? 0.2489 0.2416 0.3536 -0.0185 0.0337  0.0034  91  PRO   A CD  
678  N N   . ALA   A 86  ? 0.2263 0.2339 0.3487 -0.0247 0.0354  0.0051  92  ALA   A N   
679  C CA  . ALA   A 86  ? 0.2365 0.2505 0.3600 -0.0256 0.0326  0.0015  92  ALA   A CA  
680  C C   . ALA   A 86  ? 0.2382 0.2507 0.3602 -0.0266 0.0276  -0.0064 92  ALA   A C   
681  O O   . ALA   A 86  ? 0.2432 0.2504 0.3700 -0.0284 0.0273  -0.0092 92  ALA   A O   
682  C CB  . ALA   A 86  ? 0.2419 0.2592 0.3793 -0.0286 0.0349  0.0031  92  ALA   A CB  
683  N N   . ARG   A 87  ? 0.2368 0.2526 0.3500 -0.0248 0.0241  -0.0094 93  ARG   A N   
684  C CA  . ARG   A 87  ? 0.2274 0.2408 0.3360 -0.0249 0.0198  -0.0163 93  ARG   A CA  
685  C C   . ARG   A 87  ? 0.2169 0.2354 0.3185 -0.0233 0.0160  -0.0189 93  ARG   A C   
686  O O   . ARG   A 87  ? 0.2186 0.2418 0.3183 -0.0218 0.0170  -0.0154 93  ARG   A O   
687  C CB  . ARG   A 87  ? 0.2259 0.2332 0.3265 -0.0229 0.0210  -0.0162 93  ARG   A CB  
688  C CG  . ARG   A 87  ? 0.2202 0.2292 0.3091 -0.0195 0.0210  -0.0137 93  ARG   A CG  
689  C CD  . ARG   A 87  ? 0.2116 0.2164 0.2967 -0.0176 0.0235  -0.0103 93  ARG   A CD  
690  N NE  . ARG   A 87  ? 0.2256 0.2307 0.3004 -0.0151 0.0223  -0.0109 93  ARG   A NE  
691  C CZ  . ARG   A 87  ? 0.2067 0.2151 0.2755 -0.0134 0.0219  -0.0081 93  ARG   A CZ  
692  N NH1 . ARG   A 87  ? 0.2156 0.2234 0.2764 -0.0115 0.0211  -0.0087 93  ARG   A NH1 
693  N NH2 . ARG   A 87  ? 0.1882 0.2002 0.2591 -0.0136 0.0228  -0.0049 93  ARG   A NH2 
694  N N   . TYR   A 88  ? 0.2152 0.2320 0.3117 -0.0231 0.0120  -0.0249 94  TYR   A N   
695  C CA  . TYR   A 88  ? 0.2227 0.2432 0.3106 -0.0209 0.0085  -0.0269 94  TYR   A CA  
696  C C   . TYR   A 88  ? 0.2086 0.2252 0.2840 -0.0179 0.0098  -0.0259 94  TYR   A C   
697  O O   . TYR   A 88  ? 0.2322 0.2431 0.3046 -0.0178 0.0106  -0.0280 94  TYR   A O   
698  C CB  . TYR   A 88  ? 0.2377 0.2585 0.3257 -0.0220 0.0031  -0.0336 94  TYR   A CB  
699  C CG  . TYR   A 88  ? 0.2629 0.2889 0.3645 -0.0250 0.0010  -0.0346 94  TYR   A CG  
700  C CD1 . TYR   A 88  ? 0.2860 0.3196 0.3902 -0.0243 -0.0014 -0.0339 94  TYR   A CD1 
701  C CD2 . TYR   A 88  ? 0.2899 0.3135 0.4033 -0.0286 0.0020  -0.0358 94  TYR   A CD2 
702  C CE1 . TYR   A 88  ? 0.3058 0.3452 0.4248 -0.0271 -0.0028 -0.0342 94  TYR   A CE1 
703  C CE2 . TYR   A 88  ? 0.3083 0.3372 0.4364 -0.0318 0.0007  -0.0360 94  TYR   A CE2 
704  C CZ  . TYR   A 88  ? 0.3255 0.3626 0.4567 -0.0310 -0.0017 -0.0352 94  TYR   A CZ  
705  O OH  . TYR   A 88  ? 0.3586 0.4015 0.5063 -0.0343 -0.0028 -0.0354 94  TYR   A OH  
706  N N   . GLN   A 89  ? 0.1865 0.2060 0.2557 -0.0156 0.0103  -0.0228 95  GLN   A N   
707  C CA  . GLN   A 89  ? 0.1744 0.1907 0.2329 -0.0130 0.0112  -0.0218 95  GLN   A CA  
708  C C   . GLN   A 89  ? 0.1842 0.2013 0.2346 -0.0114 0.0078  -0.0254 95  GLN   A C   
709  O O   . GLN   A 89  ? 0.1973 0.2191 0.2485 -0.0109 0.0054  -0.0256 95  GLN   A O   
710  C CB  . GLN   A 89  ? 0.1729 0.1909 0.2289 -0.0115 0.0137  -0.0164 95  GLN   A CB  
711  C CG  . GLN   A 89  ? 0.1717 0.1870 0.2182 -0.0093 0.0142  -0.0156 95  GLN   A CG  
712  C CD  . GLN   A 89  ? 0.1772 0.1926 0.2223 -0.0083 0.0162  -0.0108 95  GLN   A CD  
713  O OE1 . GLN   A 89  ? 0.1716 0.1867 0.2217 -0.0091 0.0182  -0.0078 95  GLN   A OE1 
714  N NE2 . GLN   A 89  ? 0.1565 0.1719 0.1943 -0.0065 0.0157  -0.0099 95  GLN   A NE2 
715  N N   . SER   A 90  ? 0.1787 0.1912 0.2215 -0.0102 0.0077  -0.0278 96  SER   A N   
716  C CA  . SER   A 90  ? 0.1819 0.1941 0.2155 -0.0083 0.0049  -0.0308 96  SER   A CA  
717  C C   . SER   A 90  ? 0.1954 0.2075 0.2208 -0.0057 0.0063  -0.0275 96  SER   A C   
718  O O   . SER   A 90  ? 0.1897 0.2009 0.2160 -0.0055 0.0095  -0.0237 96  SER   A O   
719  C CB  . SER   A 90  ? 0.2046 0.2113 0.2335 -0.0081 0.0044  -0.0355 96  SER   A CB  
720  O OG  . SER   A 90  ? 0.2472 0.2494 0.2738 -0.0074 0.0087  -0.0339 96  SER   A OG  
721  N N   . HIS   A 91  ? 0.1875 0.2002 0.2051 -0.0036 0.0038  -0.0289 97  HIS   A N   
722  C CA  . HIS   A 91  ? 0.1789 0.1906 0.1884 -0.0011 0.0050  -0.0261 97  HIS   A CA  
723  C C   . HIS   A 91  ? 0.1648 0.1798 0.1782 -0.0012 0.0061  -0.0219 97  HIS   A C   
724  O O   . HIS   A 91  ? 0.1713 0.1844 0.1811 -0.0001 0.0083  -0.0191 97  HIS   A O   
725  C CB  . HIS   A 91  ? 0.2097 0.2162 0.2141 -0.0004 0.0086  -0.0256 97  HIS   A CB  
726  C CG  . HIS   A 91  ? 0.2402 0.2426 0.2385 0.0003  0.0081  -0.0298 97  HIS   A CG  
727  N ND1 . HIS   A 91  ? 0.2872 0.2870 0.2746 0.0030  0.0077  -0.0306 97  HIS   A ND1 
728  C CD2 . HIS   A 91  ? 0.2533 0.2532 0.2545 -0.0010 0.0081  -0.0334 97  HIS   A CD2 
729  C CE1 . HIS   A 91  ? 0.2917 0.2878 0.2747 0.0033  0.0074  -0.0348 97  HIS   A CE1 
730  N NE2 . HIS   A 91  ? 0.2782 0.2741 0.2694 0.0009  0.0074  -0.0370 97  HIS   A NE2 
731  N N   . LEU   A 92  ? 0.1536 0.1732 0.1746 -0.0023 0.0049  -0.0216 98  LEU   A N   
732  C CA  . LEU   A 92  ? 0.1608 0.1829 0.1845 -0.0020 0.0065  -0.0179 98  LEU   A CA  
733  C C   . LEU   A 92  ? 0.1705 0.1962 0.1923 0.0001  0.0043  -0.0177 98  LEU   A C   
734  O O   . LEU   A 92  ? 0.1675 0.1963 0.1916 0.0003  0.0011  -0.0201 98  LEU   A O   
735  C CB  . LEU   A 92  ? 0.1624 0.1871 0.1961 -0.0042 0.0078  -0.0169 98  LEU   A CB  
736  C CG  . LEU   A 92  ? 0.1870 0.2138 0.2230 -0.0038 0.0103  -0.0129 98  LEU   A CG  
737  C CD1 . LEU   A 92  ? 0.2004 0.2233 0.2307 -0.0030 0.0123  -0.0102 98  LEU   A CD1 
738  C CD2 . LEU   A 92  ? 0.2187 0.2476 0.2646 -0.0060 0.0121  -0.0116 98  LEU   A CD2 
739  N N   . MET   A 93  ? 0.1721 0.1973 0.1904 0.0018  0.0058  -0.0148 99  MET   A N   
740  C CA  . MET   A 93  ? 0.1743 0.2021 0.1906 0.0043  0.0044  -0.0142 99  MET   A CA  
741  C C   . MET   A 93  ? 0.1775 0.2077 0.1979 0.0046  0.0066  -0.0117 99  MET   A C   
742  O O   . MET   A 93  ? 0.1804 0.2080 0.1989 0.0042  0.0091  -0.0097 99  MET   A O   
743  C CB  . MET   A 93  ? 0.1870 0.2102 0.1939 0.0063  0.0046  -0.0133 99  MET   A CB  
744  C CG  . MET   A 93  ? 0.2011 0.2211 0.2025 0.0065  0.0034  -0.0153 99  MET   A CG  
745  S SD  . MET   A 93  ? 0.2409 0.2551 0.2323 0.0086  0.0048  -0.0135 99  MET   A SD  
746  C CE  . MET   A 93  ? 0.2272 0.2387 0.2209 0.0066  0.0083  -0.0113 99  MET   A CE  
747  N N   . LEU   A 94  ? 0.1847 0.2204 0.2110 0.0054  0.0058  -0.0117 100 LEU   A N   
748  C CA  . LEU   A 94  ? 0.1872 0.2252 0.2170 0.0061  0.0088  -0.0092 100 LEU   A CA  
749  C C   . LEU   A 94  ? 0.1790 0.2169 0.2044 0.0096  0.0090  -0.0082 100 LEU   A C   
750  O O   . LEU   A 94  ? 0.1767 0.2157 0.2005 0.0114  0.0062  -0.0093 100 LEU   A O   
751  C CB  . LEU   A 94  ? 0.1952 0.2396 0.2367 0.0048  0.0091  -0.0093 100 LEU   A CB  
752  C CG  . LEU   A 94  ? 0.2344 0.2787 0.2822 0.0012  0.0095  -0.0100 100 LEU   A CG  
753  C CD1 . LEU   A 94  ? 0.2404 0.2910 0.3013 -0.0003 0.0106  -0.0094 100 LEU   A CD1 
754  C CD2 . LEU   A 94  ? 0.2552 0.2947 0.2992 0.0003  0.0127  -0.0078 100 LEU   A CD2 
755  N N   . ALA   A 95  ? 0.1755 0.2123 0.1993 0.0106  0.0123  -0.0061 101 ALA   A N   
756  C CA  . ALA   A 95  ? 0.1779 0.2140 0.1977 0.0141  0.0131  -0.0053 101 ALA   A CA  
757  C C   . ALA   A 95  ? 0.1781 0.2156 0.1999 0.0151  0.0173  -0.0033 101 ALA   A C   
758  O O   . ALA   A 95  ? 0.1760 0.2131 0.1993 0.0131  0.0194  -0.0021 101 ALA   A O   
759  C CB  . ALA   A 95  ? 0.1981 0.2270 0.2077 0.0150  0.0126  -0.0054 101 ALA   A CB  
760  N N   . VAL   A 96  ? 0.1725 0.2109 0.1934 0.0185  0.0187  -0.0028 102 VAL   A N   
761  C CA  . VAL   A 96  ? 0.1817 0.2202 0.2020 0.0203  0.0234  -0.0010 102 VAL   A CA  
762  C C   . VAL   A 96  ? 0.1978 0.2281 0.2060 0.0211  0.0238  -0.0012 102 VAL   A C   
763  O O   . VAL   A 96  ? 0.2045 0.2304 0.2067 0.0227  0.0219  -0.0024 102 VAL   A O   
764  C CB  . VAL   A 96  ? 0.1973 0.2405 0.2229 0.0239  0.0250  -0.0005 102 VAL   A CB  
765  C CG1 . VAL   A 96  ? 0.2115 0.2538 0.2347 0.0264  0.0307  0.0013  102 VAL   A CG1 
766  C CG2 . VAL   A 96  ? 0.2022 0.2542 0.2413 0.0225  0.0236  -0.0005 102 VAL   A CG2 
767  N N   . GLY   A 97  ? 0.1956 0.2236 0.2006 0.0200  0.0260  0.0001  103 GLY   A N   
768  C CA  . GLY   A 97  ? 0.2077 0.2284 0.2019 0.0205  0.0258  -0.0003 103 GLY   A CA  
769  C C   . GLY   A 97  ? 0.2116 0.2312 0.2037 0.0192  0.0278  0.0016  103 GLY   A C   
770  O O   . GLY   A 97  ? 0.2231 0.2470 0.2226 0.0172  0.0290  0.0032  103 GLY   A O   
771  N N   . HIS   A 98  ? 0.1973 0.2109 0.1791 0.0205  0.0279  0.0015  104 HIS   A N   
772  C CA  . HIS   A 98  ? 0.1855 0.1976 0.1637 0.0197  0.0293  0.0035  104 HIS   A CA  
773  C C   . HIS   A 98  ? 0.1889 0.2001 0.1689 0.0163  0.0259  0.0038  104 HIS   A C   
774  O O   . HIS   A 98  ? 0.1942 0.2026 0.1726 0.0150  0.0221  0.0020  104 HIS   A O   
775  C CB  . HIS   A 98  ? 0.2100 0.2154 0.1752 0.0224  0.0298  0.0029  104 HIS   A CB  
776  C CG  . HIS   A 98  ? 0.2290 0.2325 0.1888 0.0222  0.0307  0.0053  104 HIS   A CG  
777  N ND1 . HIS   A 98  ? 0.2385 0.2453 0.2008 0.0232  0.0358  0.0087  104 HIS   A ND1 
778  C CD2 . HIS   A 98  ? 0.2395 0.2387 0.1931 0.0210  0.0270  0.0052  104 HIS   A CD2 
779  C CE1 . HIS   A 98  ? 0.2559 0.2595 0.2118 0.0229  0.0352  0.0107  104 HIS   A CE1 
780  N NE2 . HIS   A 98  ? 0.2442 0.2435 0.1948 0.0216  0.0295  0.0086  104 HIS   A NE2 
781  N N   . SER   A 99  ? 0.1866 0.1995 0.1695 0.0151  0.0276  0.0065  105 SER   A N   
782  C CA  . SER   A 99  ? 0.1883 0.2000 0.1726 0.0125  0.0250  0.0074  105 SER   A CA  
783  C C   . SER   A 99  ? 0.2142 0.2264 0.1989 0.0125  0.0280  0.0111  105 SER   A C   
784  O O   . SER   A 99  ? 0.2337 0.2489 0.2219 0.0135  0.0325  0.0131  105 SER   A O   
785  C CB  . SER   A 99  ? 0.2228 0.2374 0.2162 0.0097  0.0231  0.0060  105 SER   A CB  
786  O OG  . SER   A 99  ? 0.2770 0.2965 0.2798 0.0087  0.0256  0.0072  105 SER   A OG  
787  N N   . GLU   A 100 ? 0.2040 0.2130 0.1847 0.0118  0.0257  0.0123  106 GLU   A N   
788  C CA  . GLU   A 100 ? 0.2260 0.2348 0.2066 0.0119  0.0280  0.0163  106 GLU   A CA  
789  C C   . GLU   A 100 ? 0.2554 0.2631 0.2392 0.0098  0.0245  0.0171  106 GLU   A C   
790  O O   . GLU   A 100 ? 0.2548 0.2617 0.2396 0.0085  0.0205  0.0145  106 GLU   A O   
791  C CB  . GLU   A 100 ? 0.2819 0.2870 0.2500 0.0154  0.0300  0.0181  106 GLU   A CB  
792  C CG  . GLU   A 100 ? 0.3380 0.3380 0.2953 0.0164  0.0250  0.0159  106 GLU   A CG  
793  C CD  . GLU   A 100 ? 0.3245 0.3202 0.2679 0.0201  0.0268  0.0168  106 GLU   A CD  
794  O OE1 . GLU   A 100 ? 0.3613 0.3544 0.2980 0.0211  0.0259  0.0197  106 GLU   A OE1 
795  O OE2 . GLU   A 100 ? 0.2849 0.2794 0.2232 0.0223  0.0288  0.0145  106 GLU   A OE2 
796  N N   . PRO   A 101 ? 0.2728 0.2806 0.2596 0.0094  0.0265  0.0211  107 PRO   A N   
797  C CA  . PRO   A 101 ? 0.2966 0.3032 0.2866 0.0079  0.0233  0.0221  107 PRO   A CA  
798  C C   . PRO   A 101 ? 0.2890 0.2922 0.2699 0.0090  0.0183  0.0210  107 PRO   A C   
799  O O   . PRO   A 101 ? 0.3097 0.3100 0.2796 0.0115  0.0178  0.0216  107 PRO   A O   
800  C CB  . PRO   A 101 ? 0.3205 0.3265 0.3119 0.0085  0.0268  0.0272  107 PRO   A CB  
801  C CG  . PRO   A 101 ? 0.3080 0.3167 0.3031 0.0087  0.0322  0.0281  107 PRO   A CG  
802  C CD  . PRO   A 101 ? 0.2742 0.2828 0.2615 0.0106  0.0319  0.0252  107 PRO   A CD  
803  N N   . GLY   A 102 ? 0.2535 0.2570 0.2395 0.0072  0.0146  0.0190  108 GLY   A N   
804  C CA  . GLY   A 102 ? 0.2411 0.2424 0.2225 0.0073  0.0094  0.0172  108 GLY   A CA  
805  C C   . GLY   A 102 ? 0.2200 0.2217 0.2032 0.0060  0.0080  0.0130  108 GLY   A C   
806  O O   . GLY   A 102 ? 0.2241 0.2247 0.2081 0.0051  0.0042  0.0115  108 GLY   A O   
807  N N   . ASP   A 103 ? 0.1910 0.1943 0.1757 0.0061  0.0113  0.0114  109 ASP   A N   
808  C CA  . ASP   A 103 ? 0.1747 0.1778 0.1599 0.0055  0.0101  0.0079  109 ASP   A CA  
809  C C   . ASP   A 103 ? 0.1748 0.1798 0.1686 0.0034  0.0101  0.0068  109 ASP   A C   
810  O O   . ASP   A 103 ? 0.1842 0.1885 0.1781 0.0029  0.0090  0.0044  109 ASP   A O   
811  C CB  . ASP   A 103 ? 0.1954 0.1993 0.1779 0.0070  0.0131  0.0067  109 ASP   A CB  
812  C CG  . ASP   A 103 ? 0.2206 0.2211 0.1927 0.0095  0.0129  0.0063  109 ASP   A CG  
813  O OD1 . ASP   A 103 ? 0.2281 0.2250 0.1947 0.0096  0.0092  0.0053  109 ASP   A OD1 
814  O OD2 . ASP   A 103 ? 0.2031 0.2046 0.1728 0.0115  0.0167  0.0069  109 ASP   A OD2 
815  N N   . CYS   A 104 ? 0.1704 0.1773 0.1710 0.0023  0.0113  0.0084  110 CYS   A N   
816  C CA  . CYS   A 104 ? 0.1625 0.1705 0.1701 0.0006  0.0115  0.0070  110 CYS   A CA  
817  C C   . CYS   A 104 ? 0.1732 0.1796 0.1812 -0.0001 0.0089  0.0062  110 CYS   A C   
818  O O   . CYS   A 104 ? 0.1981 0.2034 0.2047 0.0001  0.0064  0.0076  110 CYS   A O   
819  C CB  . CYS   A 104 ? 0.1784 0.1876 0.1929 -0.0003 0.0133  0.0087  110 CYS   A CB  
820  S SG  . CYS   A 104 ? 0.1984 0.2099 0.2160 -0.0004 0.0168  0.0092  110 CYS   A SG  
821  N N   . GLY   A 105 ? 0.1600 0.1665 0.1700 -0.0008 0.0093  0.0041  111 GLY   A N   
822  C CA  . GLY   A 105 ? 0.1707 0.1759 0.1825 -0.0016 0.0076  0.0037  111 GLY   A CA  
823  C C   . GLY   A 105 ? 0.1777 0.1806 0.1843 -0.0012 0.0063  0.0022  111 GLY   A C   
824  O O   . GLY   A 105 ? 0.1812 0.1830 0.1899 -0.0020 0.0059  0.0016  111 GLY   A O   
825  N N   . GLY   A 106 ? 0.1701 0.1722 0.1704 0.0002  0.0063  0.0015  112 GLY   A N   
826  C CA  . GLY   A 106 ? 0.1700 0.1693 0.1653 0.0008  0.0055  -0.0002 112 GLY   A CA  
827  C C   . GLY   A 106 ? 0.1679 0.1673 0.1648 0.0007  0.0073  -0.0012 112 GLY   A C   
828  O O   . GLY   A 106 ? 0.1820 0.1839 0.1808 0.0010  0.0091  -0.0014 112 GLY   A O   
829  N N   . ILE   A 107 ? 0.1639 0.1603 0.1601 0.0003  0.0065  -0.0017 113 ILE   A N   
830  C CA  . ILE   A 107 ? 0.1634 0.1593 0.1602 0.0006  0.0084  -0.0021 113 ILE   A CA  
831  C C   . ILE   A 107 ? 0.1643 0.1592 0.1558 0.0027  0.0090  -0.0030 113 ILE   A C   
832  O O   . ILE   A 107 ? 0.1787 0.1711 0.1661 0.0037  0.0080  -0.0037 113 ILE   A O   
833  C CB  . ILE   A 107 ? 0.1791 0.1721 0.1787 -0.0009 0.0082  -0.0016 113 ILE   A CB  
834  C CG1 . ILE   A 107 ? 0.1971 0.1926 0.2040 -0.0025 0.0089  -0.0004 113 ILE   A CG1 
835  C CG2 . ILE   A 107 ? 0.1983 0.1889 0.1957 0.0000  0.0103  -0.0015 113 ILE   A CG2 
836  C CD1 . ILE   A 107 ? 0.2137 0.2074 0.2261 -0.0043 0.0087  0.0006  113 ILE   A CD1 
837  N N   . LEU   A 108 ? 0.1595 0.1561 0.1509 0.0035  0.0105  -0.0033 114 LEU   A N   
838  C CA  . LEU   A 108 ? 0.1596 0.1557 0.1471 0.0058  0.0108  -0.0038 114 LEU   A CA  
839  C C   . LEU   A 108 ? 0.1722 0.1648 0.1580 0.0060  0.0117  -0.0032 114 LEU   A C   
840  O O   . LEU   A 108 ? 0.1760 0.1690 0.1636 0.0051  0.0130  -0.0028 114 LEU   A O   
841  C CB  . LEU   A 108 ? 0.1759 0.1766 0.1648 0.0065  0.0110  -0.0046 114 LEU   A CB  
842  C CG  . LEU   A 108 ? 0.1864 0.1878 0.1723 0.0091  0.0106  -0.0051 114 LEU   A CG  
843  C CD1 . LEU   A 108 ? 0.1897 0.1906 0.1736 0.0111  0.0103  -0.0050 114 LEU   A CD1 
844  C CD2 . LEU   A 108 ? 0.2011 0.2072 0.1898 0.0091  0.0100  -0.0062 114 LEU   A CD2 
845  N N   . ARG   A 109 ? 0.1784 0.1672 0.1606 0.0074  0.0115  -0.0029 115 ARG   A N   
846  C CA  . ARG   A 109 ? 0.1782 0.1629 0.1585 0.0078  0.0129  -0.0016 115 ARG   A CA  
847  C C   . ARG   A 109 ? 0.1976 0.1810 0.1730 0.0110  0.0128  -0.0014 115 ARG   A C   
848  O O   . ARG   A 109 ? 0.2002 0.1839 0.1742 0.0127  0.0117  -0.0022 115 ARG   A O   
849  C CB  . ARG   A 109 ? 0.2199 0.1997 0.2019 0.0062  0.0127  -0.0011 115 ARG   A CB  
850  C CG  . ARG   A 109 ? 0.2643 0.2450 0.2524 0.0031  0.0129  -0.0005 115 ARG   A CG  
851  C CD  . ARG   A 109 ? 0.3038 0.2799 0.2949 0.0011  0.0120  -0.0002 115 ARG   A CD  
852  N NE  . ARG   A 109 ? 0.3001 0.2774 0.2989 -0.0016 0.0127  0.0009  115 ARG   A NE  
853  C CZ  . ARG   A 109 ? 0.3006 0.2762 0.3027 -0.0024 0.0158  0.0030  115 ARG   A CZ  
854  N NH1 . ARG   A 109 ? 0.2521 0.2244 0.2495 -0.0005 0.0184  0.0043  115 ARG   A NH1 
855  N NH2 . ARG   A 109 ? 0.3107 0.2883 0.3211 -0.0046 0.0167  0.0041  115 ARG   A NH2 
856  N N   . CYS   A 110 ? 0.2081 0.1895 0.1806 0.0122  0.0142  0.0001  116 CYS   A N   
857  C CA  . CYS   A 110 ? 0.2144 0.1934 0.1819 0.0155  0.0140  0.0011  116 CYS   A CA  
858  C C   . CYS   A 110 ? 0.2201 0.1921 0.1862 0.0152  0.0162  0.0034  116 CYS   A C   
859  O O   . CYS   A 110 ? 0.2343 0.2045 0.2045 0.0123  0.0174  0.0038  116 CYS   A O   
860  C CB  . CYS   A 110 ? 0.2213 0.2034 0.1854 0.0175  0.0134  0.0010  116 CYS   A CB  
861  S SG  . CYS   A 110 ? 0.2125 0.1924 0.1739 0.0166  0.0162  0.0024  116 CYS   A SG  
862  N N   . GLN   A 111 ? 0.2328 0.2011 0.1941 0.0182  0.0168  0.0053  117 GLN   A N   
863  C CA  . GLN   A 111 ? 0.2491 0.2102 0.2094 0.0180  0.0194  0.0081  117 GLN   A CA  
864  C C   . GLN   A 111 ? 0.2487 0.2089 0.2094 0.0164  0.0227  0.0101  117 GLN   A C   
865  O O   . GLN   A 111 ? 0.2565 0.2113 0.2187 0.0153  0.0256  0.0127  117 GLN   A O   
866  C CB  . GLN   A 111 ? 0.2930 0.2501 0.2473 0.0222  0.0195  0.0103  117 GLN   A CB  
