data_7HUT
# 
_entry.id   7HUT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HUT         pdb_00007hut 10.2210/pdb7hut/pdb 
WWPDB D_1001407958 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HUT 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                 15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-{[2-chloro-5-(trifluoromethyl)phenyl]acetyl}piperidine-3-carboxamide' 348.748   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                    65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                          78.133    1   ?         ? ? ? 
5 water       nat water                                                                         18.015    367 ?         ? ? ? 
# 
_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-{[2-chloro-5-(trifluoromethyl)phenyl]acetyl}piperidine-3-carboxamide' A1BON 
3 'ZINC ION'                                                                    ZN    
4 'DIMETHYL SULFOXIDE'                                                          DMS   
5 water                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BON non-polymer         . '(3S)-1-{[2-chloro-5-(trifluoromethyl)phenyl]acetyl}piperidine-3-carboxamide' ? 'C15 H16 Cl F3 N2 O2' 
348.748 
ALA   'L-peptide linking' y ALANINE                                                                       ? 'C3 H7 N O2'          
89.093  
ARG   'L-peptide linking' y ARGININE                                                                      ? 'C6 H15 N4 O2 1'      
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                    ? 'C4 H8 N2 O3'         
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                               ? 'C4 H7 N O4'          
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                      ? 'C3 H7 N O2 S'        
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                          ? 'C2 H6 O S'           
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                     ? 'C5 H10 N2 O3'        
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                               ? 'C5 H9 N O4'          
147.129 
GLY   'peptide linking'   y GLYCINE                                                                       ? 'C2 H5 N O2'          
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                     ? 'C6 H10 N3 O2 1'      
156.162 
HOH   non-polymer         . WATER                                                                         ? 'H2 O'                
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                    ? 'C6 H13 N O2'         
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                       ? 'C6 H13 N O2'         
131.173 
LYS   'L-peptide linking' y LYSINE                                                                        ? 'C6 H15 N2 O2 1'      
147.195 
MET   'L-peptide linking' y METHIONINE                                                                    ? 'C5 H11 N O2 S'       
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                 ? 'C9 H11 N O2'         
165.189 
PRO   'L-peptide linking' y PROLINE                                                                       ? 'C5 H9 N O2'          
115.130 
SER   'L-peptide linking' y SERINE                                                                        ? 'C3 H7 N O3'          
105.093 
THR   'L-peptide linking' y THREONINE                                                                     ? 'C4 H9 N O3'          
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                    ? 'C11 H12 N2 O2'       
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                      ? 'C9 H11 N O3'         
181.189 
VAL   'L-peptide linking' y VALINE                                                                        ? 'C5 H11 N O2'         
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                    ? 'Zn 2'                
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU 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        A1BON 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BON 
_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 A1BON 1   201 201 A1BON LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   301 345 HOH   HOH A . 
G 5 HOH   2   302 280 HOH   HOH A . 
G 5 HOH   3   303 97  HOH   HOH A . 
G 5 HOH   4   304 143 HOH   HOH A . 
G 5 HOH   5   305 324 HOH   HOH A . 
G 5 HOH   6   306 293 HOH   HOH A . 
G 5 HOH   7   307 326 HOH   HOH A . 
G 5 HOH   8   308 179 HOH   HOH A . 
G 5 HOH   9   309 333 HOH   HOH A . 
G 5 HOH   10  310 296 HOH   HOH A . 
G 5 HOH   11  311 239 HOH   HOH A . 
G 5 HOH   12  312 223 HOH   HOH A . 
G 5 HOH   13  313 291 HOH   HOH A . 
G 5 HOH   14  314 297 HOH   HOH A . 
G 5 HOH   15  315 369 HOH   HOH A . 
G 5 HOH   16  316 70  HOH   HOH A . 
G 5 HOH   17  317 131 HOH   HOH A . 
G 5 HOH   18  318 106 HOH   HOH A . 
G 5 HOH   19  319 275 HOH   HOH A . 
G 5 HOH   20  320 216 HOH   HOH A . 
G 5 HOH   21  321 146 HOH   HOH A . 
G 5 HOH   22  322 98  HOH   HOH A . 
G 5 HOH   23  323 298 HOH   HOH A . 
G 5 HOH   24  324 242 HOH   HOH A . 
G 5 HOH   25  325 108 HOH   HOH A . 
G 5 HOH   26  326 135 HOH   HOH A . 
G 5 HOH   27  327 244 HOH   HOH A . 
G 5 HOH   28  328 321 HOH   HOH A . 
G 5 HOH   29  329 23  HOH   HOH A . 
G 5 HOH   30  330 218 HOH   HOH A . 
G 5 HOH   31  331 182 HOH   HOH A . 
G 5 HOH   32  332 312 HOH   HOH A . 
G 5 HOH   33  333 80  HOH   HOH A . 
G 5 HOH   34  334 273 HOH   HOH A . 
G 5 HOH   35  335 163 HOH   HOH A . 
G 5 HOH   36  336 14  HOH   HOH A . 
G 5 HOH   37  337 75  HOH   HOH A . 
G 5 HOH   38  338 264 HOH   HOH A . 
G 5 HOH   39  339 15  HOH   HOH A . 
G 5 HOH   40  340 9   HOH   HOH A . 
G 5 HOH   41  341 311 HOH   HOH A . 
G 5 HOH   42  342 122 HOH   HOH A . 
G 5 HOH   43  343 282 HOH   HOH A . 
G 5 HOH   44  344 129 HOH   HOH A . 
G 5 HOH   45  345 127 HOH   HOH A . 
G 5 HOH   46  346 221 HOH   HOH A . 
G 5 HOH   47  347 306 HOH   HOH A . 
G 5 HOH   48  348 111 HOH   HOH A . 
G 5 HOH   49  349 99  HOH   HOH A . 
G 5 HOH   50  350 133 HOH   HOH A . 
G 5 HOH   51  351 142 HOH   HOH A . 
G 5 HOH   52  352 66  HOH   HOH A . 
G 5 HOH   53  353 7   HOH   HOH A . 
G 5 HOH   54  354 159 HOH   HOH A . 
G 5 HOH   55  355 43  HOH   HOH A . 
G 5 HOH   56  356 149 HOH   HOH A . 
G 5 HOH   57  357 153 HOH   HOH A . 
G 5 HOH   58  358 193 HOH   HOH A . 
G 5 HOH   59  359 219 HOH   HOH A . 
G 5 HOH   60  360 185 HOH   HOH A . 
G 5 HOH   61  361 167 HOH   HOH A . 
G 5 HOH   62  362 342 HOH   HOH A . 
G 5 HOH   63  363 92  HOH   HOH A . 
G 5 HOH   64  364 235 HOH   HOH A . 
G 5 HOH   65  365 34  HOH   HOH A . 
G 5 HOH   66  366 5   HOH   HOH A . 
G 5 HOH   67  367 336 HOH   HOH A . 
G 5 HOH   68  368 281 HOH   HOH A . 
G 5 HOH   69  369 74  HOH   HOH A . 
G 5 HOH   70  370 199 HOH   HOH A . 
G 5 HOH   71  371 125 HOH   HOH A . 
G 5 HOH   72  372 30  HOH   HOH A . 
G 5 HOH   73  373 276 HOH   HOH A . 
G 5 HOH   74  374 21  HOH   HOH A . 
G 5 HOH   75  375 248 HOH   HOH A . 
G 5 HOH   76  376 285 HOH   HOH A . 
G 5 HOH   77  377 58  HOH   HOH A . 
G 5 HOH   78  378 299 HOH   HOH A . 
G 5 HOH   79  379 77  HOH   HOH A . 
G 5 HOH   80  380 294 HOH   HOH A . 
G 5 HOH   81  381 36  HOH   HOH A . 
G 5 HOH   82  382 222 HOH   HOH A . 
G 5 HOH   83  383 6   HOH   HOH A . 
G 5 HOH   84  384 65  HOH   HOH A . 
G 5 HOH   85  385 228 HOH   HOH A . 
G 5 HOH   86  386 11  HOH   HOH A . 
G 5 HOH   87  387 151 HOH   HOH A . 
G 5 HOH   88  388 118 HOH   HOH A . 
G 5 HOH   89  389 358 HOH   HOH A . 
G 5 HOH   90  390 205 HOH   HOH A . 
G 5 HOH   91  391 39  HOH   HOH A . 
G 5 HOH   92  392 137 HOH   HOH A . 
G 5 HOH   93  393 231 HOH   HOH A . 
G 5 HOH   94  394 40  HOH   HOH A . 
G 5 HOH   95  395 266 HOH   HOH A . 
G 5 HOH   96  396 277 HOH   HOH A . 
G 5 HOH   97  397 214 HOH   HOH A . 
G 5 HOH   98  398 220 HOH   HOH A . 
G 5 HOH   99  399 46  HOH   HOH A . 
G 5 HOH   100 400 17  HOH   HOH A . 
G 5 HOH   101 401 84  HOH   HOH A . 
G 5 HOH   102 402 217 HOH   HOH A . 
G 5 HOH   103 403 368 HOH   HOH A . 
G 5 HOH   104 404 346 HOH   HOH A . 
G 5 HOH   105 405 86  HOH   HOH A . 
G 5 HOH   106 406 288 HOH   HOH A . 
G 5 HOH   107 407 8   HOH   HOH A . 
G 5 HOH   108 408 210 HOH   HOH A . 
G 5 HOH   109 409 56  HOH   HOH A . 
G 5 HOH   110 410 104 HOH   HOH A . 
G 5 HOH   111 411 318 HOH   HOH A . 
G 5 HOH   112 412 304 HOH   HOH A . 
G 5 HOH   113 413 241 HOH   HOH A . 
G 5 HOH   114 414 177 HOH   HOH A . 
G 5 HOH   115 415 258 HOH   HOH A . 
G 5 HOH   116 416 139 HOH   HOH A . 
G 5 HOH   117 417 26  HOH   HOH A . 
G 5 HOH   118 418 69  HOH   HOH A . 
G 5 HOH   119 419 115 HOH   HOH A . 
G 5 HOH   120 420 301 HOH   HOH A . 
G 5 HOH   121 421 45  HOH   HOH A . 
G 5 HOH   122 422 81  HOH   HOH A . 
G 5 HOH   123 423 290 HOH   HOH A . 
G 5 HOH   124 424 61  HOH   HOH A . 
G 5 HOH   125 425 181 HOH   HOH A . 
G 5 HOH   126 426 27  HOH   HOH A . 
G 5 HOH   127 427 211 HOH   HOH A . 
G 5 HOH   128 428 259 HOH   HOH A . 
G 5 HOH   129 429 51  HOH   HOH A . 
G 5 HOH   130 430 85  HOH   HOH A . 
G 5 HOH   131 431 19  HOH   HOH A . 
G 5 HOH   132 432 101 HOH   HOH A . 
G 5 HOH   133 433 4   HOH   HOH A . 
G 5 HOH   134 434 300 HOH   HOH A . 
G 5 HOH   135 435 169 HOH   HOH A . 
G 5 HOH   136 436 194 HOH   HOH A . 
G 5 HOH   137 437 251 HOH   HOH A . 
G 5 HOH   138 438 232 HOH   HOH A . 
G 5 HOH   139 439 230 HOH   HOH A . 
G 5 HOH   140 440 16  HOH   HOH A . 
G 5 HOH   141 441 287 HOH   HOH A . 
G 5 HOH   142 442 132 HOH   HOH A . 
G 5 HOH   143 443 317 HOH   HOH A . 
G 5 HOH   144 444 117 HOH   HOH A . 
G 5 HOH   145 445 102 HOH   HOH A . 
G 5 HOH   146 446 343 HOH   HOH A . 
G 5 HOH   147 447 350 HOH   HOH A . 
G 5 HOH   148 448 271 HOH   HOH A . 
G 5 HOH   149 449 207 HOH   HOH A . 
G 5 HOH   150 450 310 HOH   HOH A . 
G 5 HOH   151 451 183 HOH   HOH A . 
G 5 HOH   152 452 270 HOH   HOH A . 
G 5 HOH   153 453 252 HOH   HOH A . 
G 5 HOH   154 454 307 HOH   HOH A . 
G 5 HOH   155 455 332 HOH   HOH A . 
G 5 HOH   156 456 250 HOH   HOH A . 
G 5 HOH   157 457 292 HOH   HOH A . 
G 5 HOH   158 458 197 HOH   HOH A . 
G 5 HOH   159 459 255 HOH   HOH A . 
G 5 HOH   160 460 147 HOH   HOH A . 
G 5 HOH   161 461 240 HOH   HOH A . 
G 5 HOH   162 462 168 HOH   HOH A . 
G 5 HOH   163 463 344 HOH   HOH A . 
G 5 HOH   164 464 365 HOH   HOH A . 
G 5 HOH   165 465 206 HOH   HOH A . 
G 5 HOH   166 466 198 HOH   HOH A . 
G 5 HOH   167 467 360 HOH   HOH A . 
G 5 HOH   168 468 370 HOH   HOH A . 
G 5 HOH   169 469 357 HOH   HOH A . 
G 5 HOH   170 470 201 HOH   HOH A . 
G 5 HOH   171 471 196 HOH   HOH A . 
G 5 HOH   172 472 366 HOH   HOH A . 
G 5 HOH   173 473 371 HOH   HOH A . 
G 5 HOH   174 474 138 HOH   HOH A . 
G 5 HOH   175 475 329 HOH   HOH A . 
G 5 HOH   176 476 156 HOH   HOH A . 
G 5 HOH   177 477 96  HOH   HOH A . 
G 5 HOH   178 478 330 HOH   HOH A . 
G 5 HOH   179 479 91  HOH   HOH A . 
G 5 HOH   180 480 109 HOH   HOH A . 
G 5 HOH   181 481 334 HOH   HOH A . 
G 5 HOH   182 482 254 HOH   HOH A . 
G 5 HOH   183 483 188 HOH   HOH A . 
G 5 HOH   184 484 272 HOH   HOH A . 
G 5 HOH   185 485 335 HOH   HOH A . 
G 5 HOH   186 486 361 HOH   HOH A . 
G 5 HOH   187 487 367 HOH   HOH A . 
H 5 HOH   1   301 87  HOH   HOH C . 
H 5 HOH   2   302 316 HOH   HOH C . 
H 5 HOH   3   303 234 HOH   HOH C . 
H 5 HOH   4   304 202 HOH   HOH C . 
H 5 HOH   5   305 160 HOH   HOH C . 
H 5 HOH   6   306 124 HOH   HOH C . 
H 5 HOH   7   307 145 HOH   HOH C . 
H 5 HOH   8   308 356 HOH   HOH C . 
H 5 HOH   9   309 103 HOH   HOH C . 
H 5 HOH   10  310 175 HOH   HOH C . 
H 5 HOH   11  311 351 HOH   HOH C . 
H 5 HOH   12  312 95  HOH   HOH C . 
H 5 HOH   13  313 247 HOH   HOH C . 
H 5 HOH   14  314 20  HOH   HOH C . 
H 5 HOH   15  315 184 HOH   HOH C . 
H 5 HOH   16  316 113 HOH   HOH C . 
H 5 HOH   17  317 305 HOH   HOH C . 
H 5 HOH   18  318 18  HOH   HOH C . 
H 5 HOH   19  319 53  HOH   HOH C . 
H 5 HOH   20  320 209 HOH   HOH C . 
H 5 HOH   21  321 257 HOH   HOH C . 
H 5 HOH   22  322 90  HOH   HOH C . 
H 5 HOH   23  323 161 HOH   HOH C . 
H 5 HOH   24  324 49  HOH   HOH C . 
H 5 HOH   25  325 225 HOH   HOH C . 
H 5 HOH   26  326 67  HOH   HOH C . 
H 5 HOH   27  327 226 HOH   HOH C . 
H 5 HOH   28  328 353 HOH   HOH C . 
H 5 HOH   29  329 57  HOH   HOH C . 
H 5 HOH   30  330 352 HOH   HOH C . 
H 5 HOH   31  331 253 HOH   HOH C . 
H 5 HOH   32  332 25  HOH   HOH C . 
H 5 HOH   33  333 112 HOH   HOH C . 
H 5 HOH   34  334 121 HOH   HOH C . 
H 5 HOH   35  335 68  HOH   HOH C . 
H 5 HOH   36  336 262 HOH   HOH C . 
H 5 HOH   37  337 203 HOH   HOH C . 
H 5 HOH   38  338 178 HOH   HOH C . 
H 5 HOH   39  339 243 HOH   HOH C . 
H 5 HOH   40  340 236 HOH   HOH C . 
H 5 HOH   41  341 1   HOH   HOH C . 
H 5 HOH   42  342 286 HOH   HOH C . 
H 5 HOH   43  343 320 HOH   HOH C . 
H 5 HOH   44  344 10  HOH   HOH C . 
H 5 HOH   45  345 170 HOH   HOH C . 
H 5 HOH   46  346 174 HOH   HOH C . 
H 5 HOH   47  347 315 HOH   HOH C . 
H 5 HOH   48  348 283 HOH   HOH C . 
H 5 HOH   49  349 48  HOH   HOH C . 
H 5 HOH   50  350 166 HOH   HOH C . 
H 5 HOH   51  351 322 HOH   HOH C . 
H 5 HOH   52  352 191 HOH   HOH C . 
H 5 HOH   53  353 362 HOH   HOH C . 
H 5 HOH   54  354 263 HOH   HOH C . 
H 5 HOH   55  355 28  HOH   HOH C . 
H 5 HOH   56  356 165 HOH   HOH C . 
H 5 HOH   57  357 349 HOH   HOH C . 
H 5 HOH   58  358 31  HOH   HOH C . 
H 5 HOH   59  359 22  HOH   HOH C . 
H 5 HOH   60  360 186 HOH   HOH C . 
H 5 HOH   61  361 140 HOH   HOH C . 
H 5 HOH   62  362 279 HOH   HOH C . 
H 5 HOH   63  363 55  HOH   HOH C . 
H 5 HOH   64  364 192 HOH   HOH C . 
H 5 HOH   65  365 12  HOH   HOH C . 
H 5 HOH   66  366 37  HOH   HOH C . 
H 5 HOH   67  367 173 HOH   HOH C . 
H 5 HOH   68  368 302 HOH   HOH C . 
H 5 HOH   69  369 107 HOH   HOH C . 
H 5 HOH   70  370 327 HOH   HOH C . 
H 5 HOH   71  371 76  HOH   HOH C . 
H 5 HOH   72  372 144 HOH   HOH C . 
H 5 HOH   73  373 212 HOH   HOH C . 
H 5 HOH   74  374 340 HOH   HOH C . 
H 5 HOH   75  375 155 HOH   HOH C . 
H 5 HOH   76  376 89  HOH   HOH C . 
H 5 HOH   77  377 267 HOH   HOH C . 
H 5 HOH   78  378 73  HOH   HOH C . 
H 5 HOH   79  379 227 HOH   HOH C . 
H 5 HOH   80  380 33  HOH   HOH C . 
H 5 HOH   81  381 52  HOH   HOH C . 
H 5 HOH   82  382 47  HOH   HOH C . 
H 5 HOH   83  383 60  HOH   HOH C . 
H 5 HOH   84  384 71  HOH   HOH C . 
H 5 HOH   85  385 354 HOH   HOH C . 
H 5 HOH   86  386 180 HOH   HOH C . 
H 5 HOH   87  387 123 HOH   HOH C . 
H 5 HOH   88  388 120 HOH   HOH C . 
H 5 HOH   89  389 152 HOH   HOH C . 
H 5 HOH   90  390 24  HOH   HOH C . 
H 5 HOH   91  391 303 HOH   HOH C . 
H 5 HOH   92  392 337 HOH   HOH C . 
H 5 HOH   93  393 63  HOH   HOH C . 
H 5 HOH   94  394 35  HOH   HOH C . 
H 5 HOH   95  395 29  HOH   HOH C . 
H 5 HOH   96  396 213 HOH   HOH C . 
H 5 HOH   97  397 278 HOH   HOH C . 
H 5 HOH   98  398 274 HOH   HOH C . 
H 5 HOH   99  399 249 HOH   HOH C . 
H 5 HOH   100 400 32  HOH   HOH C . 
H 5 HOH   101 401 172 HOH   HOH C . 
H 5 HOH   102 402 190 HOH   HOH C . 
H 5 HOH   103 403 150 HOH   HOH C . 
H 5 HOH   104 404 308 HOH   HOH C . 
H 5 HOH   105 405 54  HOH   HOH C . 
H 5 HOH   106 406 189 HOH   HOH C . 
H 5 HOH   107 407 295 HOH   HOH C . 
H 5 HOH   108 408 79  HOH   HOH C . 
H 5 HOH   109 409 289 HOH   HOH C . 
H 5 HOH   110 410 208 HOH   HOH C . 
H 5 HOH   111 411 309 HOH   HOH C . 
H 5 HOH   112 412 187 HOH   HOH C . 
H 5 HOH   113 413 105 HOH   HOH C . 
H 5 HOH   114 414 176 HOH   HOH C . 
H 5 HOH   115 415 83  HOH   HOH C . 
H 5 HOH   116 416 325 HOH   HOH C . 
H 5 HOH   117 417 341 HOH   HOH C . 
H 5 HOH   118 418 126 HOH   HOH C . 
H 5 HOH   119 419 148 HOH   HOH C . 
H 5 HOH   120 420 62  HOH   HOH C . 
H 5 HOH   121 421 136 HOH   HOH C . 
H 5 HOH   122 422 72  HOH   HOH C . 
H 5 HOH   123 423 204 HOH   HOH C . 
H 5 HOH   124 424 88  HOH   HOH C . 
H 5 HOH   125 425 82  HOH   HOH C . 
H 5 HOH   126 426 2   HOH   HOH C . 
H 5 HOH   127 427 41  HOH   HOH C . 
H 5 HOH   128 428 200 HOH   HOH C . 
H 5 HOH   129 429 38  HOH   HOH C . 
H 5 HOH   130 430 42  HOH   HOH C . 
H 5 HOH   131 431 94  HOH   HOH C . 
H 5 HOH   132 432 233 HOH   HOH C . 
H 5 HOH   133 433 13  HOH   HOH C . 
H 5 HOH   134 434 314 HOH   HOH C . 
H 5 HOH   135 435 162 HOH   HOH C . 
H 5 HOH   136 436 284 HOH   HOH C . 
H 5 HOH   137 437 171 HOH   HOH C . 
H 5 HOH   138 438 157 HOH   HOH C . 
H 5 HOH   139 439 154 HOH   HOH C . 
H 5 HOH   140 440 339 HOH   HOH C . 
H 5 HOH   141 441 128 HOH   HOH C . 
H 5 HOH   142 442 3   HOH   HOH C . 
H 5 HOH   143 443 50  HOH   HOH C . 
H 5 HOH   144 444 141 HOH   HOH C . 
H 5 HOH   145 445 134 HOH   HOH C . 
H 5 HOH   146 446 323 HOH   HOH C . 
H 5 HOH   147 447 313 HOH   HOH C . 
H 5 HOH   148 448 100 HOH   HOH C . 
H 5 HOH   149 449 110 HOH   HOH C . 
H 5 HOH   150 450 224 HOH   HOH C . 
H 5 HOH   151 451 359 HOH   HOH C . 
H 5 HOH   152 452 59  HOH   HOH C . 
H 5 HOH   153 453 93  HOH   HOH C . 
H 5 HOH   154 454 114 HOH   HOH C . 
H 5 HOH   155 455 347 HOH   HOH C . 
H 5 HOH   156 456 116 HOH   HOH C . 
H 5 HOH   157 457 119 HOH   HOH C . 
H 5 HOH   158 458 348 HOH   HOH C . 
H 5 HOH   159 459 319 HOH   HOH C . 
H 5 HOH   160 460 229 HOH   HOH C . 
H 5 HOH   161 461 265 HOH   HOH C . 
H 5 HOH   162 462 246 HOH   HOH C . 
H 5 HOH   163 463 215 HOH   HOH C . 
H 5 HOH   164 464 237 HOH   HOH C . 
H 5 HOH   165 465 130 HOH   HOH C . 
H 5 HOH   166 466 355 HOH   HOH C . 
H 5 HOH   167 467 328 HOH   HOH C . 
H 5 HOH   168 468 238 HOH   HOH C . 
H 5 HOH   169 469 64  HOH   HOH C . 
H 5 HOH   170 470 269 HOH   HOH C . 
H 5 HOH   171 471 268 HOH   HOH C . 
H 5 HOH   172 472 164 HOH   HOH C . 
H 5 HOH   173 473 331 HOH   HOH C . 
H 5 HOH   174 474 363 HOH   HOH C . 
H 5 HOH   175 475 158 HOH   HOH C . 
H 5 HOH   176 476 245 HOH   HOH C . 
H 5 HOH   177 477 261 HOH   HOH C . 
H 5 HOH   178 478 260 HOH   HOH C . 
H 5 HOH   179 479 364 HOH   HOH C . 