867  C CG  . GLN   A 111 ? 0.3744 0.3345 0.3227 0.0251  0.0192  0.0113  117 GLN   A CG  
868  C CD  . GLN   A 111 ? 0.4940 0.4513 0.4367 0.0298  0.0182  0.0135  117 GLN   A CD  
869  O OE1 . GLN   A 111 ? 0.5416 0.5035 0.4836 0.0324  0.0150  0.0121  117 GLN   A OE1 
870  N NE2 . GLN   A 111 ? 0.4758 0.4257 0.4154 0.0309  0.0210  0.0171  117 GLN   A NE2 
871  N N   . HIS   A 112 ? 0.2349 0.2001 0.1945 0.0163  0.0227  0.0090  118 HIS   A N   
872  C CA  . HIS   A 112 ? 0.2374 0.2018 0.1962 0.0156  0.0263  0.0106  118 HIS   A CA  
873  C C   . HIS   A 112 ? 0.2205 0.1876 0.1874 0.0118  0.0273  0.0095  118 HIS   A C   
874  O O   . HIS   A 112 ? 0.2333 0.1992 0.2013 0.0111  0.0312  0.0112  118 HIS   A O   
875  C CB  . HIS   A 112 ? 0.2580 0.2249 0.2093 0.0183  0.0257  0.0099  118 HIS   A CB  
876  C CG  . HIS   A 112 ? 0.2673 0.2322 0.2106 0.0224  0.0240  0.0111  118 HIS   A CG  
877  N ND1 . HIS   A 112 ? 0.2747 0.2443 0.2168 0.0242  0.0195  0.0087  118 HIS   A ND1 
878  C CD2 . HIS   A 112 ? 0.2892 0.2483 0.2261 0.0251  0.0262  0.0148  118 HIS   A CD2 
879  C CE1 . HIS   A 112 ? 0.2882 0.2550 0.2235 0.0281  0.0187  0.0109  118 HIS   A CE1 
880  N NE2 . HIS   A 112 ? 0.2975 0.2576 0.2290 0.0288  0.0226  0.0147  118 HIS   A NE2 
881  N N   . GLY   A 113 ? 0.2010 0.1716 0.1731 0.0100  0.0242  0.0070  119 GLY   A N   
882  C CA  . GLY   A 113 ? 0.1894 0.1627 0.1692 0.0068  0.0245  0.0062  119 GLY   A CA  
883  C C   . GLY   A 113 ? 0.1816 0.1604 0.1631 0.0063  0.0214  0.0034  119 GLY   A C   
884  O O   . GLY   A 113 ? 0.2026 0.1829 0.1811 0.0078  0.0188  0.0020  119 GLY   A O   
885  N N   . VAL   A 114 ? 0.1785 0.1601 0.1656 0.0043  0.0220  0.0029  120 VAL   A N   
886  C CA  . VAL   A 114 ? 0.1743 0.1605 0.1638 0.0036  0.0197  0.0009  120 VAL   A CA  
887  C C   . VAL   A 114 ? 0.1763 0.1649 0.1615 0.0054  0.0196  -0.0007 120 VAL   A C   
888  O O   . VAL   A 114 ? 0.1911 0.1788 0.1738 0.0062  0.0219  -0.0005 120 VAL   A O   
889  C CB  . VAL   A 114 ? 0.1902 0.1784 0.1875 0.0013  0.0204  0.0012  120 VAL   A CB  
890  C CG1 . VAL   A 114 ? 0.1919 0.1842 0.1911 0.0009  0.0185  -0.0004 120 VAL   A CG1 
891  C CG2 . VAL   A 114 ? 0.1953 0.1819 0.1977 -0.0007 0.0190  0.0022  120 VAL   A CG2 
892  N N   . VAL   A 115 ? 0.1832 0.1748 0.1677 0.0060  0.0169  -0.0022 121 VAL   A N   
893  C CA  . VAL   A 115 ? 0.1826 0.1769 0.1647 0.0072  0.0158  -0.0041 121 VAL   A CA  
894  C C   . VAL   A 115 ? 0.1921 0.1898 0.1796 0.0054  0.0156  -0.0055 121 VAL   A C   
895  O O   . VAL   A 115 ? 0.1857 0.1844 0.1727 0.0056  0.0158  -0.0071 121 VAL   A O   
896  C CB  . VAL   A 115 ? 0.1970 0.1931 0.1770 0.0090  0.0133  -0.0046 121 VAL   A CB  
897  C CG1 . VAL   A 115 ? 0.2090 0.2093 0.1893 0.0097  0.0115  -0.0067 121 VAL   A CG1 
898  C CG2 . VAL   A 115 ? 0.2023 0.1945 0.1766 0.0113  0.0136  -0.0031 121 VAL   A CG2 
899  N N   . GLY   A 116 ? 0.1778 0.1769 0.1700 0.0040  0.0148  -0.0049 122 GLY   A N   
900  C CA  . GLY   A 116 ? 0.1790 0.1809 0.1764 0.0025  0.0147  -0.0056 122 GLY   A CA  
901  C C   . GLY   A 116 ? 0.1741 0.1768 0.1747 0.0015  0.0138  -0.0043 122 GLY   A C   
902  O O   . GLY   A 116 ? 0.1772 0.1779 0.1762 0.0016  0.0131  -0.0034 122 GLY   A O   
903  N N   . ILE   A 117 ? 0.1646 0.1696 0.1694 0.0005  0.0137  -0.0043 123 ILE   A N   
904  C CA  . ILE   A 117 ? 0.1614 0.1669 0.1679 0.0000  0.0127  -0.0028 123 ILE   A CA  
905  C C   . ILE   A 117 ? 0.1671 0.1752 0.1745 0.0002  0.0127  -0.0028 123 ILE   A C   
906  O O   . ILE   A 117 ? 0.1576 0.1675 0.1677 -0.0001 0.0134  -0.0038 123 ILE   A O   
907  C CB  . ILE   A 117 ? 0.1909 0.1961 0.2025 -0.0013 0.0130  -0.0015 123 ILE   A CB  
908  C CG1 . ILE   A 117 ? 0.2091 0.2152 0.2249 -0.0018 0.0148  -0.0023 123 ILE   A CG1 
909  C CG2 . ILE   A 117 ? 0.2127 0.2158 0.2249 -0.0018 0.0128  -0.0008 123 ILE   A CG2 
910  C CD1 . ILE   A 117 ? 0.2307 0.2368 0.2527 -0.0027 0.0152  -0.0005 123 ILE   A CD1 
911  N N   . VAL   A 118 ? 0.1548 0.1628 0.1601 0.0008  0.0120  -0.0015 124 VAL   A N   
912  C CA  . VAL   A 118 ? 0.1546 0.1651 0.1612 0.0011  0.0130  -0.0007 124 VAL   A CA  
913  C C   . VAL   A 118 ? 0.1554 0.1670 0.1681 -0.0003 0.0140  0.0003  124 VAL   A C   
914  O O   . VAL   A 118 ? 0.1588 0.1691 0.1732 -0.0010 0.0136  0.0014  124 VAL   A O   
915  C CB  . VAL   A 118 ? 0.1548 0.1640 0.1568 0.0023  0.0126  0.0007  124 VAL   A CB  
916  C CG1 . VAL   A 118 ? 0.1641 0.1758 0.1677 0.0028  0.0147  0.0023  124 VAL   A CG1 
917  C CG2 . VAL   A 118 ? 0.1754 0.1826 0.1714 0.0039  0.0118  -0.0005 124 VAL   A CG2 
918  N N   . SER   A 119 ? 0.1420 0.1563 0.1589 -0.0007 0.0152  -0.0003 125 SER   A N   
919  C CA  . SER   A 119 ? 0.1445 0.1591 0.1677 -0.0022 0.0164  0.0004  125 SER   A CA  
920  C C   . SER   A 119 ? 0.1630 0.1798 0.1900 -0.0025 0.0182  0.0020  125 SER   A C   
921  O O   . SER   A 119 ? 0.1646 0.1809 0.1961 -0.0034 0.0195  0.0039  125 SER   A O   
922  C CB  . SER   A 119 ? 0.1571 0.1716 0.1830 -0.0031 0.0161  -0.0027 125 SER   A CB  
923  O OG  . SER   A 119 ? 0.1714 0.1855 0.2036 -0.0046 0.0172  -0.0028 125 SER   A OG  
924  N N   . THR   A 120 ? 0.1443 0.1639 0.1707 -0.0016 0.0186  0.0016  126 THR   A N   
925  C CA  . THR   A 120 ? 0.1635 0.1857 0.1949 -0.0019 0.0211  0.0035  126 THR   A CA  
926  C C   . THR   A 120 ? 0.1687 0.1925 0.1954 0.0004  0.0222  0.0045  126 THR   A C   
927  O O   . THR   A 120 ? 0.1685 0.1910 0.1888 0.0019  0.0206  0.0031  126 THR   A O   
928  C CB  . THR   A 120 ? 0.1788 0.2044 0.2188 -0.0036 0.0208  0.0011  126 THR   A CB  
929  O OG1 . THR   A 120 ? 0.1947 0.2228 0.2331 -0.0025 0.0191  -0.0014 126 THR   A OG1 
930  C CG2 . THR   A 120 ? 0.1836 0.2069 0.2269 -0.0055 0.0196  -0.0012 126 THR   A CG2 
931  N N   . GLY   A 121 ? 0.1734 0.1993 0.2033 0.0008  0.0254  0.0070  127 GLY   A N   
932  C CA  . GLY   A 121 ? 0.1938 0.2213 0.2201 0.0032  0.0273  0.0078  127 GLY   A CA  
933  C C   . GLY   A 121 ? 0.2101 0.2405 0.2421 0.0033  0.0318  0.0109  127 GLY   A C   
934  O O   . GLY   A 121 ? 0.2163 0.2470 0.2550 0.0013  0.0333  0.0127  127 GLY   A O   
935  N N   . GLY   A 122 ? 0.2140 0.2458 0.2429 0.0059  0.0343  0.0118  128 GLY   A N   
936  C CA  . GLY   A 122 ? 0.2514 0.2858 0.2848 0.0067  0.0397  0.0153  128 GLY   A CA  
937  C C   . GLY   A 122 ? 0.2745 0.3134 0.3107 0.0090  0.0421  0.0149  128 GLY   A C   
938  O O   . GLY   A 122 ? 0.2875 0.3300 0.3294 0.0086  0.0394  0.0120  128 GLY   A O   
939  N N   . ASN   A 123 ? 0.2721 0.3107 0.3046 0.0116  0.0474  0.0181  129 ASN   A N   
940  C CA  . ASN   A 123 ? 0.2589 0.3018 0.2947 0.0144  0.0514  0.0186  129 ASN   A CA  
941  C C   . ASN   A 123 ? 0.2432 0.2872 0.2773 0.0163  0.0480  0.0148  129 ASN   A C   
942  O O   . ASN   A 123 ? 0.2403 0.2908 0.2850 0.0167  0.0485  0.0141  129 ASN   A O   
943  C CB  . ASN   A 123 ? 0.3084 0.3584 0.3612 0.0122  0.0547  0.0206  129 ASN   A CB  
944  C CG  . ASN   A 123 ? 0.4132 0.4615 0.4677 0.0108  0.0592  0.0252  129 ASN   A CG  
945  O OD1 . ASN   A 123 ? 0.4577 0.5023 0.5023 0.0135  0.0637  0.0284  129 ASN   A OD1 
946  N ND2 . ASN   A 123 ? 0.4340 0.4841 0.4997 0.0067  0.0579  0.0254  129 ASN   A ND2 
947  N N   . GLY   A 124 ? 0.2258 0.2637 0.2474 0.0176  0.0446  0.0126  130 GLY   A N   
948  C CA  . GLY   A 124 ? 0.2111 0.2487 0.2298 0.0196  0.0417  0.0095  130 GLY   A CA  
949  C C   . GLY   A 124 ? 0.2000 0.2391 0.2235 0.0171  0.0359  0.0066  130 GLY   A C   
950  O O   . GLY   A 124 ? 0.2161 0.2555 0.2386 0.0188  0.0336  0.0045  130 GLY   A O   
951  N N   . LEU   A 125 ? 0.1729 0.2123 0.2008 0.0135  0.0339  0.0066  131 LEU   A N   
952  C CA  . LEU   A 125 ? 0.1680 0.2074 0.1979 0.0113  0.0287  0.0038  131 LEU   A CA  
953  C C   . LEU   A 125 ? 0.1717 0.2048 0.1934 0.0099  0.0265  0.0034  131 LEU   A C   
954  O O   . LEU   A 125 ? 0.1845 0.2146 0.2023 0.0096  0.0283  0.0054  131 LEU   A O   
955  C CB  . LEU   A 125 ? 0.1816 0.2260 0.2238 0.0082  0.0279  0.0034  131 LEU   A CB  
956  C CG  . LEU   A 125 ? 0.2106 0.2625 0.2642 0.0088  0.0288  0.0035  131 LEU   A CG  
957  C CD1 . LEU   A 125 ? 0.2236 0.2797 0.2900 0.0051  0.0286  0.0034  131 LEU   A CD1 
958  C CD2 . LEU   A 125 ? 0.2161 0.2699 0.2689 0.0106  0.0246  0.0007  131 LEU   A CD2 
959  N N   . VAL   A 126 ? 0.1416 0.1730 0.1612 0.0092  0.0226  0.0009  132 VAL   A N   
960  C CA  . VAL   A 126 ? 0.1411 0.1676 0.1557 0.0076  0.0205  0.0004  132 VAL   A CA  
961  C C   . VAL   A 126 ? 0.1620 0.1895 0.1802 0.0059  0.0177  -0.0019 132 VAL   A C   
962  O O   . VAL   A 126 ? 0.1840 0.2138 0.2035 0.0070  0.0161  -0.0035 132 VAL   A O   
963  C CB  . VAL   A 126 ? 0.1566 0.1778 0.1613 0.0093  0.0195  0.0001  132 VAL   A CB  
964  C CG1 . VAL   A 126 ? 0.1800 0.2009 0.1822 0.0115  0.0183  -0.0016 132 VAL   A CG1 
965  C CG2 . VAL   A 126 ? 0.1572 0.1745 0.1592 0.0074  0.0174  -0.0002 132 VAL   A CG2 
966  N N   . GLY   A 127 ? 0.1471 0.1732 0.1674 0.0035  0.0172  -0.0019 133 GLY   A N   
967  C CA  . GLY   A 127 ? 0.1515 0.1777 0.1743 0.0021  0.0149  -0.0044 133 GLY   A CA  
968  C C   . GLY   A 127 ? 0.1589 0.1804 0.1764 0.0017  0.0140  -0.0047 133 GLY   A C   
969  O O   . GLY   A 127 ? 0.1673 0.1864 0.1831 0.0013  0.0149  -0.0030 133 GLY   A O   
970  N N   . PHE   A 128 ? 0.1566 0.1769 0.1712 0.0021  0.0123  -0.0068 134 PHE   A N   
971  C CA  . PHE   A 128 ? 0.1549 0.1711 0.1653 0.0019  0.0121  -0.0069 134 PHE   A CA  
972  C C   . PHE   A 128 ? 0.1611 0.1766 0.1731 0.0007  0.0118  -0.0089 134 PHE   A C   
973  O O   . PHE   A 128 ? 0.1548 0.1718 0.1667 0.0011  0.0104  -0.0111 134 PHE   A O   
974  C CB  . PHE   A 128 ? 0.1534 0.1674 0.1574 0.0038  0.0113  -0.0070 134 PHE   A CB  
975  C CG  . PHE   A 128 ? 0.1554 0.1694 0.1569 0.0054  0.0115  -0.0059 134 PHE   A CG  
976  C CD1 . PHE   A 128 ? 0.1603 0.1713 0.1590 0.0053  0.0119  -0.0046 134 PHE   A CD1 
977  C CD2 . PHE   A 128 ? 0.1603 0.1773 0.1624 0.0072  0.0111  -0.0063 134 PHE   A CD2 
978  C CE1 . PHE   A 128 ? 0.1682 0.1782 0.1635 0.0070  0.0121  -0.0041 134 PHE   A CE1 
979  C CE2 . PHE   A 128 ? 0.1651 0.1815 0.1645 0.0092  0.0119  -0.0054 134 PHE   A CE2 
980  C CZ  . PHE   A 128 ? 0.1667 0.1791 0.1621 0.0090  0.0125  -0.0044 134 PHE   A CZ  
981  N N   . ALA   A 129 ? 0.1497 0.1626 0.1625 -0.0003 0.0130  -0.0083 135 ALA   A N   
982  C CA  . ALA   A 129 ? 0.1560 0.1672 0.1694 -0.0009 0.0135  -0.0103 135 ALA   A CA  
983  C C   . ALA   A 129 ? 0.1565 0.1652 0.1632 0.0006  0.0136  -0.0108 135 ALA   A C   
984  O O   . ALA   A 129 ? 0.1705 0.1772 0.1755 0.0008  0.0145  -0.0088 135 ALA   A O   
985  C CB  . ALA   A 129 ? 0.1526 0.1621 0.1701 -0.0021 0.0152  -0.0089 135 ALA   A CB  
986  N N   . ASP   A 130 ? 0.1512 0.1595 0.1541 0.0015  0.0125  -0.0132 136 ASP   A N   
987  C CA  . ASP   A 130 ? 0.1690 0.1744 0.1646 0.0033  0.0130  -0.0132 136 ASP   A CA  
988  C C   . ASP   A 130 ? 0.1839 0.1858 0.1788 0.0030  0.0160  -0.0129 136 ASP   A C   
989  O O   . ASP   A 130 ? 0.1922 0.1937 0.1905 0.0020  0.0170  -0.0144 136 ASP   A O   
990  C CB  . ASP   A 130 ? 0.1978 0.2038 0.1886 0.0047  0.0106  -0.0159 136 ASP   A CB  
991  C CG  . ASP   A 130 ? 0.2806 0.2833 0.2624 0.0071  0.0110  -0.0153 136 ASP   A CG  
992  O OD1 . ASP   A 130 ? 0.2971 0.2988 0.2769 0.0080  0.0117  -0.0128 136 ASP   A OD1 
993  O OD2 . ASP   A 130 ? 0.3305 0.3310 0.3068 0.0081  0.0110  -0.0175 136 ASP   A OD2 
994  N N   . VAL   A 131 ? 0.1659 0.1651 0.1569 0.0040  0.0179  -0.0109 137 VAL   A N   
995  C CA  . VAL   A 131 ? 0.1788 0.1750 0.1698 0.0041  0.0216  -0.0103 137 VAL   A CA  
996  C C   . VAL   A 131 ? 0.2001 0.1929 0.1823 0.0063  0.0233  -0.0102 137 VAL   A C   
997  O O   . VAL   A 131 ? 0.2115 0.2016 0.1929 0.0068  0.0273  -0.0093 137 VAL   A O   
998  C CB  . VAL   A 131 ? 0.2011 0.1974 0.1985 0.0027  0.0233  -0.0074 137 VAL   A CB  
999  C CG1 . VAL   A 131 ? 0.2008 0.1999 0.2055 0.0010  0.0217  -0.0072 137 VAL   A CG1 
1000 C CG2 . VAL   A 131 ? 0.1965 0.1918 0.1918 0.0030  0.0227  -0.0052 137 VAL   A CG2 
1001 N N   . ARG   A 132 ? 0.2069 0.1998 0.1827 0.0079  0.0208  -0.0106 138 ARG   A N   
1002 C CA  . ARG   A 132 ? 0.1932 0.1824 0.1597 0.0104  0.0223  -0.0096 138 ARG   A CA  
1003 C C   . ARG   A 132 ? 0.2220 0.2085 0.1815 0.0120  0.0239  -0.0119 138 ARG   A C   
1004 O O   . ARG   A 132 ? 0.2360 0.2185 0.1879 0.0141  0.0270  -0.0104 138 ARG   A O   
1005 C CB  . ARG   A 132 ? 0.2009 0.1910 0.1627 0.0122  0.0187  -0.0092 138 ARG   A CB  
1006 C CG  . ARG   A 132 ? 0.1982 0.1894 0.1648 0.0114  0.0179  -0.0069 138 ARG   A CG  
1007 C CD  . ARG   A 132 ? 0.2077 0.2000 0.1702 0.0136  0.0146  -0.0068 138 ARG   A CD  
1008 N NE  . ARG   A 132 ? 0.2077 0.2049 0.1738 0.0132  0.0110  -0.0095 138 ARG   A NE  
1009 C CZ  . ARG   A 132 ? 0.2196 0.2197 0.1853 0.0148  0.0077  -0.0099 138 ARG   A CZ  
1010 N NH1 . ARG   A 132 ? 0.2109 0.2089 0.1720 0.0174  0.0074  -0.0077 138 ARG   A NH1 
1011 N NH2 . ARG   A 132 ? 0.2183 0.2235 0.1897 0.0139  0.0049  -0.0121 138 ARG   A NH2 
1012 N N   . ASP   A 133 ? 0.2187 0.2066 0.1805 0.0110  0.0222  -0.0156 139 ASP   A N   
1013 C CA  . ASP   A 133 ? 0.2338 0.2182 0.1882 0.0126  0.0237  -0.0187 139 ASP   A CA  
1014 C C   . ASP   A 133 ? 0.2400 0.2217 0.1975 0.0122  0.0294  -0.0181 139 ASP   A C   
1015 O O   . ASP   A 133 ? 0.2398 0.2176 0.1902 0.0140  0.0319  -0.0203 139 ASP   A O   
1016 C CB  . ASP   A 133 ? 0.2580 0.2444 0.2137 0.0117  0.0191  -0.0235 139 ASP   A CB  
1017 C CG  . ASP   A 133 ? 0.2998 0.2889 0.2675 0.0086  0.0191  -0.0241 139 ASP   A CG  
1018 O OD1 . ASP   A 133 ? 0.3056 0.2977 0.2808 0.0071  0.0192  -0.0209 139 ASP   A OD1 
1019 O OD2 . ASP   A 133 ? 0.3462 0.3339 0.3154 0.0078  0.0190  -0.0277 139 ASP   A OD2 
1020 N N   . LEU   A 134 ? 0.2309 0.2146 0.1987 0.0102  0.0315  -0.0152 140 LEU   A N   
1021 C CA  . LEU   A 134 ? 0.2153 0.1975 0.1883 0.0099  0.0367  -0.0142 140 LEU   A CA  
1022 C C   . LEU   A 134 ? 0.2191 0.1984 0.1884 0.0115  0.0419  -0.0107 140 LEU   A C   
1023 O O   . LEU   A 134 ? 0.2146 0.1953 0.1912 0.0102  0.0435  -0.0070 140 LEU   A O   
1024 C CB  . LEU   A 134 ? 0.2126 0.1986 0.1985 0.0072  0.0358  -0.0126 140 LEU   A CB  
1025 C CG  . LEU   A 134 ? 0.2493 0.2380 0.2394 0.0056  0.0313  -0.0151 140 LEU   A CG  
1026 C CD1 . LEU   A 134 ? 0.2521 0.2442 0.2533 0.0034  0.0305  -0.0126 140 LEU   A CD1 
1027 C CD2 . LEU   A 134 ? 0.2564 0.2425 0.2443 0.0062  0.0320  -0.0194 140 LEU   A CD2 
1028 N N   . LEU   A 135 ? 0.2326 0.2076 0.1902 0.0144  0.0444  -0.0118 141 LEU   A N   
1029 C CA  . LEU   A 135 ? 0.2424 0.2140 0.1950 0.0163  0.0497  -0.0080 141 LEU   A CA  
1030 C C   . LEU   A 135 ? 0.2496 0.2211 0.2111 0.0157  0.0564  -0.0052 141 LEU   A C   
1031 O O   . LEU   A 135 ? 0.2679 0.2387 0.2320 0.0157  0.0601  -0.0009 141 LEU   A O   
1032 C CB  . LEU   A 135 ? 0.2531 0.2196 0.1894 0.0199  0.0510  -0.0098 141 LEU   A CB  
1033 C CG  . LEU   A 135 ? 0.2685 0.2356 0.1961 0.0208  0.0439  -0.0129 141 LEU   A CG  
1034 C CD1 . LEU   A 135 ? 0.2894 0.2508 0.1993 0.0250  0.0453  -0.0139 141 LEU   A CD1 
1035 C CD2 . LEU   A 135 ? 0.2802 0.2506 0.2116 0.0196  0.0395  -0.0102 141 LEU   A CD2 
1036 N N   . TRP   A 136 ? 0.2467 0.2190 0.2144 0.0152  0.0577  -0.0076 142 TRP   A N   
1037 C CA  . TRP   A 136 ? 0.2534 0.2264 0.2313 0.0149  0.0638  -0.0051 142 TRP   A CA  
1038 C C   . TRP   A 136 ? 0.2549 0.2327 0.2474 0.0119  0.0624  -0.0013 142 TRP   A C   
1039 O O   . TRP   A 136 ? 0.2667 0.2457 0.2691 0.0115  0.0673  0.0016  142 TRP   A O   
1040 C CB  . TRP   A 136 ? 0.2535 0.2258 0.2343 0.0155  0.0652  -0.0088 142 TRP   A CB  
1041 C CG  . TRP   A 136 ? 0.2547 0.2299 0.2404 0.0133  0.0585  -0.0118 142 TRP   A CG  
1042 C CD1 . TRP   A 136 ? 0.2608 0.2347 0.2388 0.0134  0.0537  -0.0162 142 TRP   A CD1 
1043 C CD2 . TRP   A 136 ? 0.2513 0.2311 0.2508 0.0106  0.0560  -0.0102 142 TRP   A CD2 
1044 N NE1 . TRP   A 136 ? 0.2589 0.2362 0.2458 0.0109  0.0492  -0.0172 142 TRP   A NE1 
1045 C CE2 . TRP   A 136 ? 0.2526 0.2333 0.2520 0.0094  0.0507  -0.0135 142 TRP   A CE2 
1046 C CE3 . TRP   A 136 ? 0.2536 0.2369 0.2660 0.0093  0.0577  -0.0062 142 TRP   A CE3 
1047 C CZ2 . TRP   A 136 ? 0.2481 0.2326 0.2583 0.0072  0.0475  -0.0125 142 TRP   A CZ2 
1048 C CZ3 . TRP   A 136 ? 0.2508 0.2379 0.2736 0.0073  0.0538  -0.0057 142 TRP   A CZ3 
1049 C CH2 . TRP   A 136 ? 0.2470 0.2343 0.2680 0.0064  0.0492  -0.0086 142 TRP   A CH2 
1050 N N   . LEU   A 137 ? 0.2454 0.2260 0.2398 0.0097  0.0558  -0.0014 143 LEU   A N   
1051 C CA  . LEU   A 137 ? 0.2597 0.2442 0.2664 0.0070  0.0539  0.0016  143 LEU   A CA  
1052 C C   . LEU   A 137 ? 0.3122 0.2954 0.3212 0.0068  0.0579  0.0058  143 LEU   A C   
1053 O O   . LEU   A 137 ? 0.3058 0.2919 0.3270 0.0047  0.0581  0.0083  143 LEU   A O   
1054 C CB  . LEU   A 137 ? 0.2401 0.2267 0.2459 0.0053  0.0468  0.0006  143 LEU   A CB  
1055 C CG  . LEU   A 137 ? 0.2432 0.2322 0.2514 0.0045  0.0427  -0.0022 143 LEU   A CG  
1056 C CD1 . LEU   A 137 ? 0.2629 0.2537 0.2688 0.0034  0.0369  -0.0028 143 LEU   A CD1 
1057 C CD2 . LEU   A 137 ? 0.2414 0.2334 0.2622 0.0031  0.0431  -0.0009 143 LEU   A CD2 
1058 N N   . ASP   A 138 ? 0.3625 0.3413 0.3599 0.0090  0.0607  0.0065  144 ASP   A N   
1059 C CA  . ASP   A 138 ? 0.4258 0.4019 0.4223 0.0094  0.0650  0.0106  144 ASP   A CA  
1060 C C   . ASP   A 138 ? 0.4786 0.4534 0.4792 0.0105  0.0735  0.0134  144 ASP   A C   
1061 O O   . ASP   A 138 ? 0.4934 0.4661 0.4953 0.0105  0.0777  0.0174  144 ASP   A O   
1062 C CB  . ASP   A 138 ? 0.4724 0.4437 0.4525 0.0123  0.0650  0.0103  144 ASP   A CB  
1063 C CG  . ASP   A 138 ? 0.5635 0.5352 0.5393 0.0117  0.0582  0.0093  144 ASP   A CG  
1064 O OD1 . ASP   A 138 ? 0.5731 0.5478 0.5582 0.0089  0.0542  0.0097  144 ASP   A OD1 
1065 O OD2 . ASP   A 138 ? 0.6279 0.5968 0.5906 0.0143  0.0567  0.0083  144 ASP   A OD2 
1066 N N   . GLU   A 139 ? 0.5065 0.4815 0.5073 0.0121  0.0768  0.0113  145 GLU   A N   
1067 C CA  . GLU   A 139 ? 0.5519 0.5256 0.5565 0.0138  0.0858  0.0139  145 GLU   A CA  
1068 C C   . GLU   A 139 ? 0.5693 0.5476 0.5890 0.0126  0.0868  0.0134  145 GLU   A C   
1069 O O   . GLU   A 139 ? 0.5806 0.5637 0.6122 0.0096  0.0814  0.0137  145 GLU   A O   
1070 C CB  . GLU   A 139 ? 0.6027 0.5703 0.5901 0.0181  0.0910  0.0123  145 GLU   A CB  
1071 C CG  . GLU   A 139 ? 0.6907 0.6567 0.6663 0.0195  0.0856  0.0065  145 GLU   A CG  
1072 C CD  . GLU   A 139 ? 0.8160 0.7786 0.7757 0.0210  0.0814  0.0054  145 GLU   A CD  
1073 O OE1 . GLU   A 139 ? 0.8442 0.8039 0.7912 0.0232  0.0792  0.0010  145 GLU   A OE1 
1074 O OE2 . GLU   A 139 ? 0.8479 0.8104 0.8080 0.0200  0.0802  0.0089  145 GLU   A OE2 
1075 N N   . SER   B 1   ? 0.3582 0.3323 0.3378 0.0113  -0.0139 -0.0135 7   SER   C N   
1076 C CA  . SER   B 1   ? 0.3568 0.3357 0.3481 0.0120  -0.0149 -0.0148 7   SER   C CA  
1077 C C   . SER   B 1   ? 0.3400 0.3214 0.3353 0.0120  -0.0136 -0.0140 7   SER   C C   
1078 O O   . SER   B 1   ? 0.3432 0.3212 0.3320 0.0117  -0.0136 -0.0123 7   SER   C O   
1079 C CB  . SER   B 1   ? 0.3991 0.3754 0.3930 0.0133  -0.0211 -0.0168 7   SER   C CB  
1080 O OG  . SER   B 1   ? 0.4611 0.4318 0.4493 0.0141  -0.0254 -0.0160 7   SER   C OG  
1081 N N   . GLY   B 2   ? 0.2987 0.2857 0.3043 0.0121  -0.0125 -0.0153 8   GLY   C N   
1082 C CA  . GLY   B 2   ? 0.2812 0.2706 0.2909 0.0122  -0.0111 -0.0155 8   GLY   C CA  
1083 C C   . GLY   B 2   ? 0.2639 0.2603 0.2816 0.0110  -0.0070 -0.0163 8   GLY   C C   
1084 O O   . GLY   B 2   ? 0.2784 0.2772 0.2969 0.0098  -0.0046 -0.0155 8   GLY   C O   
1085 N N   . ALA   B 3   ? 0.2360 0.2354 0.2598 0.0113  -0.0061 -0.0179 9   ALA   C N   
1086 C CA  . ALA   B 3   ? 0.2274 0.2333 0.2575 0.0096  -0.0016 -0.0188 9   ALA   C CA  
1087 C C   . ALA   B 3   ? 0.2252 0.2325 0.2560 0.0094  0.0007  -0.0199 9   ALA   C C   
1088 O O   . ALA   B 3   ? 0.2423 0.2461 0.2723 0.0112  -0.0019 -0.0209 9   ALA   C O   
1089 C CB  . ALA   B 3   ? 0.2318 0.2416 0.2724 0.0100  -0.0026 -0.0215 9   ALA   C CB  
1090 N N   . ILE   B 4   ? 0.2116 0.2235 0.2434 0.0071  0.0055  -0.0199 10  ILE   C N   
1091 C CA  . ILE   B 4   ? 0.2030 0.2169 0.2358 0.0066  0.0082  -0.0218 10  ILE   C CA  
1092 C C   . ILE   B 4   ? 0.2124 0.2322 0.2553 0.0063  0.0106  -0.0255 10  ILE   C C   
1093 O O   . ILE   B 4   ? 0.2092 0.2327 0.2551 0.0043  0.0127  -0.0248 10  ILE   C O   
1094 C CB  . ILE   B 4   ? 0.2033 0.2182 0.2293 0.0036  0.0119  -0.0193 10  ILE   C CB  
1095 C CG1 . ILE   B 4   ? 0.2180 0.2284 0.2359 0.0036  0.0100  -0.0159 10  ILE   C CG1 
1096 C CG2 . ILE   B 4   ? 0.2101 0.2267 0.2359 0.0027  0.0148  -0.0219 10  ILE   C CG2 
1097 C CD1 . ILE   B 4   ? 0.2251 0.2371 0.2381 0.0008  0.0126  -0.0129 10  ILE   C CD1 
1098 N N   . TYR   B 5   ? 0.2156 0.2365 0.2645 0.0081  0.0105  -0.0294 11  TYR   C N   
1099 C CA  . TYR   B 5   ? 0.2294 0.2568 0.2893 0.0079  0.0135  -0.0336 11  TYR   C CA  
1100 C C   . TYR   B 5   ? 0.2518 0.2817 0.3101 0.0064  0.0186  -0.0362 11  TYR   C C   
1101 O O   . TYR   B 5   ? 0.2625 0.2893 0.3200 0.0084  0.0173  -0.0382 11  TYR   C O   
1102 C CB  . TYR   B 5   ? 0.2361 0.2630 0.3063 0.0119  0.0087  -0.0370 11  TYR   C CB  
1103 C CG  . TYR   B 5   ? 0.2505 0.2751 0.3220 0.0130  0.0034  -0.0350 11  TYR   C CG  
1104 C CD1 . TYR   B 5   ? 0.2608 0.2906 0.3409 0.0119  0.0040  -0.0360 11  TYR   C CD1 
1105 C CD2 . TYR   B 5   ? 0.2811 0.2981 0.3445 0.0146  -0.0020 -0.0321 11  TYR   C CD2 
1106 C CE1 . TYR   B 5   ? 0.2838 0.3109 0.3644 0.0127  -0.0011 -0.0345 11  TYR   C CE1 
1107 C CE2 . TYR   B 5   ? 0.3012 0.3156 0.3639 0.0152  -0.0066 -0.0305 11  TYR   C CE2 
1108 C CZ  . TYR   B 5   ? 0.3069 0.3262 0.3783 0.0144  -0.0064 -0.0319 11  TYR   C CZ  
1109 O OH  . TYR   B 5   ? 0.3436 0.3597 0.4137 0.0150  -0.0112 -0.0306 11  TYR   C OH  
1110 N N   . VAL   B 6   ? 0.2467 0.2816 0.3039 0.0027  0.0243  -0.0361 12  VAL   C N   
1111 C CA  . VAL   B 6   ? 0.2529 0.2900 0.3067 0.0006  0.0296  -0.0386 12  VAL   C CA  
1112 C C   . VAL   B 6   ? 0.2670 0.3118 0.3279 -0.0021 0.0357  -0.0416 12  VAL   C C   
1113 O O   . VAL   B 6   ? 0.2608 0.3079 0.3216 -0.0050 0.0371  -0.0388 12  VAL   C O   
1114 C CB  . VAL   B 6   ? 0.2743 0.3078 0.3144 -0.0024 0.0304  -0.0342 12  VAL   C CB  
1115 C CG1 . VAL   B 6   ? 0.2712 0.3048 0.3074 -0.0049 0.0301  -0.0291 12  VAL   C CG1 
1116 C CG2 . VAL   B 6   ? 0.2882 0.3238 0.3236 -0.0051 0.0357  -0.0369 12  VAL   C CG2 
1117 N N   . GLY   B 7   ? 0.2790 0.3279 0.3481 -0.0009 0.0389  -0.0478 13  GLY   C N   
1118 C CA  . GLY   B 7   ? 0.2894 0.3465 0.3668 -0.0035 0.0453  -0.0515 13  GLY   C CA  
1119 C C   . GLY   B 7   ? 0.2893 0.3500 0.3777 -0.0031 0.0433  -0.0506 13  GLY   C C   
1120 O O   . GLY   B 7   ? 0.2893 0.3481 0.3854 0.0011  0.0372  -0.0513 13  GLY   C O   
1121 N N   . ASN   B 8   ? 0.2802 0.3452 0.3681 -0.0078 0.0477  -0.0486 14  ASN   C N   
1122 C CA  . ASN   B 8   ? 0.2780 0.3458 0.3761 -0.0079 0.0455  -0.0475 14  ASN   C CA  
1123 C C   . ASN   B 8   ? 0.2564 0.3184 0.3455 -0.0092 0.0412  -0.0407 14  ASN   C C   
1124 O O   . ASN   B 8   ? 0.2618 0.3259 0.3549 -0.0117 0.0415  -0.0387 14  ASN   C O   
1125 C CB  . ASN   B 8   ? 0.3178 0.3945 0.4250 -0.0120 0.0527  -0.0503 14  ASN   C CB  
1126 C CG  . ASN   B 8   ? 0.4079 0.4916 0.5281 -0.0099 0.0566  -0.0581 14  ASN   C CG  
1127 O OD1 . ASN   B 8   ? 0.4277 0.5128 0.5611 -0.0051 0.0520  -0.0617 14  ASN   C OD1 
1128 N ND2 . ASN   B 8   ? 0.4279 0.5158 0.5446 -0.0135 0.0649  -0.0611 14  ASN   C ND2 
1129 N N   . TYR   B 9   ? 0.2338 0.2886 0.3117 -0.0074 0.0372  -0.0375 15  TYR   C N   
1130 C CA  . TYR   B 9   ? 0.2147 0.2640 0.2846 -0.0081 0.0333  -0.0317 15  TYR   C CA  
1131 C C   . TYR   B 9   ? 0.2146 0.2581 0.2832 -0.0035 0.0264  -0.0310 15  TYR   C C   
1132 O O   . TYR   B 9   ? 0.2237 0.2650 0.2916 -0.0005 0.0246  -0.0331 15  TYR   C O   
1133 C CB  . TYR   B 9   ? 0.2161 0.2621 0.2721 -0.0110 0.0355  -0.0278 15  TYR   C CB  
1134 C CG  . TYR   B 9   ? 0.2362 0.2861 0.2891 -0.0164 0.0419  -0.0272 15  TYR   C CG  
1135 C CD1 . TYR   B 9   ? 0.2615 0.3143 0.3193 -0.0197 0.0438  -0.0257 15  TYR   C CD1 
1136 C CD2 . TYR   B 9   ? 0.2600 0.3102 0.3048 -0.0186 0.0460  -0.0282 15  TYR   C CD2 
1137 C CE1 . TYR   B 9   ? 0.2772 0.3331 0.3313 -0.0253 0.0499  -0.0246 15  TYR   C CE1 
1138 C CE2 . TYR   B 9   ? 0.2751 0.3283 0.3152 -0.0240 0.0519  -0.0274 15  TYR   C CE2 
1139 C CZ  . TYR   B 9   ? 0.2930 0.3488 0.3373 -0.0275 0.0539  -0.0253 15  TYR   C CZ  
1140 O OH  . TYR   B 9   ? 0.3291 0.3870 0.3673 -0.0336 0.0597  -0.0239 15  TYR   C OH  
1141 N N   . ARG   B 10  ? 0.1919 0.2321 0.2588 -0.0033 0.0225  -0.0276 16  ARG   C N   
1142 C CA  . ARG   B 10  ? 0.1903 0.2244 0.2535 0.0002  0.0164  -0.0262 16  ARG   C CA  
1143 C C   . ARG   B 10  ? 0.1891 0.2191 0.2423 -0.0014 0.0162  -0.0214 16  ARG   C C   
1144 O O   . ARG   B 10  ? 0.1996 0.2307 0.2535 -0.0040 0.0175  -0.0194 16  ARG   C O   
1145 C CB  . ARG   B 10  ? 0.2080 0.2423 0.2800 0.0021  0.0119  -0.0279 16  ARG   C CB  
1146 C CG  . ARG   B 10  ? 0.2123 0.2399 0.2785 0.0044  0.0061  -0.0258 16  ARG   C CG  
1147 C CD  . ARG   B 10  ? 0.2277 0.2554 0.3024 0.0062  0.0011  -0.0280 16  ARG   C CD  
1148 N NE  . ARG   B 10  ? 0.2777 0.3009 0.3477 0.0062  -0.0023 -0.0259 16  ARG   C NE  
1149 C CZ  . ARG   B 10  ? 0.3276 0.3448 0.3924 0.0086  -0.0077 -0.0257 16  ARG   C CZ  
1150 N NH1 . ARG   B 10  ? 0.3170 0.3316 0.3804 0.0112  -0.0108 -0.0268 16  ARG   C NH1 
1151 N NH2 . ARG   B 10  ? 0.3207 0.3341 0.3811 0.0083  -0.0100 -0.0245 16  ARG   C NH2 
1152 N N   . VAL   B 11  ? 0.1866 0.2122 0.2312 -0.0001 0.0146  -0.0196 17  VAL   C N   
1153 C CA  . VAL   B 11  ? 0.1855 0.2079 0.2220 -0.0013 0.0144  -0.0155 17  VAL   C CA  
1154 C C   . VAL   B 11  ? 0.1818 0.1994 0.2159 0.0014  0.0101  -0.0148 17  VAL   C C   
1155 O O   . VAL   B 11  ? 0.1898 0.2048 0.2219 0.0036  0.0078  -0.0159 17  VAL   C O   
1156 C CB  . VAL   B 11  ? 0.2035 0.2250 0.2323 -0.0023 0.0163  -0.0141 17  VAL   C CB  
1157 C CG1 . VAL   B 11  ? 0.2146 0.2338 0.2374 -0.0036 0.0159  -0.0099 17  VAL   C CG1 
1158 C CG2 . VAL   B 11  ? 0.2100 0.2355 0.2396 -0.0048 0.0206  -0.0157 17  VAL   C CG2 
1159 N N   . VAL   B 12  ? 0.1621 0.1783 0.1960 0.0010  0.0090  -0.0131 18  VAL   C N   
1160 C CA  . VAL   B 12  ? 0.1829 0.1944 0.2136 0.0032  0.0054  -0.0130 18  VAL   C CA  
1161 C C   . VAL   B 12  ? 0.1722 0.1818 0.1985 0.0026  0.0060  -0.0103 18  VAL   C C   
1162 O O   . VAL   B 12  ? 0.1701 0.1815 0.1973 0.0004  0.0082  -0.0083 18  VAL   C O   
1163 C CB  . VAL   B 12  ? 0.1941 0.2055 0.2312 0.0041  0.0023  -0.0153 18  VAL   C CB  
1164 C CG1 . VAL   B 12  ? 0.2218 0.2350 0.2646 0.0055  0.0007  -0.0183 18  VAL   C CG1 
1165 C CG2 . VAL   B 12  ? 0.1851 0.1990 0.2278 0.0017  0.0038  -0.0147 18  VAL   C CG2 
1166 N N   . ASN   B 13  ? 0.1681 0.1738 0.1900 0.0044  0.0041  -0.0103 19  ASN   C N   
1167 C CA  . ASN   B 13  ? 0.1717 0.1758 0.1917 0.0043  0.0046  -0.0087 19  ASN   C CA  
1168 C C   . ASN   B 13  ? 0.1746 0.1788 0.2004 0.0035  0.0037  -0.0092 19  ASN   C C   
1169 O O   . ASN   B 13  ? 0.1778 0.1812 0.2066 0.0041  0.0014  -0.0115 19  ASN   C O   
1170 C CB  . ASN   B 13  ? 0.1897 0.1898 0.2042 0.0063  0.0031  -0.0098 19  ASN   C CB  
1171 C CG  . ASN   B 13  ? 0.2105 0.2099 0.2193 0.0066  0.0041  -0.0089 19  ASN   C CG  
1172 O OD1 . ASN   B 13  ? 0.2117 0.2094 0.2179 0.0072  0.0025  -0.0099 19  ASN   C OD1 
1173 N ND2 . ASN   B 13  ? 0.1864 0.1869 0.1936 0.0060  0.0063  -0.0071 19  ASN   C ND2 
1174 N N   . ARG   B 14  ? 0.1709 0.1758 0.1985 0.0019  0.0050  -0.0068 20  ARG   C N   
1175 C CA  . ARG   B 14  ? 0.1693 0.1735 0.2022 0.0007  0.0041  -0.0068 20  ARG   C CA  
1176 C C   . ARG   B 14  ? 0.1630 0.1632 0.1963 0.0027  0.0013  -0.0093 20  ARG   C C   
1177 O O   . ARG   B 14  ? 0.1749 0.1748 0.2129 0.0021  -0.0005 -0.0109 20  ARG   C O   
1178 C CB  . ARG   B 14  ? 0.1881 0.1921 0.2216 -0.0011 0.0052  -0.0033 20  ARG   C CB  
1179 C CG  . ARG   B 14  ? 0.2146 0.2176 0.2536 -0.0034 0.0045  -0.0022 20  ARG   C CG  
1180 C CD  . ARG   B 14  ? 0.2328 0.2337 0.2714 -0.0044 0.0044  0.0015  20  ARG   C CD  
1181 N NE  . ARG   B 14  ? 0.2295 0.2284 0.2724 -0.0072 0.0036  0.0036  20  ARG   C NE  
1182 C CZ  . ARG   B 14  ? 0.2320 0.2267 0.2787 -0.0064 0.0012  0.0027  20  ARG   C CZ  
1183 N NH1 . ARG   B 14  ? 0.2261 0.2187 0.2726 -0.0028 -0.0003 -0.0009 20  ARG   C NH1 
1184 N NH2 . ARG   B 14  ? 0.2305 0.2229 0.2810 -0.0094 0.0003  0.0052  20  ARG   C NH2 
1185 N N   . HIS   B 15  ? 0.1700 0.1675 0.1981 0.0049  0.0011  -0.0101 21  HIS   C N   
1186 C CA  . HIS   B 15  ? 0.1803 0.1736 0.2069 0.0066  -0.0012 -0.0130 21  HIS   C CA  
1187 C C   . HIS   B 15  ? 0.1876 0.1796 0.2125 0.0074  -0.0040 -0.0157 21  HIS   C C   
1188 O O   . HIS   B 15  ? 0.2051 0.1934 0.2291 0.0082  -0.0066 -0.0184 21  HIS   C O   
1189 C CB  . HIS   B 15  ? 0.1811 0.1724 0.2028 0.0084  0.0002  -0.0135 21  HIS   C CB  
1190 C CG  . HIS   B 15  ? 0.1960 0.1874 0.2106 0.0093  0.0013  -0.0138 21  HIS   C CG  
1191 N ND1 . HIS   B 15  ? 0.2011 0.1956 0.2146 0.0086  0.0036  -0.0112 21  HIS   C ND1 
1192 C CD2 . HIS   B 15  ? 0.2175 0.2055 0.2253 0.0105  0.0005  -0.0161 21  HIS   C CD2 
1193 C CE1 . HIS   B 15  ? 0.2168 0.2098 0.2236 0.0093  0.0041  -0.0120 21  HIS   C CE1 
1194 N NE2 . HIS   B 15  ? 0.2351 0.2242 0.2378 0.0103  0.0023  -0.0147 21  HIS   C NE2 
1195 N N   . LEU   B 16  ? 0.1885 0.1831 0.2131 0.0071  -0.0039 -0.0153 22  LEU   C N   
1196 C CA  . LEU   B 16  ? 0.2055 0.1987 0.2296 0.0080  -0.0075 -0.0176 22  LEU   C CA  
1197 C C   . LEU   B 16  ? 0.2168 0.2141 0.2502 0.0068  -0.0085 -0.0183 22  LEU   C C   
1198 O O   . LEU   B 16  ? 0.2342 0.2312 0.2694 0.0077  -0.0118 -0.0202 22  LEU   C O   
1199 C CB  . LEU   B 16  ? 0.2069 0.1991 0.2242 0.0091  -0.0074 -0.0171 22  LEU   C CB  
1200 C CG  . LEU   B 16  ? 0.2234 0.2121 0.2314 0.0099  -0.0060 -0.0166 22  LEU   C CG  
1201 C CD1 . LEU   B 16  ? 0.2325 0.2200 0.2341 0.0102  -0.0060 -0.0156 22  LEU   C CD1 
1202 C CD2 . LEU   B 16  ? 0.2392 0.2227 0.2423 0.0108  -0.0086 -0.0192 22  LEU   C CD2 
1203 N N   . ALA   B 17  ? 0.1941 0.1950 0.2336 0.0046  -0.0056 -0.0167 23  ALA   C N   
1204 C CA  . ALA   B 17  ? 0.2026 0.2082 0.2513 0.0029  -0.0054 -0.0176 23  ALA   C CA  
1205 C C   . ALA   B 17  ? 0.2092 0.2136 0.2638 0.0030  -0.0097 -0.0202 23  ALA   C C   
1206 O O   . ALA   B 17  ? 0.2174 0.2176 0.2699 0.0033  -0.0117 -0.0208 23  ALA   C O   
1207 C CB  . ALA   B 17  ? 0.1974 0.2062 0.2497 -0.0003 -0.0015 -0.0150 23  ALA   C CB  
1208 N N   . THR   B 18  ? 0.2072 0.2155 0.2696 0.0029  -0.0111 -0.0222 24  THR   C N   
1209 C CA  . THR   B 18  ? 0.2117 0.2196 0.2811 0.0029  -0.0159 -0.0249 24  THR   C CA  
1210 C C   . THR   B 18  ? 0.2044 0.2160 0.2839 -0.0005 -0.0140 -0.0247 24  THR   C C   
1211 O O   . THR   B 18  ? 0.2094 0.2244 0.2902 -0.0030 -0.0089 -0.0224 24  THR   C O   
1212 C CB  . THR   B 18  ? 0.2237 0.2341 0.2982 0.0048  -0.0190 -0.0274 24  THR   C CB  
1213 O OG1 . THR   B 18  ? 0.2346 0.2523 0.3179 0.0033  -0.0147 -0.0275 24  THR   C OG1 
1214 C CG2 . THR   B 18  ? 0.2308 0.2366 0.2950 0.0077  -0.0211 -0.0270 24  THR   C CG2 
1215 N N   . HIS   B 19  ? 0.2113 0.2226 0.2982 -0.0010 -0.0184 -0.0271 25  HIS   C N   
1216 C CA  . HIS   B 19  ? 0.2262 0.2415 0.3238 -0.0048 -0.0166 -0.0269 25  HIS   C CA  
1217 C C   . HIS   B 19  ? 0.2132 0.2372 0.3196 -0.0067 -0.0118 -0.0270 25  HIS   C C   
1218 O O   . HIS   B 19  ? 0.2111 0.2385 0.3215 -0.0106 -0.0069 -0.0251 25  HIS   C O   
1219 C CB  . HIS   B 19  ? 0.2726 0.2863 0.3775 -0.0051 -0.0228 -0.0300 25  HIS   C CB  
1220 C CG  . HIS   B 19  ? 0.3508 0.3696 0.4659 -0.0041 -0.0260 -0.0330 25  HIS   C CG  
1221 N ND1 . HIS   B 19  ? 0.3885 0.4154 0.5184 -0.0071 -0.0236 -0.0341 25  HIS   C ND1 
1222 C CD2 . HIS   B 19  ? 0.3878 0.4049 0.5009 -0.0006 -0.0314 -0.0352 25  HIS   C CD2 
1223 C CE1 . HIS   B 19  ? 0.3875 0.4179 0.5253 -0.0049 -0.0277 -0.0372 25  HIS   C CE1 
1224 N NE2 . HIS   B 19  ? 0.3942 0.4186 0.5221 -0.0009 -0.0328 -0.0378 25  HIS   C NE2 
1225 N N   . ASN   B 20  ? 0.2046 0.2316 0.3132 -0.0040 -0.0129 -0.0292 26  ASN   C N   
1226 C CA  . ASN   B 20  ? 0.2215 0.2566 0.3386 -0.0052 -0.0082 -0.0303 26  ASN   C CA  
1227 C C   . ASN   B 20  ? 0.2098 0.2456 0.3186 -0.0067 -0.0015 -0.0273 26  ASN   C C   
1228 O O   . ASN   B 20  ? 0.2101 0.2518 0.3240 -0.0100 0.0042  -0.0270 26  ASN   C O   
1229 C CB  . ASN   B 20  ? 0.2694 0.3065 0.3914 -0.0015 -0.0119 -0.0336 26  ASN   C CB  
1230 C CG  . ASN   B 20  ? 0.3635 0.4095 0.4969 -0.0023 -0.0073 -0.0360 26  ASN   C CG  
1231 O OD1 . ASN   B 20  ? 0.3926 0.4453 0.5392 -0.0050 -0.0054 -0.0379 26  ASN   C OD1 
1232 N ND2 . ASN   B 20  ? 0.3914 0.4377 0.5206 0.0001  -0.0055 -0.0365 26  ASN   C ND2 
1233 N N   . ASP   B 21  ? 0.2125 0.2424 0.3083 -0.0047 -0.0021 -0.0250 27  ASP   C N   
1234 C CA  . ASP   B 21  ? 0.2010 0.2311 0.2890 -0.0062 0.0034  -0.0220 27  ASP   C CA  
1235 C C   . ASP   B 21  ? 0.2076 0.2379 0.2959 -0.0106 0.0066  -0.0189 27  ASP   C C   
1236 O O   . ASP   B 21  ? 0.2189 0.2528 0.3068 -0.0138 0.0118  -0.0174 27  ASP   C O   
1237 C CB  . ASP   B 21  ? 0.1888 0.2127 0.2643 -0.0035 0.0016  -0.0202 27  ASP   C CB  
1238 C CG  . ASP   B 21  ? 0.2090 0.2319 0.2815 0.0001  -0.0005 -0.0220 27  ASP   C CG  
1239 O OD1 . ASP   B 21  ? 0.2387 0.2661 0.3151 0.0001  0.0020  -0.0236 27  ASP   C OD1 
1240 O OD2 . ASP   B 21  ? 0.2121 0.2295 0.2780 0.0026  -0.0045 -0.0220 27  ASP   C OD2 
1241 N N   . TRP   B 22  ? 0.2050 0.2308 0.2935 -0.0110 0.0032  -0.0181 28  TRP   C N   
1242 C CA  . TRP   B 22  ? 0.2075 0.2321 0.2966 -0.0151 0.0054  -0.0148 28  TRP   C CA  
1243 C C   . TRP   B 22  ? 0.2101 0.2408 0.3101 -0.0196 0.0085  -0.0154 28  TRP   C C   
1244 O O   . TRP   B 22  ? 0.2252 0.2567 0.3239 -0.0240 0.0126  -0.0122 28  TRP   C O   
1245 C CB  . TRP   B 22  ? 0.2139 0.2315 0.3012 -0.0141 0.0007  -0.0144 28  TRP   C CB  
1246 C CG  . TRP   B 22  ? 0.2154 0.2273 0.2921 -0.0116 0.0000  -0.0123 28  TRP   C CG  
1247 C CD1 . TRP   B 22  ? 0.2210 0.2292 0.2916 -0.0074 -0.0029 -0.0141 28  TRP   C CD1 