H 5 HOH   180 480 256 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           7HUT 
_cell.length_a           87.008 
_cell.length_b           57.557 
_cell.length_c           64.931 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.60 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HUT 
_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          7HUT 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.55 
_exptl_crystal.density_percent_sol   51.75 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-10-10 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92208 
_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        0.92208 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUT 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             27.39 
_reflns.d_resolution_high            1.47 
_reflns.number_obs                   52733 
_reflns.percent_possible_obs         97.0 
_reflns.pdbx_Rmerge_I_obs            0.144 
_reflns.pdbx_netI_over_sigmaI        9.6 
_reflns.pdbx_redundancy              6.8 
_reflns.pdbx_Rrim_I_all              0.156 
_reflns.pdbx_Rpim_I_all              0.059 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     358807 
_reflns.pdbx_chi_squared             0.93 
_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                  1.47 
_reflns_shell.d_res_low                   1.49 
_reflns_shell.number_measured_all         13280 
_reflns_shell.number_unique_obs           2505 
_reflns_shell.Rmerge_I_obs                1.934 
_reflns_shell.pdbx_chi_squared            0.44 
_reflns_shell.pdbx_redundancy             5.3 
_reflns_shell.percent_possible_obs        94.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             2.151 
_reflns_shell.pdbx_Rpim_I_all             0.922 
_reflns_shell.pdbx_CC_half                0.217 
_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                                 7HUT 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     52711 
_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                             21.50 
_refine.ls_d_res_high                            1.470 
_refine.ls_percent_reflns_obs                    96.8 
_refine.ls_R_factor_obs                          0.1898 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1886 
_refine.ls_R_factor_R_free                       0.2121 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.960 
_refine.ls_number_reflns_R_free                  2615 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               22.04 
_refine.aniso_B[1][1]                            0.49430 
_refine.aniso_B[2][2]                            -0.21940 
_refine.aniso_B[3][3]                            -0.27490 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.60370 
_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             0.069 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.069 
_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                        7HUT 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_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        2157 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             367 
_refine_hist.number_atoms_total               2553 
_refine_hist.d_res_high                       1.470 
_refine_hist.d_res_low                        21.50 
# 
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  2262 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.99  ? 2.00  3088 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  759  '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 2262 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.28  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.85 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  '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  2092 '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                       1.47 
_refine_ls_shell.d_res_low                        1.48 
_refine_ls_shell.number_reflns_R_work             1002 
_refine_ls_shell.R_factor_R_work                  0.3113 
_refine_ls_shell.percent_reflns_obs               93.72 
_refine_ls_shell.R_factor_R_free                  0.3131 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.02 
_refine_ls_shell.number_reflns_R_free             53 
_refine_ls_shell.number_reflns_all                1055 
_refine_ls_shell.R_factor_all                     0.3114 
# 
_struct.entry_id                  7HUT 
_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-0031936-001 (A71EV2A-x3208)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUT 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HUT A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HUT 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,G 
2 1 B,E,F,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.319 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 111.9 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 105.9 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.7 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 106.2 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.1 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.8 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.7 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.2 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.5 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.4 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.3 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
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 
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 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 121 ? GLY A 119 GLY A 127 
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 TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
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 VAL B 68  ? O VAL C 74  N GLY B 55  ? N GLY C 61  
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 ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HUT 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O C HOH 343 ? ? O C HOH 423 ? ? 1.98 
2 1 O C HOH 378 ? ? O C HOH 440 ? ? 2.07 
3 1 O A HOH 312 ? ? O A HOH 419 ? ? 2.16 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    CYS 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     56 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -170.38 
_pdbx_validate_torsion.psi             -179.68 
# 
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 14.8645 8.2708   14.5545 -0.0130 -0.0228 -0.0138 0.0070 -0.0047 0.0006 1.1019 0.7209 0.6862 0.6057 
-0.1407 -0.1577 -0.0312 0.0442 0.0761 0.0150 0.0531 0.0079 -0.0078 -0.0430 -0.0219 
'X-RAY DIFFRACTION' 2 ? refined 25.9838 -20.3552 17.8346 -0.0206 -0.0188 0.0055  0.0022 -0.0040 0.0256 0.4941 0.8877 0.5382 0.1101 
-0.0391 -0.3180 0.0234  0.0187 0.1352 0.0027 0.0703 0.0726 0.0525  0.0058  -0.0937 
# 
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                       487 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.81 
_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 ALA 147 ? B ALA 141 
7 1 Y 1 C MET 148 ? B MET 142 
8 1 Y 1 C GLU 149 ? B GLU 143 
9 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 
A1BON N1   N  N N 1   
A1BON C4   C  N N 2   
A1BON C5   C  N N 3   
A1BON C6   C  N N 4   
A1BON C7   C  Y N 5   
A1BON C8   C  Y N 6   
A1BON C10  C  N N 7   
A1BON C13  C  Y N 8   
A1BON CL   CL N N 9   
A1BON C12  C  Y N 10  
A1BON C11  C  Y N 11  
A1BON C9   C  Y N 12  
A1BON F2   F  N N 13  
A1BON F1   F  N N 14  
A1BON F    F  N N 15  
A1BON O1   O  N N 16  
A1BON C3   C  N N 17  
A1BON C2   C  N N 18  
A1BON C14  C  N N 19  
A1BON C1   C  N S 20  
A1BON C    C  N N 21  
A1BON O    O  N N 22  
A1BON N    N  N N 23  
A1BON H8   H  N N 24  
A1BON H7   H  N N 25  
A1BON H10  H  N N 26  
A1BON H9   H  N N 27  
A1BON H11  H  N N 28  
A1BON H13  H  N N 29  
A1BON H12  H  N N 30  
A1BON H6   H  N N 31  
A1BON H5   H  N N 32  
A1BON H4   H  N N 33  
A1BON H3   H  N N 34  
A1BON H15  H  N N 35  
A1BON H14  H  N N 36  
A1BON H    H  N N 37  
A1BON H1   H  N N 38  
A1BON H2   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1BON N   C    sing N N 1   
A1BON O   C    doub N N 2   
A1BON C   C1   sing N N 3   
A1BON C1  C2   sing N N 4   
A1BON C2  C3   sing N N 5   
A1BON C3  C4   sing N N 6   
A1BON C4  N1   sing N N 7   
A1BON N1  C5   sing N N 8   
A1BON O1  C5   doub N N 9   
A1BON C5  C6   sing N N 10  
A1BON C6  C7   sing N N 11  
A1BON C7  C8   doub Y N 12  
A1BON C8  C9   sing Y N 13  
A1BON C10 C9   sing N N 14  
A1BON F   C10  sing N N 15  
A1BON F1  C10  sing N N 16  
A1BON F2  C10  sing N N 17  
A1BON C9  C11  doub Y N 18  
A1BON C11 C12  sing Y N 19  
A1BON C12 C13  doub Y N 20  
A1BON C7  C13  sing Y N 21  
A1BON C13 CL   sing N N 22  
A1BON C14 N1   sing N N 23  
A1BON C1  C14  sing N N 24  
A1BON C4  H8   sing N N 25  
A1BON C4  H7   sing N N 26  
A1BON C6  H10  sing N N 27  
A1BON C6  H9   sing N N 28  
A1BON C8  H11  sing N N 29  
A1BON C12 H13  sing N N 30  
A1BON C11 H12  sing N N 31  
A1BON C3  H6   sing N N 32  
A1BON C3  H5   sing N N 33  
A1BON C2  H4   sing N N 34  
A1BON C2  H3   sing N N 35  
A1BON C14 H15  sing N N 36  
A1BON C14 H14  sing N N 37  
A1BON C1  H    sing N N 38  
A1BON N   H1   sing N N 39  
A1BON N   H2   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HUT 
_atom_sites.fract_transf_matrix[1][1]   0.011493 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000925 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017374 
_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]   0.015451 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
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   ? 17.531 8.288   24.812 1.00 18.01 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.785 8.364   24.049 1.00 18.44 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.949 7.134   23.144 1.00 18.24 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.213 6.134   23.304 1.00 18.43 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.966 8.472   25.018 1.00 21.81 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.089 7.246   25.722 1.00 23.58 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.887 7.214   22.198 1.00 16.71 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.161 6.091   21.310 1.00 15.70 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.600 6.529   19.922 1.00 15.59 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.262 7.635   19.485 1.00 16.09 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.307 5.646   19.217 1.00 14.09 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.791 5.991   17.884 1.00 14.52 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.788 4.763   16.981 1.00 14.33 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.650 3.634   17.463 1.00 15.03 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.223 6.540   18.008 1.00 15.37 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.902 4.982   15.660 1.00 13.60 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.116 3.914   14.674 1.00 13.31 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.591 4.012   14.307 1.00 13.98 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.087 5.125   14.032 1.00 14.53 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.277 4.117   13.400 1.00 14.36 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.786 4.283   13.705 1.00 15.72 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.531 2.967   12.414 1.00 14.24 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.971 4.819   12.470 1.00 15.93 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.311 2.871   14.292 1.00 13.86 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.733 2.871   13.922 1.00 14.56 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.864 2.018   12.625 1.00 15.82 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.831 0.799   12.698 1.00 16.35 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.584 2.276   15.065 1.00 14.67 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.619 3.172   16.283 1.00 15.02 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.453 4.287   16.331 1.00 15.68 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.737 2.976   17.343 1.00 15.74 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.466 5.135   17.433 1.00 16.43 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.745 3.829   18.454 1.00 16.52 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.583 4.927   18.471 1.00 17.24 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.619 5.805   19.541 1.00 19.72 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.933 2.684   11.459 1.00 15.58 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.015 2.025   10.156 1.00 16.19 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.249 2.532   9.466  1.00 17.73 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.467 3.737   9.411  1.00 17.52 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.734 2.255   9.290  1.00 17.02 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.321 3.743   9.221  1.00 17.43 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.905 1.667   7.896  1.00 17.85 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.130 1.615   9.017  1.00 18.31 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.386 2.030   8.385  1.00 17.94 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.184 2.948   9.302  1.00 18.41 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.283 2.668   10.505 1.00 17.83 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.648 4.097   8.769  1.00 17.45 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.327 5.075   9.618  1.00 16.90 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.402 6.261   9.940  1.00 16.49 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.865 7.418   10.045 1.00 17.42 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.663 5.517   9.051  1.00 18.66 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.725 4.440   9.170  1.00 22.66 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.508 4.393   10.128 1.00 25.28 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.775 3.561   8.198  1.00 22.43 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.123 5.958   10.176 1.00 15.69 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.141 6.999   10.513 1.00 15.61 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.440 6.679   11.826 1.00 15.98 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.180 5.497   12.148 1.00 15.94 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.053 7.090   9.417  1.00 15.33 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.552 7.488   8.043  1.00 16.74 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.232 8.689   7.841  1.00 18.28 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.368 6.656   6.958  1.00 17.61 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.682 9.059   6.574  1.00 19.00 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.801 7.019   5.691  1.00 18.47 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.447 8.223   5.499  1.00 20.17 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.893 8.577   4.244  1.00 23.80 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.095 7.753   12.566 1.00 14.70 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.319 7.705   13.797 1.00 13.64 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.093 8.567   13.525 1.00 14.08 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.242 9.755   13.208 1.00 14.90 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.134 8.294   14.983 1.00 13.14 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.307 8.598   16.244 1.00 14.38 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.218 8.948   17.436 1.00 16.21 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.674 10.042  18.259 1.00 16.55 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.967 9.868   19.370 1.00 18.88 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.680 8.640   19.798 1.00 18.89 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.515 10.921  20.046 1.00 18.16 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.879 7.944   13.571 1.00 12.82 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.610 8.661   13.298 1.00 13.14 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.929 8.873   14.634 1.00 14.32 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.627 7.901   15.340 1.00 13.85 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.688 7.859   12.365 1.00 13.35 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.473 8.711   11.927 1.00 14.32 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.441 7.348   11.142 1.00 13.99 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.668 10.143  14.982 1.00 13.89 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.010 10.465  16.247 0.50 13.06 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.099 10.559  16.274 0.50 15.16 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.886 11.488  16.018 1.00 14.30 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.778 12.116  14.941 1.00 15.15 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.034 11.059  17.254 0.50 11.70 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.169 11.398  17.098 0.50 17.63 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.986 10.004  17.776 0.50 11.12 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.884 11.383  18.598 0.50 17.91 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.762 12.269  16.667 0.50 10.12 ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.618 10.982  16.837 0.50 19.79 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.039 11.697  17.062 1.00 13.55 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.005 12.736  16.979 1.00 13.43 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.801 14.060  16.998 1.00 13.59 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.721 14.231  17.828 1.00 14.52 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.146 12.721  18.238 1.00 13.55 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.287 11.488  18.351 1.00 15.21 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.670 10.503  19.004 1.00 16.13 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.094 11.536  17.728 1.00 14.05 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.499 14.994  16.070 1.00 12.66 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.260 16.271  16.046 1.00 13.28 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.186 16.974  17.403 1.00 15.42 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.168 17.551  17.849 1.00 16.84 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.647 17.186  14.963 1.00 14.51 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.449 18.467  14.671 1.00 15.88 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.662 19.356  13.707 1.00 17.24 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.409 20.537  13.242 1.00 21.27 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.449 21.701  13.887 1.00 22.58 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.874 21.827  15.083 1.00 20.51 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.096 22.744  13.354 1.00 21.50 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.008 16.900  18.077 1.00 14.94 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.859 17.604  19.354 1.00 15.30 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.683 17.004  20.506 1.00 16.50 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.813 17.655  21.552 1.00 17.65 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.368 17.764  19.738 1.00 16.22 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.709 16.530  20.281 1.00 15.80 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.088 15.602  19.445 1.00 16.39 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.539 16.137  21.572 1.00 16.50 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.605 14.660  20.257 1.00 16.81 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.802 14.972  21.543 1.00 17.12 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.252 15.802  20.313 1.00 15.78 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.108 15.145  21.318 1.00 16.10 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.596 15.071  20.892 1.00 16.63 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.412 14.417  21.554 1.00 17.15 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.560 13.753  21.661 1.00 16.59 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.145 13.737  22.217 1.00 18.23 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.744 12.305  22.541 1.00 18.68 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.050 14.573  23.530 1.00 18.98 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.946 15.693  19.745 1.00 16.00 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.331 15.677  19.282 1.00 16.01 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.266 16.345  20.273 1.00 17.45 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.898 17.341  20.911 1.00 18.09 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.441 16.343  17.917 1.00 15.84 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.444 15.734  20.437 1.00 17.26 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.473 16.233  21.353 1.00 17.75 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.395 17.230  20.622 1.00 17.35 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.352 17.350  19.384 1.00 17.06 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.340 15.050  21.849 1.00 19.51 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.079 14.510  20.734 1.00 20.39 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.518 13.944  22.491 1.00 20.46 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.289 17.924  21.370 1.00 17.26 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.275 18.793  20.748 1.00 18.49 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.164 17.981  19.800 1.00 18.57 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.436 18.458  18.705 1.00 18.50 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.147 19.505  21.810 1.00 21.43 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.382 20.149  21.234 1.00 29.57 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.320 21.372  20.586 1.00 33.71 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.655 19.681  21.171 1.00 32.68 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.557 21.648  20.205 1.00 34.50 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.401 20.655  20.523 1.00 35.31 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.568 16.739  20.189 1.00 17.67 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.395 15.928  19.295 1.00 18.25 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.650 15.632  17.991 1.00 16.63 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.279 15.601  16.941 1.00 17.26 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.871 14.621  19.936 1.00 20.12 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.860 13.906  19.052 1.00 27.65 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.019 14.338  18.927 1.00 31.04 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.416 12.862  18.348 1.00 29.57 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.310 15.436  18.053 1.00 15.66 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.544 15.190  16.832 1.00 14.97 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.629 16.421  15.906 1.00 16.00 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.865 16.266  14.706 1.00 16.37 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.060 14.896  17.129 1.00 15.31 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.814 13.540  17.744 1.00 17.95 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.497 12.546  17.314 1.00 16.24 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.936 13.453  18.650 1.00 17.20 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.411 17.634  16.456 1.00 16.20 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.485 18.858  15.652 1.00 16.88 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.895 19.120  15.117 1.00 17.60 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.032 19.678  14.033 1.00 17.82 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.984 20.085  16.477 1.00 17.28 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.487 20.136  16.587 1.00 17.65 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.707 19.767  17.653 1.00 18.55 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.590 20.559  15.559 1.00 17.81 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.372 19.993  17.363 1.00 18.44 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.274 20.443  16.063 1.00 18.65 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.773 21.008  14.249 1.00 18.66 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.156 20.806  15.302 1.00 19.32 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.678 21.340  13.494 1.00 19.29 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.393 21.257  14.015 1.00 19.42 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.937 18.730  15.866 1.00 17.18 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.327 18.923  15.428 1.00 18.40 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.760 17.901  14.366 1.00 19.12 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.807 18.081  13.748 1.00 19.72 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.264 18.845  16.639 1.00 19.79 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.945 16.840  14.135 1.00 17.91 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.233 15.797  13.130 1.00 17.74 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.982 15.595  12.258 1.00 17.30 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.609 14.465  11.926 1.00 17.17 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.641 14.491  13.847 1.00 18.26 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.967 14.666  14.553 1.00 22.03 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.016 14.623  13.905 1.00 22.74 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.947 14.952  15.868 1.00 21.80 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.326 16.704  11.902 1.00 16.81 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.057 16.693  11.192 1.00 16.36 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.137 16.210  9.765  1.00 17.16 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.970 16.697  8.983  1.00 18.53 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.467 18.121  11.195 1.00 15.57 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.081 18.260  10.580 1.00 17.56 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.050 17.431  11.374 1.00 18.04 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.632 19.706  10.573 1.00 19.90 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.219 15.309  9.397  1.00 15.92 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.101 14.869  8.005  1.00 16.36 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.866 15.559  7.381  1.00 17.13 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.940 16.087  6.267  1.00 18.30 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.972 13.321  7.913  1.00 16.81 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.652 12.886  6.479  1.00 17.38 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.252 12.638  8.410  1.00 18.34 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.710 15.502  8.095  1.00 15.75 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.458 16.053  7.559  1.00 17.00 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.462 16.245  8.698  1.00 17.12 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.475 15.462  9.653  1.00 16.45 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.856 15.037  6.553  1.00 17.72 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.449 15.302  6.085  1.00 18.84 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 22.063 16.121  5.062  1.00 20.90 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.248 14.654  6.557  1.00 18.48 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.693 16.044  4.885  1.00 21.61 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.166 15.174  5.810  1.00 20.08 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.979 13.727  7.566  1.00 19.11 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.833 14.733  5.998  1.00 19.99 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.665 13.313  7.761  1.00 19.59 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.610 13.816  6.988  1.00 19.56 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.631 17.280  8.621  1.00 16.88 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.604 17.476  9.633  1.00 16.41 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.369 18.072  8.988  1.00 17.32 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.485 18.821  7.997  1.00 17.76 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.095 18.345  10.798 1.00 17.02 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.722 19.680  10.391 1.00 17.99 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.762 20.841  10.171 1.00 22.55 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.120 21.766  9.403  1.00 23.16 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.638 20.818  10.729 1.00 21.78 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.195 17.790  9.570  1.00 16.33 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.959 18.364  9.034  1.00 16.07 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.986 18.557  10.176 1.00 17.10 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.444 17.578  10.695 1.00 16.69 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.370 17.448  7.938  1.00 19.04 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.173 18.011  7.199  1.00 25.10 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.369 18.706  7.830  1.00 26.70 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 16.030 17.722  5.988  1.00 28.14 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.772 19.819  10.589 1.00 18.09 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.860 20.151  11.683 0.50 18.09 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.875 20.099  11.701 0.50 18.33 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.430 19.690  11.404 1.00 18.14 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.731 19.230  12.319 1.00 18.11 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.870 21.658  11.959 0.50 19.84 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.948 21.570  12.108 0.50 20.71 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.871 22.019  12.899 0.50 21.61 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.583 22.389  11.013 0.50 23.54 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.973 19.843  10.142 1.00 17.62 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.598 19.443  9.798  1.00 18.18 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.364 17.941  9.978  1.00 18.04 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.216 17.534  10.102 1.00 18.99 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.223 19.894  8.381  1.00 20.54 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.831 19.090  7.380  1.00 24.75 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.431 17.116  9.992  1.00 16.24 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.308 15.663  10.204 1.00 15.29 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.750 15.215  11.632 1.00 14.94 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.643 14.022  11.962 1.00 14.64 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.169 14.897  9.172  1.00 15.79 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.658 15.075  7.734  1.00 16.76 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.550 14.354  6.726  1.00 17.31 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.421 12.903  6.875  1.00 17.02 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.564 12.028  5.886  1.00 17.79 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.797 12.450  4.643  1.00 19.28 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.415 10.719  6.119  1.00 17.52 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.314 16.157  12.443 1.00 13.26 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.890 15.808  13.744 1.00 13.04 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.028 14.801  13.586 1.00 13.24 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.257 13.972  14.478 1.00 14.21 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.863 15.317  14.787 1.00 14.12 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.460 15.095  16.166 1.00 15.31 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.274 15.937  16.607 1.00 15.73 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.089 14.094  16.828 1.00 15.28 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.827 14.915  12.479 1.00 13.02 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.952 13.972  12.305 1.00 12.95 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.288 14.690  12.199 1.00 14.02 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.358 15.783  11.618 1.00 14.73 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.809 13.107  11.046 1.00 13.06 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.674 12.050  11.082 1.00 14.40 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.558 11.321  9.748  1.00 16.02 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.897 11.008  12.210 1.00 14.89 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.348 14.012  12.668 1.00 13.05 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.713 14.500  12.516 1.00 13.44 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.593 13.277  12.359 1.00 14.41 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.403 12.273  13.058 1.00 15.17 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.176 15.341  13.739 1.00 13.06 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.614 15.933  13.653 1.00 14.32 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.678 17.290  14.304 1.00 15.17 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.653 14.991  14.328 1.00 15.62 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.569 13.351  11.440 1.00 14.16 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.508 12.253  11.229 1.00 14.14 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.922 12.774  11.399 1.00 14.64 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.279 13.794  10.797 1.00 15.07 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.318 11.644  9.823  1.00 14.07 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.350 10.557  9.565  1.00 15.62 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.881 11.103  9.643  1.00 14.42 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.730 12.072  12.229 1.00 13.92 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.136 12.438  12.413 1.00 14.61 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.041 11.274  11.969 1.00 16.25 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.566 10.135  11.761 1.00 16.32 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.406 12.817  13.867 1.00 15.12 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.096 11.756  14.750 1.00 15.49 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.344 11.557  11.791 1.00 15.93 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.272 10.499  11.370 1.00 17.52 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.907 9.787   12.583 1.00 19.20 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.076 10.397  13.654 1.00 19.98 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.365 11.088  10.482 1.00 19.75 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.062 12.071  11.234 1.00 22.21 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.246 8.484   12.416 1.00 19.24 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.828 7.689   13.496 1.00 20.22 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.172 7.095   13.078 1.00 22.57 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.419 6.897   11.886 1.00 22.53 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.892 6.529   13.911 1.00 20.78 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.746 5.605   12.829 1.00 22.63 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.523 7.020   14.342 1.00 20.10 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 35.027 6.791   14.059 1.00 24.02 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.308 6.157   13.763 1.00 25.80 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.095 4.645   13.590 1.00 25.95 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.622 4.055   12.644 1.00 27.45 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.341 6.526   14.831 1.00 29.16 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.864 6.086   16.091 1.00 32.82 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.601 8.025   14.883 1.00 29.42 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.279 4.033   14.461 1.00 25.32 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 35.011 2.590   14.353 1.00 25.41 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.814 2.297   13.446 1.00 24.24 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.879 3.107   13.386 1.00 23.38 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.744 2.009   15.732 1.00 26.59 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.836 1.127   12.761 1.00 23.06 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.745 0.689   11.894 1.00 23.58 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.592 0.121   12.714 1.00 23.10 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.826 -0.595  13.688 1.00 23.48 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.243 -0.370  10.904 1.00 26.96 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 34.040 0.228   9.747  1.00 32.34 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.438 -0.827  8.749  1.00 38.31 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.245 -1.719  9.037  1.00 38.28 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.867 -0.744  7.553  1.00 41.03 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.359 0.498   12.357 1.00 20.48 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.170 0.043   13.050 1.00 19.91 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.605 -1.231  12.463 1.00 18.63 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.993 -1.651  11.368 1.00 19.14 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.677 -1.869  13.230 1.00 17.88 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 27.095 -3.175  12.843 1.00 18.47 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.649 -3.135  12.395 1.00 18.61 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 25.136 -4.186  11.938 1.00 19.37 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.270 -4.215  13.949 1.00 19.54 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.993 -4.625  14.292 1.00 22.64 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.979 -1.970  12.520 1.00 17.01 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.587 -1.897  12.084 1.00 17.08 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.507 -1.842  10.554 1.00 18.01 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.406 -1.306  9.915  1.00 18.12 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.916 -0.644  12.696 1.00 16.85 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.822 -0.687  14.220 1.00 18.34 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.541 -1.792  14.764 1.00 18.89 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.989 0.385   14.870 1.00 17.34 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.429 -2.383  9.972  1.00 18.48 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.181 -2.275  8.526  1.00 19.26 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.844 -1.562  8.347  1.00 18.54 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.923 -1.770  9.147  1.00 20.22 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 22.095 -3.630  7.862  1.00 22.30 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 21.078 -4.355  8.524  1.00 25.61 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 23.413 -4.385  7.990  1.00 23.55 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.738 -0.735  7.291  1.00 17.44 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.502 0.003   7.074  1.00 16.18 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.541 -0.795  6.191  1.00 17.10 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.934 -1.331  5.133  1.00 18.18 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.797 1.389   6.428  1.00 16.17 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.886 2.178   7.216  1.00 16.28 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.501 2.240   6.322  1.00 16.89 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.464 2.480   8.713  1.00 16.96 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.279 -0.830  6.580  1.00 16.08 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.233 -1.456  5.790  1.00 16.60 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.981 -0.611  4.514  1.00 17.64 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.973 0.638   4.558  1.00 17.38 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.953 -1.486  6.606  1.00 15.58 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.780 -1.306  3.360  1.00 18.23 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.455 -0.620  2.106  1.00 19.07 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.165 -1.331  1.603  1.00 21.45 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.196 -2.289  0.817  1.00 22.56 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.622 -0.705  1.098  1.00 18.97 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.958 -0.134  1.627  1.00 19.79 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.951 1.384   1.842  1.00 20.08 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.256 1.851   2.344  1.00 19.46 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.450 3.007   2.972  1.00 21.31 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.447 3.860   3.137  1.00 20.15 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.654 3.328   3.428  1.00 21.41 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 13.038 -0.858  2.082  1.00 21.70 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.759 -1.560  1.922  1.00 22.76 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.576 -0.613  2.163  1.00 23.96 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.754 0.563   2.504  1.00 24.13 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.744 -2.683  2.949  1.00 21.78 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.605 -2.062  4.648  1.00 21.52 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.332  -1.171  2.085  1.00 25.64 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 8.165  -0.380  2.422  1.00 27.42 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.363  -1.060  3.536  1.00 26.64 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 6.148  -0.903  3.586  1.00 27.51 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.288  -0.108  1.186  1.00 34.14 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.701  -1.344  0.541  1.00 44.58 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 7.018  -2.474  1.002  1.00 45.59 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.925  -1.189  -0.434 1.00 50.70 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 8.029  -1.780  4.461  1.00 24.40 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.357  -2.389  5.625  1.00 21.95 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.597  -1.345  6.414  1.00 20.99 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 7.057  -0.212  6.575  1.00 21.97 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.354  -3.096  6.543  1.00 20.23 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 9.052  -4.655  5.916  1.00 21.97 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.448  -1.744  6.945  1.00 19.03 ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.678  -0.897  7.865  1.00 18.87 ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.365  -1.640  9.182  1.00 17.28 ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.482  -1.241  9.946  1.00 17.62 ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.434  -0.278  7.212  1.00 21.57 ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.768  0.758   6.095  1.00 26.12 ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 4.903  1.816   6.313  1.00 33.70 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 5.873  2.078   5.524  1.00 31.75 ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 4.797  2.503   7.391  1.00 34.48 ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 5.118  -2.724  9.448  1.00 15.75 ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 5.108  -3.424  10.715 1.00 16.26 ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.589  -3.659  11.110 1.00 15.31 ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.466  -3.872  10.253 1.00 17.18 ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.326  -4.731  10.708 1.00 20.22 ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.946  -5.640  9.827  1.00 24.40 ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.898  -4.547  10.293 1.00 20.73 ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.850  -3.541  12.393 1.00 13.97 ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.206  -3.738  12.904 1.00 14.26 ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.210  -3.837  14.413 1.00 14.62 ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.167  -4.070  15.013 1.00 15.70 ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.370  -3.634  15.033 1.00 13.43 ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.526  -3.713  16.480 1.00 12.80 ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.396 -2.538  16.906 1.00 12.78 ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.378 -2.244  16.230 1.00 13.81 ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.259 -5.033  16.815 1.00 14.52 ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.685 -5.084  18.283 1.00 16.37 ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.376  -6.243  16.441 1.00 15.06 ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 10.022 -1.851  17.982 1.00 12.33 ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.857 -0.727  18.462 1.00 12.19 ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.286 -0.959  19.905 1.00 12.51 ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.579 -1.607  20.679 1.00 13.27 ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.134 0.646   18.319 1.00 12.27 ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.127  0.980   19.402 1.00 12.38 ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.857  0.415   19.400 1.00 13.98 ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.424  1.903   20.392 1.00 12.66 ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.927  0.720   20.391 1.00 14.06 ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.486  2.251   21.369 1.00 12.71 ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.245  1.634   21.374 1.00 13.71 ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.281  1.902   22.323 1.00 15.77 ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.402 -0.316  20.292 1.00 13.12 ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.889 -0.384  21.668 1.00 13.23 ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.398 0.824   22.447 1.00 13.35 ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.609 1.967   22.032 1.00 13.86 ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.432 -0.407  21.717 1.00 13.17 ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.920 -0.543  23.132 1.00 13.65 ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.591 -1.651  23.890 1.00 13.75 ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.639 0.480   23.742 1.00 14.36 ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.978 -1.752  25.220 1.00 15.21 ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 16.009 0.405   25.076 1.00 15.10 ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.736 -0.741  25.795 1.00 16.34 ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.112 -0.815  27.118 1.00 18.42 ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.820 0.540   23.617 1.00 12.34 ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.236 1.550   24.523 1.00 13.30 ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.063 1.546   25.816 1.00 14.27 ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.872 0.652   26.654 1.00 14.96 ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.781  1.181   24.802 1.00 13.41 ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 8.981  2.250   26.037 1.00 14.81 ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.978 2.537   25.987 1.00 13.15 ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.834 2.570   27.175 1.00 13.87 ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.056 2.723   28.494 1.00 14.71 ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.463 2.154   29.512 1.00 15.74 ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.930 3.630   27.056 1.00 16.13 ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.447 4.959   27.114 1.00 18.96 ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.926 3.468   28.473 1.00 13.45 ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.108 3.677   29.680 1.00 12.96 ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.383 2.389   30.148 1.00 12.93 ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.727  2.409   31.185 1.00 14.55 ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.098 4.806   29.463 1.00 14.00 ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.132  4.486   28.468 1.00 15.68 ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.470 1.294   29.380 1.00 13.03 ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.908  -0.007  29.805 1.00 14.01 ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.987 -1.138  29.694 1.00 16.48 ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.654 -2.301  29.959 1.00 17.72 ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.730  -0.399  28.892 1.00 14.27 ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.524  0.545   29.012 1.00 15.61 ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.761  0.228   30.271 1.00 15.04 ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.591  1.105   30.453 1.00 15.66 ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.631  2.267   31.096 1.00 17.40 ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.771  2.701   31.634 1.00 18.27 ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.523  2.998   31.232 1.00 18.22 ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.213 -0.828  29.191 1.00 17.53 ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.256 -1.856  28.944 1.00 18.40 ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.695 -3.012  28.106 1.00 19.04 ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.903 -4.192  28.415 1.00 20.58 ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.811 -2.409  30.255 1.00 21.11 ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.916 -1.589  30.778 1.00 23.22 ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.657 -2.380  31.855 1.00 24.15 ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.402 -1.404  32.615 1.00 25.32 ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 16.062 -0.970  33.818 1.00 22.71 ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 15.027 -1.516  34.466 1.00 22.85 ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.782 -0.031  34.412 1.00 21.54 ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.896 -2.658  27.105 1.00 17.03 ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.214 -3.657  26.294 1.00 17.47 ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.143 -3.289  24.848 1.00 16.75 ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 11.051 -2.111  24.501 1.00 16.46 ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.768  -3.827  26.782 1.00 21.71 ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.632  -4.777  27.973 1.00 30.83 ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 8.211  -5.260  28.157 1.00 39.14 ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 8.046  -6.027  29.453 1.00 45.51 ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.481  -5.222  30.632 1.00 49.57 ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 11.105 -4.318  23.998 1.00 16.00 ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.906 -4.145  22.559 1.00 15.10 ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.455  -4.510  22.271 1.00 16.83 ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.975  -5.555  22.746 1.00 18.79 ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.828 -5.115  21.783 1.00 14.65 ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.294 -4.816  21.946 1.00 16.10 ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 14.026 -4.131  20.964 1.00 20.05 ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 14.138 -5.184  22.939 1.00 17.11 ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.277 -4.094  21.411 1.00 19.22 ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.394 -4.698  22.588 1.00 19.79 ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.727  -3.627  21.554 1.00 15.04 ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.305  -3.848  21.244 1.00 14.51 ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 7.048  -3.966  19.764 1.00 14.24 ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.510  -3.104  19.001 1.00 13.69 ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.454  -2.651  21.756 1.00 14.37 ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.398  -2.517  23.265 1.00 14.39 ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.636  -3.390  24.038 1.00 14.46 ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.123  -1.534  23.919 1.00 14.92 ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.532  -3.239  25.422 1.00 15.55 ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 7.031  -1.370  25.300 1.00 15.61 ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.251  -2.241  26.053 1.00 16.60 ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.191  -2.089  27.428 1.00 18.93 ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.237  -4.941  19.336 1.00 14.73 ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.823  -4.976  17.916 1.00 15.46 ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.805  -3.855  17.644 1.00 17.35 ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.948  -3.575  18.497 1.00 20.28 ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.098  -6.325  17.788 1.00 17.61 ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.684  -6.675  19.153 1.00 18.02 ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.607  -6.012  20.135 1.00 15.26 ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.910  -3.201  16.493 1.00 15.16 ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.979  -2.118  16.149 1.00 16.05 ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.663  -2.082  14.673 1.00 15.85 ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.493  -2.478  13.842 1.00 15.62 ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.528  -0.733  16.545 1.00 18.27 ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.468  -0.518  18.042 1.00 20.86 ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.935  -0.531  16.001 1.00 18.16 ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.482  -1.544  14.335 1.00 15.95 ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 2.072  -1.176  12.985 1.00 16.73 ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.277  0.333   12.920 1.00 16.29 ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.862  1.051   13.872 1.00 16.96 ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.579  -1.445  12.785 1.00 20.88 ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.353  -2.842  12.769 1.00 27.78 ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.922  0.838   11.856 1.00 15.48 ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.202  2.262   11.769 1.00 15.52 ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.795  2.834   10.423 1.00 16.80 ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.740  2.120   9.401  1.00 18.37 ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.678  2.552   12.116 1.00 15.03 ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.693  1.747   11.334 1.00 15.40 ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.142  0.527   11.799 1.00 15.41 ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.293  2.267   10.201 1.00 16.08 ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 7.092  -0.203  11.090 1.00 16.52 ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.230  1.524   9.484  1.00 17.06 ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.639  0.308   9.952  1.00 16.84 ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.426  4.130   10.430 1.00 16.57 ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 2.026  4.835   9.221  1.00 16.93 ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.189  5.090   8.246  1.00 17.17 ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.350  4.945   8.624  1.00 17.62 ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.310  6.145   9.590  1.00 18.74 ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.185  7.083   10.210 1.00 20.09 ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.888  5.464   7.002  1.00 17.17 ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.933  5.769   6.022  1.00 17.81 ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.577  7.118   6.361  1.00 18.73 ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.910  7.985   6.941  1.00 19.19 ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.327  5.767   4.603  1.00 20.10 ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.911  4.360   4.189  1.00 23.45 ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.686  4.273   2.688  1.00 30.71 ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.222  2.907   2.247  1.00 36.72 ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.312  2.755   0.766  1.00 40.40 ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.868  7.316   6.042  1.00 18.61 ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.518  8.603   6.368  1.00 19.23 ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.739  9.796   5.773  1.00 19.87 ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.343  9.758   4.616  1.00 20.78 ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.925  8.478   5.754  1.00 21.40 ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.092  7.068   5.291  1.00 23.13 ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.766  6.378   5.327  1.00 19.64 ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.410  10.759  6.621  1.00 19.63 ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.606  11.891  6.195  1.00 20.84 ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.899  13.161  7.016  1.00 19.72 ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.750  13.149  7.904  1.00 18.67 ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.127  11.517  6.226  1.00 26.14 ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.697  11.405  7.566  1.00 31.51 ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.252  14.275  6.624  1.00 20.51 ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.413  15.594  7.226  1.00 21.49 ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.359  15.716  8.331  1.00 22.55 ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.155  15.678  8.063  1.00 23.87 ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.205  16.656  6.122  1.00 22.32 ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.574  18.102  6.418  1.00 25.50 ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.076  18.261  6.699  1.00 25.87 ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.160  19.009  5.227  1.00 27.01 ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.800  15.814  9.574  1.00 21.11 ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.900  15.823  10.739 1.00 22.18 ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.187  16.985  11.679 1.00 23.02 ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.343  17.329  11.923 1.00 21.99 ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.098  14.488  11.504 1.00 23.44 ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.813  13.273  10.579 1.00 26.29 ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.304  14.450  12.823 1.00 23.91 ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 2.900  11.957  11.211 1.00 28.33 ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 2.132  17.598  12.205 1.00 23.47 ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.285  18.716  13.123 1.00 24.91 ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.790  18.219  14.478 1.00 25.46 ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 2.245  17.273  15.034 1.00 25.88 ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.947  19.460  13.312 1.00 26.35 ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.186  20.804  13.939 1.00 29.36 ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.842  21.803  13.240 1.00 31.38 ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.812  21.051  15.240 1.00 31.49 ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 2.097  23.031  13.819 1.00 33.56 ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 1.071  22.288  15.825 1.00 32.48 ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.698  23.272  15.107 1.00 33.23 ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.870  18.832  14.984 1.00 24.35 ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 4.407  18.505  16.298 1.00 24.26 ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 4.322  19.753  17.200 1.00 25.63 ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.812  20.817  16.807 1.00 26.05 ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.853  18.005  16.179 1.00 23.74 ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 6.425  17.708  17.565 1.00 23.35 ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.909  16.755  15.286 1.00 23.71 ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.743  19.596  18.390 1.00 27.28 ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.605  20.701  19.306 1.00 29.59 ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.936  21.246  19.788 1.00 30.40 ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.945  20.556  19.732 1.00 30.68 ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.675  20.311  20.479 1.00 33.61 ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 1.284  20.922  20.332 1.00 42.72 ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 1.365  22.440  20.232 1.00 52.00 ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 1.954  23.052  21.151 1.00 52.55 ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? 