1248 C CD2 . TRP   B 22  ? 0.2106 0.2201 0.2820 -0.0133 0.0023  -0.0081 28  TRP   C CD2 
1249 N NE1 . TRP   B 22  ? 0.2256 0.2301 0.2887 -0.0064 -0.0020 -0.0116 28  TRP   C NE1 
1250 C CE2 . TRP   B 22  ? 0.2200 0.2252 0.2838 -0.0098 0.0007  -0.0078 28  TRP   C CE2 
1251 C CE3 . TRP   B 22  ? 0.2206 0.2311 0.2927 -0.0177 0.0055  -0.0043 28  TRP   C CE3 
1252 C CZ2 . TRP   B 22  ? 0.2233 0.2256 0.2822 -0.0101 0.0017  -0.0043 28  TRP   C CZ2 
1253 C CZ3 . TRP   B 22  ? 0.2311 0.2377 0.2966 -0.0182 0.0059  -0.0002 28  TRP   C CZ3 
1254 C CH2 . TRP   B 22  ? 0.2299 0.2328 0.2897 -0.0141 0.0038  -0.0004 28  TRP   C CH2 
1255 N N   . ALA   B 23  ? 0.2026 0.2378 0.3130 -0.0187 0.0066  -0.0195 29  ALA   C N   
1256 C CA  . ALA   B 23  ? 0.2121 0.2546 0.3347 -0.0230 0.0101  -0.0208 29  ALA   C CA  
1257 C C   . ALA   B 23  ? 0.2202 0.2697 0.3433 -0.0248 0.0172  -0.0212 29  ALA   C C   
1258 O O   . ALA   B 23  ? 0.2382 0.2939 0.3693 -0.0294 0.0221  -0.0216 29  ALA   C O   
1259 C CB  . ALA   B 23  ? 0.1988 0.2445 0.3338 -0.0209 0.0053  -0.0254 29  ALA   C CB  
1260 N N   . ASN   B 24  ? 0.2035 0.2523 0.3191 -0.0213 0.0177  -0.0219 30  ASN   C N   
1261 C CA  . ASN   B 24  ? 0.1989 0.2532 0.3133 -0.0225 0.0240  -0.0229 30  ASN   C CA  
1262 C C   . ASN   B 24  ? 0.2003 0.2498 0.2995 -0.0230 0.0260  -0.0188 30  ASN   C C   
1263 O O   . ASN   B 24  ? 0.2022 0.2530 0.2965 -0.0216 0.0284  -0.0199 30  ASN   C O   
1264 C CB  . ASN   B 24  ? 0.2082 0.2661 0.3288 -0.0178 0.0221  -0.0279 30  ASN   C CB  
1265 C CG  . ASN   B 24  ? 0.2570 0.3208 0.3943 -0.0177 0.0203  -0.0320 30  ASN   C CG  
1266 O OD1 . ASN   B 24  ? 0.2576 0.3295 0.4051 -0.0210 0.0257  -0.0341 30  ASN   C OD1 
1267 N ND2 . ASN   B 24  ? 0.2492 0.3094 0.3897 -0.0143 0.0126  -0.0332 30  ASN   C ND2 
1268 N N   . LEU   B 25  ? 0.2060 0.2498 0.2987 -0.0250 0.0247  -0.0142 31  LEU   C N   
1269 C CA  . LEU   B 25  ? 0.2089 0.2477 0.2885 -0.0253 0.0253  -0.0102 31  LEU   C CA  
1270 C C   . LEU   B 25  ? 0.2252 0.2672 0.2992 -0.0293 0.0316  -0.0087 31  LEU   C C   
1271 O O   . LEU   B 25  ? 0.2416 0.2871 0.3188 -0.0344 0.0360  -0.0078 31  LEU   C O   
1272 C CB  . LEU   B 25  ? 0.2048 0.2372 0.2816 -0.0268 0.0223  -0.0059 31  LEU   C CB  
1273 C CG  . LEU   B 25  ? 0.2189 0.2459 0.2843 -0.0271 0.0219  -0.0012 31  LEU   C CG  
1274 C CD1 . LEU   B 25  ? 0.2291 0.2535 0.2889 -0.0217 0.0189  -0.0025 31  LEU   C CD1 
1275 C CD2 . LEU   B 25  ? 0.2293 0.2503 0.2949 -0.0286 0.0188  0.0023  31  LEU   C CD2 
1276 N N   . VAL   B 26  ? 0.2238 0.2642 0.2885 -0.0275 0.0320  -0.0081 32  VAL   C N   
1277 C CA  . VAL   B 26  ? 0.2262 0.2679 0.2826 -0.0311 0.0370  -0.0065 32  VAL   C CA  
1278 C C   . VAL   B 26  ? 0.2400 0.2752 0.2854 -0.0324 0.0347  -0.0007 32  VAL   C C   
1279 O O   . VAL   B 26  ? 0.2616 0.2957 0.3010 -0.0375 0.0373  0.0031  32  VAL   C O   
1280 C CB  . VAL   B 26  ? 0.2411 0.2859 0.2961 -0.0282 0.0388  -0.0108 32  VAL   C CB  
1281 C CG1 . VAL   B 26  ? 0.2574 0.3025 0.3017 -0.0318 0.0433  -0.0093 32  VAL   C CG1 
1282 C CG2 . VAL   B 26  ? 0.2394 0.2911 0.3072 -0.0270 0.0410  -0.0166 32  VAL   C CG2 
1283 N N   . TRP   B 27  ? 0.2154 0.2461 0.2581 -0.0279 0.0297  0.0000  33  TRP   C N   
1284 C CA  . TRP   B 27  ? 0.2175 0.2425 0.2517 -0.0282 0.0270  0.0048  33  TRP   C CA  
1285 C C   . TRP   B 27  ? 0.2105 0.2319 0.2461 -0.0230 0.0221  0.0043  33  TRP   C C   
1286 O O   . TRP   B 27  ? 0.2105 0.2333 0.2489 -0.0193 0.0211  0.0005  33  TRP   C O   
1287 C CB  . TRP   B 27  ? 0.2255 0.2512 0.2503 -0.0291 0.0291  0.0054  33  TRP   C CB  
1288 C CG  . TRP   B 27  ? 0.2417 0.2625 0.2588 -0.0283 0.0256  0.0096  33  TRP   C CG  
1289 C CD1 . TRP   B 27  ? 0.2657 0.2828 0.2770 -0.0318 0.0244  0.0149  33  TRP   C CD1 
1290 C CD2 . TRP   B 27  ? 0.2354 0.2548 0.2507 -0.0240 0.0227  0.0087  33  TRP   C CD2 
1291 N NE1 . TRP   B 27  ? 0.2719 0.2858 0.2790 -0.0294 0.0206  0.0171  33  TRP   C NE1 
1292 C CE2 . TRP   B 27  ? 0.2529 0.2685 0.2626 -0.0248 0.0199  0.0133  33  TRP   C CE2 
1293 C CE3 . TRP   B 27  ? 0.2411 0.2617 0.2591 -0.0197 0.0219  0.0048  33  TRP   C CE3 
1294 C CZ2 . TRP   B 27  ? 0.2560 0.2701 0.2636 -0.0216 0.0171  0.0135  33  TRP   C CZ2 
1295 C CZ3 . TRP   B 27  ? 0.2495 0.2679 0.2641 -0.0170 0.0193  0.0054  33  TRP   C CZ3 
1296 C CH2 . TRP   B 27  ? 0.2446 0.2604 0.2546 -0.0179 0.0172  0.0096  33  TRP   C CH2 
1297 N N   . GLU   B 28  ? 0.1982 0.2147 0.2317 -0.0229 0.0189  0.0080  34  GLU   C N   
1298 C CA  . GLU   B 28  ? 0.1947 0.2078 0.2285 -0.0183 0.0150  0.0073  34  GLU   C CA  
1299 C C   . GLU   B 28  ? 0.2086 0.2176 0.2379 -0.0184 0.0127  0.0116  34  GLU   C C   
1300 O O   . GLU   B 28  ? 0.2200 0.2270 0.2473 -0.0221 0.0128  0.0157  34  GLU   C O   
1301 C CB  . GLU   B 28  ? 0.2092 0.2207 0.2501 -0.0162 0.0126  0.0049  34  GLU   C CB  
1302 C CG  . GLU   B 28  ? 0.2319 0.2411 0.2771 -0.0194 0.0120  0.0071  34  GLU   C CG  
1303 C CD  . GLU   B 28  ? 0.2793 0.2828 0.3228 -0.0197 0.0092  0.0111  34  GLU   C CD  
1304 O OE1 . GLU   B 28  ? 0.3431 0.3447 0.3873 -0.0238 0.0095  0.0146  34  GLU   C OE1 
1305 O OE2 . GLU   B 28  ? 0.2341 0.2350 0.2760 -0.0160 0.0067  0.0108  34  GLU   C OE2 
1306 N N   . ASP   B 29  ? 0.1969 0.2045 0.2250 -0.0146 0.0106  0.0109  35  ASP   C N   
1307 C CA  . ASP   B 29  ? 0.1940 0.1985 0.2200 -0.0140 0.0081  0.0144  35  ASP   C CA  
1308 C C   . ASP   B 29  ? 0.1866 0.1894 0.2157 -0.0095 0.0061  0.0121  35  ASP   C C   
1309 O O   . ASP   B 29  ? 0.1901 0.1947 0.2175 -0.0070 0.0067  0.0097  35  ASP   C O   
1310 C CB  . ASP   B 29  ? 0.2221 0.2283 0.2417 -0.0154 0.0089  0.0163  35  ASP   C CB  
1311 C CG  . ASP   B 29  ? 0.2878 0.2912 0.3061 -0.0154 0.0057  0.0204  35  ASP   C CG  
1312 O OD1 . ASP   B 29  ? 0.3033 0.3040 0.3265 -0.0127 0.0031  0.0206  35  ASP   C OD1 
1313 O OD2 . ASP   B 29  ? 0.2960 0.2997 0.3085 -0.0179 0.0055  0.0231  35  ASP   C OD2 
1314 N N   . SER   B 30  ? 0.1766 0.1755 0.2101 -0.0085 0.0037  0.0127  36  SER   C N   
1315 C CA  A SER   B 30  ? 0.1937 0.1908 0.2301 -0.0044 0.0023  0.0100  36  SER   C CA  
1316 C CA  B SER   B 30  ? 0.1914 0.1885 0.2277 -0.0044 0.0023  0.0099  36  SER   C CA  
1317 C C   . SER   B 30  ? 0.1971 0.1952 0.2319 -0.0023 0.0020  0.0107  36  SER   C C   
1318 O O   . SER   B 30  ? 0.2082 0.2070 0.2429 0.0007  0.0027  0.0077  36  SER   C O   
1319 C CB  A SER   B 30  ? 0.2309 0.2232 0.2725 -0.0041 -0.0003 0.0106  36  SER   C CB  
1320 C CB  B SER   B 30  ? 0.2217 0.2140 0.2632 -0.0039 -0.0002 0.0102  36  SER   C CB  
1321 O OG  A SER   B 30  ? 0.2633 0.2537 0.3072 -0.0001 -0.0011 0.0071  36  SER   C OG  
1322 O OG  B SER   B 30  ? 0.2375 0.2272 0.2800 -0.0053 -0.0023 0.0148  36  SER   C OG  
1323 N N   . SER   B 31  ? 0.1752 0.1735 0.2085 -0.0043 0.0009  0.0150  37  SER   C N   
1324 C CA  . SER   B 31  ? 0.1901 0.1899 0.2234 -0.0026 0.0001  0.0158  37  SER   C CA  
1325 C C   . SER   B 31  ? 0.1877 0.1915 0.2165 -0.0024 0.0026  0.0138  37  SER   C C   
1326 O O   . SER   B 31  ? 0.2124 0.2179 0.2423 -0.0005 0.0025  0.0133  37  SER   C O   
1327 C CB  . SER   B 31  ? 0.2275 0.2261 0.2603 -0.0049 -0.0027 0.0210  37  SER   C CB  
1328 O OG  . SER   B 31  ? 0.2851 0.2854 0.3108 -0.0086 -0.0014 0.0228  37  SER   C OG  
1329 N N   . ARG   B 32  ? 0.1723 0.1776 0.1972 -0.0041 0.0047  0.0125  38  ARG   C N   
1330 C CA  . ARG   B 32  ? 0.1666 0.1746 0.1874 -0.0037 0.0066  0.0106  38  ARG   C CA  
1331 C C   . ARG   B 32  ? 0.1744 0.1823 0.1953 -0.0016 0.0078  0.0065  38  ARG   C C   
1332 O O   . ARG   B 32  ? 0.1684 0.1775 0.1861 -0.0011 0.0089  0.0049  38  ARG   C O   
1333 C CB  . ARG   B 32  ? 0.1810 0.1907 0.1973 -0.0071 0.0080  0.0116  38  ARG   C CB  
1334 C CG  . ARG   B 32  ? 0.1843 0.1936 0.1979 -0.0097 0.0065  0.0158  38  ARG   C CG  
1335 C CD  . ARG   B 32  ? 0.1772 0.1878 0.1848 -0.0135 0.0084  0.0163  38  ARG   C CD  
1336 N NE  . ARG   B 32  ? 0.1881 0.2010 0.1927 -0.0129 0.0102  0.0135  38  ARG   C NE  
1337 C CZ  . ARG   B 32  ? 0.2112 0.2251 0.2100 -0.0156 0.0114  0.0137  38  ARG   C CZ  
1338 N NH1 . ARG   B 32  ? 0.2064 0.2194 0.2007 -0.0193 0.0111  0.0167  38  ARG   C NH1 
1339 N NH2 . ARG   B 32  ? 0.2254 0.2406 0.2222 -0.0148 0.0126  0.0108  38  ARG   C NH2 
1340 N N   . ASP   B 33  ? 0.1812 0.1869 0.2053 -0.0006 0.0071  0.0050  39  ASP   C N   
1341 C CA  . ASP   B 33  ? 0.1637 0.1686 0.1875 0.0011  0.0073  0.0013  39  ASP   C CA  
1342 C C   . ASP   B 33  ? 0.1685 0.1755 0.1908 -0.0003 0.0083  0.0003  39  ASP   C C   
1343 O O   . ASP   B 33  ? 0.1698 0.1765 0.1901 0.0011  0.0082  -0.0021 39  ASP   C O   
1344 C CB  . ASP   B 33  ? 0.1701 0.1743 0.1911 0.0036  0.0076  -0.0007 39  ASP   C CB  
1345 C CG  . ASP   B 33  ? 0.1790 0.1811 0.1980 0.0051  0.0070  -0.0041 39  ASP   C CG  
1346 O OD1 . ASP   B 33  ? 0.1903 0.1906 0.2122 0.0052  0.0055  -0.0055 39  ASP   C OD1 
1347 O OD2 . ASP   B 33  ? 0.1835 0.1852 0.1979 0.0059  0.0075  -0.0052 39  ASP   C OD2 
1348 N N   . LEU   B 34  ? 0.1615 0.1703 0.1846 -0.0032 0.0093  0.0020  40  LEU   C N   
1349 C CA  . LEU   B 34  ? 0.1693 0.1807 0.1925 -0.0043 0.0108  0.0002  40  LEU   C CA  
1350 C C   . LEU   B 34  ? 0.1718 0.1843 0.2000 -0.0063 0.0114  -0.0003 40  LEU   C C   
1351 O O   . LEU   B 34  ? 0.1851 0.1965 0.2146 -0.0084 0.0113  0.0023  40  LEU   C O   
1352 C CB  . LEU   B 34  ? 0.1667 0.1803 0.1858 -0.0066 0.0128  0.0018  40  LEU   C CB  
1353 C CG  . LEU   B 34  ? 0.1935 0.2068 0.2083 -0.0053 0.0126  0.0018  40  LEU   C CG  
1354 C CD1 . LEU   B 34  ? 0.1947 0.2098 0.2052 -0.0080 0.0142  0.0029  40  LEU   C CD1 
1355 C CD2 . LEU   B 34  ? 0.2151 0.2278 0.2297 -0.0028 0.0121  -0.0014 40  LEU   C CD2 
1356 N N   . LEU   B 35  ? 0.1521 0.1668 0.1833 -0.0059 0.0120  -0.0034 41  LEU   C N   
1357 C CA  . LEU   B 35  ? 0.1618 0.1790 0.1991 -0.0082 0.0131  -0.0043 41  LEU   C CA  
1358 C C   . LEU   B 35  ? 0.1633 0.1846 0.2027 -0.0083 0.0153  -0.0073 41  LEU   C C   
1359 O O   . LEU   B 35  ? 0.1738 0.1946 0.2122 -0.0054 0.0140  -0.0095 41  LEU   C O   
1360 C CB  . LEU   B 35  ? 0.1708 0.1861 0.2135 -0.0067 0.0102  -0.0061 41  LEU   C CB  
1361 C CG  . LEU   B 35  ? 0.1831 0.2013 0.2339 -0.0093 0.0110  -0.0072 41  LEU   C CG  
1362 C CD1 . LEU   B 35  ? 0.2028 0.2174 0.2572 -0.0092 0.0080  -0.0070 41  LEU   C CD1 
1363 C CD2 . LEU   B 35  ? 0.1874 0.2095 0.2441 -0.0080 0.0109  -0.0113 41  LEU   C CD2 
1364 N N   . VAL   B 36  ? 0.1640 0.1891 0.2062 -0.0116 0.0188  -0.0073 42  VAL   C N   
1365 C CA  . VAL   B 36  ? 0.1736 0.2035 0.2194 -0.0119 0.0217  -0.0109 42  VAL   C CA  
1366 C C   . VAL   B 36  ? 0.1834 0.2174 0.2391 -0.0137 0.0231  -0.0129 42  VAL   C C   
1367 O O   . VAL   B 36  ? 0.1801 0.2144 0.2366 -0.0174 0.0247  -0.0104 42  VAL   C O   
1368 C CB  . VAL   B 36  ? 0.1787 0.2103 0.2180 -0.0149 0.0259  -0.0097 42  VAL   C CB  
1369 C CG1 . VAL   B 36  ? 0.1908 0.2275 0.2345 -0.0152 0.0296  -0.0143 42  VAL   C CG1 
1370 C CG2 . VAL   B 36  ? 0.1852 0.2130 0.2157 -0.0133 0.0241  -0.0078 42  VAL   C CG2 
1371 N N   . SER   B 37  ? 0.1828 0.2195 0.2464 -0.0112 0.0219  -0.0171 43  SER   C N   
1372 C CA  . SER   B 37  ? 0.1915 0.2332 0.2668 -0.0126 0.0230  -0.0198 43  SER   C CA  
1373 C C   . SER   B 37  ? 0.1955 0.2436 0.2771 -0.0126 0.0270  -0.0242 43  SER   C C   
1374 O O   . SER   B 37  ? 0.2003 0.2477 0.2775 -0.0105 0.0275  -0.0256 43  SER   C O   
1375 C CB  . SER   B 37  ? 0.2006 0.2402 0.2820 -0.0096 0.0171  -0.0214 43  SER   C CB  
1376 O OG  . SER   B 37  ? 0.2342 0.2718 0.3146 -0.0051 0.0134  -0.0237 43  SER   C OG  
1377 N N   . SER   B 38  ? 0.1942 0.2486 0.2868 -0.0151 0.0300  -0.0266 44  SER   C N   
1378 C CA  . SER   B 38  ? 0.2346 0.2960 0.3350 -0.0150 0.0345  -0.0315 44  SER   C CA  
1379 C C   . SER   B 38  ? 0.2712 0.3346 0.3838 -0.0102 0.0299  -0.0362 44  SER   C C   
1380 O O   . SER   B 38  ? 0.2900 0.3519 0.4082 -0.0088 0.0245  -0.0360 44  SER   C O   
1381 C CB  . SER   B 38  ? 0.2802 0.3483 0.3862 -0.0206 0.0413  -0.0320 44  SER   C CB  
1382 O OG  . SER   B 38  ? 0.3340 0.4036 0.4499 -0.0217 0.0388  -0.0317 44  SER   C OG  
1383 N N   . THR   B 39  ? 0.2877 0.3539 0.4039 -0.0076 0.0314  -0.0405 45  THR   C N   
1384 C CA  . THR   B 39  ? 0.3293 0.3969 0.4573 -0.0028 0.0264  -0.0449 45  THR   C CA  
1385 C C   . THR   B 39  ? 0.3633 0.4404 0.5057 -0.0032 0.0319  -0.0509 45  THR   C C   
1386 O O   . THR   B 39  ? 0.3631 0.4444 0.5029 -0.0068 0.0399  -0.0519 45  THR   C O   
1387 C CB  . THR   B 39  ? 0.3635 0.4241 0.4830 0.0017  0.0221  -0.0447 45  THR   C CB  
1388 O OG1 . THR   B 39  ? 0.3936 0.4563 0.5100 0.0012  0.0277  -0.0470 45  THR   C OG1 
1389 C CG2 . THR   B 39  ? 0.3715 0.4238 0.4763 0.0017  0.0185  -0.0393 45  THR   C CG2 
1390 N N   . THR   B 40  ? 0.3878 0.4681 0.5454 0.0006  0.0275  -0.0552 46  THR   C N   
1391 C CA  . THR   B 40  ? 0.4172 0.5070 0.5910 0.0012  0.0322  -0.0618 46  THR   C CA  
1392 C C   . THR   B 40  ? 0.4512 0.5390 0.6247 0.0057  0.0316  -0.0656 46  THR   C C   
1393 O O   . THR   B 40  ? 0.4669 0.5616 0.6486 0.0055  0.0381  -0.0710 46  THR   C O   
1394 C CB  . THR   B 40  ? 0.4297 0.5247 0.6227 0.0030  0.0273  -0.0648 46  THR   C CB  
1395 O OG1 . THR   B 40  ? 0.4513 0.5383 0.6417 0.0076  0.0166  -0.0630 46  THR   C OG1 
1396 C CG2 . THR   B 40  ? 0.4348 0.5340 0.6318 -0.0023 0.0298  -0.0626 46  THR   C CG2 
1397 N N   . ALA   B 41  ? 0.4603 0.5387 0.6246 0.0096  0.0241  -0.0630 47  ALA   C N   
1398 C CA  . ALA   B 41  ? 0.4650 0.5400 0.6287 0.0138  0.0226  -0.0661 47  ALA   C CA  
1399 C C   . ALA   B 41  ? 0.4741 0.5442 0.6202 0.0117  0.0270  -0.0636 47  ALA   C C   
1400 O O   . ALA   B 41  ? 0.4888 0.5554 0.6214 0.0084  0.0279  -0.0582 47  ALA   C O   
1401 C CB  . ALA   B 41  ? 0.4726 0.5397 0.6363 0.0188  0.0118  -0.0645 47  ALA   C CB  
1402 N N   . GLN   B 42  ? 0.4630 0.5330 0.6101 0.0138  0.0293  -0.0679 48  GLN   C N   
1403 C CA  . GLN   B 42  ? 0.4578 0.5234 0.5892 0.0119  0.0331  -0.0663 48  GLN   C CA  
1404 C C   . GLN   B 42  ? 0.4313 0.4862 0.5506 0.0142  0.0257  -0.0616 48  GLN   C C   
1405 O O   . GLN   B 42  ? 0.4441 0.4946 0.5686 0.0186  0.0190  -0.0626 48  GLN   C O   
1406 C CB  . GLN   B 42  ? 0.4975 0.5664 0.6347 0.0133  0.0381  -0.0733 48  GLN   C CB  
1407 C CG  . GLN   B 42  ? 0.5726 0.6394 0.6944 0.0097  0.0441  -0.0727 48  GLN   C CG  
1408 C CD  . GLN   B 42  ? 0.6452 0.7190 0.7638 0.0037  0.0531  -0.0727 48  GLN   C CD  
1409 O OE1 . GLN   B 42  ? 0.6585 0.7403 0.7889 0.0022  0.0565  -0.0748 48  GLN   C OE1 
1410 N NE2 . GLN   B 42  ? 0.6639 0.7348 0.7666 -0.0002 0.0569  -0.0703 48  GLN   C NE2 
1411 N N   . GLY   B 43  ? 0.3861 0.4368 0.4899 0.0109  0.0269  -0.0563 49  GLY   C N   
1412 C CA  . GLY   B 43  ? 0.3617 0.4032 0.4535 0.0123  0.0213  -0.0517 49  GLY   C CA  
1413 C C   . GLY   B 43  ? 0.3302 0.3683 0.4148 0.0123  0.0234  -0.0533 49  GLY   C C   
1414 O O   . GLY   B 43  ? 0.3287 0.3709 0.4111 0.0095  0.0301  -0.0558 49  GLY   C O   
1415 N N   . CYS   B 44  ? 0.3092 0.3396 0.3897 0.0151  0.0178  -0.0521 50  CYS   C N   
1416 C CA  . CYS   B 44  ? 0.3084 0.3348 0.3832 0.0154  0.0188  -0.0539 50  CYS   C CA  
1417 C C   . CYS   B 44  ? 0.2945 0.3143 0.3541 0.0133  0.0173  -0.0485 50  CYS   C C   
1418 O O   . CYS   B 44  ? 0.2963 0.3115 0.3514 0.0137  0.0168  -0.0496 50  CYS   C O   
1419 C CB  . CYS   B 44  ? 0.3204 0.3430 0.4043 0.0202  0.0141  -0.0580 50  CYS   C CB  
1420 S SG  . CYS   B 44  ? 0.4042 0.4359 0.5084 0.0230  0.0169  -0.0660 50  CYS   C SG  
1421 N N   . ASP   B 45  ? 0.2609 0.2802 0.3136 0.0111  0.0164  -0.0429 51  ASP   C N   
1422 C CA  . ASP   B 45  ? 0.2633 0.2775 0.3036 0.0091  0.0154  -0.0382 51  ASP   C CA  
1423 C C   . ASP   B 45  ? 0.2710 0.2875 0.3045 0.0055  0.0206  -0.0387 51  ASP   C C   
1424 O O   . ASP   B 45  ? 0.2859 0.3083 0.3211 0.0033  0.0255  -0.0403 51  ASP   C O   
1425 C CB  . ASP   B 45  ? 0.2764 0.2897 0.3121 0.0081  0.0133  -0.0327 51  ASP   C CB  
1426 C CG  . ASP   B 45  ? 0.3630 0.3714 0.3998 0.0109  0.0073  -0.0310 51  ASP   C CG  
1427 O OD1 . ASP   B 45  ? 0.4165 0.4191 0.4520 0.0128  0.0037  -0.0313 51  ASP   C OD1 
1428 O OD2 . ASP   B 45  ? 0.3357 0.3453 0.3739 0.0109  0.0060  -0.0291 51  ASP   C OD2 
1429 N N   . THR   B 46  ? 0.2553 0.2669 0.2811 0.0048  0.0194  -0.0377 52  THR   C N   
1430 C CA  . THR   B 46  ? 0.2718 0.2844 0.2899 0.0013  0.0232  -0.0380 52  THR   C CA  
1431 C C   . THR   B 46  ? 0.2511 0.2625 0.2609 -0.0013 0.0219  -0.0318 52  THR   C C   
1432 O O   . THR   B 46  ? 0.2524 0.2594 0.2599 -0.0002 0.0180  -0.0286 52  THR   C O   
1433 C CB  . THR   B 46  ? 0.3366 0.3443 0.3520 0.0019  0.0222  -0.0410 52  THR   C CB  
1434 O OG1 . THR   B 46  ? 0.3844 0.3941 0.4080 0.0041  0.0245  -0.0477 52  THR   C OG1 
1435 C CG2 . THR   B 46  ? 0.3563 0.3636 0.3616 -0.0021 0.0244  -0.0401 52  THR   C CG2 
1436 N N   . ILE   B 47  ? 0.2353 0.2504 0.2408 -0.0046 0.0252  -0.0302 53  ILE   C N   
1437 C CA  . ILE   B 47  ? 0.2193 0.2336 0.2183 -0.0068 0.0237  -0.0245 53  ILE   C CA  