0.925  23.014  19.211 1.00 56.75 ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.935  22.500  20.293 1.00 30.66 ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 6.135  23.135  20.833 1.00 30.48 ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.661  22.328  21.993 1.00 29.87 ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.888  21.767  22.772 1.00 29.94 ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.816  24.545  21.307 1.00 31.06 ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.962  22.195  22.062 1.00 28.62 ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.649  21.504  23.144 1.00 28.39 ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.846  22.395  23.545 1.00 28.27 ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 10.046 23.473  22.948 1.00 29.04 ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 9.147  20.141  22.662 1.00 27.92 ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 10.189 20.297  21.711 1.00 27.13 ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.649 21.952  24.524 1.00 28.06 ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.854 22.709  24.887 1.00 27.89 ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.932 22.628  23.783 1.00 26.18 ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.923 23.315  23.876 1.00 25.63 ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.441 22.220  26.220 1.00 31.52 ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 12.764 20.741  26.246 1.00 40.03 ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 13.458 20.227  27.495 1.00 49.63 ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 12.857 19.390  28.209 1.00 50.59 ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 14.612 20.646  27.749 1.00 52.72 ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.735 21.790  22.738 1.00 24.73 ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.705 21.605  21.672 1.00 23.78 ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.349 22.255  20.367 1.00 23.92 ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 14.254 22.621  19.617 1.00 23.64 ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.935 20.112  21.435 1.00 22.93 ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.519 19.445  22.656 1.00 24.03 ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.867 19.573  22.965 1.00 25.39 ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.728 18.686  23.502 1.00 26.56 ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.417 18.936  24.070 1.00 26.49 ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.262 18.066  24.624 1.00 28.17 ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.610 18.179  24.896 1.00 28.92 ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.146 17.542  25.995 1.00 31.49 ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 12.046 22.436  20.089 1.00 23.75 ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.619 23.041  18.815 1.00 23.42 ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 10.350 23.843  19.062 1.00 25.45 ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.525  23.436  19.877 1.00 25.61 ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 11.234 21.932  17.785 1.00 21.90 ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.360 21.025  17.327 1.00 19.55 ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 13.337 21.486  16.453 1.00 19.35 ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.420 19.693  17.738 1.00 19.07 ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.345 20.642  16.006 1.00 18.39 ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.410 18.843  17.285 1.00 18.86 ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.383 19.330  16.445 1.00 18.05 ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.395 18.503  16.025 1.00 16.79 ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 10.088 24.869  18.240 1.00 27.74 ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.754  25.504  18.276 1.00 29.99 ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.698  24.559  17.643 1.00 31.37 ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 8.054  23.533  17.036 1.00 31.12 ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.950  26.744  17.397 1.00 30.68 ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.960  26.307  16.381 1.00 30.80 ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.926 25.405  17.149 1.00 28.37 ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 6.406  24.920  17.703 1.00 31.81 ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.356  24.108  17.067 1.00 32.18 ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.589  24.178  15.559 1.00 30.98 ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.870  25.266  15.028 1.00 32.15 ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.997  24.666  17.419 1.00 33.54 ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.658  23.009  14.895 1.00 28.19 ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 6.019  22.998  13.486 1.00 25.83 ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.602  21.666  12.842 1.00 24.72 ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 5.224  20.745  13.551 1.00 25.28 ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.568  23.176  13.365 1.00 25.15 ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.321  21.862  13.752 1.00 24.43 ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.758  21.975  14.162 1.00 23.41 ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.602 20.800  13.888 1.00 21.02 ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.601 19.629  14.526 1.00 20.83 ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.691  19.375  15.472 1.00 21.69 ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.452 18.668  14.167 1.00 18.67 ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.815  21.552  11.513 1.00 23.85 ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.586  20.320  10.788 1.00 23.03 ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.894  19.561  10.658 1.00 20.83 ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.899  20.096  10.164 1.00 21.87 ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.979  20.584  9.407  1.00 23.60 ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.503  20.873  9.512  1.00 25.12 ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.574  19.842  9.542  1.00 26.12 ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 3.040  22.168  9.678  1.00 26.48 ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.224  20.095  9.703  1.00 27.65 ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.685  22.436  9.811  1.00 27.87 ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.782  21.391  9.854  1.00 28.56 ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.554 21.664  9.994  1.00 31.68 ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.887  18.303  11.142 1.00 19.35 ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 8.057  17.452  11.010 1.00 17.38 ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.809  16.531  9.838  1.00 17.67 ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.734  15.916  9.760  1.00 17.25 ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.342  16.669  12.316 1.00 16.06 ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.554  15.754  12.203 1.00 15.66 ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 10.087 15.276  13.553 1.00 16.55 ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 10.130 16.012  14.534 1.00 18.71 ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.559 14.030  13.608 1.00 15.60 ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.799  16.399  8.929  1.00 16.93 ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.630  15.537  7.778  1.00 16.97 ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.263  14.154  8.017  1.00 16.64 ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.045 13.967  8.962  1.00 16.55 ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.260  16.176  6.542  1.00 19.24 ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.664 16.254  6.760  1.00 21.91 ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.889  13.198  7.128  1.00 16.20 ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.403  11.827  7.145  1.00 16.30 ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.122  11.159  8.507  1.00 15.81 ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.921  10.326  8.945  1.00 15.69 ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.914 11.808  6.776  1.00 17.57 ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.195 12.362  5.403  1.00 20.10 ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.256 11.543  4.289  1.00 22.35 ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.388 13.640  5.010  1.00 21.51 ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.504 12.344  3.263  1.00 22.35 ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.579 13.610  3.646  1.00 22.25 ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.983  11.492  9.120  1.00 15.46 ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.600  10.955  10.436 1.00 15.81 ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.528  9.877   10.294 1.00 15.47 ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.605  10.027  9.499  1.00 16.64 ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.078  12.117  11.317 1.00 16.65 ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.742  11.783  12.790 1.00 18.87 ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 7.989  11.375  13.546 1.00 18.49 ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.072  13.014  13.502 1.00 18.86 ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.667  8.777   11.062 1.00 14.53 ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.695  7.662   11.048 1.00 14.63 ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.119  7.498   12.445 1.00 15.86 ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.871  7.528   13.423 1.00 15.77 ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.433  6.380   10.653 1.00 15.24 ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.139  6.520   9.291  1.00 16.43 ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.200  5.117   8.803  1.00 19.64 ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.471  5.222   10.034 1.00 21.02 ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.802  7.320   12.552 1.00 15.17 ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.190  7.178   13.880 1.00 15.93 ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.702  5.769   14.147 1.00 16.45 ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.256  5.081   13.215 1.00 16.20 ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 1.969  8.118   14.045 1.00 17.92 ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.244  9.600   13.993 1.00 21.25 ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.939  10.394  14.254 1.00 23.41 ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.284  10.030  15.055 1.00 22.24 ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.707  5.370   15.434 1.00 16.28 ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.206  4.069   15.852 1.00 16.31 ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.567  4.208   17.234 1.00 15.93 ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.845  5.165   17.972 1.00 15.99 ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.380  3.059   15.948 1.00 16.55 ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.738  3.223   17.598 1.00 14.41 ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.209  3.144   18.946 1.00 14.85 ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.256  2.375   19.773 1.00 16.82 ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.656  1.269   19.414 1.00 17.86 ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.141 2.424   18.961 1.00 14.98 ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.629 2.240   20.395 1.00 16.13 ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.143 3.235   18.131 1.00 15.50 ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.756  3.025   20.794 1.00 16.94 ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.771  2.437   21.661 1.00 17.77 ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.182  3.398   22.765 1.00 17.28 ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 2.944  4.602   22.669 1.00 18.02 ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.758  2.853   23.853 1.00 16.53 ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.208  3.699   24.949 1.00 16.64 ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.492  4.460   24.554 1.00 15.59 ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.435  3.895   23.978 1.00 15.57 ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.499  2.882   26.243 1.00 17.06 ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 4.872  3.776   27.397 1.00 17.60 ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 3.945  4.622   27.987 1.00 18.98 ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.075  3.972   27.998 1.00 17.40 ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.630  5.333   28.888 1.00 18.93 ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 5.915  4.966   28.924 1.00 17.93 ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.551  5.706   24.960 1.00 16.31 ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.754  6.510   24.836 1.00 15.61 ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 6.731  7.671   25.837 1.00 17.96 ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.647  8.102   26.271 1.00 19.41 ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.025  6.985   23.403 1.00 17.53 ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 6.009  7.901   22.992 1.00 18.45 ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 7.951  8.086   26.258 1.00 17.44 ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.308  9.228   27.132 1.00 18.36 ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.446  10.012  26.447 1.00 19.23 ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.132 9.492   25.522 1.00 19.04 ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 8.771  8.743   28.528 1.00 19.22 ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.725  7.819   29.122 1.00 20.67 ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 7.891  7.337   30.545 1.00 22.52 ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.688  7.911   31.320 1.00 25.09 ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.179  6.376   30.895 1.00 21.54 ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.661  11.280  26.815 1.00 20.75 ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.670 12.085  26.087 1.00 21.35 ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.050 11.419  25.909 1.00 20.74 ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.643 11.436  24.808 1.00 21.34 ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 10.727 13.377  26.910 1.00 22.95 ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.364  13.501  27.472 1.00 23.19 ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 8.913  12.104  27.794 1.00 21.42 ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.518 10.783  26.972 1.00 18.29 ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 13.802 10.099  27.017 1.00 17.71 ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 13.890 8.846   26.174 1.00 15.97 ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 14.987 8.285   26.029 1.00 16.78 ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.766 8.385   25.612 1.00 14.66 ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.754 7.236   24.702 1.00 14.15 ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.287 7.597   23.299 1.00 14.92 ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.571 6.688   22.510 1.00 14.42 ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.338 6.624   24.579 1.00 14.22 ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 10.960 5.906   25.849 1.00 15.72 ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.841 5.271   26.442 1.00 15.44 ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.765  5.927   26.212 1.00 16.57 ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.480 8.907   22.998 1.00 14.81 ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.021 9.284   21.674 1.00 14.80 ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.373 8.586   21.427 1.00 14.46 ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.205 8.474   22.329 1.00 15.12 ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.159 10.793  21.542 1.00 16.13 ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.579 11.637  21.352 1.00 17.48 ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.551 8.074   20.215 1.00 14.16 ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.763 7.368   19.868 1.00 14.44 ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.596 5.861   19.800 1.00 14.79 ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.462 5.177   19.254 1.00 14.62 ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.520 5.332   20.397 1.00 14.39 ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.283 3.892   20.332 1.00 14.55 ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.071 3.445   18.893 1.00 13.22 ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.402 4.131   18.114 1.00 13.56 ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.661 2.305   18.506 1.00 12.48 ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.528 1.825   17.133 1.00 11.95 ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.176 1.167   16.817 1.00 12.98 ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.683 0.330   17.593 1.00 12.89 ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.702 0.854   16.815 1.00 12.69 ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.964 1.691   16.553 1.00 13.43 ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.405 -0.075  15.592 1.00 13.36 ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.203 0.876   16.328 1.00 15.80 ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.640 1.478   15.613 1.00 12.18 ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.505 0.752   15.049 1.00 12.43 ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.152 -0.134  13.948 1.00 12.43 ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.932 0.406   13.124 1.00 13.36 ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.509 1.720   14.391 1.00 13.44 ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.419 1.082   13.523 1.00 15.16 ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.459  0.270   14.377 1.00 14.70 ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.634  2.183   12.740 1.00 15.59 ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.818 -1.439  13.887 1.00 12.22 ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.430 -2.280  12.857 1.00 11.84 ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.377 -3.237  12.289 1.00 14.44 ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.395 -3.556  12.928 1.00 14.96 ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.586 -3.092  13.462 1.00 14.34 ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 14.130 -4.060  14.549 1.00 15.71 ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.376 -4.784  15.113 1.00 17.04 ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.182 -3.912  15.978 1.00 18.51 ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.501 -3.736  15.880 1.00 18.74 ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 18.172 -4.248  14.854 1.00 17.70 ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 18.141 -2.955  16.746 1.00 17.96 ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.649 -3.749  11.108 1.00 15.12 ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.781 -4.734  10.450 1.00 17.35 ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.664 -5.939  10.018 1.00 20.48 ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.836 -5.998  10.393 1.00 20.12 ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 11.107 -4.074  9.258  1.00 18.47 ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.273 -3.653  7.930  1.00 18.22 ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 12.106 -6.913  9.232  1.00 22.57 ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.923 -8.049  8.811  1.00 25.30 ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 14.151 -7.632  7.953  1.00 26.31 ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 15.135 -8.370  7.892  1.00 28.13 ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 12.065 -9.085  8.040  1.00 29.36 ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.492 -8.538  6.738  1.00 35.57 ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.611 -9.509  5.982  1.00 43.01 ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 9.374  -9.446  6.050  1.00 45.15 ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 11.224 -10.398 5.215  1.00 43.35 ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 14.098 -6.451  7.318  1.00 24.16 ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 15.178 -5.993  6.419  1.00 22.25 ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.288 -5.175  7.100  1.00 21.53 ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.319 -4.898  6.471  1.00 23.28 ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.579 -5.167  5.262  1.00 21.15 ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.469 -5.892  4.555  1.00 23.45 ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 12.144 -5.546  4.747  1.00 24.54 ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.531 -6.895  3.643  1.00 25.40 ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.432 -6.368  3.987  1.00 27.11 ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 12.225 -7.213  3.316  1.00 27.03 ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 16.065 -4.760  8.356  1.00 19.46 ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 17.057 -3.939  9.037  1.00 18.45 ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.434 -2.769  9.788  1.00 15.89 ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.256 -2.812  10.145 1.00 16.29 ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.246 -1.725  10.062 1.00 14.79 ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.774 -0.559  10.821 1.00 13.58 ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.920 0.338   9.938  1.00 13.39 ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.346 0.750   8.848  1.00 13.01 ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.987 0.239   11.402 1.00 14.67 ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.534 1.521   12.096 1.00 14.88 ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.779 -0.631  12.380 1.00 15.22 ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.754 0.721   10.446 1.00 13.09 ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.793 1.558   9.730  1.00 13.80 ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.926 3.047   10.139 1.00 13.63 ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.782 3.964   9.320  1.00 14.45 ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.354 1.042   10.026 1.00 15.02 ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.286 1.996   9.455  1.00 15.24 ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.163 -0.348  9.464  1.00 15.73 ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.138 3.289   11.430 1.00 13.72 ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.229 4.655   11.938 1.00 13.61 ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.441 4.695   13.432 1.00 13.42 ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.795 3.673   14.034 1.00 12.75 ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.292 5.882   14.047 1.00 13.31 ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.481 6.010   15.504 1.00 12.34 ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.342 6.786   16.120 1.00 12.47 ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.737 7.638   15.445 1.00 13.36 ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.810 6.728   15.854 1.00 13.22 ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 15.926 8.048   15.104 1.00 13.63 ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 17.007 5.819   15.616 1.00 13.37 ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.208 8.859   15.632 1.00 14.55 ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.013 6.509   17.400 1.00 11.86 ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 11.971 7.264   18.099 1.00 12.11 ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.305 8.767   18.077 1.00 12.78 ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.449 9.124   18.363 1.00 13.21 ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.822 6.785   19.573 1.00 13.54 ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.812 7.656   20.345 1.00 14.29 ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.382 5.315   19.613 1.00 14.76 ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.315 9.629   17.727 1.00 12.76 ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.526 11.070  17.649 1.00 14.57 ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.419 11.853  18.335 1.00 16.22 ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.683 12.949  18.792 1.00 17.31 ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.644 11.506  16.191 1.00 17.44 ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.779 12.909  16.010 1.00 17.53 ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.180  11.301  18.441 1.00 14.17 ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.078  12.065  19.093 1.00 15.45 ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.207  11.048  19.888 1.00 16.97 ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.356  9.826   19.729 1.00 16.70 ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.186  12.787  18.019 1.00 17.23 ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.392  11.829  17.331 1.00 17.64 ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 7.958  13.652  17.011 1.00 17.88 ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.264  11.563  20.675 1.00 16.97 ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.338  10.682  21.378 1.00 18.55 ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.182  11.429  21.991 1.00 21.36 ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.212  12.652  22.097 1.00 23.57 ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.176  10.658  22.370 1.00 22.59 ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 1.950  11.195  22.963 1.00 24.24 ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.315  10.198  23.905 1.00 25.10 ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.963  9.226   24.329 1.00 26.37 ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.074  10.438  24.269 1.00 25.38 ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.650 9.526   25.137 1.00 24.52 ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -0.974 8.257   24.390 1.00 22.19 ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.036 8.142   23.756 1.00 21.79 ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.925 10.157  25.687 1.00 27.32 ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -2.374 9.480   26.979 1.00 31.86 ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.798 8.464   27.435 1.00 33.30 ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -3.428 10.005  27.582 1.00 32.72 ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.077 7.293   24.510 1.00 19.24 ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.255 6.030   23.826 1.00 18.57 ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.150  6.077   22.375 1.00 17.54 ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? -0.108 5.101   21.670 1.00 18.89 ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.839  7.160   21.927 1.00 16.90 ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.390  7.217   20.563 1.00 16.85 ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.913  7.324   20.625 1.00 17.10 ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.470  7.883   21.605 1.00 18.11 ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.876  8.433   19.813 1.00 18.11 ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.625 8.384   19.617 1.00 20.01 ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.167 9.781   19.287 1.00 21.36 ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.977 7.309   18.531 1.00 20.25 ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.578  6.811   19.593 1.00 14.57 ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.010  6.955   19.455 1.00 14.74 ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.284  7.315   17.964 1.00 14.10 ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.660  6.760   17.073 1.00 14.61 ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.758  5.672   19.922 1.00 15.65 ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.266  4.447   19.159 1.00 16.46 ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.269  5.837   19.744 1.00 15.86 ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.204  8.228   17.713 1.00 