1438 C C   . ILE   B 47  ? 0.2135 0.2254 0.2046 -0.0093 0.0233  -0.0239 53  ILE   C C   
1439 O O   . ILE   B 47  ? 0.2247 0.2373 0.2125 -0.0111 0.0261  -0.0272 53  ILE   C O   
1440 C CB  . ILE   B 47  ? 0.2345 0.2532 0.2330 -0.0094 0.0265  -0.0225 53  ILE   C CB  
1441 C CG1 . ILE   B 47  ? 0.2612 0.2831 0.2687 -0.0076 0.0274  -0.0240 53  ILE   C CG1 
1442 C CG2 . ILE   B 47  ? 0.2378 0.2554 0.2314 -0.0110 0.0242  -0.0167 53  ILE   C CG2 
1443 C CD1 . ILE   B 47  ? 0.2870 0.3062 0.2981 -0.0045 0.0230  -0.0219 53  ILE   C CD1 
1444 N N   . ALA   B 48  ? 0.1955 0.2045 0.1835 -0.0094 0.0201  -0.0200 54  ALA   C N   
1445 C CA  . ALA   B 48  ? 0.1954 0.2024 0.1768 -0.0119 0.0190  -0.0189 54  ALA   C CA  
1446 C C   . ALA   B 48  ? 0.1880 0.1977 0.1640 -0.0155 0.0204  -0.0167 54  ALA   C C   
1447 O O   . ALA   B 48  ? 0.1954 0.2076 0.1728 -0.0158 0.0206  -0.0137 54  ALA   C O   
1448 C CB  . ALA   B 48  ? 0.1944 0.1990 0.1757 -0.0114 0.0156  -0.0150 54  ALA   C CB  
1449 N N   . ARG   B 49  ? 0.1879 0.1967 0.1573 -0.0183 0.0207  -0.0180 55  ARG   C N   
1450 C CA  . ARG   B 49  ? 0.1849 0.1951 0.1472 -0.0222 0.0210  -0.0154 55  ARG   C CA  
1451 C C   . ARG   B 49  ? 0.1890 0.1966 0.1468 -0.0239 0.0173  -0.0139 55  ARG   C C   
1452 O O   . ARG   B 49  ? 0.2071 0.2125 0.1599 -0.0255 0.0175  -0.0172 55  ARG   C O   
1453 C CB  . ARG   B 49  ? 0.1937 0.2054 0.1515 -0.0244 0.0255  -0.0195 55  ARG   C CB  
1454 C CG  . ARG   B 49  ? 0.1990 0.2140 0.1636 -0.0226 0.0293  -0.0218 55  ARG   C CG  
1455 C CD  . ARG   B 49  ? 0.2131 0.2303 0.1800 -0.0230 0.0289  -0.0169 55  ARG   C CD  
1456 N NE  . ARG   B 49  ? 0.2355 0.2561 0.2093 -0.0218 0.0327  -0.0195 55  ARG   C NE  
1457 C CZ  . ARG   B 49  ? 0.2496 0.2719 0.2287 -0.0210 0.0323  -0.0166 55  ARG   C CZ  
1458 N NH1 . ARG   B 49  ? 0.2465 0.2674 0.2248 -0.0210 0.0287  -0.0114 55  ARG   C NH1 
1459 N NH2 . ARG   B 49  ? 0.2418 0.2676 0.2280 -0.0202 0.0355  -0.0194 55  ARG   C NH2 
1460 N N   . CYS   B 50  ? 0.1799 0.1878 0.1404 -0.0235 0.0140  -0.0093 56  CYS   C N   
1461 C CA  . CYS   B 50  ? 0.1994 0.2055 0.1587 -0.0246 0.0105  -0.0078 56  CYS   C CA  
1462 C C   . CYS   B 50  ? 0.2076 0.2156 0.1706 -0.0246 0.0076  -0.0026 56  CYS   C C   
1463 O O   . CYS   B 50  ? 0.1958 0.2058 0.1620 -0.0232 0.0083  -0.0003 56  CYS   C O   
1464 C CB  . CYS   B 50  ? 0.2189 0.2221 0.1820 -0.0224 0.0104  -0.0105 56  CYS   C CB  
1465 S SG  . CYS   B 50  ? 0.2016 0.2053 0.1726 -0.0186 0.0104  -0.0083 56  CYS   C SG  
1466 N N   . ASP   B 51  ? 0.2100 0.2175 0.1736 -0.0259 0.0044  -0.0011 57  ASP   C N   
1467 C CA  . ASP   B 51  ? 0.2118 0.2219 0.1809 -0.0255 0.0020  0.0031  57  ASP   C CA  
1468 C C   . ASP   B 51  ? 0.2141 0.2237 0.1885 -0.0242 0.0020  0.0029  57  ASP   C C   
1469 O O   . ASP   B 51  ? 0.2163 0.2280 0.1951 -0.0249 0.0000  0.0054  57  ASP   C O   
1470 C CB  . ASP   B 51  ? 0.2346 0.2457 0.2013 -0.0286 -0.0021 0.0056  57  ASP   C CB  
1471 C CG  . ASP   B 51  ? 0.3081 0.3172 0.2712 -0.0313 -0.0044 0.0038  57  ASP   C CG  
1472 O OD1 . ASP   B 51  ? 0.3081 0.3144 0.2706 -0.0308 -0.0027 0.0006  57  ASP   C OD1 
1473 O OD2 . ASP   B 51  ? 0.3801 0.3897 0.3410 -0.0340 -0.0084 0.0058  57  ASP   C OD2 
1474 N N   . CYS   B 52  ? 0.1919 0.1986 0.1663 -0.0224 0.0041  0.0001  58  CYS   C N   
1475 C CA  . CYS   B 52  ? 0.1823 0.1875 0.1603 -0.0216 0.0041  0.0005  58  CYS   C CA  
1476 C C   . CYS   B 52  ? 0.1811 0.1896 0.1645 -0.0204 0.0045  0.0036  58  CYS   C C   
1477 O O   . CYS   B 52  ? 0.1816 0.1922 0.1667 -0.0185 0.0055  0.0044  58  CYS   C O   
1478 C CB  . CYS   B 52  ? 0.2052 0.2063 0.1823 -0.0193 0.0057  -0.0022 58  CYS   C CB  
1479 S SG  . CYS   B 52  ? 0.2185 0.2147 0.1912 -0.0205 0.0052  -0.0066 58  CYS   C SG  
1480 N N   . GLN   B 53  ? 0.1660 0.1747 0.1523 -0.0214 0.0042  0.0048  59  GLN   C N   
1481 C CA  . GLN   B 53  ? 0.1676 0.1792 0.1591 -0.0202 0.0056  0.0068  59  GLN   C CA  
1482 C C   . GLN   B 53  ? 0.1811 0.1893 0.1717 -0.0201 0.0072  0.0066  59  GLN   C C   
1483 O O   . GLN   B 53  ? 0.1813 0.1919 0.1755 -0.0203 0.0088  0.0081  59  GLN   C O   
1484 C CB  . GLN   B 53  ? 0.1746 0.1913 0.1719 -0.0220 0.0040  0.0091  59  GLN   C CB  
1485 C CG  . GLN   B 53  ? 0.1723 0.1922 0.1715 -0.0213 0.0022  0.0104  59  GLN   C CG  
1486 C CD  . GLN   B 53  ? 0.2171 0.2420 0.2236 -0.0226 0.0000  0.0125  59  GLN   C CD  
1487 O OE1 . GLN   B 53  ? 0.2414 0.2670 0.2471 -0.0249 -0.0037 0.0133  59  GLN   C OE1 
1488 N NE2 . GLN   B 53  ? 0.1842 0.2127 0.1980 -0.0212 0.0020  0.0132  59  GLN   C NE2 
1489 N N   . THR   B 54  ? 0.1858 0.1884 0.1718 -0.0200 0.0068  0.0048  60  THR   C N   
1490 C CA  . THR   B 54  ? 0.1905 0.1884 0.1744 -0.0199 0.0076  0.0050  60  THR   C CA  
1491 C C   . THR   B 54  ? 0.1875 0.1809 0.1682 -0.0171 0.0072  0.0028  60  THR   C C   
1492 O O   . THR   B 54  ? 0.1963 0.1895 0.1763 -0.0164 0.0065  0.0004  60  THR   C O   
1493 C CB  . THR   B 54  ? 0.2592 0.2538 0.2422 -0.0231 0.0065  0.0055  60  THR   C CB  
1494 O OG1 . THR   B 54  ? 0.2992 0.2900 0.2795 -0.0235 0.0043  0.0030  60  THR   C OG1 
1495 C CG2 . THR   B 54  ? 0.2775 0.2771 0.2651 -0.0261 0.0065  0.0073  60  THR   C CG2 
1496 N N   . GLY   B 55  ? 0.1762 0.1664 0.1552 -0.0157 0.0077  0.0033  61  GLY   C N   
1497 C CA  . GLY   B 55  ? 0.1834 0.1696 0.1607 -0.0128 0.0067  0.0013  61  GLY   C CA  
1498 C C   . GLY   B 55  ? 0.1791 0.1610 0.1534 -0.0119 0.0065  0.0026  61  GLY   C C   
1499 O O   . GLY   B 55  ? 0.2027 0.1834 0.1749 -0.0141 0.0073  0.0050  61  GLY   C O   
1500 N N   . VAL   B 56  ? 0.1714 0.1507 0.1453 -0.0091 0.0051  0.0011  62  VAL   C N   
1501 C CA  . VAL   B 56  ? 0.1876 0.1616 0.1574 -0.0082 0.0037  0.0023  62  VAL   C CA  
1502 C C   . VAL   B 56  ? 0.1974 0.1737 0.1689 -0.0053 0.0037  0.0011  62  VAL   C C   
1503 O O   . VAL   B 56  ? 0.1981 0.1767 0.1738 -0.0034 0.0032  -0.0014 62  VAL   C O   
1504 C CB  . VAL   B 56  ? 0.1963 0.1624 0.1641 -0.0075 0.0000  0.0016  62  VAL   C CB  
1505 C CG1 . VAL   B 56  ? 0.2140 0.1737 0.1766 -0.0065 -0.0024 0.0032  62  VAL   C CG1 
1506 C CG2 . VAL   B 56  ? 0.2000 0.1628 0.1663 -0.0105 -0.0003 0.0026  62  VAL   C CG2 
1507 N N   . TYR   B 57  ? 0.1911 0.1668 0.1591 -0.0053 0.0045  0.0025  63  TYR   C N   
1508 C CA  . TYR   B 57  ? 0.1958 0.1729 0.1651 -0.0027 0.0040  0.0012  63  TYR   C CA  
1509 C C   . TYR   B 57  ? 0.2008 0.1713 0.1643 -0.0018 0.0011  0.0017  63  TYR   C C   
1510 O O   . TYR   B 57  ? 0.2101 0.1754 0.1669 -0.0037 0.0007  0.0039  63  TYR   C O   
1511 C CB  . TYR   B 57  ? 0.1970 0.1802 0.1686 -0.0028 0.0073  0.0014  63  TYR   C CB  
1512 C CG  . TYR   B 57  ? 0.2137 0.1959 0.1803 -0.0042 0.0094  0.0030  63  TYR   C CG  
1513 C CD1 . TYR   B 57  ? 0.2328 0.2155 0.1977 -0.0070 0.0117  0.0048  63  TYR   C CD1 
1514 C CD2 . TYR   B 57  ? 0.2314 0.2126 0.1953 -0.0028 0.0095  0.0022  63  TYR   C CD2 
1515 C CE1 . TYR   B 57  ? 0.2553 0.2380 0.2163 -0.0086 0.0146  0.0058  63  TYR   C CE1 
1516 C CE2 . TYR   B 57  ? 0.2411 0.2214 0.1997 -0.0043 0.0121  0.0030  63  TYR   C CE2 
1517 C CZ  . TYR   B 57  ? 0.2640 0.2454 0.2214 -0.0071 0.0151  0.0047  63  TYR   C CZ  
1518 O OH  . TYR   B 57  ? 0.2964 0.2780 0.2493 -0.0088 0.0188  0.0051  63  TYR   C OH  
1519 N N   . TYR   B 58  ? 0.1910 0.1615 0.1569 0.0009  -0.0012 -0.0002 64  TYR   C N   
1520 C CA  . TYR   B 58  ? 0.1932 0.1574 0.1535 0.0018  -0.0048 0.0003  64  TYR   C CA  
1521 C C   . TYR   B 58  ? 0.1994 0.1647 0.1553 0.0014  -0.0028 0.0006  64  TYR   C C   
1522 O O   . TYR   B 58  ? 0.2038 0.1745 0.1648 0.0025  -0.0010 -0.0010 64  TYR   C O   
1523 C CB  . TYR   B 58  ? 0.2009 0.1644 0.1670 0.0049  -0.0090 -0.0022 64  TYR   C CB  
1524 C CG  . TYR   B 58  ? 0.2301 0.1865 0.1902 0.0058  -0.0140 -0.0015 64  TYR   C CG  
1525 C CD1 . TYR   B 58  ? 0.2447 0.1926 0.1973 0.0048  -0.0175 0.0008  64  TYR   C CD1 
1526 C CD2 . TYR   B 58  ? 0.2582 0.2155 0.2187 0.0072  -0.0156 -0.0029 64  TYR   C CD2 
1527 C CE1 . TYR   B 58  ? 0.2639 0.2042 0.2091 0.0052  -0.0226 0.0020  64  TYR   C CE1 
1528 C CE2 . TYR   B 58  ? 0.2650 0.2152 0.2187 0.0078  -0.0207 -0.0022 64  TYR   C CE2 
1529 C CZ  . TYR   B 58  ? 0.2806 0.2223 0.2261 0.0067  -0.0242 0.0004  64  TYR   C CZ  
1530 O OH  . TYR   B 58  ? 0.3217 0.2555 0.2591 0.0069  -0.0300 0.0015  64  TYR   C OH  
1531 N N   . CYS   B 59  ? 0.2113 0.1708 0.1573 -0.0004 -0.0031 0.0026  65  CYS   C N   
1532 C CA  . CYS   B 59  ? 0.2125 0.1723 0.1528 -0.0011 -0.0006 0.0023  65  CYS   C CA  
1533 C C   . CYS   B 59  ? 0.2321 0.1846 0.1648 -0.0001 -0.0056 0.0021  65  CYS   C C   
1534 O O   . CYS   B 59  ? 0.2490 0.1938 0.1721 -0.0018 -0.0080 0.0045  65  CYS   C O   
1535 C CB  . CYS   B 59  ? 0.2213 0.1809 0.1555 -0.0045 0.0039  0.0045  65  CYS   C CB  
1536 S SG  . CYS   B 59  ? 0.2727 0.2322 0.1989 -0.0056 0.0079  0.0036  65  CYS   C SG  
1537 N N   . SER   B 60  ? 0.2272 0.1817 0.1642 0.0023  -0.0076 -0.0004 66  SER   C N   
1538 C CA  . SER   B 60  ? 0.2621 0.2099 0.1931 0.0034  -0.0135 -0.0008 66  SER   C CA  
1539 C C   . SER   B 60  ? 0.2668 0.2086 0.1836 0.0011  -0.0127 0.0003  66  SER   C C   
1540 O O   . SER   B 60  ? 0.2910 0.2245 0.1987 0.0007  -0.0180 0.0016  66  SER   C O   
1541 C CB  . SER   B 60  ? 0.3384 0.2897 0.2776 0.0061  -0.0158 -0.0039 66  SER   C CB  
1542 O OG  . SER   B 60  ? 0.4358 0.3921 0.3767 0.0060  -0.0113 -0.0056 66  SER   C OG  
1543 N N   . SER   B 61  ? 0.2612 0.2069 0.1756 -0.0005 -0.0062 -0.0003 67  SER   C N   
1544 C CA  . SER   B 61  ? 0.2738 0.2144 0.1740 -0.0031 -0.0041 0.0002  67  SER   C CA  
1545 C C   . SER   B 61  ? 0.2847 0.2192 0.1744 -0.0067 -0.0034 0.0040  67  SER   C C   
1546 O O   . SER   B 61  ? 0.2866 0.2157 0.1625 -0.0095 -0.0019 0.0049  67  SER   C O   
1547 C CB  . SER   B 61  ? 0.2683 0.2153 0.1708 -0.0034 0.0030  -0.0024 67  SER   C CB  
1548 O OG  . SER   B 61  ? 0.2912 0.2447 0.2011 -0.0044 0.0082  -0.0013 67  SER   C OG  
1549 N N   . ARG   B 62  ? 0.2678 0.2024 0.1629 -0.0069 -0.0048 0.0063  68  ARG   C N   
1550 C CA  . ARG   B 62  ? 0.2683 0.1961 0.1543 -0.0104 -0.0053 0.0103  68  ARG   C CA  
1551 C C   . ARG   B 62  ? 0.2903 0.2114 0.1780 -0.0088 -0.0134 0.0120  68  ARG   C C   
1552 O O   . ARG   B 62  ? 0.3076 0.2214 0.1881 -0.0114 -0.0153 0.0156  68  ARG   C O   
1553 C CB  . ARG   B 62  ? 0.2825 0.2164 0.1740 -0.0127 0.0012  0.0114  68  ARG   C CB  
1554 C CG  . ARG   B 62  ? 0.2798 0.2201 0.1704 -0.0145 0.0091  0.0098  68  ARG   C CG  
1555 C CD  . ARG   B 62  ? 0.3036 0.2371 0.1779 -0.0187 0.0114  0.0118  68  ARG   C CD  
1556 N NE  . ARG   B 62  ? 0.3269 0.2668 0.2008 -0.0204 0.0198  0.0095  68  ARG   C NE  
1557 C CZ  . ARG   B 62  ? 0.3935 0.3347 0.2643 -0.0189 0.0216  0.0060  68  ARG   C CZ  
1558 N NH1 . ARG   B 62  ? 0.3986 0.3349 0.2660 -0.0162 0.0155  0.0046  68  ARG   C NH1 
1559 N NH2 . ARG   B 62  ? 0.4065 0.3538 0.2783 -0.0202 0.0294  0.0035  68  ARG   C NH2 
1560 N N   . ARG   B 63  ? 0.2826 0.2061 0.1803 -0.0045 -0.0181 0.0094  69  ARG   C N   
1561 C CA  . ARG   B 63  ? 0.3046 0.2236 0.2076 -0.0022 -0.0254 0.0099  69  ARG   C CA  
1562 C C   . ARG   B 63  ? 0.3217 0.2404 0.2285 -0.0035 -0.0239 0.0117  69  ARG   C C   
1563 O O   . ARG   B 63  ? 0.3598 0.2701 0.2628 -0.0040 -0.0290 0.0143  69  ARG   C O   
1564 C CB  . ARG   B 63  ? 0.3509 0.2582 0.2419 -0.0027 -0.0330 0.0123  69  ARG   C CB  
1565 C CG  . ARG   B 63  ? 0.4167 0.3238 0.3075 -0.0003 -0.0373 0.0098  69  ARG   C CG  
1566 C CD  . ARG   B 63  ? 0.5185 0.4140 0.4007 -0.0001 -0.0468 0.0122  69  ARG   C CD  
1567 N NE  . ARG   B 63  ? 0.5949 0.4879 0.4698 0.0002  -0.0500 0.0107  69  ARG   C NE  
1568 C CZ  . ARG   B 63  ? 0.6595 0.5435 0.5161 -0.0030 -0.0519 0.0132  69  ARG   C CZ  
1569 N NH1 . ARG   B 63  ? 0.6698 0.5465 0.5138 -0.0070 -0.0506 0.0176  69  ARG   C NH1 
1570 N NH2 . ARG   B 63  ? 0.6658 0.5479 0.5161 -0.0027 -0.0548 0.0111  69  ARG   C NH2 
1571 N N   . LYS   B 64  ? 0.2951 0.2223 0.2083 -0.0045 -0.0171 0.0108  70  LYS   C N   
1572 C CA  . LYS   B 64  ? 0.2938 0.2206 0.2093 -0.0065 -0.0155 0.0125  70  LYS   C CA  
1573 C C   . LYS   B 64  ? 0.2610 0.1981 0.1884 -0.0054 -0.0109 0.0100  70  LYS   C C   
1574 O O   . LYS   B 64  ? 0.2584 0.2029 0.1899 -0.0045 -0.0073 0.0079  70  LYS   C O   
1575 C CB  . LYS   B 64  ? 0.3449 0.2691 0.2498 -0.0115 -0.0109 0.0159  70  LYS   C CB  
1576 C CG  . LYS   B 64  ? 0.4916 0.4039 0.3842 -0.0144 -0.0149 0.0201  70  LYS   C CG  
1577 C CD  . LYS   B 64  ? 0.5972 0.5097 0.4819 -0.0198 -0.0085 0.0228  70  LYS   C CD  
1578 C CE  . LYS   B 64  ? 0.6768 0.5772 0.5464 -0.0238 -0.0113 0.0275  70  LYS   C CE  
1579 N NZ  . LYS   B 64  ? 0.7205 0.6222 0.5803 -0.0288 -0.0041 0.0292  70  LYS   C NZ  
1580 N N   . HIS   B 65  ? 0.2453 0.1820 0.1774 -0.0059 -0.0113 0.0102  71  HIS   C N   
1581 C CA  . HIS   B 65  ? 0.2440 0.1892 0.1851 -0.0059 -0.0073 0.0084  71  HIS   C CA  
1582 C C   . HIS   B 65  ? 0.2672 0.2139 0.2051 -0.0101 -0.0028 0.0108  71  HIS   C C   
1583 O O   . HIS   B 65  ? 0.2967 0.2363 0.2272 -0.0131 -0.0037 0.0139  71  HIS   C O   
1584 C CB  . HIS   B 65  ? 0.2533 0.1970 0.2012 -0.0041 -0.0104 0.0066  71  HIS   C CB  
1585 C CG  . HIS   B 65  ? 0.2610 0.2046 0.2146 -0.0001 -0.0144 0.0037  71  HIS   C CG  
1586 N ND1 . HIS   B 65  ? 0.2900 0.2414 0.2527 0.0021  -0.0125 0.0003  71  HIS   C ND1 
1587 C CD2 . HIS   B 65  ? 0.2742 0.2106 0.2261 0.0019  -0.0203 0.0039  71  HIS   C CD2 
1588 C CE1 . HIS   B 65  ? 0.2712 0.2209 0.2383 0.0053  -0.0167 -0.0018 71  HIS   C CE1 
1589 N NE2 . HIS   B 65  ? 0.2986 0.2394 0.2600 0.0055  -0.0218 0.0002  71  HIS   C NE2 
1590 N N   . TYR   B 66  ? 0.2373 0.1928 0.1811 -0.0105 0.0018  0.0097  72  TYR   C N   
1591 C CA  . TYR   B 66  ? 0.2363 0.1950 0.1799 -0.0143 0.0060  0.0115  72  TYR   C CA  
1592 C C   . TYR   B 66  ? 0.2251 0.1899 0.1772 -0.0144 0.0071  0.0102  72  TYR   C C   
1593 O O   . TYR   B 66  ? 0.2161 0.1864 0.1742 -0.0119 0.0073  0.0079  72  TYR   C O   
1594 C CB  . TYR   B 66  ? 0.2392 0.2034 0.1818 -0.0150 0.0108  0.0115  72  TYR   C CB  
1595 C CG  . TYR   B 66  ? 0.2854 0.2437 0.2174 -0.0161 0.0111  0.0128  72  TYR   C CG  
1596 C CD1 . TYR   B 66  ? 0.3159 0.2693 0.2399 -0.0203 0.0127  0.0158  72  TYR   C CD1 
1597 C CD2 . TYR   B 66  ? 0.3149 0.2730 0.2446 -0.0135 0.0103  0.0110  72  TYR   C CD2 
1598 C CE1 . TYR   B 66  ? 0.3487 0.2964 0.2613 -0.0219 0.0133  0.0171  72  TYR   C CE1 
1599 C CE2 . TYR   B 66  ? 0.3458 0.2981 0.2644 -0.0148 0.0103  0.0120  72  TYR   C CE2 
1600 C CZ  . TYR   B 66  ? 0.3760 0.3230 0.2854 -0.0191 0.0120  0.0151  72  TYR   C CZ  
1601 O OH  . TYR   B 66  ? 0.4138 0.3545 0.3103 -0.0211 0.0124  0.0163  72  TYR   C OH  
1602 N N   . PRO   B 67  ? 0.2274 0.1907 0.1794 -0.0177 0.0075  0.0118  73  PRO   C N   
1603 C CA  . PRO   B 67  ? 0.2222 0.1913 0.1814 -0.0184 0.0083  0.0106  73  PRO   C CA  
1604 C C   . PRO   B 67  ? 0.2323 0.2102 0.1960 -0.0194 0.0125  0.0110  73  PRO   C C   
1605 O O   . PRO   B 67  ? 0.2419 0.2204 0.2030 -0.0216 0.0155  0.0126  73  PRO   C O   
1606 C CB  . PRO   B 67  ? 0.2325 0.1964 0.1897 -0.0219 0.0071  0.0124  73  PRO   C CB  
1607 C CG  . PRO   B 67  ? 0.2390 0.1977 0.1888 -0.0244 0.0081  0.0154  73  PRO   C CG  
1608 C CD  . PRO   B 67  ? 0.2246 0.1807 0.1696 -0.0214 0.0071  0.0149  73  PRO   C CD  
1609 N N   . VAL   B 68  ? 0.2057 0.1902 0.1758 -0.0179 0.0128  0.0093  74  VAL   C N   
1610 C CA  . VAL   B 68  ? 0.2245 0.2171 0.2004 -0.0183 0.0158  0.0096  74  VAL   C CA  
1611 C C   . VAL   B 68  ? 0.2108 0.2085 0.1929 -0.0190 0.0147  0.0091  74  VAL   C C   
1612 O O   . VAL   B 68  ? 0.2201 0.2160 0.2017 -0.0181 0.0122  0.0078  74  VAL   C O   
1613 C CB  . VAL   B 68  ? 0.2607 0.2561 0.2377 -0.0151 0.0170  0.0084  74  VAL   C CB  
1614 C CG1 . VAL   B 68  ? 0.2907 0.2823 0.2613 -0.0150 0.0187  0.0088  74  VAL   C CG1 
1615 C CG2 . VAL   B 68  ? 0.2658 0.2605 0.2437 -0.0122 0.0144  0.0066  74  VAL   C CG2 
1616 N N   . SER   B 69  ? 0.2059 0.2101 0.1941 -0.0205 0.0166  0.0100  75  SER   C N   
1617 C CA  . SER   B 69  ? 0.2026 0.2123 0.1970 -0.0206 0.0151  0.0099  75  SER   C CA  
1618 C C   . SER   B 69  ? 0.1788 0.1925 0.1766 -0.0174 0.0160  0.0093  75  SER   C C   
1619 O O   . SER   B 69  ? 0.1871 0.2017 0.1852 -0.0162 0.0187  0.0091  75  SER   C O   
1620 C CB  . SER   B 69  ? 0.2497 0.2645 0.2504 -0.0237 0.0160  0.0112  75  SER   C CB  
1621 O OG  . SER   B 69  ? 0.3138 0.3248 0.3119 -0.0271 0.0151  0.0119  75  SER   C OG  
1622 N N   . PHE   B 70  ? 0.1710 0.1867 0.1709 -0.0164 0.0137  0.0090  76  PHE   C N   
1623 C CA  . PHE   B 70  ? 0.1614 0.1800 0.1647 -0.0137 0.0140  0.0088  76  PHE   C CA  
1624 C C   . PHE   B 70  ? 0.1634 0.1861 0.1716 -0.0142 0.0114  0.0100  76  PHE   C C   
1625 O O   . PHE   B 70  ? 0.1642 0.1866 0.1712 -0.0164 0.0092  0.0104  76  PHE   C O   
1626 C CB  . PHE   B 70  ? 0.1575 0.1721 0.1560 -0.0114 0.0137  0.0075  76  PHE   C CB  
1627 C CG  . PHE   B 70  ? 0.1603 0.1718 0.1546 -0.0120 0.0117  0.0066  76  PHE   C CG  
1628 C CD1 . PHE   B 70  ? 0.1766 0.1832 0.1662 -0.0126 0.0115  0.0056  76  PHE   C CD1 
1629 C CD2 . PHE   B 70  ? 0.1702 0.1832 0.1649 -0.0120 0.0103  0.0065  76  PHE   C CD2 
1630 C CE1 . PHE   B 70  ? 0.1885 0.1924 0.1754 -0.0128 0.0100  0.0039  76  PHE   C CE1 
1631 C CE2 . PHE   B 70  ? 0.1786 0.1891 0.1694 -0.0126 0.0094  0.0050  76  PHE   C CE2 
1632 C CZ  . PHE   B 70  ? 0.1807 0.1870 0.1681 -0.0128 0.0094  0.0033  76  PHE   C CZ  
1633 N N   . SER   B 71  ? 0.1546 0.1805 0.1682 -0.0123 0.0115  0.0104  77  SER   C N   
1634 C CA  . SER   B 71  ? 0.1707 0.2000 0.1894 -0.0127 0.0083  0.0121  77  SER   C CA  
1635 C C   . SER   B 71  ? 0.1835 0.2101 0.1969 -0.0129 0.0058  0.0126  77  SER   C C   
1636 O O   . SER   B 71  ? 0.1930 0.2160 0.2002 -0.0126 0.0069  0.0112  77  SER   C O   
1637 C CB  . SER   B 71  ? 0.1830 0.2160 0.2100 -0.0102 0.0090  0.0123  77  SER   C CB  
1638 O OG  . SER   B 71  ? 0.2046 0.2350 0.2293 -0.0078 0.0099  0.0114  77  SER   C OG  
1639 N N   . LYS   B 72  ? 0.1690 0.1976 0.1850 -0.0139 0.0023  0.0146  78  LYS   C N   
1640 C CA  . LYS   B 72  ? 0.1770 0.2030 0.1872 -0.0147 0.0004  0.0154  78  LYS   C CA  
1641 C C   . LYS   B 72  ? 0.1917 0.2170 0.2038 -0.0122 0.0012  0.0158  78  LYS   C C   
1642 O O   . LYS   B 72  ? 0.2214 0.2487 0.2406 -0.0100 0.0016  0.0160  78  LYS   C O   
1643 C CB  . LYS   B 72  ? 0.2092 0.2367 0.2204 -0.0170 -0.0043 0.0180  78  LYS   C CB  
1644 C CG  . LYS   B 72  ? 0.2616 0.2894 0.2707 -0.0198 -0.0056 0.0173  78  LYS   C CG  
1645 C CD  . LYS   B 72  ? 0.3703 0.3989 0.3791 -0.0222 -0.0111 0.0198  78  LYS   C CD  
1646 C CE  . LYS   B 72  ? 0.4552 0.4845 0.4638 -0.0250 -0.0131 0.0192  78  LYS   C CE  
1647 N NZ  . LYS   B 72  ? 0.5263 0.5583 0.5397 -0.0266 -0.0190 0.0220  78  LYS   C NZ  
1648 N N   . PRO   B 73  ? 0.1895 0.2120 0.1958 -0.0127 0.0014  0.0157  79  PRO   C N   
1649 C CA  . PRO   B 73  ? 0.1964 0.2178 0.2047 -0.0109 0.0020  0.0162  79  PRO   C CA  
1650 C C   . PRO   B 73  ? 0.2142 0.2368 0.2287 -0.0102 -0.0013 0.0191  79  PRO   C C   
1651 O O   . PRO   B 73  ? 0.2254 0.2483 0.2392 -0.0123 -0.0049 0.0217  79  PRO   C O   
1652 C CB  . PRO   B 73  ? 0.2076 0.2265 0.2087 -0.0128 0.0026  0.0160  79  PRO   C CB  
1653 C CG  . PRO   B 73  ? 0.2329 0.2514 0.2285 -0.0146 0.0035  0.0142  79  PRO   C CG  
1654 C CD  . PRO   B 73  ? 0.1952 0.2154 0.1932 -0.0152 0.0017  0.0147  79  PRO   C CD  
1655 N N   . SER   B 74  ? 0.2203 0.2434 0.2413 -0.0073 -0.0003 0.0184  80  SER   C N   
1656 C CA  . SER   B 74  ? 0.2403 0.2644 0.2691 -0.0060 -0.0035 0.0206  80  SER   C CA  
1657 C C   . SER   B 74  ? 0.2188 0.2413 0.2523 -0.0031 -0.0025 0.0196  80  SER   C C   
1658 O O   . SER   B 74  ? 0.1896 0.2104 0.2199 -0.0023 0.0007  0.0171  80  SER   C O   
1659 C CB  . SER   B 74  ? 0.2977 0.3262 0.3339 -0.0054 -0.0042 0.0203  80  SER   C CB  
1660 O OG  . SER   B 74  ? 0.3503 0.3806 0.3897 -0.0033 0.0002  0.0170  80  SER   C OG  
1661 N N   . LEU   B 75  ? 0.2145 0.2371 0.2558 -0.0016 -0.0058 0.0214  81  LEU   C N   
1662 C CA  . LEU   B 75  ? 0.2247 0.2452 0.2716 0.0012  -0.0056 0.0205  81  LEU   C CA  
1663 C C   . LEU   B 75  ? 0.2216 0.2458 0.2764 0.0044  -0.0026 0.0168  81  LEU   C C   
1664 O O   . LEU   B 75  ? 0.2322 0.2605 0.2948 0.0052  -0.0038 0.0170  81  LEU   C O   
1665 C CB  . LEU   B 75  ? 0.2552 0.2736 0.3073 0.0013  -0.0112 0.0244  81  LEU   C CB  
1666 C CG  . LEU   B 75  ? 0.3230 0.3358 0.3723 0.0003  -0.0137 0.0272  81  LEU   C CG  
1667 C CD1 . LEU   B 75  ? 0.3489 0.3596 0.4075 0.0022  -0.0189 0.0298  81  LEU   C CD1 
1668 C CD2 . LEU   B 75  ? 0.3300 0.3404 0.3766 0.0010  -0.0100 0.0244  81  LEU   C CD2 
1669 N N   . ILE   B 76  ? 0.1908 0.2138 0.2435 0.0060  0.0014  0.0132  82  ILE   C N   
1670 C CA  . ILE   B 76  ? 0.1990 0.2249 0.2563 0.0083  0.0053  0.0093  82  ILE   C CA  
1671 C C   . ILE   B 76  ? 0.2095 0.2325 0.2697 0.0112  0.0065  0.0063  82  ILE   C C   
1672 O O   . ILE   B 76  ? 0.2103 0.2290 0.2648 0.0108  0.0064  0.0061  82  ILE   C O   
1673 C CB  . ILE   B 76  ? 0.2364 0.2628 0.2853 0.0066  0.0091  0.0076  82  ILE   C CB  
1674 C CG1 . ILE   B 76  ? 0.2776 0.3065 0.3242 0.0037  0.0077  0.0101  82  ILE   C CG1 
1675 C CG2 . ILE   B 76  ? 0.2457 0.2739 0.2959 0.0083  0.0138  0.0036  82  ILE   C CG2 
1676 C CD1 . ILE   B 76  ? 0.3375 0.3657 0.3762 0.0019  0.0101  0.0092  82  ILE   C CD1 
1677 N N   . PHE   B 77  ? 0.2162 0.2417 0.2858 0.0141  0.0078  0.0037  83  PHE   C N   
1678 C CA  . PHE   B 77  ? 0.2321 0.2546 0.3048 0.0170  0.0091  0.0001  83  PHE   C CA  
1679 C C   . PHE   B 77  ? 0.2280 0.2489 0.2918 0.0168  0.0137  -0.0037 83  PHE   C C   
1680 O O   . PHE   B 77  ? 0.2298 0.2538 0.2901 0.0159  0.0174  -0.0051 83  PHE   C O   
1681 C CB  . PHE   B 77  ? 0.2426 0.2688 0.3284 0.0204  0.0099  -0.0025 83  PHE   C CB  
1682 C CG  . PHE   B 77  ? 0.2635 0.2863 0.3526 0.0236  0.0115  -0.0071 83  PHE   C CG  
1683 C CD1 . PHE   B 77  ? 0.2906 0.3151 0.3782 0.0249  0.0173  -0.0126 83  PHE   C CD1 
1684 C CD2 . PHE   B 77  ? 0.2939 0.3111 0.3859 0.0249  0.0072  -0.0059 83  PHE   C CD2 
1685 C CE1 . PHE   B 77  ? 0.3119 0.3327 0.4013 0.0277  0.0188  -0.0174 83  PHE   C CE1 
1686 C CE2 . PHE   B 77  ? 0.3075 0.3210 0.4024 0.0277  0.0084  -0.0105 83  PHE   C CE2 
1687 C CZ  . PHE   B 77  ? 0.3082 0.3237 0.4018 0.0293  0.0142  -0.0165 83  PHE   C CZ  
1688 N N   . VAL   B 78  ? 0.2266 0.2423 0.2864 0.0174  0.0129  -0.0050 84  VAL   C N   
1689 C CA  . VAL   B 78  ? 0.2229 0.2359 0.2739 0.0173  0.0159  -0.0084 84  VAL   C CA  
1690 C C   . VAL   B 78  ? 0.2285 0.2381 0.2831 0.0201  0.0163  -0.0125 84  VAL   C C   
1691 O O   . VAL   B 78  ? 0.2162 0.2224 0.2752 0.0209  0.0128  -0.0115 84  VAL   C O   
1692 C CB  . VAL   B 78  ? 0.2240 0.2338 0.2667 0.0149  0.0139  -0.0062 84  VAL   C CB  
1693 C CG1 . VAL   B 78  ? 0.2249 0.2316 0.2591 0.0149  0.0158  -0.0096 84  VAL   C CG1 
1694 C CG2 . VAL   B 78  ? 0.2183 0.2309 0.2579 0.0122  0.0133  -0.0025 84  VAL   C CG2 
1695 N N   . GLU   B 79  ? 0.2389 0.2488 0.2908 0.0213  0.0206  -0.0173 85  GLU   C N   
1696 C CA  . GLU   B 79  ? 0.2522 0.2588 0.3063 0.0239  0.0216  -0.0223 85  GLU   C CA  
1697 C C   . GLU   B 79  ? 0.2362 0.2363 0.2846 0.0234  0.0185  -0.0226 85  GLU   C C   
1698 O O   . GLU   B 79  ? 0.2349 0.2337 0.2755 0.0210  0.0171  -0.0203 85  GLU   C O   
1699 C CB  . GLU   B 79  ? 0.2954 0.3032 0.3440 0.0243  0.0274  -0.0273 85  GLU   C CB  
1700 C CG  . GLU   B 79  ? 0.3887 0.4034 0.4417 0.0241  0.0317  -0.0275 85  GLU   C CG  
1701 C CD  . GLU   B 79  ? 0.5046 0.5230 0.5717 0.0274  0.0333  -0.0305 85  GLU   C CD  
1702 O OE1 . GLU   B 79  ? 0.5458 0.5709 0.6201 0.0271  0.0354  -0.0297 85  GLU   C OE1 
1703 O OE2 . GLU   B 79  ? 0.5160 0.5308 0.5879 0.0302  0.0320  -0.0338 85  GLU   C OE2 
1704 N N   . ALA   B 80  ? 0.2373 0.2332 0.2902 0.0257  0.0173  -0.0261 86  ALA   C N   
1705 C CA  . ALA   B 80  ? 0.2305 0.2203 0.2792 0.0250  0.0142  -0.0269 86  ALA   C CA  
1706 C C   . ALA   B 80  ? 0.2343 0.2222 0.2707 0.0237  0.0158  -0.0294 86  ALA   C C   
1707 O O   . ALA   B 80  ? 0.2430 0.2324 0.2739 0.0240  0.0199  -0.0324 86  ALA   C O   
1708 C CB  . ALA   B 80  ? 0.2260 0.2113 0.2812 0.0279  0.0132  -0.0312 86  ALA   C CB  
1709 N N   . SER   B 81  ? 0.2098 0.1944 0.2419 0.0219  0.0124  -0.0280 87  SER   C N   
1710 C CA  . SER   B 81  ? 0.2188 0.2005 0.2401 0.0208  0.0122  -0.0302 87  SER   C CA  
1711 C C   . SER   B 81  ? 0.2343 0.2108 0.2570 0.0206  0.0079  -0.0315 87  SER   C C   
1712 O O   . SER   B 81  ? 0.2503 0.2255 0.2818 0.0211  0.0059  -0.0306 87  SER   C O   
1713 C CB  . SER   B 81  ? 0.2241 0.2086 0.2400 0.0185  0.0119  -0.0263 87  SER   C CB  
1714 O OG  . SER   B 81  ? 0.2322 0.2175 0.2531 0.0171  0.0088  -0.0224 87  SER   C OG  
1715 N N   . GLU   B 82  ? 0.2405 0.2136 0.2551 0.0196  0.0062  -0.0337 88  GLU   C N   
1716 C CA  . GLU   B 82  ? 0.2623 0.2312 0.2792 0.0190  0.0017  -0.0347 88  GLU   C CA  
1717 C C   . GLU   B 82  ? 0.2557 0.2272 0.2795 0.0170  -0.0008 -0.0296 88  GLU   C C   
1718 O O   . GLU   B 82  ? 0.2588 0.2277 0.2883 0.0161  -0.0038 -0.0296 88  GLU   C O   
1719 C CB  . GLU   B 82  ? 0.3356 0.3009 0.3428 0.0182  -0.0006 -0.0376 88  GLU   C CB  
1720 C CG  . GLU   B 82  ? 0.4572 0.4247 0.4562 0.0170  0.0002  -0.0354 88  GLU   C CG  
1721 C CD  . GLU   B 82  ? 0.5965 0.5637 0.5863 0.0177  0.0044  -0.0375 88  GLU   C CD  
1722 O OE1 . GLU   B 82  ? 0.6570 0.6194 0.6372 0.0177  0.0037  -0.0414 88  GLU   C OE1 
1723 O OE2 . GLU   B 82  ? 0.5752 0.5468 0.5673 0.0179  0.0084  -0.0354 88  GLU   C OE2 
1724 N N   . TYR   B 83  ? 0.2390 0.2154 0.2623 0.0159  0.0008  -0.0256 89  TYR   C N   
1725 C CA  . TYR   B 83  ? 0.2377 0.2168 0.2656 0.0136  -0.0006 -0.0212 89  TYR   C CA  
1726 C C   . TYR   B 83  ? 0.2360 0.2167 0.2711 0.0132  -0.0002 -0.0175 89  TYR   C C   
1727 O O   . TYR   B 83  ? 0.2582 0.2396 0.2973 0.0109  -0.0017 -0.0144 89  TYR   C O   
1728 C CB  . TYR   B 83  ? 0.2342 0.2171 0.2569 0.0126  0.0006  -0.0192 89  TYR   C CB  
1729 C CG  . TYR   B 83  ? 0.2579 0.2385 0.2730 0.0129  -0.0007 -0.0220 89  TYR   C CG  
1730 C CD1 . TYR   B 83  ? 0.2810 0.2601 0.2971 0.0119  -0.0043 -0.0229 89  TYR   C CD1 
1731 C CD2 . TYR   B 83  ? 0.2740 0.2538 0.2809 0.0138  0.0014  -0.0235 89  TYR   C CD2 
1732 C CE1 . TYR   B 83  ? 0.3030 0.2796 0.3121 0.0122  -0.0065 -0.0251 89  TYR   C CE1 
1733 C CE2 . TYR   B 83  ? 0.3038 0.2805 0.3024 0.0137  -0.0005 -0.0254 89  TYR   C CE2 
1734 C CZ  . TYR   B 83  ? 0.3226 0.2976 0.3223 0.0131  -0.0048 -0.0261 89  TYR   C CZ  
1735 O OH  . TYR   B 83  ? 0.3718 0.3433 0.3635 0.0130  -0.0077 -0.0276 89  TYR   C OH  
1736 N N   . TYR   B 84  ? 0.2105 0.1920 0.2475 0.0151  0.0017  -0.0177 90  TYR   C N   
1737 C CA  . TYR   B 84  ? 0.2066 0.1896 0.2502 0.0148  0.0013  -0.0137 90  TYR   C CA  
1738 C C   . TYR   B 84  ? 0.2268 0.2083 0.2757 0.0178  0.0019  -0.0160 90  TYR   C C   
1739 O O   . TYR   B 84  ? 0.2217 0.2040 0.2680 0.0199  0.0046  -0.0200 90  TYR   C O   
1740 C CB  . TYR   B 84  ? 0.2002 0.1885 0.2416 0.0137  0.0031  -0.0101 90  TYR   C CB  
1741 C CG  . TYR   B 84  ? 0.2002 0.1907 0.2377 0.0109  0.0029  -0.0077 90  TYR   C CG  
1742 C CD1 . TYR   B 84  ? 0.2092 0.2017 0.2403 0.0108  0.0045  -0.0088 90  TYR   C CD1 
1743 C CD2 . TYR   B 84  ? 0.2000 0.1903 0.2402 0.0083  0.0013  -0.0042 90  TYR   C CD2 
1744 C CE1 . TYR   B 84  ? 0.2037 0.1982 0.2324 0.0086  0.0043  -0.0071 90  TYR   C CE1 
1745 C CE2 . TYR   B 84  ? 0.2019 0.1947 0.2392 0.0058  0.0019  -0.0027 90  TYR   C CE2 
1746 C CZ  . TYR   B 84  ? 0.2047 0.1998 0.2369 0.0063  0.0033  -0.0044 90  TYR   C CZ  
1747 O OH  . TYR   B 84  ? 0.2014 0.1989 0.2321 0.0043  0.0037  -0.0035 90  TYR   C OH  
1748 N N   . PRO   B 85  ? 0.2386 0.2185 0.2951 0.0179  -0.0004 -0.0132 91  PRO   C N   
1749 C CA  . PRO   B 85  ? 0.2341 0.2137 0.2976 0.0212  0.0000  -0.0150 91  PRO   C CA  
1750 C C   . PRO   B 85  ? 0.2399 0.2257 0.3035 0.0218  0.0026  -0.0136 91  PRO   C C   
1751 O O   . PRO   B 85  ? 0.2318 0.2211 0.2908 0.0193  0.0031  -0.0101 91  PRO   C O   
1752 C CB  . PRO   B 85  ? 0.2487 0.2246 0.3197 0.0204  -0.0043 -0.0108 91  PRO   C CB  
1753 C CG  . PRO   B 85  ? 0.2543 0.2317 0.3209 0.0162  -0.0054 -0.0052 91  PRO   C CG  
1754 C CD  . PRO   B 85  ? 0.2256 0.2043 0.2846 0.0149  -0.0034 -0.0078 91  PRO   C CD  
1755 N N   . ALA   B 86  ? 0.2358 0.2234 0.3059 0.0249  0.0042  -0.0162 92  ALA   C N   
1756 C CA  . ALA   B 86  ? 0.2421 0.2359 0.3152 0.0254  0.0061  -0.0147 92  ALA   C CA  
1757 C C   . ALA   B 86  ? 0.2426 0.2370 0.3188 0.0233  0.0019  -0.0079 92  ALA   C C   
1758 O O   . ALA   B 86  ? 0.2450 0.2347 0.3258 0.0232  -0.0022 -0.0056 92  ALA   C O   
1759 C CB  . ALA   B 86  ? 0.2366 0.2318 0.3197 0.0294  0.0077  -0.0189 92  ALA   C CB  
1760 N N   . ARG   B 87  ? 0.2366 0.2354 0.3083 0.0209  0.0027  -0.0047 93  ARG   C N   
1761 C CA  . ARG   B 87  ? 0.2307 0.2293 0.3024 0.0183  -0.0012 0.0015  93  ARG   C CA  
1762 C C   . ARG   B 87  ? 0.2334 0.2376 0.3019 0.0166  0.0000  0.0038  93  ARG   C C   
1763 O O   . ARG   B 87  ? 0.2353 0.2432 0.3011 0.0171  0.0039  0.0008  93  ARG   C O   
1764 C CB  . ARG   B 87  ? 0.2273 0.2221 0.2921 0.0151  -0.0024 0.0036  93  ARG   C CB  
1765 C CG  . ARG   B 87  ? 0.2145 0.2121 0.2697 0.0130  0.0007  0.0028  93  ARG   C CG  
1766 C CD  . ARG   B 87  ? 0.2210 0.2155 0.2716 0.0115  0.0008  0.0016  93  ARG   C CD  
1767 N NE  . ARG   B 87  ? 0.2139 0.2107 0.2578 0.0087  0.0020  0.0030  93  ARG   C NE  
1768 C CZ  . ARG   B 87  ? 0.2253 0.2246 0.2640 0.0089  0.0045  0.0009  93  ARG   C CZ  
1769 N NH1 . ARG   B 87  ? 0.2081 0.2089 0.2418 0.0066  0.0051  0.0020  93  ARG   C NH1 
1770 N NH2 . ARG   B 87  ? 0.2197 0.2198 0.2580 0.0113  0.0065  -0.0024 93  ARG   C NH2 
1771 N N   . TYR   B 88  ? 0.2363 0.2406 0.3041 0.0141  -0.0034 0.0090  94  TYR   C N   
1772 C CA  . TYR   B 88  ? 0.2406 0.2494 0.3042 0.0119  -0.0027 0.0110  94  TYR   C CA  
1773 C C   . TYR   B 88  ? 0.2124 0.2199 0.2657 0.0086  -0.0015 0.0121  94  TYR   C C   
1774 O O   . TYR   B 88  ? 0.2134 0.2173 0.2644 0.0067  -0.0035 0.0146  94  TYR   C O   
1775 C CB  . TYR   B 88  ? 0.2654 0.2746 0.3328 0.0108  -0.0074 0.0159  94  TYR   C CB  
1776 C CG  . TYR   B 88  ? 0.2991 0.3109 0.3785 0.0143  -0.0087 0.0146  94  TYR   C CG  
1777 C CD1 . TYR   B 88  ? 0.3217 0.3398 0.4048 0.0149  -0.0069 0.0132  94  TYR   C CD1 
1778 C CD2 . TYR   B 88  ? 0.3339 0.3422 0.4219 0.0172  -0.0113 0.0140  94  TYR   C CD2 
1779 C CE1 . TYR   B 88  ? 0.3428 0.3644 0.4387 0.0182  -0.0075 0.0113  94  TYR   C CE1 
1780 C CE2 . TYR   B 88  ? 0.3533 0.3645 0.4541 0.0209  -0.0121 0.0119  94  TYR   C CE2 
1781 C CZ  . TYR   B 88  ? 0.3681 0.3864 0.4731 0.0214  -0.0100 0.0105  94  TYR   C CZ  
1782 O OH  . TYR   B 88  ? 0.4249 0.4469 0.5441 0.0252  -0.0104 0.0079  94  TYR   C OH  
1783 N N   . GLN   B 89  ? 0.1796 0.1898 0.2272 0.0080  0.0018  0.0101  95  GLN   C N   
1784 C CA  . GLN   B 89  ? 0.1744 0.1840 0.2137 0.0053  0.0029  0.0106  95  GLN   C CA  
1785 C C   . GLN   B 89  ? 0.1902 0.2022 0.2263 0.0026  0.0018  0.0138  95  GLN   C C   
1786 O O   . GLN   B 89  ? 0.2028 0.2180 0.2407 0.0031  0.0021  0.0137  95  GLN   C O   
1787 C CB  . GLN   B 89  ? 0.1822 0.1923 0.2170 0.0061  0.0063  0.0067  95  GLN   C CB  
1788 C CG  . GLN   B 89  ? 0.1905 0.2002 0.2183 0.0038  0.0070  0.0070  95  GLN   C CG  
1789 C CD  . GLN   B 89  ? 0.1894 0.1979 0.2137 0.0049  0.0088  0.0034  95  GLN   C CD  
1790 O OE1 . GLN   B 89  ? 0.1979 0.2042 0.2237 0.0068  0.0090  0.0010  95  GLN   C OE1 
1791 N NE2 . GLN   B 89  ? 0.1780 0.1873 0.1972 0.0038  0.0098  0.0030  95  GLN   C NE2 
1792 N N   . SER   B 90  ? 0.1879 0.1984 0.2191 -0.0003 0.0007  0.0163  96  SER   C N   
1793 C CA  . SER   B 90  ? 0.1881 0.2000 0.2146 -0.0032 -0.0004 0.0190  96  SER   C CA  
1794 C C   . SER   B 90  ? 0.1776 0.1910 0.1976 -0.0046 0.0025  0.0168  96  SER   C C   
1795 O O   . SER   B 90  ? 0.1809 0.1937 0.1996 -0.0036 0.0049  0.0139  96  SER   C O   
1796 C CB  . SER   B 90  ? 0.2004 0.2095 0.2242 -0.0062 -0.0031 0.0231  96  SER   C CB  
1797 O OG  . SER   B 90  ? 0.2358 0.2431 0.2560 -0.0078 -0.0010 0.0223  96  SER   C OG  
1798 N N   . HIS   B 91  ? 0.1776 0.1926 0.1938 -0.0067 0.0018  0.0181  97  HIS   C N   
1799 C CA  . HIS   B 91  ? 0.1635 0.1793 0.1736 -0.0081 0.0040  0.0163  97  HIS   C CA  
1800 C C   . HIS   B 91  ? 0.1828 0.1994 0.1943 -0.0058 0.0063  0.0129  97  HIS   C C   
1801 O O   . HIS   B 91  ? 0.2008 0.2167 0.2086 -0.0059 0.0082  0.0107  97  HIS   C O   
1802 C CB  . HIS   B 91  ? 0.1773 0.1918 0.1828 -0.0101 0.0056  0.0157  97  HIS   C CB  
1803 C CG  . HIS   B 91  ? 0.2018 0.2150 0.2037 -0.0134 0.0039  0.0192  97  HIS   C CG  
1804 N ND1 . HIS   B 91  ? 0.2462 0.2596 0.2411 -0.0165 0.0040  0.0198  97  HIS   C ND1 
1805 C CD2 . HIS   B 91  ? 0.2326 0.2436 0.2362 -0.0141 0.0020  0.0222  97  HIS   C CD2 
1806 C CE1 . HIS   B 91  ? 0.2483 0.2598 0.2399 -0.0194 0.0022  0.0234  97  HIS   C CE1 
1807 N NE2 . HIS   B 91  ? 0.2531 0.2629 0.2501 -0.0181 0.0007  0.0253  97  HIS   C NE2 
1808 N N   . LEU   B 92  ? 0.1728 0.1907 0.1895 -0.0037 0.0062  0.0126  98  LEU   C N   
1809 C CA  . LEU   B 92  ? 0.1742 0.1923 0.1909 -0.0020 0.0087  0.0098  98  LEU   C CA  
1810 C C   . LEU   B 92  ? 0.1783 0.1988 0.1949 -0.0031 0.0090  0.0101  98  LEU   C C   
1811 O O   . LEU   B 92  ? 0.1804 0.2034 0.2011 -0.0038 0.0071  0.0121  98  LEU   C O   
1812 C CB  . LEU   B 92  ? 0.1792 0.1973 0.2014 0.0007  0.0093  0.0086  98  LEU   C CB  
1813 C CG  . LEU   B 92  ? 0.2013 0.2189 0.2220 0.0023  0.0122  0.0056  98  LEU   C CG  
1814 C CD1 . LEU   B 92  ? 0.2066 0.2209 0.2213 0.0023  0.0127  0.0039  98  LEU   C CD1 
1815 C CD2 . LEU   B 92  ? 0.2313 0.2489 0.2574 0.0048  0.0130  0.0039  98  LEU   C CD2 
1816 N N   . MET   B 93  ? 0.1712 0.1906 0.1835 -0.0034 0.0109  0.0084  99  MET   C N   
1817 C CA  . MET   B 93  ? 0.1709 0.1918 0.1827 -0.0049 0.0114  0.0086  99  MET   C CA  