14.27 ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.526  8.648   16.348 1.00 14.28 ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 7.977  8.344   16.027 1.00 14.31 ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.846  8.520   16.892 1.00 14.79 ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.252  7.885   14.785 1.00 13.68 ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.611  7.500   14.375 1.00 13.91 ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.091 8.316   13.199 1.00 14.15 ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.338  8.528   12.245 1.00 14.72 ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.583  6.028   13.939 1.00 13.61 ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.987  5.100   14.997 1.00 13.11 ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.767  4.625   16.051 1.00 12.89 ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.673  4.665   14.899 1.00 14.24 ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.225  3.765   17.008 1.00 13.71 ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.147  3.792   15.839 1.00 14.80 ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.928  3.350   16.885 1.00 14.24 ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.352 8.780   13.254 1.00 13.07 ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 11.960 9.481   12.114 1.00 14.11 ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.469 8.394   11.176 1.00 14.07 ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.361 7.603   11.547 1.00 13.76 ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.124 10.334  12.612 1.00 14.44 ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.919 8.346   9.940  1.00 14.46 ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.337 7.341   8.969  1.00 15.02 ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.759 7.640   8.466  1.00 15.19 ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.122 8.820   8.292  1.00 15.76 ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.386 7.393   7.748  1.00 16.60 ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.697 6.348   6.684  1.00 24.30 ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.884 5.174   7.044  1.00 19.53 ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.826 6.724   5.493  1.00 31.78 ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.551 6.586   8.185  1.00 13.96 ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.864 6.774   7.542  1.00 13.79 ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 16.001 5.938   6.252  1.00 15.04 ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.080 5.958   5.651  1.00 15.60 ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.056 6.451   8.484  1.00 14.40 ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.054 7.388   9.715  1.00 13.87 ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.062 4.972   8.908  1.00 14.92 ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.955 5.183   5.844  1.00 14.81 ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 15.077 4.278   4.706  1.00 14.40 ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.378 4.968   3.371  1.00 16.26 ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.875 4.319   2.432  1.00 17.35 ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.840 3.384   4.596  1.00 14.77 ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.693 2.438   5.790  1.00 14.53 ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.374 1.688   5.637  1.00 14.81 ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.215 2.577   5.891  1.00 16.21 ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.951  2.152   5.947  1.00 18.57 ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.659  0.880   5.686  1.00 18.92 ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.967  3.006   6.251  1.00 17.98 ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 15.003 6.241   3.249  1.00 15.49 ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.273 6.972   1.994  1.00 16.44 ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.719 7.524   1.898  1.00 16.69 ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 17.091 8.048   0.827  1.00 17.47 ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.259 8.124   1.841  1.00 17.90 ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.456 9.187   2.925  1.00 22.26 ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.558 8.816   4.116  1.00 21.69 ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.548 10.381  2.579  1.00 23.94 ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.499 7.448   2.995  1.00 16.45 ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.872 8.020   3.047  1.00 16.01 ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.849 7.007   2.492  1.00 16.51 ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.517 6.299   3.254  1.00 17.38 ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.228 8.425   4.491  1.00 16.24 ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.240 9.429   5.126  1.00 16.81 ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.651 9.733   6.550  1.00 16.51 ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.203 10.739  4.329  1.00 18.97 ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.867 6.870   1.158  1.00 16.63 ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.648 5.808   0.531  1.00 17.08 ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.143 5.914   0.775  1.00 17.24 ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.837 4.887   0.795  1.00 17.91 ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.345 5.694   -0.985 1.00 18.49 ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.835 5.631   -1.326 1.00 21.31 ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.640 5.410   -2.831 1.00 23.48 ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 18.073 4.562   -0.509 1.00 21.56 ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.644 7.153   0.927  1.00 17.05 ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 24.054 7.402   1.144  1.00 17.25 ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.600 6.813   2.458  1.00 18.10 ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.824 6.671   2.602  1.00 18.56 ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.362 8.915   1.022  1.00 17.27 ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.521 9.743   1.947  1.00 16.63 ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.348 10.379  1.654  1.00 17.64 ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.829 10.066  3.312  1.00 17.18 ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.899 11.067  2.761  1.00 17.90 ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.809 10.910  3.779  1.00 17.67 ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.899 9.757   4.165  1.00 18.11 ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.807 11.412  5.083  1.00 18.77 ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.921 10.302  5.437  1.00 18.52 ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.871 11.095  5.889  1.00 18.37 ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.707 6.425   3.401  1.00 17.16 ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.190 5.792   4.636  1.00 18.58 ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.880 4.445   4.350  1.00 21.22 ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.692 4.024   5.174  1.00 20.82 ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 23.043 5.557   5.614  1.00 17.17 ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.464 6.794   6.262  1.00 16.88 ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.219 6.433   7.061  1.00 16.90 ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.527 7.455   7.248  1.00 16.68 ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.573 3.798   3.196  1.00 23.68 ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.130 2.495   2.788  1.00 27.12 ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.497 2.555   2.131  1.00 31.07 ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 27.006 1.495   1.756  1.00 31.36 ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.194 1.785   1.784  1.00 28.58 ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.841 1.398   2.317  1.00 33.94 ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.660 1.447   3.537  1.00 36.11 ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.940 1.057   1.496  1.00 38.19 ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 27.085 3.754   1.928  1.00 33.11 ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.410 3.822   1.282  1.00 35.54 ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.298 4.955   1.790  1.00 35.79 ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.842 5.765   2.600  1.00 36.19 ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 28.274 3.901   -0.240 1.00 40.23 ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.672 5.201   -0.733 1.00 47.88 ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.244 5.096   -1.228 1.00 57.15 ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 25.802 6.013   -1.959 1.00 59.56 ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.565 4.100   -0.889 1.00 60.61 ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . SER   B 1 1   ? 21.976 -21.256 7.760  1.00 24.78 ? 7   SER   C N   1 
ATOM   1083 C  CA  . SER   B 1 1   ? 20.840 -21.093 8.673  1.00 25.08 ? 7   SER   C CA  1 
ATOM   1084 C  C   . SER   B 1 1   ? 20.816 -22.195 9.759  1.00 23.94 ? 7   SER   C C   1 
ATOM   1085 O  O   . SER   B 1 1   ? 21.502 -23.211 9.619  1.00 25.02 ? 7   SER   C O   1 
ATOM   1086 C  CB  . SER   B 1 1   ? 19.538 -21.117 7.875  1.00 27.68 ? 7   SER   C CB  1 
ATOM   1087 O  OG  . SER   B 1 1   ? 19.317 -22.435 7.386  1.00 31.78 ? 7   SER   C OG  1 
ATOM   1088 N  N   . GLY   B 1 2   ? 20.047 -21.967 10.827 1.00 21.92 ? 8   GLY   C N   1 
ATOM   1089 C  CA  . GLY   B 1 2   ? 19.915 -22.938 11.904 1.00 20.37 ? 8   GLY   C CA  1 
ATOM   1090 C  C   . GLY   B 1 2   ? 19.668 -22.319 13.265 1.00 18.88 ? 8   GLY   C C   1 
ATOM   1091 O  O   . GLY   B 1 2   ? 20.082 -21.193 13.530 1.00 19.16 ? 8   GLY   C O   1 
ATOM   1092 N  N   . ALA   B 1 3   ? 19.025 -23.077 14.156 1.00 17.87 ? 9   ALA   C N   1 
ATOM   1093 C  CA  . ALA   B 1 3   ? 18.724 -22.586 15.500 1.00 17.75 ? 9   ALA   C CA  1 
ATOM   1094 C  C   . ALA   B 1 3   ? 18.834 -23.718 16.526 1.00 16.98 ? 9   ALA   C C   1 
ATOM   1095 O  O   . ALA   B 1 3   ? 18.859 -24.893 16.155 1.00 17.49 ? 9   ALA   C O   1 
ATOM   1096 C  CB  . ALA   B 1 3   ? 17.303 -22.002 15.532 1.00 19.28 ? 9   ALA   C CB  1 
ATOM   1097 N  N   . ILE   B 1 4   ? 18.906 -23.353 17.821 1.00 16.39 ? 10  ILE   C N   1 
ATOM   1098 C  CA  . ILE   B 1 4   ? 18.833 -24.301 18.929 1.00 16.58 ? 10  ILE   C CA  1 
ATOM   1099 C  C   . ILE   B 1 4   ? 17.429 -24.092 19.537 1.00 17.16 ? 10  ILE   C C   1 
ATOM   1100 O  O   . ILE   B 1 4   ? 17.002 -22.944 19.734 1.00 18.15 ? 10  ILE   C O   1 
ATOM   1101 C  CB  . ILE   B 1 4   ? 19.876 -23.991 20.003 1.00 16.83 ? 10  ILE   C CB  1 
ATOM   1102 C  CG1 . ILE   B 1 4   ? 21.311 -23.887 19.431 1.00 17.71 ? 10  ILE   C CG1 1 
ATOM   1103 C  CG2 . ILE   B 1 4   ? 19.769 -25.010 21.149 1.00 17.62 ? 10  ILE   C CG2 1 
ATOM   1104 C  CD1 . ILE   B 1 4   ? 22.336 -23.262 20.443 1.00 18.84 ? 10  ILE   C CD1 1 
ATOM   1105 N  N   . TYR   B 1 5   ? 16.707 -25.181 19.840 1.00 16.05 ? 11  TYR   C N   1 
ATOM   1106 C  CA  . TYR   B 1 5   ? 15.368 -25.109 20.423 1.00 17.41 ? 11  TYR   C CA  1 
ATOM   1107 C  C   . TYR   B 1 5   ? 15.433 -25.809 21.806 1.00 18.28 ? 11  TYR   C C   1 
ATOM   1108 O  O   . TYR   B 1 5   ? 15.471 -27.025 21.875 1.00 19.05 ? 11  TYR   C O   1 
ATOM   1109 C  CB  . TYR   B 1 5   ? 14.331 -25.797 19.492 1.00 17.53 ? 11  TYR   C CB  1 
ATOM   1110 C  CG  . TYR   B 1 5   ? 14.138 -25.044 18.197 1.00 18.38 ? 11  TYR   C CG  1 
ATOM   1111 C  CD1 . TYR   B 1 5   ? 13.317 -23.928 18.141 1.00 18.52 ? 11  TYR   C CD1 1 
ATOM   1112 C  CD2 . TYR   B 1 5   ? 14.840 -25.394 17.053 1.00 19.91 ? 11  TYR   C CD2 1 
ATOM   1113 C  CE1 . TYR   B 1 5   ? 13.143 -23.224 16.965 1.00 20.40 ? 11  TYR   C CE1 1 
ATOM   1114 C  CE2 . TYR   B 1 5   ? 14.695 -24.677 15.870 1.00 21.20 ? 11  TYR   C CE2 1 
ATOM   1115 C  CZ  . TYR   B 1 5   ? 13.850 -23.589 15.834 1.00 22.28 ? 11  TYR   C CZ  1 
ATOM   1116 O  OH  . TYR   B 1 5   ? 13.716 -22.858 14.679 1.00 24.42 ? 11  TYR   C OH  1 
ATOM   1117 N  N   . VAL   B 1 6   ? 15.501 -25.044 22.896 1.00 18.00 ? 12  VAL   C N   1 
ATOM   1118 C  CA  . VAL   B 1 6   ? 15.610 -25.605 24.246 1.00 18.21 ? 12  VAL   C CA  1 
ATOM   1119 C  C   . VAL   B 1 6   ? 14.494 -25.009 25.093 1.00 19.22 ? 12  VAL   C C   1 
ATOM   1120 O  O   . VAL   B 1 6   ? 14.312 -23.800 25.081 1.00 19.49 ? 12  VAL   C O   1 
ATOM   1121 C  CB  . VAL   B 1 6   ? 17.022 -25.352 24.860 1.00 19.12 ? 12  VAL   C CB  1 
ATOM   1122 C  CG1 . VAL   B 1 6   ? 17.449 -23.883 24.733 1.00 19.17 ? 12  VAL   C CG1 1 
ATOM   1123 C  CG2 . VAL   B 1 6   ? 17.059 -25.842 26.309 1.00 19.43 ? 12  VAL   C CG2 1 
ATOM   1124 N  N   . GLY   B 1 7   ? 13.679 -25.845 25.761 1.00 19.37 ? 13  GLY   C N   1 
ATOM   1125 C  CA  . GLY   B 1 7   ? 12.555 -25.328 26.553 1.00 19.15 ? 13  GLY   C CA  1 
ATOM   1126 C  C   . GLY   B 1 7   ? 11.641 -24.465 25.693 1.00 20.33 ? 13  GLY   C C   1 
ATOM   1127 O  O   . GLY   B 1 7   ? 11.347 -24.842 24.559 1.00 22.00 ? 13  GLY   C O   1 
ATOM   1128 N  N   . ASN   B 1 8   ? 11.295 -23.256 26.161 1.00 20.19 ? 14  ASN   C N   1 
ATOM   1129 C  CA  . ASN   B 1 8   ? 10.506 -22.349 25.331 1.00 20.13 ? 14  ASN   C CA  1 
ATOM   1130 C  C   . ASN   B 1 8   ? 11.408 -21.239 24.750 1.00 19.39 ? 14  ASN   C C   1 
ATOM   1131 O  O   . ASN   B 1 8   ? 10.975 -20.102 24.591 1.00 19.43 ? 14  ASN   C O   1 
ATOM   1132 C  CB  . ASN   B 1 8   ? 9.286  -21.798 26.058 1.00 22.62 ? 14  ASN   C CB  1 
ATOM   1133 C  CG  . ASN   B 1 8   ? 8.194  -22.852 26.231 1.00 28.63 ? 14  ASN   C CG  1 
ATOM   1134 O  OD1 . ASN   B 1 8   ? 7.258  -22.965 25.415 1.00 29.82 ? 14  ASN   C OD1 1 
ATOM   1135 N  ND2 . ASN   B 1 8   ? 8.310  -23.652 27.275 1.00 29.42 ? 14  ASN   C ND2 1 
ATOM   1136 N  N   . TYR   B 1 9   ? 12.616 -21.599 24.361 1.00 18.52 ? 15  TYR   C N   1 
ATOM   1137 C  CA  . TYR   B 1 9   ? 13.562 -20.637 23.758 1.00 18.69 ? 15  TYR   C CA  1 
ATOM   1138 C  C   . TYR   B 1 9   ? 14.045 -21.113 22.376 1.00 18.12 ? 15  TYR   C C   1 
ATOM   1139 O  O   . TYR   B 1 9   ? 14.243 -22.313 22.149 1.00 18.22 ? 15  TYR   C O   1 
ATOM   1140 C  CB  . TYR   B 1 9   ? 14.802 -20.465 24.656 1.00 19.39 ? 15  TYR   C CB  1 
ATOM   1141 C  CG  . TYR   B 1 9   ? 14.509 -19.952 26.060 1.00 21.19 ? 15  TYR   C CG  1 
ATOM   1142 C  CD1 . TYR   B 1 9   ? 13.942 -18.702 26.260 1.00 23.18 ? 15  TYR   C CD1 1 
ATOM   1143 C  CD2 . TYR   B 1 9   ? 14.848 -20.703 27.183 1.00 22.78 ? 15  TYR   C CD2 1 
ATOM   1144 C  CE1 . TYR   B 1 9   ? 13.704 -18.213 27.549 1.00 24.29 ? 15  TYR   C CE1 1 
ATOM   1145 C  CE2 . TYR   B 1 9   ? 14.614 -20.227 28.473 1.00 24.43 ? 15  TYR   C CE2 1 
ATOM   1146 C  CZ  . TYR   B 1 9   ? 14.072 -18.967 28.649 1.00 26.59 ? 15  TYR   C CZ  1 
ATOM   1147 O  OH  . TYR   B 1 9   ? 13.846 -18.504 29.932 1.00 29.58 ? 15  TYR   C OH  1 
ATOM   1148 N  N   . ARG   B 1 10  ? 14.281 -20.149 21.483 1.00 15.92 ? 16  ARG   C N   1 
ATOM   1149 C  CA  . ARG   B 1 10  ? 14.859 -20.346 20.148 1.00 15.84 ? 16  ARG   C CA  1 
ATOM   1150 C  C   . ARG   B 1 10  ? 16.132 -19.488 20.120 1.00 16.53 ? 16  ARG   C C   1 
ATOM   1151 O  O   . ARG   B 1 10  ? 16.050 -18.274 20.337 1.00 17.08 ? 16  ARG   C O   1 
ATOM   1152 C  CB  . ARG   B 1 10  ? 13.881 -19.884 19.037 1.00 17.52 ? 16  ARG   C CB  1 
ATOM   1153 C  CG  . ARG   B 1 10  ? 14.513 -19.713 17.631 1.00 18.97 ? 16  ARG   C CG  1 
ATOM   1154 C  CD  . ARG   B 1 10  ? 13.449 -19.489 16.562 1.00 20.45 ? 16  ARG   C CD  1 
ATOM   1155 N  NE  . ARG   B 1 10  ? 13.864 -18.512 15.543 1.00 21.16 ? 16  ARG   C NE  1 
ATOM   1156 C  CZ  . ARG   B 1 10  ? 14.367 -18.817 14.346 1.00 22.57 ? 16  ARG   C CZ  1 
ATOM   1157 N  NH1 . ARG   B 1 10  ? 14.609 -20.083 14.018 1.00 20.98 ? 16  ARG   C NH1 1 
ATOM   1158 N  NH2 . ARG   B 1 10  ? 14.674 -17.856 13.484 1.00 22.88 ? 16  ARG   C NH2 1 
ATOM   1159 N  N   . VAL   B 1 11  ? 17.301 -20.114 19.903 1.00 15.39 ? 17  VAL   C N   1 
ATOM   1160 C  CA  . VAL   B 1 11  ? 18.594 -19.422 19.877 1.00 14.95 ? 17  VAL   C CA  1 
ATOM   1161 C  C   . VAL   B 1 11  ? 19.069 -19.371 18.441 1.00 15.66 ? 17  VAL   C C   1 
ATOM   1162 O  O   . VAL   B 1 11  ? 19.244 -20.421 17.814 1.00 15.98 ? 17  VAL   C O   1 
ATOM   1163 C  CB  . VAL   B 1 11  ? 19.658 -20.154 20.740 1.00 15.29 ? 17  VAL   C CB  1 
ATOM   1164 C  CG1 . VAL   B 1 11  ? 20.933 -19.298 20.860 1.00 17.31 ? 17  VAL   C CG1 1 
ATOM   1165 C  CG2 . VAL   B 1 11  ? 19.093 -20.537 22.116 1.00 16.37 ? 17  VAL   C CG2 1 
ATOM   1166 N  N   . VAL   B 1 12  ? 19.302 -18.149 17.915 1.00 15.69 ? 18  VAL   C N   1 
ATOM   1167 C  CA  A VAL   B 1 12  ? 19.738 -17.989 16.535 0.50 15.17 ? 18  VAL   C CA  1 
ATOM   1168 C  CA  B VAL   B 1 12  ? 19.648 -17.898 16.512 0.50 16.65 ? 18  VAL   C CA  1 
ATOM   1169 C  C   . VAL   B 1 12  ? 20.884 -16.978 16.444 1.00 16.31 ? 18  VAL   C C   1 
ATOM   1170 O  O   . VAL   B 1 12  ? 21.144 -16.201 17.394 1.00 15.95 ? 18  VAL   C O   1 
ATOM   1171 C  CB  A VAL   B 1 12  ? 18.563 -17.489 15.644 0.50 14.91 ? 18  VAL   C CB  1 
ATOM   1172 C  CB  B VAL   B 1 12  ? 18.461 -17.131 15.782 0.50 19.11 ? 18  VAL   C CB  1 
ATOM   1173 C  CG1 A VAL   B 1 12  ? 17.538 -18.577 15.410 0.50 15.55 ? 18  VAL   C CG1 1 
ATOM   1174 C  CG1 B VAL   B 1 12  ? 18.493 -17.320 14.272 0.50 19.52 ? 18  VAL   C CG1 1 
ATOM   1175 C  CG2 A VAL   B 1 12  ? 17.940 -16.203 16.210 0.50 13.76 ? 18  VAL   C CG2 1 
ATOM   1176 C  CG2 B VAL   B 1 12  ? 17.077 -17.482 16.324 0.50 21.18 ? 18  VAL   C CG2 1 
ATOM   1177 N  N   . ASN   B 1 13  ? 21.564 -16.921 15.259 1.00 14.65 ? 19  ASN   C N   1 
ATOM   1178 C  CA  . ASN   B 1 13  ? 22.580 -15.911 15.047 1.00 14.77 ? 19  ASN   C CA  1 
ATOM   1179 C  C   . ASN   B 1 13  ? 21.795 -14.565 14.998 1.00 15.32 ? 19  ASN   C C   1 
ATOM   1180 O  O   . ASN   B 1 13  ? 20.766 -14.481 14.316 1.00 15.68 ? 19  ASN   C O   1 
ATOM   1181 C  CB  . ASN   B 1 13  ? 23.249 -16.089 13.682 1.00 14.87 ? 19  ASN   C CB  1 
ATOM   1182 C  CG  . ASN   B 1 13  ? 24.087 -17.357 13.589 1.00 16.67 ? 19  ASN   C CG  1 
ATOM   1183 O  OD1 . ASN   B 1 13  ? 23.600 -18.419 13.127 1.00 17.35 ? 19  ASN   C OD1 1 
ATOM   1184 N  ND2 . ASN   B 1 13  ? 25.352 -17.259 14.015 1.00 15.43 ? 19  ASN   C ND2 1 
ATOM   1185 N  N   . ARG   B 1 14  ? 22.253 -13.538 15.735 1.00 15.22 ? 20  ARG   C N   1 
ATOM   1186 C  CA  . ARG   B 1 14  ? 21.518 -12.253 15.757 1.00 15.57 ? 20  ARG   C CA  1 
ATOM   1187 C  C   . ARG   B 1 14  ? 21.381 -11.689 14.324 1.00 17.08 ? 20  ARG   C C   1 
ATOM   1188 O  O   . ARG   B 1 14  ? 20.336 -11.126 13.993 1.00 18.28 ? 20  ARG   C O   1 
ATOM   1189 C  CB  . ARG   B 1 14  ? 22.298 -11.239 16.609 1.00 16.75 ? 20  ARG   C CB  1 
ATOM   1190 C  CG  . ARG   B 1 14  ? 21.524 -9.928  16.895 1.00 18.13 ? 20  ARG   C CG  1 
ATOM   1191 C  CD  . ARG   B 1 14  ? 22.432 -8.960  17.640 1.00 18.79 ? 20  ARG   C CD  1 
ATOM   1192 N  NE  . ARG   B 1 14  ? 21.764 -7.715  18.083 1.00 18.40 ? 20  ARG   C NE  1 
ATOM   1193 C  CZ  . ARG   B 1 14  ? 21.608 -6.638  17.318 1.00 19.95 ? 20  ARG   C CZ  1 
ATOM   1194 N  NH1 . ARG   B 1 14  ? 21.972 -6.662  16.039 1.00 20.58 ? 20  ARG   C NH1 1 
ATOM   1195 N  NH2 . ARG   B 1 14  ? 21.076 -5.525  17.823 1.00 18.54 ? 20  ARG   C NH2 1 
ATOM   1196 N  N   . HIS   B 1 15  ? 22.419 -11.878 13.465 1.00 16.26 ? 21  HIS   C N   1 
ATOM   1197 C  CA  . HIS   B 1 15  ? 22.339 -11.345 12.094 1.00 16.01 ? 21  HIS   C CA  1 
ATOM   1198 C  C   . HIS   B 1 15  ? 21.308 -12.070 11.188 1.00 17.81 ? 21  HIS   C C   1 
ATOM   1199 O  O   . HIS   B 1 15  ? 20.992 -11.560 10.104 1.00 19.42 ? 21  HIS   C O   1 
ATOM   1200 C  CB  . HIS   B 1 15  ? 23.736 -11.286 11.414 1.00 16.11 ? 21  HIS   C CB  1 
ATOM   1201 C  CG  . HIS   B 1 15  ? 24.256 -12.608 10.942 1.00 17.39 ? 21  HIS   C CG  1 
ATOM   1202 N  ND1 . HIS   B 1 15  ? 25.006 -13.434 11.777 1.00 19.59 ? 21  HIS   C ND1 1 
ATOM   1203 C  CD2 . HIS   B 1 15  ? 24.184 -13.167 9.713  1.00 18.82 ? 21  HIS   C CD2 1 
ATOM   1204 C  CE1 . HIS   B 1 15  ? 25.338 -14.488 11.033 1.00 20.66 ? 21  HIS   C CE1 1 
ATOM   1205 N  NE2 . HIS   B 1 15  ? 24.888 -14.355 9.777  1.00 20.00 ? 21  HIS   C NE2 1 
ATOM   1206 N  N   . LEU   B 1 16  ? 20.764 -13.204 11.637 1.00 17.37 ? 22  LEU   C N   1 
ATOM   1207 C  CA  . LEU   B 1 16  ? 19.730 -13.951 10.893 1.00 18.80 ? 22  LEU   C CA  1 
ATOM   1208 C  C   . LEU   B 1 16  ? 18.342 -13.898 11.582 1.00 19.37 ? 22  LEU   C C   1 
ATOM   1209 O  O   . LEU   B 1 16  ? 17.425 -14.607 11.163 1.00 19.93 ? 22  LEU   C O   1 
ATOM   1210 C  CB  . LEU   B 1 16  ? 20.184 -15.408 10.677 1.00 19.13 ? 22  LEU   C CB  1 
ATOM   1211 C  CG  . LEU   B 1 16  ? 21.487 -15.570 9.875  1.00 20.09 ? 22  LEU   C CG  1 
ATOM   1212 C  CD1 . LEU   B 1 16  ? 21.864 -17.043 9.724  1.00 20.15 ? 22  LEU   C CD1 1 
ATOM   1213 C  CD2 . LEU   B 1 16  ? 21.357 -14.925 8.473  1.00 19.90 ? 22  LEU   C CD2 1 
ATOM   1214 N  N   . ALA   B 1 17  ? 18.201 -13.116 12.675 1.00 19.05 ? 23  ALA   C N   1 
ATOM   1215 C  CA  . ALA   B 1 17  ? 16.926 -13.047 13.391 1.00 20.10 ? 23  ALA   C CA  1 
ATOM   1216 C  C   . ALA   B 1 17  ? 15.825 -12.483 12.511 1.00 21.81 ? 23  ALA   C C   1 
ATOM   1217 O  O   . ALA   B 1 17  ? 16.070 -11.578 11.696 1.00 22.31 ? 23  ALA   C O   1 
ATOM   1218 C  CB  . ALA   B 1 17  ? 17.066 -12.218 14.654 1.00 20.83 ? 23  ALA   C CB  1 
ATOM   1219 N  N   . THR   B 1 18  ? 14.631 -13.083 12.633 1.00 21.67 ? 24  THR   C N   1 
ATOM   1220 C  CA  . THR   B 1 18  ? 13.461 -12.670 11.863 1.00 21.75 ? 24  THR   C CA  1 
ATOM   1221 C  C   . THR   B 1 18  ? 12.655 -11.598 12.629 1.00 22.63 ? 24  THR   C C   1 
ATOM   1222 O  O   . THR   B 1 18  ? 12.887 -11.344 13.818 1.00 22.33 ? 24  THR   C O   1 
ATOM   1223 C  CB  . THR   B 1 18  ? 12.554 -13.918 11.643 1.00 23.11 ? 24  THR   C CB  1 
ATOM   1224 O  OG1 . THR   B 1 18  ? 12.000 -14.337 12.897 1.00 24.09 ? 24  THR   C OG1 1 
ATOM   1225 C  CG2 . THR   B 1 18  ? 13.279 -15.076 10.961 1.00 23.99 ? 24  THR   C CG2 1 
ATOM   1226 N  N   . HIS   B 1 19  ? 11.613 -11.012 11.966 1.00 22.46 ? 25  HIS   C N   1 
ATOM   1227 C  CA  . HIS   B 1 19  ? 10.708 -10.085 12.650 1.00 23.43 ? 25  HIS   C CA  1 
ATOM   1228 C  C   . HIS   B 1 19  ? 10.036 -10.797 13.814 1.00 22.86 ? 25  HIS   C C   1 
ATOM   1229 O  O   . HIS   B 1 19  ? 9.949  -10.206 14.883 1.00 24.06 ? 25  HIS   C O   1 
ATOM   1230 C  CB  . HIS   B 1 19  ? 9.619  -9.561  11.678 1.00 24.96 ? 25  HIS   C CB  1 
ATOM   1231 C  CG  . HIS   B 1 19  ? 8.463  -8.881  12.370 1.00 29.21 ? 25  HIS   C CG  1 
ATOM   1232 N  ND1 . HIS   B 1 19  ? 8.562  -7.585  12.831 1.00 31.57 ? 25  HIS   C ND1 1 
ATOM   1233 C  CD2 . HIS   B 1 19  ? 7.251  -9.372  12.714 1.00 31.63 ? 25  HIS   C CD2 1 
ATOM   1234 C  CE1 . HIS   B 1 19  ? 7.387  -7.293  13.369 1.00 32.65 ? 25  HIS   C CE1 1 
ATOM   1235 N  NE2 . HIS   B 1 19  ? 6.563  -8.338  13.333 1.00 32.80 ? 25  HIS   C NE2 1 
ATOM   1236 N  N   . ASN   B 1 20  ? 9.600  -12.080 13.638 1.00 22.27 ? 26  ASN   C N   1 
ATOM   1237 C  CA  . ASN   B 1 20  ? 8.960  -12.797 14.744 1.00 22.61 ? 26  ASN   C CA  1 
ATOM   1238 C  C   . ASN   B 1 20  ? 9.917  -12.949 15.930 1.00 22.67 ? 26  ASN   C C   1 
ATOM   1239 O  O   . ASN   B 1 20  ? 9.474  -12.905 17.074 1.00 22.00 ? 26  ASN   C O   1 
ATOM   1240 C  CB  . ASN   B 1 20  ? 8.433  -14.175 14.324 1.00 24.74 ? 26  ASN   C CB  1 
ATOM   1241 C  CG  . ASN   B 1 20  ? 7.628  -14.819 15.436 1.00 31.29 ? 26  ASN   C CG  1 
ATOM   1242 O  OD1 . ASN   B 1 20  ? 6.509  -14.408 15.713 1.00 33.20 ? 26  ASN   C OD1 1 
ATOM   1243 N  ND2 . ASN   B 1 20  ? 8.206  -15.796 16.150 1.00 32.63 ? 26  ASN   C ND2 1 
ATOM   1244 N  N   . ASP   B 1 21  ? 11.232 -13.139 15.660 1.00 21.83 ? 27  ASP   C N   1 
ATOM   1245 C  CA  . ASP   B 1 21  ? 12.197 -13.255 16.754 1.00 21.15 ? 27  ASP   C CA  1 
ATOM   1246 C  C   . ASP   B 1 21  ? 12.250 -11.933 17.542 1.00 21.11 ? 27  ASP   C C   1 
ATOM   1247 O  O   . ASP   B 1 21  ? 12.232 -11.950 18.779 1.00 21.55 ? 27  ASP   C O   1 
ATOM   1248 C  CB  . ASP   B 1 21  ? 13.612 -13.575 16.224 1.00 21.10 ? 27  ASP   C CB  1 
ATOM   1249 C  CG  . ASP   B 1 21  ? 13.784 -14.989 15.723 1.00 21.17 ? 27  ASP   C CG  1 
ATOM   1250 O  OD1 . ASP   B 1 21  ? 13.222 -15.922 16.366 1.00 21.38 ? 27  ASP   C OD1 1 
ATOM   1251 O  OD2 . ASP   B 1 21  ? 14.480 -15.171 14.690 1.00 20.91 ? 27  ASP   C OD2 1 
ATOM   1252 N  N   . TRP   B 1 22  ? 12.343 -10.792 16.836 1.00 21.07 ? 28  TRP   C N   1 
ATOM   1253 C  CA  . TRP   B 1 22  ? 12.378 -9.493  17.510 1.00 21.73 ? 28  TRP   C CA  1 
ATOM   1254 C  C   . TRP   B 1 22  ? 11.061 -9.161  18.242 1.00 22.72 ? 28  TRP   C C   1 
ATOM   1255 O  O   . TRP   B 1 22  ? 11.082 -8.527  19.297 1.00 23.03 ? 28  TRP   C O   1 
ATOM   1256 C  CB  . TRP   B 1 22  ? 12.732 -8.378  16.515 1.00 21.35 ? 28  TRP   C CB  1 
ATOM   1257 C  CG  . TRP   B 1 22  ? 14.198 -8.338  16.194 1.00 20.97 ? 28  TRP   C CG  1 
ATOM   1258 C  CD1 . TRP   B 1 22  ? 14.812 -8.819  15.069 1.00 21.58 ? 28  TRP   C CD1 1 
ATOM   1259 C  CD2 . TRP   B 1 22  ? 15.241 -7.794  17.021 1.00 20.38 ? 28  TRP   C CD2 1 
ATOM   1260 N  NE1 . TRP   B 1 22  ? 16.171 -8.567  15.126 1.00 21.69 ? 28  TRP   C NE1 1 
ATOM   1261 C  CE2 . TRP   B 1 22  ? 16.462 -7.965  16.328 1.00 20.43 ? 28  TRP   C CE2 1 
ATOM   1262 C  CE3 . TRP   B 1 22  ? 15.260 -7.159  18.274 1.00 20.81 ? 28  TRP   C CE3 1 
ATOM   1263 C  CZ2 . TRP   B 1 22  ? 17.682 -7.509  16.829 1.00 20.11 ? 28  TRP   C CZ2 1 
ATOM   1264 C  CZ3 . TRP   B 1 22  ? 16.482 -6.718  18.781 1.00 21.39 ? 28  TRP   C CZ3 1 
ATOM   1265 C  CH2 . TRP   B 1 22  ? 17.677 -6.900  18.054 1.00 20.68 ? 28  TRP   C CH2 1 
ATOM   1266 N  N   . ALA   B 1 23  ? 9.909  -9.621  17.703 1.00 22.88 ? 29  ALA   C N   1 
ATOM   1267 C  CA  . ALA   B 1 23  ? 8.598  -9.402  18.333 1.00 24.36 ? 29  ALA   C CA  1 
ATOM   1268 C  C   . ALA   B 1 23  ? 8.387  -10.287 19.579 1.00 24.81 ? 29  ALA   C C   1 
ATOM   1269 O  O   . ALA   B 1 23  ? 7.426  -10.071 20.331 1.00 25.50 ? 29  ALA   C O   1 
ATOM   1270 C  CB  . ALA   B 1 23  ? 7.483  -9.655  17.324 1.00 25.06 ? 29  ALA   C CB  1 
ATOM   1271 N  N   . ASN   B 1 24  ? 9.266  -11.298 19.796 1.00 24.07 ? 30  ASN   C N   1 
ATOM   1272 C  CA  . ASN   B 1 24  ? 9.152  -12.186 20.945 1.00 23.98 ? 30  ASN   C CA  1 
ATOM   1273 C  C   . ASN   B 1 24  ? 10.534 -12.285 21.621 1.00 23.69 ? 30  ASN   C C   1 
ATOM   1274 O  O   . ASN   B 1 24  ? 10.972 -13.365 22.018 1.00 22.79 ? 30  ASN   C O   1 
ATOM   1275 C  CB  . ASN   B 1 24  ? 8.658  -13.550 20.445 1.00 25.46 ? 30  ASN   C CB  1 
ATOM   1276 C  CG  . ASN   B 1 24  ? 7.229  -13.503 19.941 1.00 28.12 ? 30  ASN   C CG  1 
ATOM   1277 O  OD1 . ASN   B 1 24  ? 6.282  -13.522 20.738 1.00 29.01 ? 30  ASN   C OD1 1 
ATOM   1278 N  ND2 . ASN   B 1 24  ? 7.058  -13.440 18.626 1.00 27.62 ? 30  ASN   C ND2 1 
ATOM   1279 N  N   . LEU   B 1 25  ? 11.258 -11.145 21.701 1.00 23.96 ? 31  LEU   C N   1 
ATOM   1280 C  CA  . LEU   B 1 25  ? 12.623 -11.097 22.201 1.00 23.60 ? 31  LEU   C CA  1 
ATOM   1281 C  C   . LEU   B 1 25  ? 12.789 -11.424 23.669 1.00 24.25 ? 31  LEU   C C   1 
ATOM   1282 O  O   . LEU   B 1 25  ? 12.071 -10.874 24.516 1.00 25.97 ? 31  LEU   C O   1 
ATOM   1283 C  CB  . LEU   B 1 25  ? 13.209 -9.708  21.928 1.00 23.28 ? 31  LEU   C CB  1 
ATOM   1284 C  CG  . LEU   B 1 25  ? 14.682 -9.537  22.285 1.00 23.32 ? 31  LEU   C CG  1 
ATOM   1285 C  CD1 . LEU   B 1 25  ? 15.561 -10.457 21.429 1.00 23.64 ? 31  LEU   C CD1 1 
ATOM   1286 C  CD2 . LEU   B 1 25  ? 15.115 -8.112  22.084 1.00 23.58 ? 31  LEU   C CD2 1 
ATOM   1287 N  N   . VAL   B 1 26  ? 13.758 -12.288 23.981 1.00 22.38 ? 32  VAL   C N   1 
ATOM   1288 C  CA  . VAL   B 1 26  ? 14.112 -12.595 25.363 1.00 21.66 ? 32  VAL   C CA  1 
ATOM   1289 C  C   . VAL   B 1 26  ? 15.434 -11.881 25.699 1.00 21.84 ? 32  VAL   C C   1 
ATOM   1290 O  O   . VAL   B 1 26  ? 15.552 -11.211 26.735 1.00 22.59 ? 32  VAL   C O   1 
ATOM   1291 C  CB  . VAL   B 1 26  ? 14.251 -14.124 25.606 1.00 22.19 ? 32  VAL   C CB  1 
ATOM   1292 C  CG1 . VAL   B 1 26  ? 14.816 -14.409 26.995 1.00 21.91 ? 32  VAL   C CG1 1 
ATOM   1293 C  CG2 . VAL   B 1 26  ? 12.919 -14.841 25.406 1.00 22.58 ? 32  VAL   C CG2 1 
ATOM   1294 N  N   . TRP   B 1 27  ? 16.451 -12.037 24.822 1.00 20.10 ? 33  TRP   C N   1 
ATOM   1295 C  CA  . TRP   B 1 27  ? 17.775 -11.462 25.071 1.00 19.70 ? 33  TRP   C CA  1 
ATOM   1296 C  C   . TRP   B 1 27  ? 18.568 -11.426 23.764 1.00 19.69 ? 33  TRP   C C   1 
ATOM   1297 O  O   . TRP   B 1 27  ? 18.394 -12.310 22.919 1.00 20.62 ? 33  TRP   C O   1 
ATOM   1298 C  CB  . TRP   B 1 27  ? 18.521 -12.358 26.101 1.00 20.50 ? 33  TRP   C CB  1 
ATOM   1299 C  CG  . TRP   B 1 27  ? 19.997 -12.105 26.285 1.00 20.94 ? 33  TRP   C CG  1 
ATOM   1300 C  CD1 . TRP   B 1 27  ? 20.580 -11.187 27.109 1.00 22.22 ? 33  TRP   C CD1 1 
ATOM   1301 C  CD2 . TRP   B 1 27  ? 21.079 -12.834 25.668 1.00 20.01 ? 33  TRP   C CD2 1 
ATOM   1302 N  NE1 . TRP   B 1 27  ? 21.962 -11.287 27.033 1.00 22.38 ? 33  TRP   C NE1 1 
ATOM   1303 C  CE2 . TRP   B 1 27  ? 22.288 -12.279 26.146 1.00 20.84 ? 33  TRP   C CE2 1 
ATOM   1304 C  CE3 . TRP   B 1 27  ? 21.142 -13.867 24.720 1.00 20.41 ? 33  TRP   C CE3 1 
ATOM   1305 C  CZ2 . TRP   B 1 27  ? 23.534 -12.771 25.769 1.00 21.11 ? 33  TRP   C CZ2 1 
ATOM   1306 C  CZ3 . TRP   B 1 27  ? 22.385 -14.332 24.332 1.00 21.18 ? 33  TRP   C CZ3 1 
ATOM   1307 C  CH2 . TRP   B 1 27  ? 23.558 -13.775 24.852 1.00 21.54 ? 33  TRP   C CH2 1 
ATOM   1308 N  N   . GLU   B 1 28  ? 19.405 -10.407 23.584 1.00 18.50 ? 34  GLU   C N   1 
ATOM   1309 C  CA  . GLU   B 1 28  ? 20.255 -10.357 22.394 1.00 17.85 ? 34  GLU   C CA  1 
ATOM   1310 C  C   . GLU   B 1 28  ? 21.587 -9.718  22.737 1.00 18.87 ? 34  GLU   C C   1 
ATOM   1311 O  O   . GLU   B 1 28  ? 21.652 -8.879  23.647 1.00 18.46 ? 34  GLU   C O   1 
ATOM   1312 C  CB  . GLU   B 1 28  ? 19.573 -9.608  21.229 1.00 20.50 ? 34  GLU   C CB  1 
ATOM   1313 C  CG  . GLU   B 1 28  ? 19.031 -8.236  21.576 1.00 22.33 ? 34  GLU   C CG  1 
ATOM   1314 C  CD  . GLU   B 1 28  ? 20.023 -7.095  21.483 1.00 24.30 ? 34  GLU   C CD  1 
ATOM   1315 O  OE1 . GLU   B 1 28  ? 19.808 -6.069  22.165 1.00 25.87 ? 34  GLU   C OE1 1 
ATOM   1316 O  OE2 . GLU   B 1 28  ? 21.017 -7.222  20.732 1.00 24.07 ? 34  GLU   C OE2 1 
ATOM   1317 N  N   . ASP   B 1 29  ? 22.647 -10.084 21.997 1.00 18.08 ? 35  ASP   C N   1 