1818 C C   . MET   B 93  ? 0.1868 0.2075 0.1986 -0.0039 0.0142  0.0070  99  MET   C C   
1819 O O   . MET   B 93  ? 0.1925 0.2100 0.2003 -0.0028 0.0152  0.0055  99  MET   C O   
1820 C CB  . MET   B 93  ? 0.1811 0.1998 0.1868 -0.0067 0.0110  0.0082  99  MET   C CB  
1821 C CG  . MET   B 93  ? 0.1962 0.2149 0.2002 -0.0082 0.0090  0.0093  99  MET   C CG  
1822 S SD  . MET   B 93  ? 0.2364 0.2524 0.2336 -0.0098 0.0093  0.0075  99  MET   C SD  
1823 C CE  . MET   B 93  ? 0.2040 0.2174 0.2003 -0.0074 0.0110  0.0050  99  MET   C CE  
1824 N N   . LEU   B 94  ? 0.1662 0.1903 0.1825 -0.0044 0.0154  0.0074  100 LEU   C N   
1825 C CA  . LEU   B 94  ? 0.1734 0.1975 0.1889 -0.0041 0.0189  0.0059  100 LEU   C CA  
1826 C C   . LEU   B 94  ? 0.1828 0.2061 0.1945 -0.0068 0.0200  0.0064  100 LEU   C C   
1827 O O   . LEU   B 94  ? 0.1832 0.2081 0.1966 -0.0088 0.0183  0.0078  100 LEU   C O   
1828 C CB  . LEU   B 94  ? 0.1848 0.2138 0.2092 -0.0029 0.0207  0.0052  100 LEU   C CB  
1829 C CG  . LEU   B 94  ? 0.2031 0.2323 0.2325 0.0000  0.0195  0.0046  100 LEU   C CG  
1830 C CD1 . LEU   B 94  ? 0.2079 0.2420 0.2472 0.0017  0.0217  0.0031  100 LEU   C CD1 
1831 C CD2 . LEU   B 94  ? 0.2188 0.2431 0.2418 0.0016  0.0203  0.0026  100 LEU   C CD2 
1832 N N   . ALA   B 95  ? 0.1861 0.2061 0.1919 -0.0071 0.0224  0.0054  101 ALA   C N   
1833 C CA  . ALA   B 95  ? 0.1902 0.2086 0.1920 -0.0100 0.0239  0.0062  101 ALA   C CA  
1834 C C   . ALA   B 95  ? 0.2000 0.2188 0.2000 -0.0103 0.0283  0.0052  101 ALA   C C   
1835 O O   . ALA   B 95  ? 0.2011 0.2195 0.2004 -0.0080 0.0297  0.0034  101 ALA   C O   
1836 C CB  . ALA   B 95  ? 0.1949 0.2066 0.1882 -0.0104 0.0217  0.0064  101 ALA   C CB  
1837 N N   . VAL   B 96  ? 0.1973 0.2169 0.1965 -0.0135 0.0308  0.0062  102 VAL   C N   
1838 C CA  . VAL   B 96  ? 0.2100 0.2291 0.2051 -0.0149 0.0355  0.0054  102 VAL   C CA  
1839 C C   . VAL   B 96  ? 0.2470 0.2570 0.2292 -0.0154 0.0340  0.0061  102 VAL   C C   
1840 O O   . VAL   B 96  ? 0.2562 0.2618 0.2342 -0.0174 0.0315  0.0080  102 VAL   C O   
1841 C CB  . VAL   B 96  ? 0.2308 0.2542 0.2303 -0.0188 0.0387  0.0066  102 VAL   C CB  
1842 C CG1 . VAL   B 96  ? 0.2391 0.2615 0.2325 -0.0210 0.0444  0.0059  102 VAL   C CG1 
1843 C CG2 . VAL   B 96  ? 0.2330 0.2656 0.2468 -0.0179 0.0389  0.0059  102 VAL   C CG2 
1844 N N   . GLY   B 97  ? 0.2828 0.2897 0.2593 -0.0136 0.0350  0.0044  103 GLY   C N   
1845 C CA  . GLY   B 97  ? 0.3182 0.3164 0.2830 -0.0139 0.0326  0.0051  103 GLY   C CA  
1846 C C   . GLY   B 97  ? 0.3392 0.3346 0.2988 -0.0116 0.0328  0.0029  103 GLY   C C   
1847 O O   . GLY   B 97  ? 0.3471 0.3470 0.3127 -0.0092 0.0344  0.0005  103 GLY   C O   
1848 N N   . HIS   B 98  ? 0.3274 0.3147 0.2758 -0.0123 0.0305  0.0037  104 HIS   C N   
1849 C CA  . HIS   B 98  ? 0.3252 0.3087 0.2666 -0.0107 0.0301  0.0017  104 HIS   C CA  
1850 C C   . HIS   B 98  ? 0.3169 0.2995 0.2618 -0.0070 0.0255  0.0002  104 HIS   C C   
1851 O O   . HIS   B 98  ? 0.3154 0.2963 0.2626 -0.0061 0.0211  0.0013  104 HIS   C O   
1852 C CB  . HIS   B 98  ? 0.3251 0.2996 0.2520 -0.0133 0.0289  0.0035  104 HIS   C CB  
1853 C CG  . HIS   B 98  ? 0.3342 0.3042 0.2524 -0.0121 0.0283  0.0013  104 HIS   C CG  
1854 N ND1 . HIS   B 98  ? 0.3621 0.3351 0.2785 -0.0124 0.0339  -0.0016 104 HIS   C ND1 
1855 C CD2 . HIS   B 98  ? 0.3303 0.2938 0.2429 -0.0102 0.0225  0.0010  104 HIS   C CD2 
1856 C CE1 . HIS   B 98  ? 0.3671 0.3346 0.2754 -0.0110 0.0312  -0.0035 104 HIS   C CE1 
1857 N NE2 . HIS   B 98  ? 0.3605 0.3222 0.2664 -0.0098 0.0240  -0.0018 104 HIS   C NE2 
1858 N N   . SER   B 99  ? 0.3169 0.3004 0.2618 -0.0050 0.0267  -0.0028 105 SER   C N   
1859 C CA  . SER   B 99  ? 0.3225 0.3043 0.2693 -0.0020 0.0226  -0.0046 105 SER   C CA  
1860 C C   . SER   B 99  ? 0.3224 0.3022 0.2645 -0.0009 0.0239  -0.0079 105 SER   C C   
1861 O O   . SER   B 99  ? 0.3361 0.3186 0.2779 -0.0015 0.0290  -0.0097 105 SER   C O   
1862 C CB  . SER   B 99  ? 0.3390 0.3264 0.2981 0.0000  0.0213  -0.0047 105 SER   C CB  
1863 O OG  . SER   B 99  ? 0.3681 0.3614 0.3346 0.0007  0.0250  -0.0061 105 SER   C OG  
1864 N N   . GLU   B 100 ? 0.3211 0.2960 0.2593 0.0006  0.0192  -0.0089 106 GLU   C N   
1865 C CA  . GLU   B 100 ? 0.3279 0.2998 0.2616 0.0018  0.0187  -0.0123 106 GLU   C CA  
1866 C C   . GLU   B 100 ? 0.3099 0.2831 0.2525 0.0046  0.0144  -0.0135 106 GLU   C C   
1867 O O   . GLU   B 100 ? 0.2958 0.2704 0.2442 0.0050  0.0115  -0.0116 106 GLU   C O   
1868 C CB  . GLU   B 100 ? 0.3864 0.3496 0.3052 0.0003  0.0157  -0.0120 106 GLU   C CB  
1869 C CG  . GLU   B 100 ? 0.4900 0.4507 0.3999 -0.0031 0.0182  -0.0091 106 GLU   C CG  
1870 C CD  . GLU   B 100 ? 0.5892 0.5446 0.4840 -0.0059 0.0213  -0.0097 106 GLU   C CD  
1871 O OE1 . GLU   B 100 ? 0.6151 0.5715 0.5074 -0.0055 0.0251  -0.0135 106 GLU   C OE1 
1872 O OE2 . GLU   B 100 ? 0.6182 0.5683 0.5034 -0.0088 0.0202  -0.0063 106 GLU   C OE2 
1873 N N   . PRO   B 101 ? 0.3308 0.3032 0.2746 0.0062  0.0140  -0.0169 107 PRO   C N   
1874 C CA  . PRO   B 101 ? 0.3422 0.3163 0.2955 0.0082  0.0103  -0.0177 107 PRO   C CA  
1875 C C   . PRO   B 101 ? 0.3421 0.3144 0.2971 0.0084  0.0048  -0.0161 107 PRO   C C   
1876 O O   . PRO   B 101 ? 0.3641 0.3404 0.3289 0.0091  0.0037  -0.0151 107 PRO   C O   
1877 C CB  . PRO   B 101 ? 0.3638 0.3346 0.3140 0.0093  0.0098  -0.0217 107 PRO   C CB  
1878 C CG  . PRO   B 101 ? 0.3690 0.3398 0.3131 0.0085  0.0155  -0.0235 107 PRO   C CG  
1879 C CD  . PRO   B 101 ? 0.3396 0.3102 0.2768 0.0061  0.0176  -0.0203 107 PRO   C CD  
1880 N N   . GLY   B 102 ? 0.3205 0.2869 0.2660 0.0077  0.0013  -0.0157 108 GLY   C N   
1881 C CA  . GLY   B 102 ? 0.2967 0.2611 0.2441 0.0082  -0.0044 -0.0146 108 GLY   C CA  
1882 C C   . GLY   B 102 ? 0.2742 0.2413 0.2262 0.0078  -0.0041 -0.0118 108 GLY   C C   
1883 O O   . GLY   B 102 ? 0.2717 0.2380 0.2272 0.0086  -0.0083 -0.0114 108 GLY   C O   
1884 N N   . ASP   B 103 ? 0.2457 0.2165 0.1987 0.0067  0.0009  -0.0103 109 ASP   C N   
1885 C CA  . ASP   B 103 ? 0.2381 0.2111 0.1949 0.0060  0.0014  -0.0080 109 ASP   C CA  
1886 C C   . ASP   B 103 ? 0.2178 0.1969 0.1861 0.0069  0.0018  -0.0081 109 ASP   C C   
1887 O O   . ASP   B 103 ? 0.2166 0.1971 0.1880 0.0065  0.0015  -0.0069 109 ASP   C O   
1888 C CB  . ASP   B 103 ? 0.2508 0.2250 0.2038 0.0039  0.0060  -0.0061 109 ASP   C CB  
1889 C CG  . ASP   B 103 ? 0.2831 0.2506 0.2238 0.0021  0.0054  -0.0049 109 ASP   C CG  
1890 O OD1 . ASP   B 103 ? 0.2822 0.2440 0.2183 0.0024  0.0004  -0.0043 109 ASP   C OD1 
1891 O OD2 . ASP   B 103 ? 0.2934 0.2615 0.2294 0.0002  0.0099  -0.0043 109 ASP   C OD2 
1892 N N   . CYS   B 104 ? 0.2008 0.1828 0.1749 0.0078  0.0025  -0.0097 110 CYS   C N   
1893 C CA  . CYS   B 104 ? 0.2030 0.1900 0.1867 0.0080  0.0028  -0.0095 110 CYS   C CA  
1894 C C   . CYS   B 104 ? 0.2121 0.1989 0.1991 0.0085  -0.0003 -0.0098 110 CYS   C C   
1895 O O   . CYS   B 104 ? 0.2193 0.2024 0.2041 0.0094  -0.0040 -0.0111 110 CYS   C O   
1896 C CB  . CYS   B 104 ? 0.2120 0.2006 0.2007 0.0087  0.0032  -0.0109 110 CYS   C CB  
1897 S SG  . CYS   B 104 ? 0.2458 0.2362 0.2344 0.0087  0.0073  -0.0107 110 CYS   C SG  
1898 N N   . GLY   B 105 ? 0.1945 0.1850 0.1863 0.0078  0.0012  -0.0089 111 GLY   C N   
1899 C CA  . GLY   B 105 ? 0.2042 0.1955 0.2006 0.0083  -0.0009 -0.0100 111 GLY   C CA  
1900 C C   . GLY   B 105 ? 0.2086 0.1976 0.2017 0.0082  -0.0017 -0.0093 111 GLY   C C   
1901 O O   . GLY   B 105 ? 0.2113 0.2016 0.2091 0.0086  -0.0024 -0.0104 111 GLY   C O   
1902 N N   . GLY   B 106 ? 0.1882 0.1739 0.1738 0.0074  -0.0010 -0.0076 112 GLY   C N   
1903 C CA  . GLY   B 106 ? 0.1852 0.1679 0.1675 0.0068  -0.0018 -0.0066 112 GLY   C CA  
1904 C C   . GLY   B 106 ? 0.1959 0.1830 0.1824 0.0057  0.0010  -0.0063 112 GLY   C C   
1905 O O   . GLY   B 106 ? 0.2050 0.1963 0.1932 0.0046  0.0040  -0.0055 112 GLY   C O   
1906 N N   . ILE   B 107 ? 0.1940 0.1797 0.1822 0.0060  -0.0004 -0.0073 113 ILE   C N   
1907 C CA  . ILE   B 107 ? 0.1933 0.1829 0.1848 0.0048  0.0021  -0.0077 113 ILE   C CA  
1908 C C   . ILE   B 107 ? 0.1877 0.1758 0.1744 0.0028  0.0033  -0.0056 113 ILE   C C   
1909 O O   . ILE   B 107 ? 0.2095 0.1922 0.1915 0.0025  0.0016  -0.0046 113 ILE   C O   
1910 C CB  . ILE   B 107 ? 0.2226 0.2123 0.2195 0.0063  0.0007  -0.0107 113 ILE   C CB  
1911 C CG1 . ILE   B 107 ? 0.2391 0.2332 0.2432 0.0074  0.0009  -0.0128 113 ILE   C CG1 
1912 C CG2 . ILE   B 107 ? 0.2454 0.2368 0.2429 0.0049  0.0029  -0.0116 113 ILE   C CG2 
1913 C CD1 . ILE   B 107 ? 0.2892 0.2841 0.3006 0.0091  -0.0003 -0.0165 113 ILE   C CD1 
1914 N N   . LEU   B 108 ? 0.1672 0.1597 0.1553 0.0011  0.0060  -0.0050 114 LEU   C N   
1915 C CA  . LEU   B 108 ? 0.1802 0.1725 0.1656 -0.0011 0.0070  -0.0035 114 LEU   C CA  
1916 C C   . LEU   B 108 ? 0.1846 0.1774 0.1718 -0.0016 0.0071  -0.0056 114 LEU   C C   
1917 O O   . LEU   B 108 ? 0.1871 0.1837 0.1773 -0.0016 0.0084  -0.0071 114 LEU   C O   
1918 C CB  . LEU   B 108 ? 0.1770 0.1739 0.1634 -0.0026 0.0092  -0.0016 114 LEU   C CB  
1919 C CG  . LEU   B 108 ? 0.1873 0.1854 0.1728 -0.0051 0.0099  -0.0002 114 LEU   C CG  
1920 C CD1 . LEU   B 108 ? 0.2070 0.2014 0.1888 -0.0063 0.0097  0.0012  114 LEU   C CD1 
1921 C CD2 . LEU   B 108 ? 0.1850 0.1882 0.1734 -0.0060 0.0112  0.0015  114 LEU   C CD2 
1922 N N   . ARG   B 109 ? 0.1701 0.1587 0.1549 -0.0023 0.0058  -0.0059 115 ARG   C N   
1923 C CA  . ARG   B 109 ? 0.1867 0.1749 0.1727 -0.0027 0.0058  -0.0085 115 ARG   C CA  
1924 C C   . ARG   B 109 ? 0.1956 0.1826 0.1785 -0.0055 0.0059  -0.0073 115 ARG   C C   
1925 O O   . ARG   B 109 ? 0.1968 0.1808 0.1770 -0.0066 0.0051  -0.0048 115 ARG   C O   
1926 C CB  . ARG   B 109 ? 0.2350 0.2180 0.2226 -0.0003 0.0032  -0.0109 115 ARG   C CB  
1927 C CG  . ARG   B 109 ? 0.3287 0.3137 0.3217 0.0024  0.0028  -0.0134 115 ARG   C CG  
1928 C CD  . ARG   B 109 ? 0.4276 0.4073 0.4237 0.0051  -0.0007 -0.0158 115 ARG   C CD  
1929 N NE  . ARG   B 109 ? 0.5304 0.5141 0.5343 0.0074  -0.0002 -0.0196 115 ARG   C NE  
1930 C CZ  . ARG   B 109 ? 0.5665 0.5513 0.5741 0.0093  -0.0019 -0.0197 115 ARG   C CZ  
1931 N NH1 . ARG   B 109 ? 0.5429 0.5238 0.5458 0.0095  -0.0047 -0.0165 115 ARG   C NH1 
1932 N NH2 . ARG   B 109 ? 0.5886 0.5780 0.6044 0.0109  -0.0010 -0.0232 115 ARG   C NH2 
1933 N N   . CYS   B 110 ? 0.1970 0.1857 0.1800 -0.0067 0.0068  -0.0092 116 CYS   C N   
1934 C CA  . CYS   B 110 ? 0.2178 0.2046 0.1981 -0.0094 0.0061  -0.0089 116 CYS   C CA  
1935 C C   . CYS   B 110 ? 0.2359 0.2184 0.2164 -0.0086 0.0052  -0.0130 116 CYS   C C   
1936 O O   . CYS   B 110 ? 0.2373 0.2190 0.2210 -0.0058 0.0051  -0.0158 116 CYS   C O   
1937 C CB  . CYS   B 110 ? 0.2062 0.1979 0.1855 -0.0119 0.0073  -0.0078 116 CYS   C CB  
1938 S SG  . CYS   B 110 ? 0.1989 0.1940 0.1778 -0.0119 0.0093  -0.0112 116 CYS   C SG  
1939 N N   . GLN   B 111 ? 0.2483 0.2287 0.2264 -0.0110 0.0045  -0.0139 117 GLN   C N   
1940 C CA  . GLN   B 111 ? 0.2668 0.2430 0.2453 -0.0102 0.0038  -0.0185 117 GLN   C CA  
1941 C C   . GLN   B 111 ? 0.2669 0.2469 0.2469 -0.0090 0.0065  -0.0230 117 GLN   C C   
1942 O O   . GLN   B 111 ? 0.2892 0.2666 0.2713 -0.0075 0.0066  -0.0277 117 GLN   C O   
1943 C CB  . GLN   B 111 ? 0.3061 0.2792 0.2812 -0.0135 0.0025  -0.0187 117 GLN   C CB  
1944 C CG  . GLN   B 111 ? 0.3370 0.3152 0.3090 -0.0164 0.0038  -0.0185 117 GLN   C CG  
1945 C CD  . GLN   B 111 ? 0.4409 0.4160 0.4099 -0.0198 0.0017  -0.0186 117 GLN   C CD  
1946 O OE1 . GLN   B 111 ? 0.4703 0.4472 0.4391 -0.0224 0.0006  -0.0148 117 GLN   C OE1 
1947 N NE2 . GLN   B 111 ? 0.4657 0.4362 0.4334 -0.0199 0.0011  -0.0234 117 GLN   C NE2 
1948 N N   . HIS   B 112 ? 0.2409 0.2273 0.2203 -0.0099 0.0089  -0.0217 118 HIS   C N   
1949 C CA  . HIS   B 112 ? 0.2316 0.2221 0.2114 -0.0099 0.0122  -0.0253 118 HIS   C CA  
1950 C C   . HIS   B 112 ? 0.2461 0.2397 0.2316 -0.0070 0.0137  -0.0261 118 HIS   C C   
1951 O O   . HIS   B 112 ? 0.2615 0.2585 0.2486 -0.0069 0.0169  -0.0296 118 HIS   C O   
1952 C CB  . HIS   B 112 ? 0.2287 0.2232 0.2031 -0.0134 0.0135  -0.0231 118 HIS   C CB  
1953 C CG  . HIS   B 112 ? 0.2378 0.2299 0.2070 -0.0165 0.0115  -0.0223 118 HIS   C CG  
1954 N ND1 . HIS   B 112 ? 0.2274 0.2203 0.1956 -0.0183 0.0092  -0.0174 118 HIS   C ND1 
1955 C CD2 . HIS   B 112 ? 0.2551 0.2443 0.2205 -0.0180 0.0114  -0.0262 118 HIS   C CD2 
1956 C CE1 . HIS   B 112 ? 0.2503 0.2409 0.2147 -0.0210 0.0075  -0.0181 118 HIS   C CE1 
1957 N NE2 . HIS   B 112 ? 0.2689 0.2568 0.2308 -0.0211 0.0085  -0.0234 118 HIS   C NE2 
1958 N N   . GLY   B 113 ? 0.2324 0.2249 0.2207 -0.0051 0.0117  -0.0231 119 GLY   C N   
1959 C CA  . GLY   B 113 ? 0.2095 0.2049 0.2034 -0.0026 0.0124  -0.0237 119 GLY   C CA  
1960 C C   . GLY   B 113 ? 0.1974 0.1945 0.1909 -0.0027 0.0116  -0.0191 119 GLY   C C   
1961 O O   . GLY   B 113 ? 0.1958 0.1908 0.1857 -0.0038 0.0101  -0.0156 119 GLY   C O   
1962 N N   . VAL   B 114 ? 0.1868 0.1875 0.1844 -0.0016 0.0128  -0.0195 120 VAL   C N   
1963 C CA  . VAL   B 114 ? 0.1816 0.1836 0.1792 -0.0014 0.0121  -0.0159 120 VAL   C CA  
1964 C C   . VAL   B 114 ? 0.1741 0.1790 0.1680 -0.0042 0.0136  -0.0127 120 VAL   C C   
1965 O O   . VAL   B 114 ? 0.1923 0.2003 0.1852 -0.0061 0.0159  -0.0134 120 VAL   C O   
1966 C CB  . VAL   B 114 ? 0.1924 0.1972 0.1962 0.0004  0.0126  -0.0176 120 VAL   C CB  
1967 C CG1 . VAL   B 114 ? 0.1984 0.2043 0.2019 0.0003  0.0120  -0.0142 120 VAL   C CG1 
1968 C CG2 . VAL   B 114 ? 0.2006 0.2022 0.2091 0.0036  0.0099  -0.0203 120 VAL   C CG2 
1969 N N   . VAL   B 115 ? 0.1676 0.1714 0.1595 -0.0044 0.0122  -0.0093 121 VAL   C N   
1970 C CA  . VAL   B 115 ? 0.1659 0.1722 0.1559 -0.0065 0.0127  -0.0062 121 VAL   C CA  
1971 C C   . VAL   B 115 ? 0.1808 0.1892 0.1736 -0.0057 0.0130  -0.0045 121 VAL   C C   
1972 O O   . VAL   B 115 ? 0.1718 0.1827 0.1645 -0.0072 0.0136  -0.0028 121 VAL   C O   
1973 C CB  . VAL   B 115 ? 0.1852 0.1898 0.1730 -0.0073 0.0113  -0.0039 121 VAL   C CB  
1974 C CG1 . VAL   B 115 ? 0.1903 0.1980 0.1786 -0.0088 0.0113  -0.0007 121 VAL   C CG1 
1975 C CG2 . VAL   B 115 ? 0.1966 0.1987 0.1816 -0.0088 0.0107  -0.0054 121 VAL   C CG2 
1976 N N   . GLY   B 116 ? 0.1714 0.1781 0.1661 -0.0034 0.0120  -0.0048 122 GLY   C N   
1977 C CA  . GLY   B 116 ? 0.1824 0.1903 0.1795 -0.0026 0.0120  -0.0036 122 GLY   C CA  
1978 C C   . GLY   B 116 ? 0.1760 0.1812 0.1736 -0.0003 0.0105  -0.0044 122 GLY   C C   
1979 O O   . GLY   B 116 ? 0.1905 0.1927 0.1869 0.0007  0.0093  -0.0058 122 GLY   C O   
1980 N N   . ILE   B 117 ? 0.1592 0.1647 0.1582 0.0006  0.0104  -0.0037 123 ILE   C N   
1981 C CA  . ILE   B 117 ? 0.1734 0.1758 0.1716 0.0025  0.0087  -0.0047 123 ILE   C CA  
1982 C C   . ILE   B 117 ? 0.1663 0.1681 0.1626 0.0027  0.0093  -0.0034 123 ILE   C C   
1983 O O   . ILE   B 117 ? 0.1661 0.1705 0.1648 0.0022  0.0105  -0.0022 123 ILE   C O   
1984 C CB  . ILE   B 117 ? 0.2075 0.2105 0.2101 0.0036  0.0077  -0.0065 123 ILE   C CB  
1985 C CG1 . ILE   B 117 ? 0.2206 0.2268 0.2269 0.0025  0.0091  -0.0056 123 ILE   C CG1 
1986 C CG2 . ILE   B 117 ? 0.2318 0.2350 0.2372 0.0041  0.0068  -0.0088 123 ILE   C CG2 
1987 C CD1 . ILE   B 117 ? 0.2673 0.2741 0.2789 0.0032  0.0079  -0.0074 123 ILE   C CD1 
1988 N N   . VAL   B 118 ? 0.1584 0.1564 0.1502 0.0036  0.0084  -0.0038 124 VAL   C N   
1989 C CA  . VAL   B 118 ? 0.1562 0.1538 0.1461 0.0038  0.0098  -0.0034 124 VAL   C CA  
1990 C C   . VAL   B 118 ? 0.1742 0.1732 0.1683 0.0049  0.0097  -0.0043 124 VAL   C C   
1991 O O   . VAL   B 118 ? 0.1727 0.1706 0.1686 0.0057  0.0078  -0.0057 124 VAL   C O   
1992 C CB  . VAL   B 118 ? 0.1729 0.1655 0.1557 0.0042  0.0088  -0.0040 124 VAL   C CB  
1993 C CG1 . VAL   B 118 ? 0.1815 0.1740 0.1620 0.0043  0.0112  -0.0044 124 VAL   C CG1 
1994 C CG2 . VAL   B 118 ? 0.1929 0.1830 0.1712 0.0028  0.0087  -0.0026 124 VAL   C CG2 
1995 N N   . SER   B 119 ? 0.1700 0.1713 0.1667 0.0048  0.0115  -0.0036 125 SER   C N   
1996 C CA  . SER   B 119 ? 0.1658 0.1678 0.1672 0.0058  0.0112  -0.0043 125 SER   C CA  
1997 C C   . SER   B 119 ? 0.1822 0.1838 0.1837 0.0069  0.0128  -0.0054 125 SER   C C   
1998 O O   . SER   B 119 ? 0.1902 0.1902 0.1934 0.0082  0.0121  -0.0071 125 SER   C O   
1999 C CB  . SER   B 119 ? 0.1788 0.1841 0.1854 0.0047  0.0111  -0.0022 125 SER   C CB  
2000 O OG  . SER   B 119 ? 0.2031 0.2082 0.2143 0.0053  0.0104  -0.0023 125 SER   C OG  
2001 N N   . THR   B 120 ? 0.1748 0.1780 0.1750 0.0064  0.0152  -0.0048 126 THR   C N   
2002 C CA  . THR   B 120 ? 0.1931 0.1970 0.1945 0.0075  0.0177  -0.0065 126 THR   C CA  
2003 C C   . THR   B 120 ? 0.2014 0.2050 0.1968 0.0063  0.0205  -0.0067 126 THR   C C   
2004 O O   . THR   B 120 ? 0.1754 0.1783 0.1669 0.0046  0.0200  -0.0050 126 THR   C O   
2005 C CB  . THR   B 120 ? 0.2164 0.2247 0.2266 0.0079  0.0183  -0.0053 126 THR   C CB  
2006 O OG1 . THR   B 120 ? 0.2205 0.2321 0.2316 0.0062  0.0190  -0.0030 126 THR   C OG1 
2007 C CG2 . THR   B 120 ? 0.2176 0.2258 0.2329 0.0083  0.0155  -0.0040 126 THR   C CG2 
2008 N N   . GLY   B 121 ? 0.2150 0.2188 0.2095 0.0069  0.0236  -0.0090 127 GLY   C N   
2009 C CA  . GLY   B 121 ? 0.2524 0.2564 0.2415 0.0051  0.0271  -0.0090 127 GLY   C CA  
2010 C C   . GLY   B 121 ? 0.2724 0.2780 0.2625 0.0060  0.0314  -0.0122 127 GLY   C C   
2011 O O   . GLY   B 121 ? 0.2564 0.2619 0.2506 0.0083  0.0312  -0.0147 127 GLY   C O   
2012 N N   . GLY   B 122 ? 0.3097 0.3169 0.2964 0.0039  0.0356  -0.0122 128 GLY   C N   
2013 C CA  . GLY   B 122 ? 0.3297 0.3392 0.3170 0.0042  0.0411  -0.0157 128 GLY   C CA  
2014 C C   . GLY   B 122 ? 0.3412 0.3576 0.3356 0.0025  0.0454  -0.0148 128 GLY   C C   
2015 O O   . GLY   B 122 ? 0.3322 0.3519 0.3333 0.0019  0.0431  -0.0118 128 GLY   C O   
2016 N N   . ASN   B 123 ? 0.3592 0.3778 0.3520 0.0015  0.0517  -0.0177 129 ASN   C N   
2017 C CA  . ASN   B 123 ? 0.3686 0.3946 0.3693 -0.0005 0.0564  -0.0173 129 ASN   C CA  
2018 C C   . ASN   B 123 ? 0.3591 0.3847 0.3559 -0.0043 0.0552  -0.0128 129 ASN   C C   
2019 O O   . ASN   B 123 ? 0.3833 0.4153 0.3898 -0.0056 0.0563  -0.0113 129 ASN   C O   
2020 C CB  . ASN   B 123 ? 0.3974 0.4308 0.4155 0.0024  0.0556  -0.0181 129 ASN   C CB  
2021 C CG  . ASN   B 123 ? 0.4440 0.4806 0.4692 0.0053  0.0598  -0.0234 129 ASN   C CG  
2022 O OD1 . ASN   B 123 ? 0.4705 0.5065 0.4893 0.0043  0.0657  -0.0270 129 ASN   C OD1 
2023 N ND2 . ASN   B 123 ? 0.4548 0.4946 0.4934 0.0088  0.0569  -0.0241 129 ASN   C ND2 
2024 N N   . GLY   B 124 ? 0.3273 0.3451 0.3106 -0.0060 0.0526  -0.0107 130 GLY   C N   
2025 C CA  . GLY   B 124 ? 0.3115 0.3275 0.2909 -0.0094 0.0509  -0.0066 130 GLY   C CA  
2026 C C   . GLY   B 124 ? 0.2806 0.2985 0.2681 -0.0084 0.0455  -0.0040 130 GLY   C C   
2027 O O   . GLY   B 124 ? 0.2950 0.3139 0.2837 -0.0110 0.0448  -0.0013 130 GLY   C O   
2028 N N   . LEU   B 125 ? 0.2481 0.2661 0.2406 -0.0048 0.0418  -0.0049 131 LEU   C N   
2029 C CA  . LEU   B 125 ? 0.2446 0.2635 0.2425 -0.0041 0.0369  -0.0026 131 LEU   C CA  
2030 C C   . LEU   B 125 ? 0.2423 0.2551 0.2338 -0.0025 0.0326  -0.0026 131 LEU   C C   
2031 O O   . LEU   B 125 ? 0.2728 0.2820 0.2592 -0.0011 0.0329  -0.0047 131 LEU   C O   
2032 C CB  . LEU   B 125 ? 0.2643 0.2894 0.2752 -0.0018 0.0363  -0.0033 131 LEU   C CB  
2033 C CG  . LEU   B 125 ? 0.3041 0.3367 0.3249 -0.0025 0.0402  -0.0042 131 LEU   C CG  
2034 C CD1 . LEU   B 125 ? 0.3298 0.3671 0.3635 0.0007  0.0386  -0.0053 131 LEU   C CD1 
2035 C CD2 . LEU   B 125 ? 0.3003 0.3356 0.3234 -0.0059 0.0395  -0.0013 131 LEU   C CD2 
2036 N N   . VAL   B 126 ? 0.1953 0.2069 0.1870 -0.0030 0.0288  -0.0005 132 VAL   C N   
2037 C CA  . VAL   B 126 ? 0.1941 0.2013 0.1824 -0.0014 0.0249  -0.0006 132 VAL   C CA  
2038 C C   . VAL   B 126 ? 0.1953 0.2059 0.1911 -0.0007 0.0224  0.0004  132 VAL   C C   
2039 O O   . VAL   B 126 ? 0.1990 0.2128 0.1987 -0.0023 0.0222  0.0021  132 VAL   C O   
2040 C CB  . VAL   B 126 ? 0.2184 0.2197 0.1981 -0.0027 0.0229  0.0004  132 VAL   C CB  
2041 C CG1 . VAL   B 126 ? 0.2373 0.2392 0.2174 -0.0052 0.0224  0.0025  132 VAL   C CG1 
2042 C CG2 . VAL   B 126 ? 0.2232 0.2211 0.2016 -0.0008 0.0190  -0.0004 132 VAL   C CG2 
2043 N N   . GLY   B 127 ? 0.1761 0.1856 0.1736 0.0013  0.0204  -0.0004 133 GLY   C N   
2044 C CA  . GLY   B 127 ? 0.1706 0.1826 0.1738 0.0014  0.0182  0.0009  133 GLY   C CA  
2045 C C   . GLY   B 127 ? 0.1708 0.1800 0.1709 0.0014  0.0158  0.0009  133 GLY   C C   
2046 O O   . GLY   B 127 ? 0.1784 0.1843 0.1753 0.0024  0.0151  -0.0006 133 GLY   C O   
2047 N N   . PHE   B 128 ? 0.1612 0.1719 0.1624 0.0000  0.0146  0.0024  134 PHE   C N   
2048 C CA  . PHE   B 128 ? 0.1607 0.1697 0.1601 -0.0003 0.0131  0.0018  134 PHE   C CA  
2049 C C   . PHE   B 128 ? 0.1581 0.1693 0.1609 -0.0008 0.0123  0.0029  134 PHE   C C   
2050 O O   . PHE   B 128 ? 0.1566 0.1701 0.1613 -0.0021 0.0119  0.0048  134 PHE   C O   
2051 C CB  . PHE   B 128 ? 0.1585 0.1666 0.1546 -0.0019 0.0128  0.0021  134 PHE   C CB  
2052 C CG  . PHE   B 128 ? 0.1633 0.1686 0.1553 -0.0022 0.0134  0.0019  134 PHE   C CG  
2053 C CD1 . PHE   B 128 ? 0.1673 0.1682 0.1552 -0.0012 0.0124  0.0007  134 PHE   C CD1 
2054 C CD2 . PHE   B 128 ? 0.1749 0.1819 0.1673 -0.0038 0.0147  0.0033  134 PHE   C CD2 
2055 C CE1 . PHE   B 128 ? 0.1799 0.1773 0.1628 -0.0020 0.0126  0.0012  134 PHE   C CE1 
2056 C CE2 . PHE   B 128 ? 0.1899 0.1941 0.1780 -0.0048 0.0156  0.0035  134 PHE   C CE2 
2057 C CZ  . PHE   B 128 ? 0.1906 0.1896 0.1733 -0.0039 0.0145  0.0026  134 PHE   C CZ  
2058 N N   . ALA   B 129 ? 0.1525 0.1627 0.1560 -0.0003 0.0118  0.0019  135 ALA   C N   
2059 C CA  . ALA   B 129 ? 0.1510 0.1626 0.1566 -0.0015 0.0114  0.0031  135 ALA   C CA  
2060 C C   . ALA   B 129 ? 0.1643 0.1767 0.1670 -0.0035 0.0118  0.0030  135 ALA   C C   
2061 O O   . ALA   B 129 ? 0.1604 0.1718 0.1618 -0.0031 0.0122  0.0007  135 ALA   C O   
2062 C CB  . ALA   B 129 ? 0.1594 0.1700 0.1673 -0.0007 0.0111  0.0017  135 ALA   C CB  
2063 N N   . ASP   B 130 ? 0.1656 0.1795 0.1672 -0.0056 0.0114  0.0051  136 ASP   C N   
2064 C CA  . ASP   B 130 ? 0.1709 0.1852 0.1687 -0.0077 0.0120  0.0045  136 ASP   C CA  
2065 C C   . ASP   B 130 ? 0.1777 0.1925 0.1752 -0.0088 0.0134  0.0033  136 ASP   C C   
2066 O O   . ASP   B 130 ? 0.1768 0.1920 0.1764 -0.0092 0.0134  0.0046  136 ASP   C O   
2067 C CB  . ASP   B 130 ? 0.1861 0.2015 0.1821 -0.0100 0.0105  0.0073  136 ASP   C CB  
2068 C CG  . ASP   B 130 ? 0.2671 0.2824 0.2578 -0.0125 0.0109  0.0064  136 ASP   C CG  
2069 O OD1 . ASP   B 130 ? 0.2565 0.2708 0.2459 -0.0119 0.0116  0.0040  136 ASP   C OD1 
2070 O OD2 . ASP   B 130 ? 0.3195 0.3352 0.3070 -0.0150 0.0104  0.0080  136 ASP   C OD2 
2071 N N   . VAL   B 131 ? 0.1641 0.1791 0.1596 -0.0094 0.0148  0.0006  137 VAL   C N   
2072 C CA  . VAL   B 131 ? 0.1647 0.1813 0.1606 -0.0108 0.0171  -0.0011 137 VAL   C CA  
2073 C C   . VAL   B 131 ? 0.1841 0.2013 0.1746 -0.0136 0.0187  -0.0021 137 VAL   C C   
2074 O O   . VAL   B 131 ? 0.1931 0.2120 0.1830 -0.0153 0.0215  -0.0039 137 VAL   C O   
2075 C CB  . VAL   B 131 ? 0.1839 0.2009 0.1846 -0.0086 0.0180  -0.0047 137 VAL   C CB  
2076 C CG1 . VAL   B 131 ? 0.1893 0.2052 0.1942 -0.0063 0.0162  -0.0040 137 VAL   C CG1 
2077 C CG2 . VAL   B 131 ? 0.1863 0.2017 0.1863 -0.0071 0.0177  -0.0076 137 VAL   C CG2 
2078 N N   . ARG   B 132 ? 0.1756 0.1915 0.1619 -0.0144 0.0171  -0.0010 138 ARG   C N   
2079 C CA  . ARG   B 132 ? 0.1609 0.1766 0.1413 -0.0170 0.0181  -0.0025 138 ARG   C CA  
2080 C C   . ARG   B 132 ? 0.1945 0.2111 0.1696 -0.0207 0.0190  -0.0005 138 ARG   C C   
2081 O O   . ARG   B 132 ? 0.2193 0.2360 0.1890 -0.0231 0.0212  -0.0029 138 ARG   C O   
2082 C CB  . ARG   B 132 ? 0.1635 0.1775 0.1415 -0.0171 0.0156  -0.0018 138 ARG   C CB  
2083 C CG  . ARG   B 132 ? 0.1625 0.1748 0.1439 -0.0143 0.0150  -0.0038 138 ARG   C CG  
2084 C CD  . ARG   B 132 ? 0.1653 0.1761 0.1446 -0.0153 0.0127  -0.0025 138 ARG   C CD  
2085 N NE  . ARG   B 132 ? 0.1599 0.1720 0.1417 -0.0151 0.0108  0.0014  138 ARG   C NE  
2086 C CZ  . ARG   B 132 ? 0.2032 0.2153 0.1858 -0.0157 0.0089  0.0030  138 ARG   C CZ  
2087 N NH1 . ARG   B 132 ? 0.1797 0.1900 0.1598 -0.0170 0.0082  0.0016  138 ARG   C NH1 
2088 N NH2 . ARG   B 132 ? 0.1895 0.2036 0.1761 -0.0151 0.0078  0.0059  138 ARG   C NH2 
2089 N N   . ASP   B 133 ? 0.1920 0.2087 0.1680 -0.0215 0.0175  0.0036  139 ASP   C N   
2090 C CA  . ASP   B 133 ? 0.2090 0.2254 0.1791 -0.0254 0.0179  0.0064  139 ASP   C CA  
2091 C C   . ASP   B 133 ? 0.2172 0.2352 0.1883 -0.0268 0.0219  0.0050  139 ASP   C C   
2092 O O   . ASP   B 133 ? 0.2229 0.2405 0.1877 -0.0309 0.0232  0.0069  139 ASP   C O   
2093 C CB  . ASP   B 133 ? 0.2376 0.2526 0.2086 -0.0257 0.0138  0.0117  139 ASP   C CB  
2094 C CG  . ASP   B 133 ? 0.2871 0.3023 0.2662 -0.0229 0.0134  0.0126  139 ASP   C CG  
2095 O OD1 . ASP   B 133 ? 0.2942 0.3102 0.2788 -0.0195 0.0142  0.0098  139 ASP   C OD1 
2096 O OD2 . ASP   B 133 ? 0.2932 0.3071 0.2726 -0.0243 0.0122  0.0162  139 ASP   C OD2 
2097 N N   . LEU   B 134 ? 0.2000 0.2197 0.1787 -0.0239 0.0238  0.0018  140 LEU   C N   
2098 C CA  . LEU   B 134 ? 0.2041 0.2263 0.1859 -0.0253 0.0276  0.0002  140 LEU   C CA  
2099 C C   . LEU   B 134 ? 0.2155 0.2401 0.1950 -0.0268 0.0323  -0.0047 140 LEU   C C   
2100 O O   . LEU   B 134 ? 0.2134 0.2401 0.1994 -0.0242 0.0341  -0.0094 140 LEU   C O   
2101 C CB  . LEU   B 134 ? 0.2064 0.2294 0.1981 -0.0215 0.0268  -0.0011 140 LEU   C CB  
2102 C CG  . LEU   B 134 ? 0.2275 0.2481 0.2217 -0.0196 0.0227  0.0027  140 LEU   C CG  
2103 C CD1 . LEU   B 134 ? 0.2385 0.2594 0.2409 -0.0160 0.0220  0.0005  140 LEU   C CD1 
2104 C CD2 . LEU   B 134 ? 0.2471 0.2664 0.2388 -0.0228 0.0220  0.0074  140 LEU   C CD2 
2105 N N   . LEU   B 135 ? 0.2135 0.2374 0.1833 -0.0312 0.0339  -0.0037 141 LEU   C N   
2106 C CA  . LEU   B 135 ? 0.2251 0.2509 0.1913 -0.0327 0.0386  -0.0090 141 LEU   C CA  
2107 C C   . LEU   B 135 ? 0.2431 0.2735 0.2155 -0.0333 0.0442  -0.0130 141 LEU   C C   
2108 O O   . LEU   B 135 ? 0.2684 0.3012 0.2435 -0.0323 0.0478  -0.0190 141 LEU   C O   
2109 C CB  . LEU   B 135 ? 0.2242 0.2478 0.1769 -0.0377 0.0390  -0.0073 141 LEU   C CB  
2110 C CG  . LEU   B 135 ? 0.2373 0.2569 0.1843 -0.0377 0.0329  -0.0028 141 LEU   C CG  
2111 C CD1 . LEU   B 135 ? 0.2574 0.2747 0.1909 -0.0426 0.0330  -0.0021 141 LEU   C CD1 
2112 C CD2 . LEU   B 135 ? 0.2394 0.2581 0.1915 -0.0333 0.0299  -0.0052 141 LEU   C CD2 
2113 N N   . TRP   B 136 ? 0.2399 0.2715 0.2156 -0.0351 0.0450  -0.0098 142 TRP   C N   
2114 C CA  . TRP   B 136 ? 0.2546 0.2912 0.2376 -0.0363 0.0504  -0.0131 142 TRP   C CA  
2115 C C   . TRP   B 136 ? 0.2663 0.3059 0.2629 -0.0309 0.0501  -0.0180 142 TRP   C C   
2116 O O   . TRP   B 136 ? 0.2700 0.3148 0.2744 -0.0314 0.0547  -0.0222 142 TRP   C O   
2117 C CB  . TRP   B 136 ? 0.2525 0.2888 0.2359 -0.0396 0.0504  -0.0079 142 TRP   C CB  
2118 C CG  . TRP   B 136 ? 0.2560 0.2889 0.2437 -0.0366 0.0441  -0.0035 142 TRP   C CG  
2119 C CD1 . TRP   B 136 ? 0.2639 0.2918 0.2453 -0.0369 0.0392  0.0020  142 TRP   C CD1 
2120 C CD2 . TRP   B 136 ? 0.2507 0.2848 0.2503 -0.0326 0.0422  -0.0048 142 TRP   C CD2 
2121 N NE1 . TRP   B 136 ? 0.2677 0.2940 0.2565 -0.0334 0.0350  0.0039  142 TRP   C NE1 
2122 C CE2 . TRP   B 136 ? 0.2595 0.2893 0.2586 -0.0311 0.0368  -0.0001 142 TRP   C CE2 
2123 C CE3 . TRP   B 136 ? 0.2520 0.2907 0.2629 -0.0304 0.0443  -0.0096 142 TRP   C CE3 
2124 C CZ2 . TRP   B 136 ? 0.2662 0.2956 0.2742 -0.0274 0.0337  -0.0004 142 TRP   C CZ2 
2125 C CZ3 . TRP   B 136 ? 0.2710 0.3091 0.2908 -0.0272 0.0406  -0.0092 142 TRP   C CZ3 
2126 C CH2 . TRP   B 136 ? 0.2728 0.3060 0.2903 -0.0259 0.0356  -0.0047 142 TRP   C CH2 
2127 N N   . LEU   B 137 ? 0.2662 0.3028 0.2657 -0.0262 0.0447  -0.0176 143 LEU   C N   
2128 C CA  . LEU   B 137 ? 0.2828 0.3211 0.2936 -0.0214 0.0435  -0.0218 143 LEU   C CA  
2129 C C   . LEU   B 137 ? 0.3307 0.3720 0.3448 -0.0204 0.0473  -0.0285 143 LEU   C C   
2130 O O   . LEU   B 137 ? 0.3446 0.3891 0.3699 -0.0175 0.0479  -0.0327 143 LEU   C O   
2131 C CB  . LEU   B 137 ? 0.2589 0.2926 0.2697 -0.0172 0.0374  -0.0199 143 LEU   C CB  
2132 C CG  . LEU   B 137 ? 0.2495 0.2809 0.2611 -0.0165 0.0334  -0.0150 143 LEU   C CG  
2133 C CD1 . LEU   B 137 ? 0.2521 0.2792 0.2620 -0.0131 0.0286  -0.0136 143 LEU   C CD1 
2134 C CD2 . LEU   B 137 ? 0.2466 0.2806 0.2684 -0.0154 0.0334  -0.0161 143 LEU   C CD2 
2135 N N   . ASP   B 138 ? 0.3735 0.4134 0.3780 -0.0225 0.0494  -0.0298 144 ASP   C N   
2136 C CA  . ASP   B 138 ? 0.4269 0.4682 0.4316 -0.0220 0.0531  -0.0363 144 ASP   C CA  
2137 C C   . ASP   B 138 ? 0.4678 0.5150 0.4743 -0.0254 0.0607  -0.0406 144 ASP   C C   
2138 O O   . ASP   B 138 ? 0.4770 0.5260 0.4854 -0.0245 0.0643  -0.0470 144 ASP   C O   
2139 C CB  . ASP   B 138 ? 0.4622 0.4991 0.4535 -0.0242 0.0522  -0.0352 144 ASP   C CB  
2140 C CG  . ASP   B 138 ? 0.5153 0.5468 0.5047 -0.0211 0.0460  -0.0332 144 ASP   C CG  
2141 O OD1 . ASP   B 138 ? 0.5263 0.5568 0.5242 -0.0167 0.0426  -0.0338 144 ASP   C OD1 
2142 O OD2 . ASP   B 138 ? 0.5544 0.5824 0.5333 -0.0234 0.0443  -0.0310 144 ASP   C OD2 
2143 N N   . GLU   B 139 ? 0.4920 0.5415 0.4958 -0.0298 0.0635  -0.0370 145 GLU   C N   
2144 C CA  . GLU   B 139 ? 0.5257 0.5809 0.5296 -0.0342 0.0717  -0.0405 145 GLU   C CA  
2145 C C   . GLU   B 139 ? 0.5436 0.6046 0.5605 -0.0346 0.0741  -0.0408 145 GLU   C C   
2146 O O   . GLU   B 139 ? 0.5615 0.6278 0.5792 -0.0390 0.0813  -0.0429 145 GLU   C O   
2147 C CB  . GLU   B 139 ? 0.5816 0.6341 0.5687 -0.0409 0.0740  -0.0361 145 GLU   C CB  
2148 C CG  . GLU   B 139 ? 0.6694 0.7187 0.6524 -0.0434 0.0701  -0.0276 145 GLU   C CG  
2149 C CD  . GLU   B 139 ? 0.7866 0.8305 0.7522 -0.0483 0.0687  -0.0222 145 GLU   C CD  
2150 O OE1 . GLU   B 139 ? 0.8031 0.8456 0.7636 -0.0528 0.0687  -0.0164 145 GLU   C OE1 
2151 O OE2 . GLU   B 139 ? 0.8239 0.8645 0.7812 -0.0477 0.0669  -0.0235 145 GLU   C OE2 
2152 N N1  . A1B5A C .   ? 0.2167 0.2380 0.2332 0.0059  0.0368  0.0203  201 A1B5A A N1  
2153 N N3  . A1B5A C .   ? 0.1839 0.1988 0.2304 -0.0071 0.0211  0.0014  201 A1B5A A N3  
2154 C C4  . A1B5A C .   ? 0.2002 0.2189 0.2224 0.0022  0.0311  0.0182  201 A1B5A A C4  
2155 C C5  . A1B5A C .   ? 0.1975 0.2148 0.2263 0.0001  0.0305  0.0190  201 A1B5A A C5  
2156 C C6  . A1B5A C .   ? 0.1892 0.2083 0.2263 -0.0023 0.0289  0.0151  201 A1B5A A C6  
2157 C C7  . A1B5A C .   ? 0.1883 0.2021 0.2293 -0.0034 0.0287  0.0187  201 A1B5A A C7  
2158 C C8  . A1B5A C .   ? 0.1969 0.2086 0.2371 -0.0036 0.0256  0.0168  201 A1B5A A C8  
2159 C C10 . A1B5A C .   ? 0.1856 0.2007 0.2317 -0.0060 0.0242  0.0089  201 A1B5A A C10 
2160 O O1  . A1B5A C .   ? 0.1915 0.2061 0.2502 -0.0095 0.0245  0.0040  201 A1B5A A O1  
2161 C C11 . A1B5A C .   ? 0.1859 0.2009 0.2370 -0.0077 0.0233  0.0045  201 A1B5A A C11 
2162 C C9  . A1B5A C .   ? 0.1932 0.2052 0.2402 -0.0056 0.0251  0.0126  201 A1B5A A C9  
2163 C C12 . A1B5A C .   ? 0.1835 0.2014 0.2321 -0.0060 0.0268  0.0108  201 A1B5A A C12 
2164 N N2  . A1B5A C .   ? 0.1884 0.2055 0.2305 -0.0039 0.0282  0.0149  201 A1B5A A N2  
2165 O O   . A1B5A C .   ? 0.1910 0.2132 0.2301 -0.0026 0.0285  0.0123  201 A1B5A A O   
2166 C C1  . A1B5A C .   ? 0.2049 0.2228 0.2204 0.0033  0.0280  0.0150  201 A1B5A A C1  
2167 S S   . A1B5A C .   ? 0.2141 0.2298 0.2293 0.0019  0.0234  0.0122  201 A1B5A A S   
2168 C C   . A1B5A C .   ? 0.2176 0.2320 0.2242 0.0036  0.0208  0.0092  201 A1B5A A C   
2169 C C3  . A1B5A C .   ? 0.2177 0.2381 0.2400 0.0036  0.0355  0.0209  201 A1B5A A C3  
2170 C C2  . A1B5A C .   ? 0.2027 0.2227 0.2132 0.0068  0.0332  0.0168  201 A1B5A A C2  
2171 N N   . A1B5A C .   ? 0.2078 0.2262 0.2176 0.0055  0.0288  0.0142  201 A1B5A A N   
2172 C C1  . GOL   D .   ? 0.5605 0.5447 0.6519 -0.0116 0.0325  -0.0028 202 GOL   A C1  
2173 O O1  . GOL   D .   ? 0.5582 0.5435 0.6530 -0.0144 0.0318  -0.0045 202 GOL   A O1  
2174 C C2  . GOL   D .   ? 0.5617 0.5492 0.6505 -0.0100 0.0322  0.0037  202 GOL   A C2  
2175 O O2  . GOL   D .   ? 0.5639 0.5514 0.6571 -0.0109 0.0336  0.0082  202 GOL   A O2  
2176 C C3  . GOL   D .   ? 0.5601 0.5462 0.6495 -0.0074 0.0329  0.0064  202 GOL   A C3  
2177 O O3  . GOL   D .   ? 0.5593 0.5491 0.6443 -0.0059 0.0312  0.0110  202 GOL   A O3  
2187 N N1  . A1B5A H .   ? 0.2785 0.2694 0.2450 0.0071  0.0301  -0.0191 201 A1B5A C N1  
2188 N N3  . A1B5A H .   ? 0.1758 0.1773 0.1932 0.0091  0.0103  -0.0058 201 A1B5A C N3  
2189 C C4  . A1B5A H .   ? 0.2516 0.2420 0.2288 0.0096  0.0222  -0.0177 201 A1B5A C C4  
2190 C C5  . A1B5A H .   ? 0.2386 0.2284 0.2227 0.0115  0.0190  -0.0189 201 A1B5A C C5  
2191 C C6  . A1B5A H .   ? 0.2151 0.2097 0.2103 0.0119  0.0186  -0.0164 201 A1B5A C C6  
2192 C C7  . A1B5A H .   ? 0.1987 0.1878 0.1973 0.0136  0.0130  -0.0193 201 A1B5A C C7  
2193 C C8  . A1B5A H .   ? 0.1956 0.1844 0.1970 0.0127  0.0092  -0.0173 201 A1B5A C C8  
2194 C C10 . A1B5A H .   ? 0.1759 0.1725 0.1868 0.0116  0.0116  -0.0117 201 A1B5A C C10 
2195 O O1  . A1B5A H .   ? 0.1701 0.1691 0.1942 0.0120  0.0103  -0.0087 201 A1B5A C O1  
2196 C C11 . A1B5A H .   ? 0.1760 0.1753 0.1942 0.0109  0.0107  -0.0086 201 A1B5A C C11 
2197 C C9  . A1B5A H .   ? 0.1910 0.1835 0.2012 0.0122  0.0091  -0.0143 201 A1B5A C C9  
2198 C C12 . A1B5A H .   ? 0.1828 0.1800 0.1928 0.0128  0.0148  -0.0138 201 A1B5A C C12 
2199 N N2  . A1B5A H .   ? 0.1991 0.1928 0.2001 0.0129  0.0157  -0.0166 201 A1B5A C N2  
2200 O O   . A1B5A H .   ? 0.2152 0.2140 0.2138 0.0112  0.0207  -0.0144 201 A1B5A C O   
2201 C C1  . A1B5A H .   ? 0.2548 0.2452 0.2289 0.0078  0.0209  -0.0144 201 A1B5A C C1  
2202 S S   . A1B5A H .   ? 0.2453 0.2359 0.2244 0.0081  0.0160  -0.0121 201 A1B5A C S   
2203 C C   . A1B5A H .   ? 0.2445 0.2340 0.2181 0.0060  0.0154  -0.0092 201 A1B5A C C   
2204 C C3  . A1B5A H .   ? 0.2681 0.2587 0.2412 0.0093  0.0268  -0.0202 201 A1B5A C C3  
2205 C C2  . A1B5A H .   ? 0.2721 0.2625 0.2365 0.0054  0.0280  -0.0154 201 A1B5A C C2  
2206 N N   . A1B5A H .   ? 0.2664 0.2566 0.2345 0.0058  0.0235  -0.0131 201 A1B5A C N   
# 