ATOM   1318 C  CA  . ASP   B 1 29  ? 23.954 -9.476  22.227 1.00 18.51 ? 35  ASP   C CA  1 
ATOM   1319 C  C   . ASP   B 1 29  ? 24.713 -9.447  20.905 1.00 17.65 ? 35  ASP   C C   1 
ATOM   1320 O  O   . ASP   B 1 29  ? 25.146 -10.485 20.414 1.00 18.25 ? 35  ASP   C O   1 
ATOM   1321 C  CB  . ASP   B 1 29  ? 24.716 -10.266 23.301 1.00 19.16 ? 35  ASP   C CB  1 
ATOM   1322 C  CG  . ASP   B 1 29  ? 26.048 -9.677  23.739 1.00 25.72 ? 35  ASP   C CG  1 
ATOM   1323 O  OD1 . ASP   B 1 29  ? 26.765 -9.117  22.884 1.00 26.45 ? 35  ASP   C OD1 1 
ATOM   1324 O  OD2 . ASP   B 1 29  ? 26.395 -9.813  24.931 1.00 27.26 ? 35  ASP   C OD2 1 
ATOM   1325 N  N   . SER   B 1 30  ? 24.854 -8.251  20.309 1.00 17.94 ? 36  SER   C N   1 
ATOM   1326 C  CA  A SER   B 1 30  ? 25.552 -8.081  19.035 0.50 17.93 ? 36  SER   C CA  1 
ATOM   1327 C  CA  B SER   B 1 30  ? 25.536 -8.131  19.026 0.50 18.34 ? 36  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 30  ? 27.009 -8.554  19.107 1.00 17.76 ? 36  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 30  ? 27.517 -9.145  18.137 1.00 18.18 ? 36  SER   C O   1 
ATOM   1330 C  CB  A SER   B 1 30  ? 25.511 -6.617  18.591 0.50 18.71 ? 36  SER   C CB  1 
ATOM   1331 C  CB  B SER   B 1 30  ? 25.401 -6.716  18.474 0.50 20.48 ? 36  SER   C CB  1 
ATOM   1332 O  OG  A SER   B 1 30  ? 26.380 -6.383  17.491 0.50 17.95 ? 36  SER   C OG  1 
ATOM   1333 O  OG  B SER   B 1 30  ? 25.927 -5.786  19.400 0.50 22.17 ? 36  SER   C OG  1 
ATOM   1334 N  N   . SER   B 1 31  ? 27.706 -8.269  20.240 1.00 18.01 ? 37  SER   C N   1 
ATOM   1335 C  CA  . SER   B 1 31  ? 29.113 -8.668  20.367 1.00 18.61 ? 37  SER   C CA  1 
ATOM   1336 C  C   . SER   B 1 31  ? 29.311 -10.181 20.320 1.00 17.66 ? 37  SER   C C   1 
ATOM   1337 O  O   . SER   B 1 31  ? 30.412 -10.630 19.983 1.00 18.04 ? 37  SER   C O   1 
ATOM   1338 C  CB  . SER   B 1 31  ? 29.734 -8.084  21.632 1.00 22.16 ? 37  SER   C CB  1 
ATOM   1339 O  OG  . SER   B 1 31  ? 29.343 -8.795  22.786 1.00 26.66 ? 37  SER   C OG  1 
ATOM   1340 N  N   . ARG   B 1 32  ? 28.259 -10.973 20.624 1.00 16.81 ? 38  ARG   C N   1 
ATOM   1341 C  CA  . ARG   B 1 32  ? 28.343 -12.438 20.549 1.00 16.41 ? 38  ARG   C CA  1 
ATOM   1342 C  C   . ARG   B 1 32  ? 27.672 -13.007 19.269 1.00 16.62 ? 38  ARG   C C   1 
ATOM   1343 O  O   . ARG   B 1 32  ? 27.683 -14.226 19.068 1.00 16.08 ? 38  ARG   C O   1 
ATOM   1344 C  CB  . ARG   B 1 32  ? 27.609 -13.063 21.786 1.00 17.50 ? 38  ARG   C CB  1 
ATOM   1345 C  CG  . ARG   B 1 32  ? 28.257 -12.708 23.110 1.00 19.20 ? 38  ARG   C CG  1 
ATOM   1346 C  CD  . ARG   B 1 32  ? 27.509 -13.302 24.310 1.00 19.79 ? 38  ARG   C CD  1 
ATOM   1347 N  NE  . ARG   B 1 32  ? 27.600 -14.766 24.352 1.00 18.23 ? 38  ARG   C NE  1 
ATOM   1348 C  CZ  . ARG   B 1 32  ? 27.579 -15.493 25.472 1.00 19.40 ? 38  ARG   C CZ  1 
ATOM   1349 N  NH1 . ARG   B 1 32  ? 27.480 -14.901 26.657 1.00 19.94 ? 38  ARG   C NH1 1 
ATOM   1350 N  NH2 . ARG   B 1 32  ? 27.722 -16.816 25.416 1.00 17.41 ? 38  ARG   C NH2 1 
ATOM   1351 N  N   . ASP   B 1 33  ? 26.975 -12.144 18.470 1.00 16.05 ? 39  ASP   C N   1 
ATOM   1352 C  CA  . ASP   B 1 33  ? 26.180 -12.594 17.327 1.00 15.03 ? 39  ASP   C CA  1 
ATOM   1353 C  C   . ASP   B 1 33  ? 25.086 -13.552 17.803 1.00 14.70 ? 39  ASP   C C   1 
ATOM   1354 O  O   . ASP   B 1 33  ? 24.741 -14.479 17.061 1.00 14.28 ? 39  ASP   C O   1 
ATOM   1355 C  CB  . ASP   B 1 33  ? 27.037 -13.206 16.200 1.00 15.06 ? 39  ASP   C CB  1 
ATOM   1356 C  CG  . ASP   B 1 33  ? 26.223 -13.558 14.959 1.00 17.41 ? 39  ASP   C CG  1 
ATOM   1357 O  OD1 . ASP   B 1 33  ? 25.319 -12.762 14.588 1.00 18.25 ? 39  ASP   C OD1 1 
ATOM   1358 O  OD2 . ASP   B 1 33  ? 26.515 -14.591 14.334 1.00 16.01 ? 39  ASP   C OD2 1 
ATOM   1359 N  N   . LEU   B 1 34  ? 24.474 -13.305 19.003 1.00 15.12 ? 40  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 34  ? 23.368 -14.167 19.475 1.00 14.97 ? 40  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 34  ? 22.093 -13.406 19.715 1.00 15.24 ? 40  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 34  ? 22.132 -12.274 20.182 1.00 16.31 ? 40  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 34  ? 23.708 -14.915 20.781 1.00 14.92 ? 40  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 34  ? 24.794 -15.994 20.677 1.00 16.24 ? 40  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 34  ? 25.076 -16.597 22.066 1.00 17.11 ? 40  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 34  ? 24.387 -17.138 19.720 1.00 17.01 ? 40  LEU   C CD2 1 
ATOM   1367 N  N   . LEU   B 1 35  ? 20.963 -14.095 19.521 1.00 14.82 ? 41  LEU   C N   1 
ATOM   1368 C  CA  . LEU   B 1 35  ? 19.643 -13.555 19.856 1.00 15.99 ? 41  LEU   C CA  1 
ATOM   1369 C  C   . LEU   B 1 35  ? 18.794 -14.751 20.300 1.00 16.39 ? 41  LEU   C C   1 
ATOM   1370 O  O   . LEU   B 1 35  ? 18.849 -15.826 19.704 1.00 16.89 ? 41  LEU   C O   1 
ATOM   1371 C  CB  . LEU   B 1 35  ? 18.988 -12.840 18.642 1.00 16.52 ? 41  LEU   C CB  1 
ATOM   1372 C  CG  . LEU   B 1 35  ? 17.597 -12.229 18.927 1.00 18.14 ? 41  LEU   C CG  1 
ATOM   1373 C  CD1 . LEU   B 1 35  ? 17.429 -10.928 18.162 1.00 20.77 ? 41  LEU   C CD1 1 
ATOM   1374 C  CD2 . LEU   B 1 35  ? 16.453 -13.199 18.549 1.00 19.13 ? 41  LEU   C CD2 1 
ATOM   1375 N  N   . VAL   B 1 36  ? 18.018 -14.572 21.363 1.00 16.85 ? 42  VAL   C N   1 
ATOM   1376 C  CA  . VAL   B 1 36  ? 17.112 -15.608 21.882 1.00 16.95 ? 42  VAL   C CA  1 
ATOM   1377 C  C   . VAL   B 1 36  ? 15.699 -15.070 21.878 1.00 18.06 ? 42  VAL   C C   1 
ATOM   1378 O  O   . VAL   B 1 36  ? 15.450 -13.992 22.432 1.00 19.01 ? 42  VAL   C O   1 
ATOM   1379 C  CB  . VAL   B 1 36  ? 17.538 -16.073 23.298 1.00 16.69 ? 42  VAL   C CB  1 
ATOM   1380 C  CG1 . VAL   B 1 36  ? 16.566 -17.124 23.857 1.00 17.62 ? 42  VAL   C CG1 1 
ATOM   1381 C  CG2 . VAL   B 1 36  ? 18.977 -16.633 23.254 1.00 16.01 ? 42  VAL   C CG2 1 
ATOM   1382 N  N   . SER   B 1 37  ? 14.761 -15.837 21.310 1.00 17.59 ? 43  SER   C N   1 
ATOM   1383 C  CA  . SER   B 1 37  ? 13.351 -15.468 21.313 1.00 18.22 ? 43  SER   C CA  1 
ATOM   1384 C  C   . SER   B 1 37  ? 12.527 -16.552 22.017 1.00 20.05 ? 43  SER   C C   1 
ATOM   1385 O  O   . SER   B 1 37  ? 13.027 -17.660 22.260 1.00 19.69 ? 43  SER   C O   1 
ATOM   1386 C  CB  . SER   B 1 37  ? 12.853 -15.248 19.888 1.00 19.96 ? 43  SER   C CB  1 
ATOM   1387 O  OG  . SER   B 1 37  ? 13.007 -16.410 19.087 1.00 21.06 ? 43  SER   C OG  1 
ATOM   1388 N  N   . SER   B 1 38  ? 11.280 -16.224 22.379 1.00 19.98 ? 44  SER   C N   1 
ATOM   1389 C  CA  . SER   B 1 38  ? 10.411 -17.196 23.046 1.00 21.44 ? 44  SER   C CA  1 
ATOM   1390 C  C   . SER   B 1 38  ? 9.576  -17.993 22.031 1.00 23.02 ? 44  SER   C C   1 
ATOM   1391 O  O   . SER   B 1 38  ? 9.244  -17.493 20.953 1.00 23.09 ? 44  SER   C O   1 
ATOM   1392 C  CB  . SER   B 1 38  ? 9.524  -16.496 24.069 1.00 24.13 ? 44  SER   C CB  1 
ATOM   1393 O  OG  . SER   B 1 38  ? 8.681  -15.576 23.397 1.00 27.57 ? 44  SER   C OG  1 
ATOM   1394 N  N   . THR   B 1 39  ? 9.228  -19.229 22.375 1.00 23.20 ? 45  THR   C N   1 
ATOM   1395 C  CA  . THR   B 1 39  ? 8.448  -20.093 21.491 1.00 24.14 ? 45  THR   C CA  1 
ATOM   1396 C  C   . THR   B 1 39  ? 7.162  -20.571 22.194 1.00 26.92 ? 45  THR   C C   1 
ATOM   1397 O  O   . THR   B 1 39  ? 7.094  -20.622 23.420 1.00 26.61 ? 45  THR   C O   1 
ATOM   1398 C  CB  . THR   B 1 39  ? 9.283  -21.332 21.064 1.00 23.82 ? 45  THR   C CB  1 
ATOM   1399 O  OG1 . THR   B 1 39  ? 9.563  -22.109 22.227 1.00 23.50 ? 45  THR   C OG1 1 
ATOM   1400 C  CG2 . THR   B 1 39  ? 10.583 -20.964 20.350 1.00 23.79 ? 45  THR   C CG2 1 
ATOM   1401 N  N   . THR   B 1 40  ? 6.156  -20.942 21.397 1.00 29.08 ? 46  THR   C N   1 
ATOM   1402 C  CA  . THR   B 1 40  ? 4.927  -21.495 21.937 1.00 31.10 ? 46  THR   C CA  1 
ATOM   1403 C  C   . THR   B 1 40  ? 5.143  -22.983 22.228 1.00 31.25 ? 46  THR   C C   1 
ATOM   1404 O  O   . THR   B 1 40  ? 4.769  -23.466 23.299 1.00 32.39 ? 46  THR   C O   1 
ATOM   1405 C  CB  . THR   B 1 40  ? 3.757  -21.194 20.987 1.00 35.03 ? 46  THR   C CB  1 
ATOM   1406 O  OG1 . THR   B 1 40  ? 4.036  -21.794 19.721 1.00 38.42 ? 46  THR   C OG1 1 
ATOM   1407 C  CG2 . THR   B 1 40  ? 3.563  -19.705 20.770 1.00 34.67 ? 46  THR   C CG2 1 
ATOM   1408 N  N   . ALA   B 1 41  ? 5.773  -23.711 21.296 1.00 29.83 ? 47  ALA   C N   1 
ATOM   1409 C  CA  . ALA   B 1 41  ? 6.024  -25.140 21.504 1.00 29.31 ? 47  ALA   C CA  1 
ATOM   1410 C  C   . ALA   B 1 41  ? 7.349  -25.385 22.230 1.00 27.50 ? 47  ALA   C C   1 
ATOM   1411 O  O   . ALA   B 1 41  ? 8.289  -24.603 22.070 1.00 26.10 ? 47  ALA   C O   1 
ATOM   1412 C  CB  . ALA   B 1 41  ? 6.028  -25.870 20.166 1.00 29.99 ? 47  ALA   C CB  1 
ATOM   1413 N  N   . GLN   B 1 42  ? 7.428  -26.466 23.006 1.00 27.49 ? 48  GLN   C N   1 
ATOM   1414 C  CA  . GLN   B 1 42  ? 8.659  -26.847 23.711 1.00 28.87 ? 48  GLN   C CA  1 
ATOM   1415 C  C   . GLN   B 1 42  ? 9.682  -27.472 22.735 1.00 28.12 ? 48  GLN   C C   1 
ATOM   1416 O  O   . GLN   B 1 42  ? 9.301  -28.213 21.823 1.00 29.21 ? 48  GLN   C O   1 
ATOM   1417 C  CB  . GLN   B 1 42  ? 8.344  -27.822 24.853 1.00 33.03 ? 48  GLN   C CB  1 
ATOM   1418 C  CG  . GLN   B 1 42  ? 7.748  -27.127 26.070 1.00 40.09 ? 48  GLN   C CG  1 
ATOM   1419 C  CD  . GLN   B 1 42  ? 7.575  -28.117 27.197 1.00 49.03 ? 48  GLN   C CD  1 
ATOM   1420 O  OE1 . GLN   B 1 42  ? 6.782  -29.065 27.114 1.00 52.53 ? 48  GLN   C OE1 1 
ATOM   1421 N  NE2 . GLN   B 1 42  ? 8.321  -27.941 28.275 1.00 50.74 ? 48  GLN   C NE2 1 
ATOM   1422 N  N   . GLY   B 1 43  ? 10.952 -27.123 22.904 1.00 25.57 ? 49  GLY   C N   1 
ATOM   1423 C  CA  . GLY   B 1 43  ? 12.040 -27.652 22.087 1.00 24.52 ? 49  GLY   C CA  1 
ATOM   1424 C  C   . GLY   B 1 43  ? 12.650 -28.890 22.713 1.00 23.56 ? 49  GLY   C C   1 
ATOM   1425 O  O   . GLY   B 1 43  ? 12.388 -29.197 23.889 1.00 25.57 ? 49  GLY   C O   1 
ATOM   1426 N  N   . CYS   B 1 44  ? 13.467 -29.607 21.952 1.00 21.60 ? 50  CYS   C N   1 
ATOM   1427 C  CA  A CYS   B 1 44  ? 14.031 -30.856 22.441 0.50 21.94 ? 50  CYS   C CA  1 
ATOM   1428 C  CA  B CYS   B 1 44  ? 14.028 -30.858 22.451 0.50 22.70 ? 50  CYS   C CA  1 
ATOM   1429 C  C   . CYS   B 1 44  ? 15.544 -30.871 22.576 1.00 22.77 ? 50  CYS   C C   1 
ATOM   1430 O  O   . CYS   B 1 44  ? 16.090 -31.897 22.988 1.00 24.89 ? 50  CYS   C O   1 
ATOM   1431 C  CB  A CYS   B 1 44  ? 13.546 -31.997 21.561 0.50 21.74 ? 50  CYS   C CB  1 
ATOM   1432 C  CB  B CYS   B 1 44  ? 13.557 -31.995 21.563 0.50 24.40 ? 50  CYS   C CB  1 
ATOM   1433 S  SG  A CYS   B 1 44  ? 11.772 -31.932 21.228 0.50 22.13 ? 50  CYS   C SG  1 
ATOM   1434 S  SG  B CYS   B 1 44  ? 14.072 -31.797 19.851 0.50 31.11 ? 50  CYS   C SG  1 
ATOM   1435 N  N   . ASP   B 1 45  ? 16.221 -29.772 22.232 1.00 19.97 ? 51  ASP   C N   1 
ATOM   1436 C  CA  . ASP   B 1 45  ? 17.678 -29.744 22.337 1.00 19.02 ? 51  ASP   C CA  1 
ATOM   1437 C  C   . ASP   B 1 45  ? 18.065 -29.566 23.806 1.00 19.26 ? 51  ASP   C C   1 
ATOM   1438 O  O   . ASP   B 1 45  ? 17.317 -28.948 24.581 1.00 21.04 ? 51  ASP   C O   1 
ATOM   1439 C  CB  . ASP   B 1 45  ? 18.288 -28.593 21.500 1.00 19.78 ? 51  ASP   C CB  1 
ATOM   1440 C  CG  . ASP   B 1 45  ? 18.109 -28.754 19.999 1.00 24.03 ? 51  ASP   C CG  1 
ATOM   1441 O  OD1 . ASP   B 1 45  ? 18.159 -29.908 19.509 1.00 24.80 ? 51  ASP   C OD1 1 
ATOM   1442 O  OD2 . ASP   B 1 45  ? 17.920 -27.722 19.307 1.00 22.91 ? 51  ASP   C OD2 1 
ATOM   1443 N  N   . THR   B 1 46  ? 19.214 -30.146 24.190 1.00 17.25 ? 52  THR   C N   1 
ATOM   1444 C  CA  . THR   B 1 46  ? 19.766 -29.975 25.533 1.00 16.59 ? 52  THR   C CA  1 
ATOM   1445 C  C   . THR   B 1 46  ? 21.085 -29.184 25.363 1.00 16.52 ? 52  THR   C C   1 
ATOM   1446 O  O   . THR   B 1 46  ? 21.891 -29.517 24.481 1.00 16.78 ? 52  THR   C O   1 
ATOM   1447 C  CB  . THR   B 1 46  ? 20.139 -31.343 26.120 1.00 18.97 ? 52  THR   C CB  1 
ATOM   1448 O  OG1 . THR   B 1 46  ? 18.945 -32.147 26.297 1.00 20.48 ? 52  THR   C OG1 1 
ATOM   1449 C  CG2 . THR   B 1 46  ? 20.921 -31.219 27.452 1.00 20.05 ? 52  THR   C CG2 1 
ATOM   1450 N  N   . ILE   B 1 47  ? 21.298 -28.183 26.203 1.00 15.44 ? 53  ILE   C N   1 
ATOM   1451 C  CA  . ILE   B 1 47  ? 22.531 -27.412 26.153 1.00 15.40 ? 53  ILE   C CA  1 
ATOM   1452 C  C   . ILE   B 1 47  ? 23.616 -28.126 26.968 1.00 13.72 ? 53  ILE   C C   1 
ATOM   1453 O  O   . ILE   B 1 47  ? 23.378 -28.553 28.104 1.00 15.02 ? 53  ILE   C O   1 
ATOM   1454 C  CB  . ILE   B 1 47  ? 22.319 -26.016 26.747 1.00 16.68 ? 53  ILE   C CB  1 
ATOM   1455 C  CG1 . ILE   B 1 47  ? 21.150 -25.272 26.084 1.00 16.13 ? 53  ILE   C CG1 1 
ATOM   1456 C  CG2 . ILE   B 1 47  ? 23.608 -25.186 26.618 1.00 16.72 ? 53  ILE   C CG2 1 
ATOM   1457 C  CD1 . ILE   B 1 47  ? 21.330 -25.152 24.516 1.00 18.25 ? 53  ILE   C CD1 1 
ATOM   1458 N  N   . ALA   B 1 48  ? 24.813 -28.213 26.413 1.00 13.28 ? 54  ALA   C N   1 
ATOM   1459 C  CA  . ALA   B 1 48  ? 25.938 -28.795 27.126 1.00 13.70 ? 54  ALA   C CA  1 
ATOM   1460 C  C   . ALA   B 1 48  ? 26.338 -27.875 28.293 1.00 14.51 ? 54  ALA   C C   1 
ATOM   1461 O  O   . ALA   B 1 48  ? 26.336 -26.646 28.133 1.00 15.33 ? 54  ALA   C O   1 
ATOM   1462 C  CB  . ALA   B 1 48  ? 27.115 -28.926 26.167 1.00 14.19 ? 54  ALA   C CB  1 
ATOM   1463 N  N   . ARG   B 1 49  ? 26.701 -28.465 29.457 1.00 13.28 ? 55  ARG   C N   1 
ATOM   1464 C  CA  . ARG   B 1 49  ? 27.177 -27.717 30.612 1.00 14.18 ? 55  ARG   C CA  1 
ATOM   1465 C  C   . ARG   B 1 49  ? 28.507 -28.397 30.980 1.00 15.45 ? 55  ARG   C C   1 
ATOM   1466 O  O   . ARG   B 1 49  ? 28.554 -29.463 31.641 1.00 16.73 ? 55  ARG   C O   1 
ATOM   1467 C  CB  . ARG   B 1 49  ? 26.158 -27.759 31.763 1.00 13.72 ? 55  ARG   C CB  1 
ATOM   1468 C  CG  . ARG   B 1 49  ? 24.799 -27.173 31.364 1.00 14.75 ? 55  ARG   C CG  1 
ATOM   1469 C  CD  . ARG   B 1 49  ? 24.828 -25.687 31.031 1.00 16.31 ? 55  ARG   C CD  1 
ATOM   1470 N  NE  . ARG   B 1 49  ? 23.478 -25.236 30.674 1.00 17.18 ? 55  ARG   C NE  1 
ATOM   1471 C  CZ  . ARG   B 1 49  ? 23.222 -24.123 29.987 1.00 18.87 ? 55  ARG   C CZ  1 
ATOM   1472 N  NH1 . ARG   B 1 49  ? 24.214 -23.316 29.610 1.00 16.84 ? 55  ARG   C NH1 1 
ATOM   1473 N  NH2 . ARG   B 1 49  ? 21.977 -23.816 29.657 1.00 19.55 ? 55  ARG   C NH2 1 
ATOM   1474 N  N   . CYS   B 1 50  ? 29.582 -27.841 30.415 1.00 15.32 ? 56  CYS   C N   1 
ATOM   1475 C  CA  . CYS   B 1 50  ? 30.881 -28.520 30.448 1.00 14.02 ? 56  CYS   C CA  1 
ATOM   1476 C  C   . CYS   B 1 50  ? 31.991 -27.595 29.955 1.00 14.66 ? 56  CYS   C C   1 
ATOM   1477 O  O   . CYS   B 1 50  ? 31.705 -26.501 29.485 1.00 14.40 ? 56  CYS   C O   1 
ATOM   1478 C  CB  . CYS   B 1 50  ? 30.779 -29.721 29.510 1.00 14.86 ? 56  CYS   C CB  1 
ATOM   1479 S  SG  . CYS   B 1 50  ? 30.683 -29.245 27.758 1.00 15.38 ? 56  CYS   C SG  1 
ATOM   1480 N  N   . ASP   B 1 51  ? 33.253 -28.114 29.931 1.00 15.31 ? 57  ASP   C N   1 
ATOM   1481 C  CA  . ASP   B 1 51  ? 34.349 -27.367 29.328 1.00 15.97 ? 57  ASP   C CA  1 
ATOM   1482 C  C   . ASP   B 1 51  ? 35.018 -28.179 28.197 1.00 16.89 ? 57  ASP   C C   1 
ATOM   1483 O  O   . ASP   B 1 51  ? 36.214 -28.037 27.954 1.00 17.26 ? 57  ASP   C O   1 
ATOM   1484 C  CB  . ASP   B 1 51  ? 35.378 -26.948 30.375 1.00 17.88 ? 57  ASP   C CB  1 
ATOM   1485 C  CG  . ASP   B 1 51  ? 36.065 -28.077 31.090 1.00 22.69 ? 57  ASP   C CG  1 
ATOM   1486 O  OD1 . ASP   B 1 51  ? 35.740 -29.262 30.805 1.00 21.88 ? 57  ASP   C OD1 1 
ATOM   1487 O  OD2 . ASP   B 1 51  ? 36.955 -27.790 31.921 1.00 28.12 ? 57  ASP   C OD2 1 
ATOM   1488 N  N   . CYS   B 1 52  ? 34.237 -29.044 27.490 1.00 16.27 ? 58  CYS   C N   1 
ATOM   1489 C  CA  . CYS   B 1 52  ? 34.759 -29.845 26.361 1.00 14.84 ? 58  CYS   C CA  1 
ATOM   1490 C  C   . CYS   B 1 52  ? 35.446 -28.970 25.353 1.00 15.21 ? 58  CYS   C C   1 
ATOM   1491 O  O   . CYS   B 1 52  ? 34.997 -27.824 25.100 1.00 15.09 ? 58  CYS   C O   1 
ATOM   1492 C  CB  . CYS   B 1 52  ? 33.656 -30.637 25.660 1.00 14.12 ? 58  CYS   C CB  1 
ATOM   1493 S  SG  . CYS   B 1 52  ? 33.035 -32.052 26.598 1.00 16.19 ? 58  CYS   C SG  1 
ATOM   1494 N  N   . GLN   B 1 53  ? 36.465 -29.529 24.735 1.00 14.44 ? 59  GLN   C N   1 
ATOM   1495 C  CA  . GLN   B 1 53  ? 37.124 -28.886 23.601 1.00 14.60 ? 59  GLN   C CA  1 
ATOM   1496 C  C   . GLN   B 1 53  ? 37.185 -29.787 22.377 1.00 14.64 ? 59  GLN   C C   1 
ATOM   1497 O  O   . GLN   B 1 53  ? 37.948 -29.523 21.434 1.00 14.95 ? 59  GLN   C O   1 
ATOM   1498 C  CB  . GLN   B 1 53  ? 38.515 -28.365 23.950 1.00 15.05 ? 59  GLN   C CB  1 
ATOM   1499 C  CG  . GLN   B 1 53  ? 38.503 -27.147 24.885 1.00 16.42 ? 59  GLN   C CG  1 
ATOM   1500 C  CD  . GLN   B 1 53  ? 39.933 -26.702 25.005 1.00 21.45 ? 59  GLN   C CD  1 
ATOM   1501 O  OE1 . GLN   B 1 53  ? 40.551 -26.851 26.078 1.00 23.78 ? 59  GLN   C OE1 1 
ATOM   1502 N  NE2 . GLN   B 1 53  ? 40.516 -26.219 23.908 1.00 18.02 ? 59  GLN   C NE2 1 
ATOM   1503 N  N   . THR   B 1 54  ? 36.380 -30.859 22.350 1.00 14.61 ? 60  THR   C N   1 
ATOM   1504 C  CA  . THR   B 1 54  ? 36.228 -31.731 21.179 1.00 15.55 ? 60  THR   C CA  1 
ATOM   1505 C  C   . THR   B 1 54  ? 34.730 -31.965 20.997 1.00 15.74 ? 60  THR   C C   1 
ATOM   1506 O  O   . THR   B 1 54  ? 33.967 -32.047 21.981 1.00 16.07 ? 60  THR   C O   1 
ATOM   1507 C  CB  . THR   B 1 54  ? 36.987 -33.036 21.271 1.00 19.51 ? 60  THR   C CB  1 
ATOM   1508 O  OG1 . THR   B 1 54  ? 36.448 -33.782 22.327 1.00 22.03 ? 60  THR   C OG1 1 
ATOM   1509 C  CG2 . THR   B 1 54  ? 38.474 -32.834 21.501 1.00 19.98 ? 60  THR   C CG2 1 
ATOM   1510 N  N   . GLY   B 1 55  ? 34.307 -32.011 19.730 1.00 13.87 ? 61  GLY   C N   1 
ATOM   1511 C  CA  . GLY   B 1 55  ? 32.894 -32.173 19.406 1.00 13.83 ? 61  GLY   C CA  1 
ATOM   1512 C  C   . GLY   B 1 55  ? 32.739 -32.432 17.917 1.00 14.08 ? 61  GLY   C C   1 
ATOM   1513 O  O   . GLY   B 1 55  ? 33.720 -32.749 17.221 1.00 14.48 ? 61  GLY   C O   1 
ATOM   1514 N  N   . VAL   B 1 56  ? 31.499 -32.289 17.426 1.00 13.74 ? 62  VAL   C N   1 
ATOM   1515 C  CA  . VAL   B 1 56  ? 31.188 -32.490 16.003 1.00 13.15 ? 62  VAL   C CA  1 
ATOM   1516 C  C   . VAL   B 1 56  ? 30.281 -31.345 15.598 1.00 13.59 ? 62  VAL   C C   1 
ATOM   1517 O  O   . VAL   B 1 56  ? 29.341 -31.017 16.337 1.00 14.12 ? 62  VAL   C O   1 
ATOM   1518 C  CB  . VAL   B 1 56  ? 30.420 -33.824 15.857 1.00 13.65 ? 62  VAL   C CB  1 
ATOM   1519 C  CG1 . VAL   B 1 56  ? 29.873 -34.001 14.439 1.00 15.39 ? 62  VAL   C CG1 1 
ATOM   1520 C  CG2 . VAL   B 1 56  ? 31.329 -35.006 16.237 1.00 13.73 ? 62  VAL   C CG2 1 
ATOM   1521 N  N   . TYR   B 1 57  ? 30.510 -30.759 14.413 1.00 13.22 ? 63  TYR   C N   1 
ATOM   1522 C  CA  . TYR   B 1 57  ? 29.629 -29.657 13.957 1.00 13.04 ? 63  TYR   C CA  1 
ATOM   1523 C  C   . TYR   B 1 57  ? 29.059 -30.004 12.588 1.00 13.89 ? 63  TYR   C C   1 
ATOM   1524 O  O   . TYR   B 1 57  ? 29.709 -30.710 11.815 1.00 14.64 ? 63  TYR   C O   1 
ATOM   1525 C  CB  . TYR   B 1 57  ? 30.357 -28.279 13.911 1.00 13.48 ? 63  TYR   C CB  1 
ATOM   1526 C  CG  . TYR   B 1 57  ? 31.222 -27.990 12.696 1.00 13.38 ? 63  TYR   C CG  1 
ATOM   1527 C  CD1 . TYR   B 1 57  ? 32.501 -28.515 12.589 1.00 14.18 ? 63  TYR   C CD1 1 
ATOM   1528 C  CD2 . TYR   B 1 57  ? 30.785 -27.115 11.696 1.00 13.01 ? 63  TYR   C CD2 1 
ATOM   1529 C  CE1 . TYR   B 1 57  ? 33.328 -28.215 11.490 1.00 14.80 ? 63  TYR   C CE1 1 
ATOM   1530 C  CE2 . TYR   B 1 57  ? 31.603 -26.793 10.606 1.00 13.79 ? 63  TYR   C CE2 1 
ATOM   1531 C  CZ  . TYR   B 1 57  ? 32.872 -27.365 10.490 1.00 15.22 ? 63  TYR   C CZ  1 
ATOM   1532 O  OH  . TYR   B 1 57  ? 33.684 -27.031 9.399  1.00 17.13 ? 63  TYR   C OH  1 
ATOM   1533 N  N   . TYR   B 1 58  ? 27.902 -29.419 12.279 1.00 13.27 ? 64  TYR   C N   1 
ATOM   1534 C  CA  . TYR   B 1 58  ? 27.276 -29.617 10.971 1.00 14.52 ? 64  TYR   C CA  1 
ATOM   1535 C  C   . TYR   B 1 58  ? 27.665 -28.457 10.050 1.00 14.53 ? 64  TYR   C C   1 
ATOM   1536 O  O   . TYR   B 1 58  ? 27.445 -27.284 10.391 1.00 14.42 ? 64  TYR   C O   1 
ATOM   1537 C  CB  . TYR   B 1 58  ? 25.757 -29.673 11.072 1.00 15.09 ? 64  TYR   C CB  1 
ATOM   1538 C  CG  . TYR   B 1 58  ? 25.143 -29.950 9.708  1.00 16.14 ? 64  TYR   C CG  1 
ATOM   1539 C  CD1 . TYR   B 1 58  ? 25.456 -31.107 9.003  1.00 17.25 ? 64  TYR   C CD1 1 
ATOM   1540 C  CD2 . TYR   B 1 58  ? 24.315 -29.025 9.100  1.00 16.21 ? 64  TYR   C CD2 1 
ATOM   1541 C  CE1 . TYR   B 1 58  ? 24.955 -31.336 7.726  1.00 18.20 ? 64  TYR   C CE1 1 
ATOM   1542 C  CE2 . TYR   B 1 58  ? 23.770 -29.266 7.843  1.00 17.69 ? 64  TYR   C CE2 1 
ATOM   1543 C  CZ  . TYR   B 1 58  ? 24.072 -30.439 7.174  1.00 19.01 ? 64  TYR   C CZ  1 
ATOM   1544 O  OH  . TYR   B 1 58  ? 23.590 -30.691 5.905  1.00 22.91 ? 64  TYR   C OH  1 
ATOM   1545 N  N   . CYS   B 1 59  ? 28.158 -28.816 8.855  1.00 14.18 ? 65  CYS   C N   1 
ATOM   1546 C  CA  . CYS   B 1 59  ? 28.591 -27.863 7.822  1.00 14.92 ? 65  CYS   C CA  1 
ATOM   1547 C  C   . CYS   B 1 59  ? 27.639 -28.030 6.628  1.00 17.14 ? 65  CYS   C C   1 
ATOM   1548 O  O   . CYS   B 1 59  ? 27.801 -28.982 5.851  1.00 17.15 ? 65  CYS   C O   1 
ATOM   1549 C  CB  . CYS   B 1 59  ? 30.032 -28.156 7.422  1.00 15.16 ? 65  CYS   C CB  1 
ATOM   1550 S  SG  . CYS   B 1 59  ? 30.631 -27.143 6.035  1.00 17.28 ? 65  CYS   C SG  1 
ATOM   1551 N  N   . SER   B 1 60  ? 26.659 -27.111 6.476  1.00 17.05 ? 66  SER   C N   1 
ATOM   1552 C  CA  A SER   B 1 60  ? 25.686 -27.274 5.400  0.50 17.87 ? 66  SER   C CA  1 
ATOM   1553 C  CA  B SER   B 1 60  ? 25.686 -27.262 5.393  0.50 17.19 ? 66  SER   C CA  1 
ATOM   1554 C  C   . SER   B 1 60  ? 26.294 -27.182 4.001  1.00 17.70 ? 66  SER   C C   1 
ATOM   1555 O  O   . SER   B 1 60  ? 25.836 -27.886 3.092  1.00 19.89 ? 66  SER   C O   1 
ATOM   1556 C  CB  A SER   B 1 60  ? 24.530 -26.303 5.566  0.50 20.63 ? 66  SER   C CB  1 
ATOM   1557 C  CB  B SER   B 1 60  ? 24.577 -26.234 5.508  0.50 18.00 ? 66  SER   C CB  1 
ATOM   1558 O  OG  A SER   B 1 60  ? 24.980 -24.980 5.791  0.50 23.22 ? 66  SER   C OG  1 
ATOM   1559 O  OG  B SER   B 1 60  ? 23.622 -26.470 4.483  0.50 17.30 ? 66  SER   C OG  1 
ATOM   1560 N  N   . SER   B 1 61  ? 27.331 -26.356 3.827  1.00 16.89 ? 67  SER   C N   1 
ATOM   1561 C  CA  . SER   B 1 61  ? 27.980 -26.207 2.505  1.00 17.62 ? 67  SER   C CA  1 
ATOM   1562 C  C   . SER   B 1 61  ? 28.738 -27.466 2.042  1.00 19.59 ? 67  SER   C C   1 
ATOM   1563 O  O   . SER   B 1 61  ? 29.226 -27.520 0.896  1.00 21.03 ? 67  SER   C O   1 
ATOM   1564 C  CB  . SER   B 1 61  ? 28.888 -24.979 2.505  1.00 19.33 ? 67  SER   C CB  1 
ATOM   1565 O  OG  . SER   B 1 61  ? 29.984 -25.115 3.397  1.00 21.93 ? 67  SER   C OG  1 
ATOM   1566 N  N   . ARG   B 1 62  ? 28.885 -28.463 2.925  1.00 18.56 ? 68  ARG   C N   1 
ATOM   1567 C  CA  . ARG   B 1 62  ? 29.530 -29.727 2.546  1.00 18.53 ? 68  ARG   C CA  1 
ATOM   1568 C  C   . ARG   B 1 62  ? 28.590 -30.928 2.802  1.00 19.29 ? 68  ARG   C C   1 
ATOM   1569 O  O   . ARG   B 1 62  ? 29.024 -32.066 2.613  1.00 20.47 ? 68  ARG   C O   1 
ATOM   1570 C  CB  . ARG   B 1 62  ? 30.816 -29.954 3.344  1.00 18.81 ? 68  ARG   C CB  1 
ATOM   1571 C  CG  . ARG   B 1 62  ? 31.901 -28.910 3.062  1.00 22.87 ? 68  ARG   C CG  1 
ATOM   1572 C  CD  . ARG   B 1 62  ? 32.572 -29.187 1.752  1.00 24.47 ? 68  ARG   C CD  1 
ATOM   1573 N  NE  . ARG   B 1 62  ? 33.597 -28.177 1.455  1.00 26.53 ? 68  ARG   C NE  1 
ATOM   1574 C  CZ  . ARG   B 1 62  ? 33.385 -27.081 0.736  1.00 33.60 ? 68  ARG   C CZ  1 
ATOM   1575 N  NH1 . ARG   B 1 62  ? 32.177 -26.827 0.235  1.00 36.38 ? 68  ARG   C NH1 1 
ATOM   1576 N  NH2 . ARG   B 1 62  ? 34.386 -26.238 0.483  1.00 33.79 ? 68  ARG   C NH2 1 
ATOM   1577 N  N   . ARG   B 1 63  ? 27.393 -30.695 3.349  1.00 20.18 ? 69  ARG   C N   1 
ATOM   1578 C  CA  . ARG   B 1 63  ? 26.454 -31.768 3.705  1.00 21.87 ? 69  ARG   C CA  1 
ATOM   1579 C  C   . ARG   B 1 63  ? 27.117 -32.779 4.642  1.00 21.91 ? 69  ARG   C C   1 
ATOM   1580 O  O   . ARG   B 1 63  ? 26.965 -33.992 4.455  1.00 22.93 ? 69  ARG   C O   1 
ATOM   1581 C  CB  . ARG   B 1 63  ? 26.016 -32.489 2.403  1.00 25.19 ? 69  ARG   C CB  1 
ATOM   1582 C  CG  . ARG   B 1 63  ? 24.576 -32.371 2.057  1.00 31.59 ? 69  ARG   C CG  1 
ATOM   1583 C  CD  . ARG   B 1 63  ? 24.152 -30.960 2.108  1.00 32.71 ? 69  ARG   C CD  1 
ATOM   1584 N  NE  . ARG   B 1 63  ? 22.975 -30.719 1.290  1.00 35.61 ? 69  ARG   C NE  1 
ATOM   1585 C  CZ  . ARG   B 1 63  ? 22.536 -29.504 0.984  1.00 37.11 ? 69  ARG   C CZ  1 
ATOM   1586 N  NH1 . ARG   B 1 63  ? 23.180 -28.421 1.429  1.00 35.16 ? 69  ARG   C NH1 1 
ATOM   1587 N  NH2 . ARG   B 1 63  ? 21.461 -29.355 0.221  1.00 36.46 ? 69  ARG   C NH2 1 
ATOM   1588 N  N   . LYS   B 1 64  ? 27.926 -32.279 5.582  1.00 19.84 ? 70  LYS   C N   1 
ATOM   1589 C  CA  . LYS   B 1 64  ? 28.725 -33.179 6.396  1.00 19.80 ? 70  LYS   C CA  1 
ATOM   1590 C  C   . LYS   B 1 64  ? 28.861 -32.712 7.804  1.00 17.73 ? 70  LYS   C C   1 
ATOM   1591 O  O   . LYS   B 1 64  ? 28.897 -31.514 8.065  1.00 17.16 ? 70  LYS   C O   1 
ATOM   1592 C  CB  . LYS   B 1 64  ? 30.146 -33.281 5.810  1.00 23.61 ? 70  LYS   C CB  1 
ATOM   1593 C  CG  . LYS   B 1 64  ? 30.286 -34.311 4.680  1.00 33.44 ? 70  LYS   C CG  1 
ATOM   1594 C  CD  . LYS   B 1 64  ? 31.735 -34.721 4.459  1.00 41.23 ? 70  LYS   C CD  1 
ATOM   1595 C  CE  . LYS   B 1 64  ? 31.886 -35.571 3.215  1.00 46.34 ? 70  LYS   C CE  1 
ATOM   1596 N  NZ  . LYS   B 1 64  ? 31.391 -34.857 2.007  1.00 50.28 ? 70  LYS   C NZ  1 
ATOM   1597 N  N   . HIS   B 1 65  ? 28.990 -33.691 8.715  1.00 16.42 ? 71  HIS   C N   1 
ATOM   1598 C  CA  . HIS   B 1 65  ? 29.281 -33.400 10.122 1.00 16.75 ? 71  HIS   C CA  1 
ATOM   1599 C  C   . HIS   B 1 65  ? 30.759 -33.679 10.290 1.00 18.32 ? 71  HIS   C C   1 
ATOM   1600 O  O   . HIS   B 1 65  ? 31.235 -34.743 9.868  1.00 21.63 ? 71  HIS   C O   1 
ATOM   1601 C  CB  . HIS   B 1 65  ? 28.457 -34.330 11.050 1.00 15.91 ? 71  HIS   C CB  1 
ATOM   1602 C  CG  . HIS   B 1 65  ? 26.986 -34.087 10.979 1.00 15.75 ? 71  HIS   C CG  1 
ATOM   1603 N  ND1 . HIS   B 1 65  ? 26.319 -33.344 11.948 1.00 18.22 ? 71  HIS   C ND1 1 
ATOM   1604 C  CD2 . HIS   B 1 65  ? 26.081 -34.557 10.093 1.00 17.42 ? 71  HIS   C CD2 1 
ATOM   1605 C  CE1 . HIS   B 1 65  ? 25.034 -33.395 11.622 1.00 18.12 ? 71  HIS   C CE1 1 
ATOM   1606 N  NE2 . HIS   B 1 65  ? 24.839 -34.086 10.507 1.00 19.79 ? 71  HIS   C NE2 1 
ATOM   1607 N  N   . TYR   B 1 66  ? 31.514 -32.727 10.867 1.00 15.52 ? 72  TYR   C N   1 
ATOM   1608 C  CA  . TYR   B 1 66  ? 32.950 -32.931 11.036 1.00 15.79 ? 72  TYR   C CA  1 
ATOM   1609 C  C   . TYR   B 1 66  ? 33.331 -33.002 12.504 1.00 14.78 ? 72  TYR   C C   1 
ATOM   1610 O  O   . TYR   B 1 66  ? 32.955 -32.097 13.268 1.00 15.25 ? 72  TYR   C O   1 
ATOM   1611 C  CB  . TYR   B 1 66  ? 33.710 -31.729 10.436 1.00 16.55 ? 72  TYR   C CB  1 
ATOM   1612 C  CG  . TYR   B 1 66  ? 33.657 -31.651 8.923  1.00 18.37 ? 72  TYR   C CG  1 
ATOM   1613 C  CD1 . TYR   B 1 66  ? 34.475 -32.447 8.141  1.00 19.73 ? 72  TYR   C CD1 1 
ATOM   1614 C  CD2 . TYR   B 1 66  ? 32.843 -30.724 8.278  1.00 19.87 ? 72  TYR   C CD2 1 
ATOM   1615 C  CE1 . TYR   B 1 66  ? 34.475 -32.334 6.748  1.00 21.10 ? 72  TYR   C CE1 1 
ATOM   1616 C  CE2 . TYR   B 1 66  ? 32.834 -30.603 6.885  1.00 20.97 ? 72  TYR   C CE2 1 
ATOM   1617 C  CZ  . TYR   B 1 66  ? 33.630 -31.431 6.125  1.00 22.43 ? 72  TYR   C CZ  1 
ATOM   1618 O  OH  . TYR   B 1 66  ? 33.616 -31.277 4.747  1.00 24.22 ? 72  TYR   C OH  1 
ATOM   1619 N  N   . PRO   B 1 67  ? 34.142 -34.002 12.898 1.00 14.67 ? 73  PRO   C N   1 
ATOM   1620 C  CA  . PRO   B 1 67  ? 34.689 -33.988 14.271 1.00 14.73 ? 73  PRO   C CA  1 
ATOM   1621 C  C   . PRO   B 1 67  ? 35.795 -32.912 14.344 1.00 15.29 ? 73  PRO   C C   1 
ATOM   1622 O  O   . PRO   B 1 67  ? 36.591 -32.781 13.395 1.00 17.49 ? 73  PRO   C O   1 
ATOM   1623 C  CB  . PRO   B 1 67  ? 35.306 -35.386 14.420 1.00 17.31 ? 73  PRO   C CB  1 
ATOM   1624 C  CG  . PRO   B 1 67  ? 35.616 -35.820 13.010 1.00 18.29 ? 73  PRO   C CG  1 
ATOM   1625 C  CD  . PRO   B 1 67  ? 34.668 -35.135 12.086 1.00 15.75 ? 73  PRO   C CD  1 
ATOM   1626 N  N   . VAL   B 1 68  ? 35.812 -32.112 15.407 1.00 13.84 ? 74  VAL   C N   1 
ATOM   1627 C  CA  . VAL   B 1 68  ? 36.778 -31.023 15.514 1.00 14.75 ? 74  VAL   C CA  1 
ATOM   1628 C  C   . VAL   B 1 68  ? 37.208 -30.824 16.949 1.00 14.40 ? 74  VAL   C C   1 
ATOM   1629 O  O   . VAL   B 1 68  ? 36.469 -31.130 17.891 1.00 14.96 ? 74  VAL   C O   1 
ATOM   1630 C  CB  . VAL   B 1 68  ? 36.164 -29.646 15.037 1.00 16.69 ? 74  VAL   C CB  1 
ATOM   1631 C  CG1 . VAL   B 1 68  ? 36.059 -29.532 13.516 1.00 18.99 ? 74  VAL   C CG1 1 
ATOM   1632 C  CG2 . VAL   B 1 68  ? 34.832 -29.345 15.716 1.00 16.38 ? 74  VAL   C CG2 1 
ATOM   1633 N  N   . SER   B 1 69  ? 38.433 -30.286 17.100 1.00 14.36 ? 75  SER   C N   1 
ATOM   1634 C  CA  . SER   B 1 69  ? 38.953 -29.726 18.340 1.00 14.60 ? 75  SER   C CA  1 
ATOM   1635 C  C   . SER   B 1 69  ? 38.679 -28.206 18.237 1.00 13.72 ? 75  SER   C C   1 
ATOM   1636 O  O   . SER   B 1 69  ? 38.813 -27.590 17.159 1.00 13.92 ? 75  SER   C O   1 
ATOM   1637 C  CB  . SER   B 1 69  ? 40.463 -29.955 18.422 1.00 17.03 ? 75  SER   C CB  1 
ATOM   1638 O  OG  . SER   B 1 69  ? 40.692 -31.342 18.602 1.00 21.38 ? 75  SER   C OG  1 
ATOM   1639 N  N   . PHE   B 1 70  ? 38.218 -27.593 19.343 1.00 13.39 ? 76  PHE   C N   1 
ATOM   1640 C  CA  . PHE   B 1 70  ? 37.894 -26.163 19.312 1.00 13.47 ? 76  PHE   C CA  1 
ATOM   1641 C  C   . PHE   B 1 70  ? 38.439 -25.447 20.549 1.00 14.72 ? 76  PHE   C C   1 
ATOM   1642 O  O   . PHE   B 1 70  ? 38.640 -26.070 21.594 1.00 14.79 ? 76  PHE   C O   1 
ATOM   1643 C  CB  . PHE   B 1 70  ? 36.392 -25.898 19.097 1.00 14.15 ? 76  PHE   C CB  1 
ATOM   1644 C  CG  . PHE   B 1 70  ? 35.525 -26.617 20.096 1.00 13.43 ? 76  PHE   C CG  1 
ATOM   1645 C  CD1 . PHE   B 1 70  ? 35.046 -27.892 19.832 1.00 13.24 ? 76  PHE   C CD1 1 
ATOM   1646 C  CD2 . PHE   B 1 70  ? 35.064 -25.960 21.230 1.00 13.69 ? 76  PHE   C CD2 1 
ATOM   1647 C  CE1 . PHE   B 1 70  ? 34.210 -28.530 20.738 1.00 13.88 ? 76  PHE   C CE1 1 
ATOM   1648 C  CE2 . PHE   B 1 70  ? 34.238 -26.600 22.136 1.00 13.94 ? 76  PHE   C CE2 1 
ATOM   1649 C  CZ  . PHE   B 1 70  ? 33.818 -27.870 21.895 1.00 14.04 ? 76  PHE   C CZ  1 
ATOM   1650 N  N   . SER   B 1 71  ? 38.746 -24.153 20.392 1.00 13.56 ? 77  SER   C N   1 
ATOM   1651 C  CA  . SER   B 1 71  ? 39.350 -23.363 21.476 1.00 14.35 ? 77  SER   C CA  1 
ATOM   1652 C  C   . SER   B 1 71  ? 38.350 -23.003 22.603 1.00 15.98 ? 77  SER   C C   1 
ATOM   1653 O  O   . SER   B 1 71  ? 37.154 -23.270 22.495 1.00 16.95 ? 77  SER   C O   1 
ATOM   1654 C  CB  . SER   B 1 71  ? 40.042 -22.127 20.905 1.00 15.76 ? 77  SER   C CB  1 
ATOM   1655 O  OG  . SER   B 1 71  ? 39.104 -21.232 20.319 1.00 16.67 ? 77  SER   C OG  1 
ATOM   1656 N  N   . LYS   B 1 72  ? 38.840 -22.380 23.682 1.00 15.32 ? 78  LYS   C N   1 
ATOM   1657 C  CA  . LYS   B 1 72  ? 37.954 -21.960 24.785 1.00 15.81 ? 78  LYS   C CA  1 
ATOM   1658 C  C   . LYS   B 1 72  ? 37.280 -20.628 24.407 1.00 15.30 ? 78  LYS   C C   1 
ATOM   1659 O  O   . LYS   B 1 72  ? 37.860 -19.822 23.668 1.00 15.91 ? 78  LYS   C O   1 
ATOM   1660 C  CB  . LYS   B 1 72  ? 38.788 -21.798 26.057 1.00 20.10 ? 78  LYS   C CB  1 
ATOM   1661 C  CG  . LYS   B 1 72  ? 39.370 -23.129 26.529 1.00 24.89 ? 78  LYS   C CG  1 
ATOM   1662 C  CD  . LYS   B 1 72  ? 39.721 -23.064 28.016 1.00 34.38 ? 78  LYS   C CD  1 
ATOM   1663 C  CE  . LYS   B 1 72  ? 40.287 -24.391 28.471 1.00 41.31 ? 78  LYS   C CE  1 
ATOM   1664 N  NZ  . LYS   B 1 72  ? 40.648 -24.343 29.918 1.00 44.86 ? 78  LYS   C NZ  1 
ATOM   1665 N  N   . PRO   B 1 73  ? 36.052 -20.366 24.896 1.00 15.09 ? 79  PRO   C N   1 
ATOM   1666 C  CA  . PRO   B 1 73  ? 35.344 -19.119 24.486 1.00 15.57 ? 79  PRO   C CA  1 
ATOM   1667 C  C   . PRO   B 1 73  ? 36.153 -17.877 24.866 1.00 16.84 ? 79  PRO   C C   1 
ATOM   1668 O  O   . PRO   B 1 73  ? 36.640 -17.765 25.999 1.00 17.97 ? 79  PRO   C O   1 
ATOM   1669 C  CB  . PRO   B 1 73  ? 34.031 -19.136 25.260 1.00 17.35 ? 79  PRO   C CB  1 
ATOM   1670 C  CG  . PRO   B 1 73  ? 33.909 -20.492 25.821 1.00 18.22 ? 79  PRO   C CG  1 
ATOM   1671 C  CD  . PRO   B 1 73  ? 35.250 -21.200 25.811 1.00 15.13 ? 79  PRO   C CD  1 
ATOM   1672 N  N   . SER   B 1 74  ? 36.373 -16.990 23.893 1.00 15.70 ? 80  SER   C N   1 
ATOM   1673 C  CA  . SER   B 1 74  ? 37.239 -15.835 24.139 1.00 17.02 ? 80  SER   C CA  1 
ATOM   1674 C  C   . SER   B 1 74  ? 36.880 -14.651 23.199 1.00 17.35 ? 80  SER   C C   1 
ATOM   1675 O  O   . SER   B 1 74  ? 35.959 -14.761 22.367 1.00 16.98 ? 80  SER   C O   1 
ATOM   1676 C  CB  . SER   B 1 74  ? 38.710 -16.255 24.004 1.00 21.59 ? 80  SER   C CB  1 
ATOM   1677 O  OG  . SER   B 1 74  ? 39.008 -16.548 22.652 1.00 27.14 ? 80  SER   C OG  1 
ATOM   1678 N  N   . LEU   B 1 75  ? 37.562 -13.502 23.393 1.00 18.25 ? 81  LEU   C N   1 
ATOM   1679 C  CA  . LEU   B 1 75  ? 37.387 -12.293 22.586 1.00 19.51 ? 81  LEU   C CA  1 
ATOM   1680 C  C   . LEU   B 1 75  ? 38.380 -12.403 21.429 1.00 20.00 ? 81  LEU   C C   1 
ATOM   1681 O  O   . LEU   B 1 75  ? 39.601 -12.427 21.653 1.00 20.47 ? 81  LEU   C O   1 
ATOM   1682 C  CB  . LEU   B 1 75  ? 37.724 -11.073 23.483 1.00 20.75 ? 81  LEU   C CB  1 
ATOM   1683 C  CG  . LEU   B 1 75  ? 37.408 -9.669  22.930 1.00 22.48 ? 81  LEU   C CG  1 
ATOM   1684 C  CD1 . LEU   B 1 75  ? 35.902 -9.474  22.694 1.00 22.53 ? 81  LEU   C CD1 1 
ATOM   1685 C  CD2 . LEU   B 1 75  ? 37.914 -8.601  23.923 1.00 24.34 ? 81  LEU   C CD2 1 
ATOM   1686 N  N   . ILE   B 1 76  ? 37.865 -12.582 20.211 1.00 18.80 ? 82  ILE   C N   1 
ATOM   1687 C  CA  . ILE   B 1 76  ? 38.685 -12.839 19.029 1.00 18.46 ? 82  ILE   C CA  1 
ATOM   1688 C  C   . ILE   B 1 76  ? 38.428 -11.770 17.962 1.00 18.79 ? 82  ILE   C C   1 
ATOM   1689 O  O   . ILE   B 1 76  ? 37.264 -11.431 17.720 1.00 18.45 ? 82  ILE   C O   1 
ATOM   1690 C  CB  . ILE   B 1 76  ? 38.269 -14.235 18.462 1.00 20.12 ? 82  ILE   C CB  1 
ATOM   1691 C  CG1 . ILE   B 1 76  ? 38.542 -15.416 19.456 1.00 22.75 ? 82  ILE   C CG1 1 
ATOM   1692 C  CG2 . ILE   B 1 76  ? 38.916 -14.505 17.077 1.00 20.90 ? 82  ILE   C CG2 1 
ATOM   1693 C  CD1 . ILE   B 1 76  ? 39.944 -15.876 19.516 1.00 25.62 ? 82  ILE   C CD1 1 
ATOM   1694 N  N   . PHE   B 1 77  ? 39.483 -11.269 17.304 1.00 18.31 ? 83  PHE   C N   1 
ATOM   1695 C  CA  . PHE   B 1 77  ? 39.299 -10.337 16.204 1.00 19.31 ? 83  PHE   C CA  1 
ATOM   1696 C  C   . PHE   B 1 77  ? 38.824 -11.156 14.989 1.00 19.78 ? 83  PHE   C C   1 
ATOM   1697 O  O   . PHE   B 1 77  ? 39.452 -12.154 14.597 1.00 21.06 ? 83  PHE   C O   1 
ATOM   1698 C  CB  . PHE   B 1 77  ? 40.598 -9.591  15.868 1.00 19.68 ? 83  PHE   C CB  1 
ATOM   1699 C  CG  . PHE   B 1 77  ? 40.329 -8.471  14.884 1.00 20.67 ? 83  PHE   C CG  1 
ATOM   1700 C  CD1 . PHE   B 1 77  ? 39.666 -7.330  15.284 1.00 21.70 ? 83  PHE   C CD1 1 
ATOM   1701 C  CD2 . PHE   B 1 77  ? 40.691 -8.595  13.539 1.00 22.21 ? 83  PHE   C CD2 1 
ATOM   1702 C  CE1 . PHE   B 1 77  ? 39.398 -6.308  14.369 1.00 23.11 ? 83  PHE   C CE1 1 
ATOM   1703 C  CE2 . PHE   B 1 77  ? 40.413 -7.576  12.630 1.00 23.01 ? 83  PHE   C CE2 1 
ATOM   1704 C  CZ  . PHE   B 1 77  ? 39.781 -6.443  13.053 1.00 23.15 ? 83  PHE   C CZ  1 
ATOM   1705 N  N   . VAL   B 1 78  ? 37.705 -10.727 14.390 1.00 17.36 ? 84  VAL   C N   1 
ATOM   1706 C  CA  . VAL   B 1 78  ? 37.149 -11.418 13.238 1.00 17.59 ? 84  VAL   C CA  1 
ATOM   1707 C  C   . VAL   B 1 78  ? 37.228 -10.482 12.024 1.00 17.35 ? 84  VAL   C C   1 
ATOM   1708 O  O   . VAL   B 1 78  ? 36.770 -9.337  12.104 1.00 17.95 ? 84  VAL   C O   1 
ATOM   1709 C  CB  . VAL   B 1 78  ? 35.684 -11.838 13.517 1.00 18.75 ? 84  VAL   C CB  1 
ATOM   1710 C  CG1 . VAL   B 1 78  ? 35.110 -12.583 12.320 1.00 19.50 ? 84  VAL   C CG1 1 
ATOM   1711 C  CG2 . VAL   B 1 78  ? 35.576 -12.680 14.781 1.00 19.58 ? 84  VAL   C CG2 1 
ATOM   1712 N  N   . GLU   B 1 79  ? 37.755 -10.970 10.892 1.00 15.74 ? 85  GLU   C N   1 
ATOM   1713 C  CA  . GLU   B 1 79  ? 37.812 -10.152 9.669  1.00 17.35 ? 85  GLU   C CA  1 
ATOM   1714 C  C   . GLU   B 1 79  ? 36.392 -9.866  9.128  1.00 17.57 ? 85  GLU   C C   1 
ATOM   1715 O  O   . GLU   B 1 79  ? 35.429 -10.550 9.474  1.00 17.18 ? 85  GLU   C O   1 
ATOM   1716 C  CB  . GLU   B 1 79  ? 38.655 -10.835 8.561  1.00 19.64 ? 85  GLU   C CB  1 
ATOM   1717 C  CG  . GLU   B 1 79  ? 40.161 -10.815 8.813  1.00 23.11 ? 85  GLU   C CG  1 
ATOM   1718 C  CD  . GLU   B 1 79  ? 40.796 -9.455  9.020  1.00 33.67 ? 85  GLU   C CD  1 
ATOM   1719 O  OE1 . GLU   B 1 79  ? 40.481 -8.501  8.269  1.00 38.00 ? 85  GLU   C OE1 1 
ATOM   1720 O  OE2 . GLU   B 1 79  ? 41.579 -9.335  9.988  1.00 33.96 ? 85  GLU   C OE2 1 
ATOM   1721 N  N   . ALA   B 1 80  ? 36.252 -8.848  8.272  1.00 18.85 ? 86  ALA   C N   1 
ATOM   1722 C  CA  . ALA   B 1 80  ? 34.967 -8.497  7.686  1.00 19.11 ? 86  ALA   C CA  1 
ATOM   1723 C  C   . ALA   B 1 80  ? 34.318 -9.685  6.980  1.00 19.23 ? 86  ALA   C C   1 
ATOM   1724 O  O   . ALA   B 1 80  ? 35.012 -10.489 6.334  1.00 19.99 ? 86  ALA   C O   1 
ATOM   1725 C  CB  . ALA   B 1 80  ? 35.160 -7.338  6.691  1.00 19.30 ? 86  ALA   C CB  1 
ATOM   1726 N  N   . SER   B 1 81  ? 33.018 -9.823  7.178  1.00 19.15 ? 87  SER   C N   1 
ATOM   1727 C  CA  . SER   B 1 81  ? 32.260 -10.867 6.511  1.00 20.17 ? 87  SER   C CA  1 
ATOM   1728 C  C   . SER   B 1 81  ? 31.126 -10.179 5.707  1.00 21.89 ? 87  SER   C C   1 
ATOM   1729 O  O   . SER   B 1 81  ? 31.022 -8.934  5.715  1.00 22.52 ? 87  SER   C O   1 
ATOM   1730 C  CB  . SER   B 1 81  ? 31.678 -11.827 7.546  1.00 19.29 ? 87  SER   C CB  1 
ATOM   1731 O  OG  . SER   B 1 81  ? 30.696 -11.119 8.280  1.00 18.94 ? 87  SER   C OG  1 
ATOM   1732 N  N   . GLU   B 1 82  ? 30.258 -10.963 5.034  1.00 23.24 ? 88  GLU   C N   1 
ATOM   1733 C  CA  . GLU   B 1 82  ? 29.174 -10.307 4.294  1.00 23.90 ? 88  GLU   C CA  1 
ATOM   1734 C  C   . GLU   B 1 82  ? 28.107 -9.694  5.240  1.00 23.66 ? 88  GLU   C C   1 
ATOM   1735 O  O   . GLU   B 1 82  ? 27.304 -8.869  4.800  1.00 25.78 ? 88  GLU   C O   1 
ATOM   1736 C  CB  . GLU   B 1 82  ? 28.570 -11.219 3.214  1.00 28.04 ? 88  GLU   C CB  1 
ATOM   1737 C  CG  . GLU   B 1 82  ? 27.793 -12.417 3.708  1.00 35.83 ? 88  GLU   C CG  1 
ATOM   1738 C  CD  . GLU   B 1 82  ? 27.257 -13.249 2.553  1.00 42.21 ? 88  GLU   C CD  1 
ATOM   1739 O  OE1 . GLU   B 1 82  ? 27.964 -13.352 1.523  1.00 41.26 ? 88  GLU   C OE1 1 
ATOM   1740 O  OE2 . GLU   B 1 82  ? 26.133 -13.791 2.676  1.00 45.23 ? 88  GLU   C OE2 1 
ATOM   1741 N  N   . TYR   B 1 83  ? 28.140 -10.028 6.545  1.00 20.44 ? 89  TYR   C N   1 
ATOM   1742 C  CA  . TYR   B 1 83  ? 27.123 -9.555  7.484  1.00 20.55 ? 89  TYR   C CA  1 
ATOM   1743 C  C   . TYR   B 1 83  ? 27.653 -8.666  8.649  1.00 20.30 ? 89  TYR   C C   1 
ATOM   1744 O  O   . TYR   B 1 83  ? 26.823 -8.059  9.348  1.00 22.00 ? 89  TYR   C O   1 
ATOM   1745 C  CB  . TYR   B 1 83  ? 26.292 -10.748 8.026  1.00 20.21 ? 89  TYR   C CB  1 
ATOM   1746 C  CG  . TYR   B 1 83  ? 27.126 -11.962 8.420  1.00 20.56 ? 89  TYR   C CG  1 
ATOM   1747 C  CD1 . TYR   B 1 83  ? 27.486 -12.928 7.478  1.00 21.33 ? 89  TYR   C CD1 1 
ATOM   1748 C  CD2 . TYR   B 1 83  ? 27.598 -12.112 9.714  1.00 20.16 ? 89  TYR   C CD2 1 
ATOM   1749 C  CE1 . TYR   B 1 83  ? 28.315 -13.995 7.819  1.00 21.51 ? 89  TYR   C CE1 1 
ATOM   1750 C  CE2 . TYR   B 1 83  ? 28.383 -13.200 10.079 1.00 21.29 ? 89  TYR   C CE2 1 
ATOM   1751 C  CZ  . TYR   B 1 83  ? 28.742 -14.141 9.131  1.00 22.17 ? 89  TYR   C CZ  1 
ATOM   1752 O  OH  . TYR   B 1 83  ? 29.539 -15.203 9.517  1.00 22.45 ? 89  TYR   C OH  1 
ATOM   1753 N  N   . TYR   B 1 84  ? 28.991 -8.592  8.895  1.00 18.17 ? 90  TYR   C N   1 
ATOM   1754 C  CA  . TYR   B 1 84  ? 29.551 -7.683  9.906  1.00 17.80 ? 90  TYR   C CA  1 
ATOM   1755 C  C   . TYR   B 1 84  ? 30.858 -7.083  9.349  1.00 18.18 ? 90  TYR   C C   1 
ATOM   1756 O  O   . TYR   B 1 84  ? 31.606 -7.765  8.622  1.00 18.43 ? 90  TYR   C O   1 
ATOM   1757 C  CB  . TYR   B 1 84  ? 29.935 -8.436  11.236 1.00 16.75 ? 90  TYR   C CB  1 
ATOM   1758 C  CG  . TYR   B 1 84  ? 28.764 -8.861  12.104 1.00 15.90 ? 90  TYR   C CG  1 
ATOM   1759 C  CD1 . TYR   B 1 84  ? 27.894 -7.920  12.667 1.00 16.26 ? 90  TYR   C CD1 1 
ATOM   1760 C  CD2 . TYR   B 1 84  ? 28.549 -10.184 12.403 1.00 15.61 ? 90  TYR   C CD2 1 
ATOM   1761 C  CE1 . TYR   B 1 84  ? 26.828 -8.310  13.489 1.00 16.33 ? 90  TYR   C CE1 1 
ATOM   1762 C  CE2 . TYR   B 1 84  ? 27.470 -10.588 13.188 1.00 15.33 ? 90  TYR   C CE2 1 
ATOM   1763 C  CZ  . TYR   B 1 84  ? 26.621 -9.650  13.776 1.00 16.56 ? 90  TYR   C CZ  1 
ATOM   1764 O  OH  . TYR   B 1 84  ? 25.568 -10.075 14.600 1.00 17.37 ? 90  TYR   C OH  1 
ATOM   1765 N  N   . PRO   B 1 85  ? 31.235 -5.897  9.841  1.00 18.42 ? 91  PRO   C N   1 
ATOM   1766 C  CA  . PRO   B 1 85  ? 32.575 -5.381  9.530  1.00 18.45 ? 91  PRO   C CA  1 
ATOM   1767 C  C   . PRO   B 1 85  ? 33.641 -6.147  10.358 1.00 18.56 ? 91  PRO   C C   1 
ATOM   1768 O  O   . PRO   B 1 85  ? 33.315 -6.969  11.250 1.00 18.19 ? 91  PRO   C O   1 
ATOM   1769 C  CB  . PRO   B 1 85  ? 32.486 -3.926  10.003 1.00 19.52 ? 91  PRO   C CB  1 
ATOM   1770 C  CG  . PRO   B 1 85  ? 31.532 -3.984  11.188 1.00 19.89 ? 91  PRO   C CG  1 
ATOM   1771 C  CD  . PRO   B 1 85  ? 30.488 -4.999  10.760 1.00 18.42 ? 91  PRO   C CD  1 
ATOM   1772 N  N   . ALA   B 1 86  ? 34.933 -5.836  10.124 1.00 18.61 ? 92  ALA   C N   1 
ATOM   1773 C  CA  . ALA   B 1 86  ? 36.041 -6.407  10.919 1.00 19.03 ? 92  ALA   C CA  1 
ATOM   1774 C  C   . ALA   B 1 86  ? 35.864 -5.872  12.348 1.00 19.99 ? 92  ALA   C C   1 
ATOM   1775 O  O   . ALA   B 1 86  ? 35.662 -4.664  12.515 1.00 21.88 ? 92  ALA   C O   1 
ATOM   1776 C  CB  . ALA   B 1 86  ? 37.386 -5.958  10.359 1.00 19.00 ? 92  ALA   C CB  1 
ATOM   1777 N  N   . ARG   B 1 87  ? 35.827 -6.766  13.343 1.00 18.21 ? 93  ARG   C N   1 
ATOM   1778 C  CA  . ARG   B 1 87  ? 35.545 -6.349  14.710 1.00 18.49 ? 93  ARG   C CA  1 
ATOM   1779 C  C   . ARG   B 1 87  ? 35.953 -7.447  15.697 1.00 18.46 ? 93  ARG   C C   1 
ATOM   1780 O  O   . ARG   B 1 87  ? 36.245 -8.575  15.283 1.00 17.94 ? 93  ARG   C O   1 
ATOM   1781 C  CB  . ARG   B 1 87  ? 34.023 -6.060  14.851 1.00 19.46 ? 93  ARG   C CB  1 
ATOM   1782 C  CG  . ARG   B 1 87  ? 33.193 -7.343  14.871 1.00 18.63 ? 93  ARG   C CG  1 
ATOM   1783 C  CD  . ARG   B 1 87  ? 31.686 -7.109  14.739 1.00 19.63 ? 93  ARG   C CD  1 
ATOM   1784 N  NE  . ARG   B 1 87  ? 31.012 -8.374  15.010 1.00 19.14 ? 93  ARG   C NE  1 
ATOM   1785 C  CZ  . ARG   B 1 87  ? 29.987 -8.576  15.819 1.00 21.05 ? 93  ARG   C CZ  1 
ATOM   1786 N  NH1 . ARG   B 1 87  ? 29.386 -7.546  16.422 1.00 20.22 ? 93  ARG   C NH1 1 
ATOM   1787 N  NH2 . ARG   B 1 87  ? 29.530 -9.811  16.024 1.00 21.18 ? 93  ARG   C NH2 1 
ATOM   1788 N  N   . TYR   B 1 88  ? 35.949 -7.141  16.999 1.00 18.88 ? 94  TYR   C N   1 
ATOM   1789 C  CA  . TYR   B 1 88  ? 36.136 -8.185  18.001 1.00 20.42 ? 94  TYR   C CA  1 
ATOM   1790 C  C   . TYR   B 1 88  ? 34.772 -8.819  18.247 1.00 18.82 ? 94  TYR   C C   1 
ATOM   1791 O  O   . TYR   B 1 88  ? 33.755 -8.120  18.368 1.00 19.60 ? 94  TYR   C O   1 
ATOM   1792 C  CB  . TYR   B 1 88  ? 36.592 -7.592  19.351 1.00 22.28 ? 94  TYR   C CB  1 
ATOM   1793 C  CG  . TYR   B 1 88  ? 38.045 -7.220  19.306 1.00 25.52 ? 94  TYR   C CG  1 
ATOM   1794 C  CD1 . TYR   B 1 88  ? 39.028 -8.167  19.535 1.00 27.43 ? 94  TYR   C CD1 1 
ATOM   1795 C  CD2 . TYR   B 1 88  ? 38.437 -5.937  18.956 1.00 27.66 ? 94  TYR   C CD2 1 
ATOM   1796 C  CE1 . TYR   B 1 88  ? 40.371 -7.847  19.411 1.00 29.23 ? 94  TYR   C CE1 1 
ATOM   1797 C  CE2 . TYR   B 1 88  ? 39.771 -5.597  18.860 1.00 29.58 ? 94  TYR   C CE2 1 
ATOM   1798 C  CZ  . TYR   B 1 88  ? 40.732 -6.553  19.096 1.00 31.16 ? 94  TYR   C CZ  1 
ATOM   1799 O  OH  . TYR   B 1 88  ? 42.034 -6.196  18.953 1.00 35.36 ? 94  TYR   C OH  1 
ATOM   1800 N  N   . GLN   B 1 89  ? 34.749 -10.151 18.370 1.00 17.25 ? 95  GLN   C N   1 
ATOM   1801 C  CA  . GLN   B 1 89  ? 33.505 -10.844 18.746 1.00 16.66 ? 95  GLN   C CA  1 
ATOM   1802 C  C   . GLN   B 1 89  ? 33.831 -11.612 20.047 1.00 17.08 ? 95  GLN   C C   1 
ATOM   1803 O  O   . GLN   B 1 89  ? 34.908 -12.228 20.163 1.00 18.10 ? 95  GLN   C O   1 
ATOM   1804 C  CB  . GLN   B 1 89  ? 33.050 -11.808 17.631 1.00 17.71 ? 95  GLN   C CB  1 
ATOM   1805 C  CG  . GLN   B 1 89  ? 31.782 -12.572 17.965 1.00 19.25 ? 95  GLN   C CG  1 
ATOM   1806 C  CD  . GLN   B 1 89  ? 31.086 -13.149 16.745 1.00 18.87 ? 95  GLN   C CD  1 
ATOM   1807 O  OE1 . GLN   B 1 89  ? 31.020 -12.518 15.657 1.00 19.32 ? 95  GLN   C OE1 1 
ATOM   1808 N  NE2 . GLN   B 1 89  ? 30.534 -14.341 16.923 1.00 18.10 ? 95  GLN   C NE2 1 
ATOM   1809 N  N   . SER   B 1 90  ? 32.906 -11.570 21.007 1.00 15.26 ? 96  SER   C N   1 
ATOM   1810 C  CA  . SER   B 1 90  ? 33.147 -12.219 22.284 1.00 16.06 ? 96  SER   C CA  1 
ATOM   1811 C  C   . SER   B 1 90  ? 32.520 -13.645 22.380 1.00 16.06 ? 96  SER   C C   1 
ATOM   1812 O  O   . SER   B 1 90  ? 31.649 -13.974 21.572 1.00 15.86 ? 96  SER   C O   1 
ATOM   1813 C  CB  . SER   B 1 90  ? 32.643 -11.321 23.419 1.00 17.92 ? 96  SER   C CB  1 
ATOM   1814 O  OG  . SER   B 1 90  ? 31.232 -11.188 23.352 1.00 18.44 ? 96  SER   C OG  1 
ATOM   1815 N  N   . HIS   B 1 91  ? 32.961 -14.465 23.390 1.00 15.12 ? 97  HIS   C N   1 
ATOM   1816 C  CA  . HIS   B 1 91  ? 32.461 -15.824 23.634 1.00 15.23 ? 97  HIS   C CA  1 
ATOM   1817 C  C   . HIS   B 1 91  ? 32.537 -16.682 22.355 1.00 14.74 ? 97  HIS   C C   1 
ATOM   1818 O  O   . HIS   B 1 91  ? 31.650 -17.510 22.096 1.00 15.44 ? 97  HIS   C O   1 
ATOM   1819 C  CB  . HIS   B 1 91  ? 31.024 -15.789 24.207 1.00 16.79 ? 97  HIS   C CB  1 
ATOM   1820 C  CG  . HIS   B 1 91  ? 30.927 -15.026 25.513 1.00 19.13 ? 97  HIS   C CG  1 
ATOM   1821 N  ND1 . HIS   B 1 91  ? 30.994 -15.674 26.737 1.00 20.60 ? 97  HIS   C ND1 1 
ATOM   1822 C  CD2 . HIS   B 1 91  ? 30.781 -13.688 25.733 1.00 20.64 ? 97  HIS   C CD2 1 
ATOM   1823 C  CE1 . HIS   B 1 91  ? 30.856 -14.722 27.660 1.00 21.32 ? 97  HIS   C CE1 1 
ATOM   1824 N  NE2 . HIS   B 1 91  ? 30.718 -13.509 27.098 1.00 21.30 ? 97  HIS   C NE2 1 
ATOM   1825 N  N   . LEU   B 1 92  ? 33.606 -16.482 21.576 1.00 14.23 ? 98  LEU   C N   1 
ATOM   1826 C  CA  . LEU   B 1 92  ? 33.818 -17.188 20.315 1.00 14.45 ? 98  LEU   C CA  1 
ATOM   1827 C  C   . LEU   B 1 92  ? 34.887 -18.278 20.472 1.00 14.38 ? 98  LEU   C C   1 
ATOM   1828 O  O   . LEU   B 1 92  ? 35.881 -18.096 21.201 1.00 15.18 ? 98  LEU   C O   1 
ATOM   1829 C  CB  . LEU   B 1 92  ? 34.254 -16.176 19.229 1.00 14.89 ? 98  LEU   C CB  1 
ATOM   1830 C  CG  . LEU   B 1 92  ? 34.359 -16.700 17.797 1.00 16.81 ? 98  LEU   C CG  1 
ATOM   1831 C  CD1 . LEU   B 1 92  ? 33.000 -17.102 17.225 1.00 17.81 ? 98  LEU   C CD1 1 
ATOM   1832 C  CD2 . LEU   B 1 92  ? 35.008 -15.654 16.844 1.00 16.92 ? 98  LEU   C CD2 1 
ATOM   1833 N  N   . MET   B 1 93  ? 34.658 -19.436 19.831 1.00 13.46 ? 99  MET   C N   1 
ATOM   1834 C  CA  . MET   B 1 93  ? 35.594 -20.576 19.856 1.00 12.68 ? 99  MET   C CA  1 
ATOM   1835 C  C   . MET   B 1 93  ? 35.980 -20.894 18.412 1.00 13.69 ? 99  MET   C C   1 
ATOM   1836 O  O   . MET   B 1 93  ? 35.095 -20.933 17.556 1.00 14.06 ? 99  MET   C O   1 
ATOM   1837 C  CB  . MET   B 1 93  ? 34.888 -21.813 20.470 1.00 14.28 ? 99  MET   C CB  1 
ATOM   1838 C  CG  . MET   B 1 93  ? 34.411 -21.511 21.874 1.00 15.76 ? 99  MET   C CG  1 
ATOM   1839 S  SD  . MET   B 1 93  ? 33.383 -22.839 22.514 1.00 17.97 ? 99  MET   C SD  1 
ATOM   1840 C  CE  . MET   B 1 93  ? 31.994 -22.771 21.479 1.00 17.93 ? 99  MET   C CE  1 
ATOM   1841 N  N   . LEU   B 1 94  ? 37.233 -21.175 18.143 1.00 13.05 ? 100 LEU   C N   1 
ATOM   1842 C  CA  . LEU   B 1 94  ? 37.676 -21.451 16.782 1.00 14.35 ? 100 LEU   C CA  1 
ATOM   1843 C  C   . LEU   B 1 94  ? 38.104 -22.902 16.613 1.00 14.58 ? 100 LEU   C C   1 
ATOM   1844 O  O   . LEU   B 1 94  ? 38.614 -23.516 17.534 1.00 14.74 ? 100 LEU   C O   1 
ATOM   1845 C  CB  . LEU   B 1 94  ? 38.910 -20.579 16.417 1.00 15.86 ? 100 LEU   C CB  1 
ATOM   1846 C  CG  . LEU   B 1 94  ? 38.751 -19.095 16.365 1.00 17.06 ? 100 LEU   C CG  1 
ATOM   1847 C  CD1 . LEU   B 1 94  ? 40.078 -18.438 15.961 1.00 19.28 ? 100 LEU   C CD1 1 
ATOM   1848 C  CD2 . LEU   B 1 94  ? 37.617 -18.679 15.411 1.00 18.65 ? 100 LEU   C CD2 1 
ATOM   1849 N  N   . ALA   B 1 95  ? 37.903 -23.437 15.389 1.00 13.93 ? 101 ALA   C N   1 
ATOM   1850 C  CA  . ALA   B 1 95  ? 38.408 -24.756 14.993 1.00 13.83 ? 101 ALA   C CA  1 
ATOM   1851 C  C   . ALA   B 1 95  ? 38.956 -24.652 13.564 1.00 14.21 ? 101 ALA   C C   1 
ATOM   1852 O  O   . ALA   B 1 95  ? 38.599 -23.729 12.832 1.00 14.83 ? 101 ALA   C O   1 
ATOM   1853 C  CB  . ALA   B 1 95  ? 37.282 -25.804 15.035 1.00 14.15 ? 101 ALA   C CB  1 
ATOM   1854 N  N   . VAL   B 1 96  ? 39.797 -25.608 13.142 1.00 13.40 ? 102 VAL   C N   1 
ATOM   1855 C  CA  . VAL   B 1 96  ? 40.264 -25.663 11.753 1.00 15.14 ? 102 VAL   C CA  1 
ATOM   1856 C  C   . VAL   B 1 96  ? 39.185 -26.397 10.980 1.00 16.66 ? 102 VAL   C C   1 
ATOM   1857 O  O   . VAL   B 1 96  ? 38.875 -27.550 11.301 1.00 17.12 ? 102 VAL   C O   1 
ATOM   1858 C  CB  . VAL   B 1 96  ? 41.599 -26.431 11.708 1.00 17.29 ? 102 VAL   C CB  1 
ATOM   1859 C  CG1 . VAL   B 1 96  ? 42.044 -26.636 10.249 1.00 18.69 ? 102 VAL   C CG1 1 
ATOM   1860 C  CG2 . VAL   B 1 96  ? 42.654 -25.666 12.490 1.00 18.02 ? 102 VAL   C CG2 1 
ATOM   1861 N  N   . GLY   B 1 97  ? 38.558 -25.713 10.036 1.00 18.90 ? 103 GLY   C N   1 
ATOM   1862 C  CA  . GLY   B 1 97  ? 37.476 -26.328 9.282  1.00 19.47 ? 103 GLY   C CA  1 
ATOM   1863 C  C   . GLY   B 1 97  ? 36.823 -25.373 8.328  1.00 20.29 ? 103 GLY   C C   1 
ATOM   1864 O  O   . GLY   B 1 97  ? 37.094 -24.166 8.354  1.00 21.15 ? 103 GLY   C O   1 
ATOM   1865 N  N   . HIS   B 1 98  ? 35.931 -25.913 7.502  1.00 19.77 ? 104 HIS   C N   1 
ATOM   1866 C  CA  . HIS   B 1 98  ? 35.267 -25.119 6.490  1.00 20.24 ? 104 HIS   C CA  1 
ATOM   1867 C  C   . HIS   B 1 98  ? 34.017 -24.401 7.036  1.00 19.14 ? 104 HIS   C C   1 
ATOM   1868 O  O   . HIS   B 1 98  ? 33.230 -25.004 7.795  1.00 18.78 ? 104 HIS   C O   1 
ATOM   1869 C  CB  . HIS   B 1 98  ? 34.877 -26.027 5.322  1.00 22.78 ? 104 HIS   C CB  1 
ATOM   1870 C  CG  . HIS   B 1 98  ? 34.344 -25.253 4.181  1.00 29.03 ? 104 HIS   C CG  1 
ATOM   1871 N  ND1 . HIS   B 1 98  ? 35.136 -24.341 3.492  1.00 30.93 ? 104 HIS   C ND1 1 
ATOM   1872 C  CD2 . HIS   B 1 98  ? 33.094 -25.247 3.663  1.00 31.21 ? 104 HIS   C CD2 1 
ATOM   1873 C  CE1 . HIS   B 1 98  ? 34.346 -23.810 2.577  1.00 32.80 ? 104 HIS   C CE1 1 
ATOM   1874 N  NE2 . HIS   B 1 98  ? 33.104 -24.337 2.631  1.00 32.71 ? 104 HIS   C NE2 1 
ATOM   1875 N  N   . SER   B 1 99  ? 33.808 -23.109 6.635  1.00 18.74 ? 105 SER   C N   1 
ATOM   1876 C  CA  . SER   B 1 99  ? 32.630 -22.306 7.034  1.00 18.72 ? 105 SER   C CA  1 
ATOM   1877 C  C   . SER   B 1 99  ? 32.359 -21.158 6.026  1.00 20.33 ? 105 SER   C C   1 
ATOM   1878 O  O   . SER   B 1 99  ? 33.162 -20.222 5.934  1.00 22.04 ? 105 SER   C O   1 
ATOM   1879 C  CB  . SER   B 1 99  ? 32.853 -21.707 8.428  1.00 19.44 ? 105 SER   C CB  1 
ATOM   1880 O  OG  . SER   B 1 99  ? 31.833 -20.808 8.853  1.00 21.94 ? 105 SER   C OG  1 
ATOM   1881 N  N   . GLU   B 1 100 ? 31.236 -21.241 5.281  1.00 20.15 ? 106 GLU   C N   1 
ATOM   1882 C  CA  . GLU   B 1 100 ? 30.787 -20.183 4.349  1.00 19.71 ? 106 GLU   C CA  1 
ATOM   1883 C  C   . GLU   B 1 100 ? 29.685 -19.405 5.110  1.00 18.57 ? 106 GLU   C C   1 
ATOM   1884 O  O   . GLU   B 1 100 ? 29.099 -19.924 6.079  1.00 17.94 ? 106 GLU   C O   1 
ATOM   1885 C  CB  . GLU   B 1 100 ? 30.155 -20.803 3.066  1.00 23.34 ? 106 GLU   C CB  1 
ATOM   1886 C  CG  . GLU   B 1 100 ? 30.932 -21.865 2.329  1.00 30.38 ? 106 GLU   C CG  1 
ATOM   1887 C  CD  . GLU   B 1 100 ? 31.774 -21.447 1.159  1.00 35.88 ? 106 GLU   C CD  1 
ATOM   1888 O  OE1 . GLU   B 1 100 ? 31.940 -20.220 0.972  1.00 39.84 ? 106 GLU   C OE1 1 
ATOM   1889 O  OE2 . GLU   B 1 100 ? 32.331 -22.340 0.488  1.00 37.25 ? 106 GLU   C OE2 1 
ATOM   1890 N  N   . PRO   B 1 101 ? 29.301 -18.210 4.646  1.00 19.16 ? 107 PRO   C N   1 
ATOM   1891 C  CA  . PRO   B 1 101 ? 28.235 -17.464 5.347  1.00 19.45 ? 107 PRO   C CA  1 
ATOM   1892 C  C   . PRO   B 1 101 ? 26.949 -18.265 5.584  1.00 19.12 ? 107 PRO   C C   1 
ATOM   1893 O  O   . PRO   B 1 101 ? 26.364 -18.168 6.661  1.00 19.59 ? 107 PRO   C O   1 
ATOM   1894 C  CB  . PRO   B 1 101 ? 27.976 -16.253 4.421  1.00 21.82 ? 107 PRO   C CB  1 
ATOM   1895 C  CG  . PRO   B 1 101 ? 29.214 -16.100 3.625  1.00 22.80 ? 107 PRO   C CG  1 
ATOM   1896 C  CD  . PRO   B 1 101 ? 29.901 -17.426 3.533  1.00 20.06 ? 107 PRO   C CD  1 
ATOM   1897 N  N   . GLY   B 1 102 ? 26.534 -19.096 4.621  1.00 17.73 ? 108 GLY   C N   1 
ATOM   1898 C  CA  . GLY   B 1 102 ? 25.320 -19.902 4.756  1.00 17.88 ? 108 GLY   C CA  1 
ATOM   1899 C  C   . GLY   B 1 102 ? 25.395 -21.014 5.796  1.00 17.43 ? 108 GLY   C C   1 
ATOM   1900 O  O   . GLY   B 1 102 ? 24.384 -21.625 6.144  1.00 18.70 ? 108 GLY   C O   1 
ATOM   1901 N  N   . ASP   B 1 103 ? 26.609 -21.313 6.274  1.00 16.16 ? 109 ASP   C N   1 
ATOM   1902 C  CA  . ASP   B 1 103 ? 26.795 -22.329 7.305  1.00 15.55 ? 109 ASP   C CA  1 
ATOM   1903 C  C   . ASP   B 1 103 ? 26.423 -21.824 8.704  1.00 15.92 ? 109 ASP   C C   1 
ATOM   1904 O  O   . ASP   B 1 103 ? 26.312 -22.641 9.626  1.00 16.22 ? 109 ASP   C O   1 
ATOM   1905 C  CB  . ASP   B 1 103 ? 28.246 -22.855 7.325  1.00 17.00 ? 109 ASP   C CB  1 
ATOM   1906 C  CG  . ASP   B 1 103 ? 28.543 -23.658 6.089  1.00 18.63 ? 109 ASP   C CG  1 
ATOM   1907 O  OD1 . ASP   B 1 103 ? 27.671 -24.398 5.649  1.00 18.88 ? 109 ASP   C OD1 1 
ATOM   1908 O  OD2 . ASP   B 1 103 ? 29.661 -23.553 5.560  1.00 18.82 ? 109 ASP   C OD2 1 
ATOM   1909 N  N   . CYS   B 1 104 ? 26.203 -20.478 8.894  1.00 15.42 ? 110 CYS   C N   1 
ATOM   1910 C  CA  . CYS   B 1 104 ? 25.854 -19.950 10.223 1.00 16.11 ? 110 CYS   C CA  1 
ATOM   1911 C  C   . CYS   B 1 104 ? 24.604 -20.624 10.740 1.00 16.78 ? 110 CYS   C C   1 
ATOM   1912 O  O   . CYS   B 1 104 ? 23.659 -20.851 9.975  1.00 17.95 ? 110 CYS   C O   1 
ATOM   1913 C  CB  . CYS   B 1 104 ? 25.681 -18.437 10.182 1.00 17.08 ? 110 CYS   C CB  1 
ATOM   1914 S  SG  . CYS   B 1 104 ? 27.231 -17.516 10.037 1.00 18.97 ? 110 CYS   C SG  1 
ATOM   1915 N  N   . GLY   B 1 105 ? 24.628 -20.979 12.004 1.00 13.96 ? 111 GLY   C N   1 
ATOM   1916 C  CA  . GLY   B 1 105 ? 23.493 -21.653 12.610 1.00 15.59 ? 111 GLY   C CA  1 
ATOM   1917 C  C   . GLY   B 1 105 ? 23.677 -23.153 12.784 1.00 15.49 ? 111 GLY   C C   1 
ATOM   1918 O  O   . GLY   B 1 105 ? 22.893 -23.777 13.509 1.00 16.12 ? 111 GLY   C O   1 
ATOM   1919 N  N   . GLY   B 1 106 ? 24.665 -23.740 12.091 1.00 15.29 ? 112 GLY   C N   1 
ATOM   1920 C  CA  . GLY   B 1 106 ? 25.000 -25.166 12.224 1.00 14.86 ? 112 GLY   C CA  1 
ATOM   1921 C  C   . GLY   B 1 106 ? 25.408 -25.477 13.657 1.00 14.52 ? 112 GLY   C C   1 
ATOM   1922 O  O   . GLY   B 1 106 ? 26.122 -24.680 14.295 1.00 14.14 ? 112 GLY   C O   1 
ATOM   1923 N  N   . ILE   B 1 107 ? 24.886 -26.583 14.216 1.00 14.32 ? 113 ILE   C N   1 
ATOM   1924 C  CA  . ILE   B 1 107 ? 25.175 -26.910 15.605 1.00 14.16 ? 113 ILE   C CA  1 
ATOM   1925 C  C   . ILE   B 1 107 ? 26.524 -27.571 15.820 1.00 13.87 ? 113 ILE   C C   1 
ATOM   1926 O  O   . ILE   B 1 107 ? 26.923 -28.479 15.075 1.00 13.54 ? 113 ILE   C O   1 
ATOM   1927 C  CB  . ILE   B 1 107 ? 24.007 -27.800 16.190 1.00 16.53 ? 113 ILE   C CB  1 
ATOM   1928 C  CG1 . ILE   B 1 107 ? 22.779 -26.874 16.589 1.00 19.02 ? 113 ILE   C CG1 1 
ATOM   1929 C  CG2 . ILE   B 1 107 ? 24.460 -28.649 17.425 1.00 17.05 ? 113 ILE   C CG2 1 
ATOM   1930 C  CD1 . ILE   B 1 107 ? 21.500 -27.578 17.119 1.00 22.45 ? 113 ILE   C CD1 1 
ATOM   1931 N  N   . LEU   B 1 108 ? 27.210 -27.158 16.907 1.00 12.69 ? 114 LEU   C N   1 
ATOM   1932 C  CA  . LEU   B 1 108 ? 28.401 -27.855 17.406 1.00 12.17 ? 114 LEU   C CA  1 
ATOM   1933 C  C   . LEU   B 1 108 ? 27.918 -28.604 18.660 1.00 12.85 ? 114 LEU   C C   1 
ATOM   1934 O  O   . LEU   B 1 108 ? 27.293 -27.986 19.525 1.00 12.28 ? 114 LEU   C O   1 
ATOM   1935 C  CB  . LEU   B 1 108 ? 29.490 -26.826 17.802 1.00 12.01 ? 114 LEU   C CB  1 
ATOM   1936 C  CG  . LEU   B 1 108 ? 30.673 -27.383 18.584 1.00 14.23 ? 114 LEU   C CG  1 
ATOM   1937 C  CD1 . LEU   B 1 108 ? 31.530 -28.317 17.680 1.00 14.48 ? 114 LEU   C CD1 1 
ATOM   1938 C  CD2 . LEU   B 1 108 ? 31.535 -26.239 19.095 1.00 15.26 ? 114 LEU   C CD2 1 
ATOM   1939 N  N   . ARG   B 1 109 ? 28.180 -29.916 18.732 1.00 13.59 ? 115 ARG   C N   1 
ATOM   1940 C  CA  . ARG   B 1 109 ? 27.721 -30.748 19.851 1.00 14.22 ? 115 ARG   C CA  1 
ATOM   1941 C  C   . ARG   B 1 109 ? 28.859 -31.606 20.424 1.00 14.95 ? 115 ARG   C C   1 
ATOM   1942 O  O   . ARG   B 1 109 ? 29.755 -32.061 19.694 1.00 14.71 ? 115 ARG   C O   1 
ATOM   1943 C  CB  . ARG   B 1 109 ? 26.585 -31.682 19.371 1.00 16.76 ? 115 ARG   C CB  1 
ATOM   1944 C  CG  . ARG   B 1 109 ? 27.059 -32.616 18.274 1.00 24.76 ? 115 ARG   C CG  1 
ATOM   1945 C  CD  . ARG   B 1 109 ? 26.083 -33.714 17.897 1.00 33.83 ? 115 ARG   C CD  1 
ATOM   1946 N  NE  . ARG   B 1 109 ? 25.199 -33.297 16.812 1.00 41.63 ? 115 ARG   C NE  1 
ATOM   1947 C  CZ  . ARG   B 1 109 ? 23.946 -32.891 16.981 1.00 46.63 ? 115 ARG   C CZ  1 
ATOM   1948 N  NH1 . ARG   B 1 109 ? 23.410 -32.853 18.197 1.00 47.50 ? 115 ARG   C NH1 1 
ATOM   1949 N  NH2 . ARG   B 1 109 ? 23.215 -32.533 15.935 1.00 47.33 ? 115 ARG   C NH2 1 
ATOM   1950 N  N   . CYS   B 1 110 ? 28.771 -31.851 21.731 1.00 13.78 ? 116 CYS   C N   1 
ATOM   1951 C  CA  . CYS   B 1 110 ? 29.717 -32.750 22.422 1.00 14.33 ? 116 CYS   C CA  1 
ATOM   1952 C  C   . CYS   B 1 110 ? 28.895 -33.843 23.126 1.00 15.58 ? 116 CYS   C C   1 
ATOM   1953 O  O   . CYS   B 1 110 ? 27.679 -33.917 22.912 1.00 15.95 ? 116 CYS   C O   1 
ATOM   1954 C  CB  . CYS   B 1 110 ? 30.554 -31.953 23.417 1.00 14.52 ? 116 CYS   C CB  1 
ATOM   1955 S  SG  . CYS   B 1 110 ? 29.560 -31.289 24.774 1.00 14.53 ? 116 CYS   C SG  1 
ATOM   1956 N  N   . GLN   B 1 111 ? 29.539 -34.703 23.976 1.00 16.17 ? 117 GLN   C N   1 
ATOM   1957 C  CA  . GLN   B 1 111 ? 28.768 -35.762 24.650 1.00 18.64 ? 117 GLN   C CA  1 
ATOM   1958 C  C   . GLN   B 1 111 ? 27.679 -35.194 25.601 1.00 18.28 ? 117 GLN   C C   1 
ATOM   1959 O  O   . GLN   B 1 111 ? 26.724 -35.899 25.958 1.00 20.07 ? 117 GLN   C O   1 
ATOM   1960 C  CB  . GLN   B 1 111 ? 29.710 -36.704 25.459 1.00 21.53 ? 117 GLN   C CB  1 
ATOM   1961 C  CG  . GLN   B 1 111 ? 30.453 -35.988 26.582 1.00 26.46 ? 117 GLN   C CG  1 
ATOM   1962 C  CD  . GLN   B 1 111 ? 31.413 -36.872 27.359 1.00 36.81 ? 117 GLN   C CD  1 
ATOM   1963 O  OE1 . GLN   B 1 111 ? 32.627 -36.853 27.122 1.00 40.33 ? 117 GLN   C OE1 1 
ATOM   1964 N  NE2 . GLN   B 1 111 ? 30.900 -37.616 28.338 1.00 36.35 ? 117 GLN   C NE2 1 
ATOM   1965 N  N   . HIS   B 1 112 ? 27.817 -33.930 26.025 1.00 16.77 ? 118 HIS   C N   1 
ATOM   1966 C  CA  . HIS   B 1 112 ? 26.880 -33.327 26.975 1.00 15.33 ? 118 HIS   C CA  1 
ATOM   1967 C  C   . HIS   B 1 112 ? 25.703 -32.590 26.315 1.00 17.10 ? 118 HIS   C C   1 
ATOM   1968 O  O   . HIS   B 1 112 ? 24.762 -32.203 27.019 1.00 18.53 ? 118 HIS   C O   1 
ATOM   1969 C  CB  . HIS   B 1 112 ? 27.634 -32.372 27.917 1.00 15.69 ? 118 HIS   C CB  1 
ATOM   1970 C  CG  . HIS   B 1 112 ? 28.812 -33.013 28.589 1.00 16.25 ? 118 HIS   C CG  1 
ATOM   1971 N  ND1 . HIS   B 1 112 ? 30.110 -32.739 28.183 1.00 16.20 ? 118 HIS   C ND1 1 
ATOM   1972 C  CD2 . HIS   B 1 112 ? 28.851 -33.844 29.661 1.00 16.94 ? 118 HIS   C CD2 1 
ATOM   1973 C  CE1 . HIS   B 1 112 ? 30.901 -33.457 28.965 1.00 17.38 ? 118 HIS   C CE1 1 
ATOM   1974 N  NE2 . HIS   B 1 112 ? 30.187 -34.146 29.879 1.00 17.25 ? 118 HIS   C NE2 1 
ATOM   1975 N  N   . GLY   B 1 113 ? 25.778 -32.350 25.000 1.00 16.56 ? 119 GLY   C N   1 
ATOM   1976 C  CA  . GLY   B 1 113 ? 24.713 -31.609 24.339 1.00 15.77 ? 119 GLY   C CA  1 
ATOM   1977 C  C   . GLY   B 1 113 ? 25.210 -30.551 23.382 1.00 13.62 ? 119 GLY   C C   1 
ATOM   1978 O  O   . GLY   B 1 113 ? 26.316 -30.672 22.846 1.00 13.70 ? 119 GLY   C O   1 
ATOM   1979 N  N   . VAL   B 1 114 ? 24.369 -29.529 23.118 1.00 12.77 ? 120 VAL   C N   1 
ATOM   1980 C  CA  . VAL   B 1 114 ? 24.726 -28.457 22.177 1.00 13.51 ? 120 VAL   C CA  1 
ATOM   1981 C  C   . VAL   B 1 114 ? 25.708 -27.480 22.842 1.00 12.93 ? 120 VAL   C C   1 
ATOM   1982 O  O   . VAL   B 1 114 ? 25.433 -26.937 23.933 1.00 13.97 ? 120 VAL   C O   1 
ATOM   1983 C  CB  . VAL   B 1 114 ? 23.452 -27.710 21.725 1.00 15.00 ? 120 VAL   C CB  1 
ATOM   1984 C  CG1 . VAL   B 1 114 ? 23.828 -26.503 20.855 1.00 15.90 ? 120 VAL   C CG1 1 
ATOM   1985 C  CG2 . VAL   B 1 114 ? 22.494 -28.656 20.983 1.00 16.11 ? 120 VAL   C CG2 1 
ATOM   1986 N  N   . VAL   B 1 115 ? 26.831 -27.231 22.172 1.00 12.55 ? 121 VAL   C N   1 
ATOM   1987 C  CA  . VAL   B 1 115 ? 27.876 -26.324 22.681 1.00 13.01 ? 121 VAL   C CA  1 
ATOM   1988 C  C   . VAL   B 1 115 ? 27.694 -24.890 22.157 1.00 14.78 ? 121 VAL   C C   1 
ATOM   1989 O  O   . VAL   B 1 115 ? 27.955 -23.889 22.860 1.00 15.62 ? 121 VAL   C O   1 
ATOM   1990 C  CB  . VAL   B 1 115 ? 29.243 -26.894 22.252 1.00 14.15 ? 121 VAL   C CB  1 
ATOM   1991 C  CG1 . VAL   B 1 115 ? 30.355 -25.900 22.586 1.00 14.09 ? 121 VAL   C CG1 1 
ATOM   1992 C  CG2 . VAL   B 1 115 ? 29.477 -28.239 22.927 1.00 15.34 ? 121 VAL   C CG2 1 
ATOM   1993 N  N   . GLY   B 1 116 ? 27.318 -24.797 20.894 1.00 14.02 ? 122 GLY   C N   1 
ATOM   1994 C  CA  . GLY   B 1 116 ? 27.109 -23.504 20.270 1.00 14.76 ? 122 GLY   C CA  1 
ATOM   1995 C  C   . GLY   B 1 116 ? 26.714 -23.640 18.822 1.00 14.40 ? 122 GLY   C C   1 
ATOM   1996 O  O   . GLY   B 1 116 ? 26.344 -24.730 18.389 1.00 13.87 ? 122 GLY   C O   1 
ATOM   1997 N  N   . ILE   B 1 117 ? 26.729 -22.502 18.092 1.00 14.12 ? 123 ILE   C N   1 
ATOM   1998 C  CA  . ILE   B 1 117 ? 26.363 -22.535 16.668 1.00 14.11 ? 123 ILE   C CA  1 
ATOM   1999 C  C   . ILE   B 1 117 ? 27.378 -21.792 15.835 1.00 12.87 ? 123 ILE   C C   1 
ATOM   2000 O  O   . ILE   B 1 117 ? 28.031 -20.847 16.315 1.00 13.49 ? 123 ILE   C O   1 
ATOM   2001 C  CB  . ILE   B 1 117 ? 24.986 -21.860 16.442 1.00 15.57 ? 123 ILE   C CB  1 
ATOM   2002 C  CG1 . ILE   B 1 117 ? 24.918 -20.469 17.087 1.00 16.12 ? 123 ILE   C CG1 1 
ATOM   2003 C  CG2 . ILE   B 1 117 ? 23.832 -22.754 16.924 1.00 17.00 ? 123 ILE   C CG2 1 
ATOM   2004 C  CD1 . ILE   B 1 117 ? 23.571 -19.663 16.659 1.00 18.42 ? 123 ILE   C CD1 1 
ATOM   2005 N  N   . VAL   B 1 118 ? 27.557 -22.226 14.579 1.00 12.52 ? 124 VAL   C N   1 
ATOM   2006 C  CA  . VAL   B 1 118 ? 28.475 -21.530 13.656 1.00 12.80 ? 124 VAL   C CA  1 
ATOM   2007 C  C   . VAL   B 1 118 ? 28.139 -20.039 13.548 1.00 14.08 ? 124 VAL   C C   1 
ATOM   2008 O  O   . VAL   B 1 118 ? 26.974 -19.699 13.382 1.00 14.11 ? 124 VAL   C O   1 
ATOM   2009 C  CB  . VAL   B 1 118 ? 28.446 -22.183 12.245 1.00 13.90 ? 124 VAL   C CB  1 
ATOM   2010 C  CG1 . VAL   B 1 118 ? 29.318 -21.410 11.247 1.00 14.66 ? 124 VAL   C CG1 1 
ATOM   2011 C  CG2 . VAL   B 1 118 ? 28.906 -23.641 12.326 1.00 14.29 ? 124 VAL   C CG2 1 
ATOM   2012 N  N   . SER   B 1 119 ? 29.174 -19.172 13.628 1.00 13.77 ? 125 SER   C N   1 
ATOM   2013 C  CA  . SER   B 1 119 ? 28.976 -17.720 13.549 1.00 14.31 ? 125 SER   C CA  1 
ATOM   2014 C  C   . SER   B 1 119 ? 29.981 -17.025 12.623 1.00 14.69 ? 125 SER   C C   1 
ATOM   2015 O  O   . SER   B 1 119 ? 29.671 -15.977 12.047 1.00 15.63 ? 125 SER   C O   1 
ATOM   2016 C  CB  . SER   B 1 119 ? 29.079 -17.128 14.950 1.00 15.68 ? 125 SER   C CB  1 
ATOM   2017 O  OG  . SER   B 1 119 ? 28.934 -15.709 14.920 1.00 16.50 ? 125 SER   C OG  1 
ATOM   2018 N  N   . THR   B 1 120 ? 31.214 -17.599 12.475 1.00 13.41 ? 126 THR   C N   1 
ATOM   2019 C  CA  . THR   B 1 120 ? 32.238 -16.961 11.643 1.00 14.32 ? 126 THR   C CA  1 
ATOM   2020 C  C   . THR   B 1 120 ? 32.926 -18.004 10.746 1.00 14.96 ? 126 THR   C C   1 
ATOM   2021 O  O   . THR   B 1 120 ? 32.817 -19.213 10.985 1.00 14.88 ? 126 THR   C O   1 
ATOM   2022 C  CB  . THR   B 1 120 ? 33.311 -16.245 12.536 1.00 14.56 ? 126 THR   C CB  1 
ATOM   2023 O  OG1 . THR   B 1 120 ? 34.185 -17.199 13.166 1.00 15.35 ? 126 THR   C OG1 1 
ATOM   2024 C  CG2 . THR   B 1 120 ? 32.723 -15.337 13.551 1.00 15.88 ? 126 THR   C CG2 1 
ATOM   2025 N  N   . GLY   B 1 121 ? 33.660 -17.528 9.747  1.00 16.31 ? 127 GLY   C N   1 
ATOM   2026 C  CA  . GLY   B 1 121 ? 34.436 -18.427 8.883  1.00 18.60 ? 127 GLY   C CA  1 
ATOM   2027 C  C   . GLY   B 1 121 ? 35.481 -17.659 8.092  1.00 23.10 ? 127 GLY   C C   1 
ATOM   2028 O  O   . GLY   B 1 121 ? 35.442 -16.433 8.038  1.00 23.76 ? 127 GLY   C O   1 
ATOM   2029 N  N   . GLY   B 1 122 ? 36.316 -18.368 7.353  1.00 25.30 ? 128 GLY   C N   1 
ATOM   2030 C  CA  . GLY   B 1 122 ? 37.365 -17.740 6.550  1.00 26.74 ? 128 GLY   C CA  1 
ATOM   2031 C  C   . GLY   B 1 122 ? 38.756 -18.138 7.026  1.00 27.29 ? 128 GLY   C C   1 
ATOM   2032 O  O   . GLY   B 1 122 ? 38.926 -18.586 8.164  1.00 27.59 ? 128 GLY   C O   1 
ATOM   2033 N  N   . ASN   B 1 123 ? 39.780 -17.963 6.172  1.00 27.14 ? 129 ASN   C N   1 
ATOM   2034 C  CA  . ASN   B 1 123 ? 41.169 -18.336 6.510  1.00 27.20 ? 129 ASN   C CA  1 
ATOM   2035 C  C   . ASN   B 1 123 ? 41.323 -19.773 6.993  1.00 25.17 ? 129 ASN   C C   1 
ATOM   2036 O  O   . ASN   B 1 123 ? 42.271 -20.078 7.721  1.00 25.57 ? 129 ASN   C O   1 
ATOM   2037 C  CB  . ASN   B 1 123 ? 41.815 -17.367 7.512  1.00 30.95 ? 129 ASN   C CB  1 
ATOM   2038 C  CG  . ASN   B 1 123 ? 42.740 -16.359 6.863  1.00 38.45 ? 129 ASN   C CG  1 
ATOM   2039 O  OD1 . ASN   B 1 123 ? 42.755 -16.194 5.639  1.00 40.38 ? 129 ASN   C OD1 1 
ATOM   2040 N  ND2 . ASN   B 1 123 ? 43.514 -15.637 7.665  1.00 40.27 ? 129 ASN   C ND2 1 
ATOM   2041 N  N   . GLY   B 1 124 ? 40.416 -20.659 6.568  1.00 23.44 ? 130 GLY   C N   1 
ATOM   2042 C  CA  . GLY   B 1 124 ? 40.501 -22.061 6.958  1.00 22.09 ? 130 GLY   C CA  1 
ATOM   2043 C  C   . GLY   B 1 124 ? 40.032 -22.345 8.376  1.00 20.33 ? 130 GLY   C C   1 
ATOM   2044 O  O   . GLY   B 1 124 ? 40.262 -23.437 8.892  1.00 19.92 ? 130 GLY   C O   1 
ATOM   2045 N  N   . LEU   B 1 125 ? 39.346 -21.381 9.001  1.00 18.37 ? 131 LEU   C N   1 
ATOM   2046 C  CA  . LEU   B 1 125 ? 38.866 -21.540 10.355 1.00 17.84 ? 131 LEU   C CA  1 
ATOM   2047 C  C   . LEU   B 1 125 ? 37.355 -21.425 10.382 1.00 17.36 ? 131 LEU   C C   1 
ATOM   2048 O  O   . LEU   B 1 125 ? 36.753 -20.809 9.499  1.00 19.57 ? 131 LEU   C O   1 
ATOM   2049 C  CB  . LEU   B 1 125 ? 39.464 -20.426 11.229 1.00 19.66 ? 131 LEU   C CB  1 
ATOM   2050 C  CG  . LEU   B 1 125 ? 40.989 -20.422 11.344 1.00 23.34 ? 131 LEU   C CG  1 
ATOM   2051 C  CD1 . LEU   B 1 125 ? 41.487 -19.201 12.077 1.00 26.17 ? 131 LEU   C CD1 1 
ATOM   2052 C  CD2 . LEU   B 1 125 ? 41.485 -21.659 12.016 1.00 24.06 ? 131 LEU   C CD2 1 
ATOM   2053 N  N   . VAL   B 1 126 ? 36.724 -22.039 11.381 1.00 14.61 ? 132 VAL   C N   1 
ATOM   2054 C  CA  . VAL   B 1 126 ? 35.297 -21.902 11.612 1.00 14.41 ? 132 VAL   C CA  1 
ATOM   2055 C  C   . VAL   B 1 126 ? 35.141 -21.450 13.065 1.00 13.44 ? 132 VAL   C C   1 
ATOM   2056 O  O   . VAL   B 1 126 ? 35.821 -21.978 13.958 1.00 13.33 ? 132 VAL   C O   1 
ATOM   2057 C  CB  . VAL   B 1 126 ? 34.511 -23.218 11.368 1.00 14.97 ? 132 VAL   C CB  1 
ATOM   2058 C  CG1 . VAL   B 1 126 ? 35.117 -24.413 12.103 1.00 17.05 ? 132 VAL   C CG1 1 
ATOM   2059 C  CG2 . VAL   B 1 126 ? 33.040 -23.067 11.754 1.00 15.24 ? 132 VAL   C CG2 1 
ATOM   2060 N  N   . GLY   B 1 127 ? 34.323 -20.420 13.283 1.00 13.42 ? 133 GLY   C N   1 
ATOM   2061 C  CA  . GLY   B 1 127 ? 34.109 -19.913 14.634 1.00 13.55 ? 133 GLY   C CA  1 
ATOM   2062 C  C   . GLY   B 1 127 ? 32.698 -20.198 15.114 1.00 14.34 ? 133 GLY   C C   1 
ATOM   2063 O  O   . GLY   B 1 127 ? 31.744 -20.055 14.340 1.00 14.77 ? 133 GLY   C O   1 
ATOM   2064 N  N   . PHE   B 1 128 ? 32.571 -20.632 16.400 1.00 13.28 ? 134 PHE   C N   1 
ATOM   2065 C  CA  . PHE   B 1 128 ? 31.282 -20.975 16.997 1.00 12.98 ? 134 PHE   C CA  1 
ATOM   2066 C  C   . PHE   B 1 128 ? 30.970 -20.011 18.143 1.00 13.73 ? 134 PHE   C C   1 
ATOM   2067 O  O   . PHE   B 1 128 ? 31.833 -19.760 19.002 1.00 13.92 ? 134 PHE   C O   1 
ATOM   2068 C  CB  . PHE   B 1 128 ? 31.370 -22.402 17.589 1.00 12.56 ? 134 PHE   C CB  1 
ATOM   2069 C  CG  . PHE   B 1 128 ? 31.839 -23.434 16.579 1.00 13.12 ? 134 PHE   C CG  1 
ATOM   2070 C  CD1 . PHE   B 1 128 ? 30.941 -24.026 15.706 1.00 12.79 ? 134 PHE   C CD1 1 
ATOM   2071 C  CD2 . PHE   B 1 128 ? 33.153 -23.881 16.578 1.00 14.13 ? 134 PHE   C CD2 1 
ATOM   2072 C  CE1 . PHE   B 1 128 ? 31.361 -24.978 14.803 1.00 13.74 ? 134 PHE   C CE1 1 
ATOM   2073 C  CE2 . PHE   B 1 128 ? 33.582 -24.848 15.674 1.00 14.76 ? 134 PHE   C CE2 1 
ATOM   2074 C  CZ  . PHE   B 1 128 ? 32.681 -25.390 14.786 1.00 13.95 ? 134 PHE   C CZ  1 
ATOM   2075 N  N   . ALA   B 1 129 ? 29.724 -19.543 18.197 1.00 13.15 ? 135 ALA   C N   1 
ATOM   2076 C  CA  . ALA   B 1 129 ? 29.273 -18.722 19.310 1.00 13.59 ? 135 ALA   C CA  1 
ATOM   2077 C  C   . ALA   B 1 129 ? 28.874 -19.686 20.444 1.00 13.53 ? 135 ALA   C C   1 
ATOM   2078 O  O   . ALA   B 1 129 ? 27.938 -20.522 20.290 1.00 13.00 ? 135 ALA   C O   1 
ATOM   2079 C  CB  . ALA   B 1 129 ? 28.058 -17.906 18.871 1.00 13.81 ? 135 ALA   C CB  1 
ATOM   2080 N  N   . ASP   B 1 130 ? 29.581 -19.599 21.576 1.00 13.83 ? 136 ASP   C N   1 
ATOM   2081 C  CA  . ASP   B 1 130 ? 29.305 -20.491 22.705 1.00 13.76 ? 136 ASP   C CA  1 
ATOM   2082 C  C   . ASP   B 1 130 ? 27.964 -20.144 23.348 1.00 14.66 ? 136 ASP   C C   1 
ATOM   2083 O  O   . ASP   B 1 130 ? 27.595 -18.957 23.412 1.00 15.41 ? 136 ASP   C O   1 
ATOM   2084 C  CB  . ASP   B 1 130 ? 30.403 -20.308 23.770 1.00 13.82 ? 136 ASP   C CB  1 
ATOM   2085 C  CG  . ASP   B 1 130 ? 30.278 -21.246 24.967 1.00 17.83 ? 136 ASP   C CG  1 
ATOM   2086 O  OD1 . ASP   B 1 130 ? 30.072 -22.442 24.761 1.00 18.92 ? 136 ASP   C OD1 1 
ATOM   2087 O  OD2 . ASP   B 1 130 ? 30.289 -20.745 26.112 1.00 19.84 ? 136 ASP   C OD2 1 
ATOM   2088 N  N   . VAL   B 1 131 ? 27.238 -21.158 23.872 1.00 13.74 ? 137 VAL   C N   1 
ATOM   2089 C  CA  . VAL   B 1 131 ? 26.028 -20.906 24.662 1.00 13.68 ? 137 VAL   C CA  1 
ATOM   2090 C  C   . VAL   B 1 131 ? 26.112 -21.592 26.037 1.00 14.40 ? 137 VAL   C C   1 
ATOM   2091 O  O   . VAL   B 1 131 ? 25.138 -21.541 26.798 1.00 15.43 ? 137 VAL   C O   1 
ATOM   2092 C  CB  . VAL   B 1 131 ? 24.734 -21.328 23.935 1.00 14.78 ? 137 VAL   C CB  1 
ATOM   2093 C  CG1 . VAL   B 1 131 ? 24.555 -20.526 22.637 1.00 15.49 ? 137 VAL   C CG1 1 
ATOM   2094 C  CG2 . VAL   B 1 131 ? 24.748 -22.821 23.623 1.00 14.66 ? 137 VAL   C CG2 1 
ATOM   2095 N  N   . ARG   B 1 132 ? 27.223 -22.308 26.341 1.00 13.83 ? 138 ARG   C N   1 
ATOM   2096 C  CA  . ARG   B 1 132 ? 27.293 -23.096 27.582 1.00 13.52 ? 138 ARG   C CA  1 
ATOM   2097 C  C   . ARG   B 1 132 ? 27.230 -22.276 28.875 1.00 15.73 ? 138 ARG   C C   1 
ATOM   2098 O  O   . ARG   B 1 132 ? 26.900 -22.828 29.933 1.00 16.89 ? 138 ARG   C O   1 
ATOM   2099 C  CB  . ARG   B 1 132 ? 28.522 -23.992 27.577 1.00 13.44 ? 138 ARG   C CB  1 
ATOM   2100 C  CG  . ARG   B 1 132 ? 28.471 -25.015 26.456 1.00 12.87 ? 138 ARG   C CG  1 
ATOM   2101 C  CD  . ARG   B 1 132 ? 29.800 -25.782 26.477 1.00 13.73 ? 138 ARG   C CD  1 
ATOM   2102 N  NE  . ARG   B 1 132 ? 30.900 -24.932 26.009 1.00 14.54 ? 138 ARG   C NE  1 
ATOM   2103 C  CZ  . ARG   B 1 132 ? 32.139 -25.362 25.826 1.00 16.62 ? 138 ARG   C CZ  1 
ATOM   2104 N  NH1 . ARG   B 1 132 ? 32.483 -26.597 26.178 1.00 15.33 ? 138 ARG   C NH1 1 
ATOM   2105 N  NH2 . ARG   B 1 132 ? 33.066 -24.546 25.332 1.00 15.37 ? 138 ARG   C NH2 1 
ATOM   2106 N  N   . ASP   B 1 133 ? 27.602 -20.996 28.797 1.00 15.04 ? 139 ASP   C N   1 
ATOM   2107 C  CA  . ASP   B 1 133 ? 27.553 -20.119 29.978 1.00 15.67 ? 139 ASP   C CA  1 
ATOM   2108 C  C   . ASP   B 1 133 ? 26.131 -19.551 30.256 1.00 16.37 ? 139 ASP   C C   1 
ATOM   2109 O  O   . ASP   B 1 133 ? 25.930 -18.922 31.306 1.00 17.22 ? 139 ASP   C O   1 
ATOM   2110 C  CB  . ASP   B 1 133 ? 28.542 -18.942 29.803 1.00 17.12 ? 139 ASP   C CB  1 
ATOM   2111 C  CG  . ASP   B 1 133 ? 28.136 -17.992 28.694 1.00 19.84 ? 139 ASP   C CG  1 
ATOM   2112 O  OD1 . ASP   B 1 133 ? 27.794 -18.476 27.600 1.00 17.88 ? 139 ASP   C OD1 1 
ATOM   2113 O  OD2 . ASP   B 1 133 ? 28.109 -16.744 28.942 1.00 22.92 ? 139 ASP   C OD2 1 
ATOM   2114 N  N   . LEU   B 1 134 ? 25.185 -19.733 29.315 1.00 14.98 ? 140 LEU   C N   1 
ATOM   2115 C  CA  . LEU   B 1 134 ? 23.820 -19.155 29.441 1.00 14.99 ? 140 LEU   C CA  1 
ATOM   2116 C  C   . LEU   B 1 134 ? 22.963 -20.109 30.229 1.00 15.70 ? 140 LEU   C C   1 
ATOM   2117 O  O   . LEU   B 1 134 ? 22.153 -20.852 29.658 1.00 16.27 ? 140 LEU   C O   1 
ATOM   2118 C  CB  . LEU   B 1 134 ? 23.244 -18.899 28.029 1.00 14.74 ? 140 LEU   C CB  1 
ATOM   2119 C  CG  . LEU   B 1 134 ? 24.100 -17.968 27.133 1.00 16.54 ? 140 LEU   C CG  1 
ATOM   2120 C  CD1 . LEU   B 1 134 ? 23.483 -17.816 25.746 1.00 17.40 ? 140 LEU   C CD1 1 
ATOM   2121 C  CD2 . LEU   B 1 134 ? 24.271 -16.578 27.771 1.00 17.76 ? 140 LEU   C CD2 1 
ATOM   2122 N  N   . LEU   B 1 135 ? 23.193 -20.156 31.561 1.00 15.88 ? 141 LEU   C N   1 
ATOM   2123 C  CA  . LEU   B 1 135 ? 22.530 -21.161 32.402 1.00 17.02 ? 141 LEU   C CA  1 
ATOM   2124 C  C   . LEU   B 1 135 ? 21.025 -21.033 32.448 1.00 18.24 ? 141 LEU   C C   1 
ATOM   2125 O  O   . LEU   B 1 135 ? 20.327 -22.049 32.637 1.00 18.73 ? 141 LEU   C O   1 
ATOM   2126 C  CB  . LEU   B 1 135 ? 23.116 -21.231 33.826 1.00 17.38 ? 141 LEU   C CB  1 
ATOM   2127 C  CG  . LEU   B 1 135 ? 24.657 -21.266 33.904 1.00 19.14 ? 141 LEU   C CG  1 
ATOM   2128 C  CD1 . LEU   B 1 135 ? 25.139 -21.356 35.355 1.00 19.06 ? 141 LEU   C CD1 1 
ATOM   2129 C  CD2 . LEU   B 1 135 ? 25.248 -22.404 33.078 1.00 19.10 ? 141 LEU   C CD2 1 
ATOM   2130 N  N   . TRP   B 1 136 ? 20.524 -19.800 32.245 1.00 18.17 ? 142 TRP   C N   1 
ATOM   2131 C  CA  . TRP   B 1 136 ? 19.082 -19.528 32.267 1.00 18.79 ? 142 TRP   C CA  1 
ATOM   2132 C  C   . TRP   B 1 136 ? 18.310 -20.223 31.125 1.00 19.26 ? 142 TRP   C C   1 
ATOM   2133 O  O   . TRP   B 1 136 ? 17.086 -20.352 31.219 1.00 21.19 ? 142 TRP   C O   1 
ATOM   2134 C  CB  . TRP   B 1 136 ? 18.820 -18.018 32.280 1.00 19.04 ? 142 TRP   C CB  1 
ATOM   2135 C  CG  . TRP   B 1 136 ? 19.498 -17.280 31.160 1.00 18.82 ? 142 TRP   C CG  1 
ATOM   2136 C  CD1 . TRP   B 1 136 ? 20.711 -16.645 31.205 1.00 20.38 ? 142 TRP   C CD1 1 
ATOM   2137 C  CD2 . TRP   B 1 136 ? 18.972 -17.048 29.842 1.00 19.41 ? 142 TRP   C CD2 1 
ATOM   2138 N  NE1 . TRP   B 1 136 ? 20.971 -16.034 29.989 1.00 20.80 ? 142 TRP   C NE1 1 
ATOM   2139 C  CE2 . TRP   B 1 136 ? 19.924 -16.275 29.134 1.00 20.36 ? 142 TRP   C CE2 1 
ATOM   2140 C  CE3 . TRP   B 1 136 ? 17.796 -17.424 29.188 1.00 19.77 ? 142 TRP   C CE3 1 
ATOM   2141 C  CZ2 . TRP   B 1 136 ? 19.727 -15.863 27.801 1.00 20.84 ? 142 TRP   C CZ2 1 
ATOM   2142 C  CZ3 . TRP   B 1 136 ? 17.590 -16.989 27.882 1.00 20.71 ? 142 TRP   C CZ3 1 
ATOM   2143 C  CH2 . TRP   B 1 136 ? 18.554 -16.233 27.202 1.00 20.83 ? 142 TRP   C CH2 1 
ATOM   2144 N  N   . LEU   B 1 137 ? 19.009 -20.719 30.088 1.00 18.22 ? 143 LEU   C N   1 
ATOM   2145 C  CA  . LEU   B 1 137 ? 18.314 -21.454 29.020 1.00 18.99 ? 143 LEU   C CA  1 
ATOM   2146 C  C   . LEU   B 1 137 ? 17.696 -22.756 29.543 1.00 21.49 ? 143 LEU   C C   1 
ATOM   2147 O  O   . LEU   B 1 137 ? 16.756 -23.263 28.924 1.00 23.15 ? 143 LEU   C O   1 
ATOM   2148 C  CB  . LEU   B 1 137 ? 19.266 -21.790 27.871 1.00 18.89 ? 143 LEU   C CB  1 
ATOM   2149 C  CG  . LEU   B 1 137 ? 19.731 -20.609 26.997 1.00 20.25 ? 143 LEU   C CG  1 
ATOM   2150 C  CD1 . LEU   B 1 137 ? 20.831 -21.046 26.040 1.00 20.55 ? 143 LEU   C CD1 1 
ATOM   2151 C  CD2 . LEU   B 1 137 ? 18.568 -20.040 26.168 1.00 21.26 ? 143 LEU   C CD2 1 
ATOM   2152 N  N   . ASP   B 1 138 ? 18.211 -23.300 30.678 1.00 21.80 ? 144 ASP   C N   1 
ATOM   2153 C  CA  . ASP   B 1 138 ? 17.727 -24.554 31.284 1.00 22.99 ? 144 ASP   C CA  1 
ATOM   2154 C  C   . ASP   B 1 138 ? 16.479 -24.419 32.142 1.00 26.30 ? 144 ASP   C C   1 
ATOM   2155 O  O   . ASP   B 1 138 ? 16.025 -25.442 32.673 1.00 26.52 ? 144 ASP   C O   1 
ATOM   2156 C  CB  . ASP   B 1 138 ? 18.819 -25.198 32.163 1.00 22.82 ? 144 ASP   C CB  1 
ATOM   2157 C  CG  . ASP   B 1 138 ? 20.043 -25.670 31.406 1.00 24.15 ? 144 ASP   C CG  1 
ATOM   2158 O  OD1 . ASP   B 1 138 ? 19.997 -25.708 30.168 1.00 23.81 ? 144 ASP   C OD1 1 
ATOM   2159 O  OD2 . ASP   B 1 138 ? 21.071 -25.994 32.071 1.00 24.01 ? 144 ASP   C OD2 1 
ATOM   2160 N  N   . GLU   B 1 139 ? 15.950 -23.206 32.343 1.00 28.72 ? 145 GLU   C N   1 
ATOM   2161 C  CA  . GLU   B 1 139 ? 14.750 -23.053 33.188 1.00 33.31 ? 145 GLU   C CA  1 
ATOM   2162 C  C   . GLU   B 1 139 ? 13.813 -21.906 32.754 1.00 36.19 ? 145 GLU   C C   1 
ATOM   2163 O  O   . GLU   B 1 139 ? 14.120 -21.189 31.806 1.00 36.04 ? 145 GLU   C O   1 
ATOM   2164 C  CB  . GLU   B 1 139 ? 15.178 -22.862 34.659 1.00 38.55 ? 145 GLU   C CB  1 
ATOM   2165 C  CG  . GLU   B 1 139 ? 15.842 -21.524 34.924 1.00 47.30 ? 145 GLU   C CG  1 
ATOM   2166 C  CD  . GLU   B 1 139 ? 17.335 -21.600 35.176 1.00 58.73 ? 145 GLU   C CD  1 
ATOM   2167 O  OE1 . GLU   B 1 139 ? 17.893 -20.629 35.739 1.00 61.21 ? 145 GLU   C OE1 1 
ATOM   2168 O  OE2 . GLU   B 1 139 ? 17.948 -22.631 34.811 1.00 62.28 ? 145 GLU   C OE2 1 
ATOM   2169 N  N   . GLU   B 1 140 ? 12.687 -21.713 33.488 1.00 38.77 ? 146 GLU   C N   1 
ATOM   2170 C  CA  . GLU   B 1 140 ? 11.738 -20.595 33.368 1.00 40.84 ? 146 GLU   C CA  1 
ATOM   2171 C  C   . GLU   B 1 140 ? 11.454 -20.191 31.939 1.00 42.58 ? 146 GLU   C C   1 
ATOM   2172 O  O   . GLU   B 1 140 ? 10.327 -19.823 31.622 1.00 44.06 ? 146 GLU   C O   1 
ATOM   2173 C  CB  . GLU   B 1 140 ? 12.233 -19.397 34.228 1.00 43.76 ? 146 GLU   C CB  1 
ATOM   2174 C  CG  . GLU   B 1 140 ? 12.264 -18.001 33.604 1.00 50.34 ? 146 GLU   C CG  1 
ATOM   2175 C  CD  . GLU   B 1 140 ? 10.942 -17.263 33.509 1.00 57.94 ? 146 GLU   C CD  1 
ATOM   2176 O  OE1 . GLU   B 1 140 ? 10.902 -16.218 32.821 1.00 60.86 ? 146 GLU   C OE1 1 
ATOM   2177 O  OE2 . GLU   B 1 140 ? 9.944  -17.733 34.104 1.00 59.70 ? 146 GLU   C OE2 1 
HETATM 2178 N  N1  . A1BON C 2 .   ? 9.135  15.848  21.649 1.00 21.20 ? 201 A1BON A N1  1 
HETATM 2179 C  C4  . A1BON C 2 .   ? 10.164 16.528  22.453 1.00 21.14 ? 201 A1BON A C4  1 
HETATM 2180 C  C5  . A1BON C 2 .   ? 8.360  14.840  22.103 1.00 21.70 ? 201 A1BON A C5  1 
HETATM 2181 C  C6  . A1BON C 2 .   ? 8.641  14.356  23.513 1.00 23.84 ? 201 A1BON A C6  1 
HETATM 2182 C  C7  . A1BON C 2 .   ? 7.700  13.251  23.926 1.00 25.89 ? 201 A1BON A C7  1 
HETATM 2183 C  C8  . A1BON C 2 .   ? 6.612  13.522  24.752 1.00 27.26 ? 201 A1BON A C8  1 
HETATM 2184 C  C10 . A1BON C 2 .   ? 4.746  12.853  26.273 1.00 33.79 ? 201 A1BON A C10 1 
HETATM 2185 C  C13 . A1BON C 2 .   ? 7.926  11.922  23.593 1.00 26.89 ? 201 A1BON A C13 1 
HETATM 2186 CL CL  . A1BON C 2 .   ? 9.255  11.512  22.552 1.00 29.01 ? 201 A1BON A CL  1 
HETATM 2187 C  C12 . A1BON C 2 .   ? 7.112  10.905  24.056 1.00 27.20 ? 201 A1BON A C12 1 
HETATM 2188 C  C11 . A1BON C 2 .   ? 6.041  11.203  24.880 1.00 28.29 ? 201 A1BON A C11 1 
HETATM 2189 C  C9  . A1BON C 2 .   ? 5.789  12.519  25.253 1.00 29.65 ? 201 A1BON A C9  1 
HETATM 2190 F  F2  . A1BON C 2 .   ? 5.212  13.625  27.225 1.00 35.21 ? 201 A1BON A F2  1 
HETATM 2191 F  F1  . A1BON C 2 .   ? 4.321  11.798  26.938 1.00 35.55 ? 201 A1BON A F1  1 
HETATM 2192 F  F   . A1BON C 2 .   ? 3.678  13.499  25.759 1.00 34.36 ? 201 A1BON A F   1 
HETATM 2193 O  O1  . A1BON C 2 .   ? 7.491  14.331  21.413 1.00 20.60 ? 201 A1BON A O1  1 
HETATM 2194 C  C3  . A1BON C 2 .   ? 11.531 16.325  21.817 1.00 20.21 ? 201 A1BON A C3  1 
HETATM 2195 C  C2  . A1BON C 2 .   ? 11.510 16.800  20.364 1.00 19.91 ? 201 A1BON A C2  1 
HETATM 2196 C  C14 . A1BON C 2 .   ? 9.070  16.276  20.247 1.00 20.23 ? 201 A1BON A C14 1 
HETATM 2197 C  C1  . A1BON C 2 .   ? 10.425 16.048  19.568 1.00 19.33 ? 201 A1BON A C1  1 
HETATM 2198 C  C   . A1BON C 2 .   ? 10.408 16.448  18.103 1.00 19.06 ? 201 A1BON A C   1 
HETATM 2199 O  O   . A1BON C 2 .   ? 9.988  17.556  17.750 1.00 19.19 ? 201 A1BON A O   1 
HETATM 2200 N  N   . A1BON C 2 .   ? 10.813 15.518  17.243 1.00 18.33 ? 201 A1BON A N   1 
HETATM 2201 ZN ZN  . ZN    D 3 .   ? 11.285 -4.021  5.866  1.00 21.22 2 202 ZN    A ZN  1 
HETATM 2202 ZN ZN  . ZN    E 3 .   ? 30.825 -31.367 26.761 1.00 15.47 2 201 ZN    C ZN  1 
HETATM 2203 S  S   . DMS   F 4 .   ? 21.372 -31.696 9.480  1.00 82.48 ? 202 DMS   C S   1 
HETATM 2204 O  O   . DMS   F 4 .   ? 20.412 -30.581 9.772  1.00 82.49 ? 202 DMS   C O   1 
HETATM 2205 C  C1  . DMS   F 4 .   ? 21.336 -32.825 10.887 1.00 82.34 ? 202 DMS   C C1  1 
HETATM 2206 C  C2  . DMS   F 4 .   ? 20.577 -32.818 8.296  1.00 82.54 ? 202 DMS   C C2  1 
HETATM 2207 O  O   . HOH   G 5 .   ? 11.292 8.666   4.263  1.00 21.01 ? 301 HOH   A O   1 
HETATM 2208 O  O   . HOH   G 5 .   ? 3.015  7.081   24.574 1.00 36.72 ? 302 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 5 .   ? 35.600 -3.960  8.012  1.00 25.59 ? 303 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 5 .   ? 2.945  9.382   9.002  1.00 35.12 ? 304 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 5 .   ? 16.099 -6.779  11.159 1.00 41.95 ? 305 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 5 .   ? 7.430  26.594  13.571 1.00 50.89 ? 306 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? -0.287 15.740  8.678  1.00 41.99 ? 307 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? 2.989  -3.475  20.834 1.00 29.28 ? 308 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 5.786  19.453  23.796 1.00 54.16 ? 309 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 36.343 -2.483  11.215 1.00 29.98 ? 310 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 14.169 17.427  4.247  1.00 41.44 ? 311 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? 15.904 7.425   -1.366 1.00 37.69 ? 312 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? 21.295 19.847  18.187 1.00 36.99 ? 313 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 8.563  25.533  23.433 1.00 39.99 ? 314 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? -0.050 16.114  15.442 1.00 37.52 ? 315 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 17.471 1.154   28.206 1.00 23.59 ? 316 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 10.288 10.007  31.401 1.00 25.85 ? 317 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 7.743  20.916  17.174 1.00 24.13 ? 318 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 33.829 14.201  9.874  1.00 35.59 ? 319 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 18.748 17.300  26.387 1.00 45.64 ? 320 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 30.472 10.674  15.738 1.00 31.29 ? 321 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 25.030 5.217   21.575 1.00 29.58 ? 322 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 21.872 2.468   -0.744 1.00 38.30 ? 323 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 22.916 13.543  24.010 1.00 46.59 ? 324 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 4.953  -3.827  29.009 1.00 29.00 ? 325 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 11.611 17.984  4.977  1.00 32.41 ? 326 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 6.532  2.993   3.099  1.00 35.67 ? 327 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 29.219 22.466  19.340 1.00 55.85 ? 328 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 19.259 10.165  19.643 1.00 15.16 ? 329 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 27.982 8.125   1.640  1.00 46.45 ? 330 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 23.520 21.719  7.102  1.00 30.43 ? 331 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 21.533 5.148   24.838 1.00 41.24 ? 332 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 29.902 11.896  18.546 1.00 32.11 ? 333 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 12.356 22.357  11.975 1.00 28.95 ? 334 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 28.240 3.103   5.172  1.00 33.26 ? 335 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 11.345 12.627  10.936 1.00 16.28 ? 336 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 18.490 21.913  9.470  1.00 23.18 ? 337 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 3.663  15.195  22.904 1.00 39.43 ? 338 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? -0.150 1.228   15.700 1.00 15.31 ? 339 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 22.662 0.960   17.513 1.00 19.66 ? 340 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 11.950 15.317  1.554  1.00 50.15 ? 341 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 5.443  5.376   32.749 1.00 25.29 ? 342 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 20.864 -1.029  3.218  1.00 32.87 ? 343 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 22.621 19.574  19.973 1.00 37.74 ? 344 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 35.276 11.003  12.447 1.00 49.60 ? 345 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 36.385 18.343  14.652 1.00 30.70 ? 346 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 15.210 11.375  0.105  1.00 42.21 ? 347 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 9.001  19.657  19.318 1.00 23.20 ? 348 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 8.388  -2.788  31.905 1.00 27.12 ? 349 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 0.364  -1.158  19.309 1.00 30.64 ? 350 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 29.078 16.049  4.532  1.00 31.86 ? 351 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 13.316 11.308  9.154  1.00 15.50 ? 352 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 29.029 3.440   12.833 1.00 19.07 ? 353 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 29.189 12.060  21.339 1.00 34.55 ? 354 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 16.611 3.929   23.723 1.00 20.04 ? 355 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 23.286 3.657   -2.389 1.00 40.36 ? 356 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 31.572 19.991  11.757 1.00 26.14 ? 357 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 17.476 -5.061  12.302 1.00 38.33 ? 358 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 20.091 17.812  24.003 1.00 36.75 ? 359 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 3.827  9.175   28.072 1.00 32.55 ? 360 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 6.841  -6.948  23.853 1.00 32.03 ? 361 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 5.312  15.829  20.558 1.00 40.24 ? 362 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 27.049 -1.337  9.047  1.00 26.18 ? 363 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 9.848  22.069  9.936  1.00 41.54 ? 364 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 11.929 11.057  29.682 1.00 23.92 ? 365 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 13.715 4.072   23.488 1.00 14.96 ? 366 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 1.287  4.665   27.127 1.00 37.69 ? 367 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 5.030  8.201   2.316  1.00 31.54 ? 368 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 21.134 -4.176  14.302 1.00 20.09 ? 369 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 23.307 11.790  21.992 1.00 30.93 ? 370 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 0.814  -0.855  9.147  1.00 39.69 ? 371 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 13.947 13.844  23.974 1.00 20.66 ? 372 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 6.267  -3.784  31.623 1.00 26.29 ? 373 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 30.561 3.041   14.991 1.00 21.32 ? 374 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 30.310 -1.361  8.890  1.00 32.73 ? 375 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 33.864 11.188  15.690 1.00 44.13 ? 376 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 20.999 -2.590  16.991 1.00 19.30 ? 377 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 17.131 -3.347  27.843 1.00 35.82 ? 378 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 17.494 10.798  26.108 1.00 24.19 ? 379 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 31.746 -2.717  15.567 1.00 53.75 ? 380 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 19.397 3.094   19.378 1.00 20.86 ? 381 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 0.741  7.205   27.704 1.00 44.61 ? 382 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 9.610  4.031   33.523 1.00 15.05 ? 383 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 11.861 -6.935  24.847 1.00 31.83 ? 384 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? -1.149 -4.417  10.914 1.00 50.23 ? 385 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 17.684 20.010  16.944 1.00 18.78 ? 386 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 0.227  5.680   5.966  1.00 25.94 ? 387 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 32.038 8.774   7.812  1.00 24.33 ? 388 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 8.366  20.949  7.466  1.00 42.38 ? 389 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 25.369 17.736  4.523  1.00 41.18 ? 390 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 16.960 6.341   26.908 1.00 26.62 ? 391 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 10.691 5.213   3.322  1.00 26.38 ? 392 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 29.420 11.243  3.292  1.00 53.69 ? 393 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 30.509 4.641   5.944  1.00 25.10 ? 394 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 3.753  -8.212  10.341 1.00 49.02 ? 395 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 3.268  0.199   29.004 1.00 35.34 ? 396 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 36.813 2.492   10.227 1.00 45.23 ? 397 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 18.263 18.004  4.178  1.00 37.76 ? 398 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 23.020 -0.700  5.441  1.00 23.58 ? 399 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 4.129  -4.150  6.026  1.00 29.69 ? 400 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 20.377 -4.495  11.343 1.00 33.52 ? 401 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 30.638 15.786  22.936 1.00 30.92 ? 402 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 3.743  12.397  18.390 1.00 46.20 ? 403 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 9.186  3.001   2.775  1.00 34.46 ? 404 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 34.030 18.729  10.917 1.00 27.51 ? 405 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 6.290  18.146  21.332 1.00 37.23 ? 406 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 4.049  -0.035  24.112 1.00 20.44 ? 407 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 36.404 -0.266  12.700 1.00 34.96 ? 408 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 8.200  6.589   33.880 1.00 22.01 ? 409 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 27.813 17.777  24.250 1.00 26.52 ? 410 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 32.345 1.924   6.234  1.00 35.49 ? 411 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 8.713  -6.476  9.711  1.00 34.09 ? 412 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 19.897 20.490  5.652  1.00 47.79 ? 413 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 20.068 13.329  2.352  1.00 35.37 ? 414 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 24.353 -3.550  16.269 1.00 38.79 ? 415 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 15.188 14.986  3.207  1.00 35.02 ? 416 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 14.612 -2.445  18.048 1.00 19.57 ? 417 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 16.875 -4.015  2.865  1.00 24.80 ? 418 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 16.390 9.513   -1.664 1.00 26.29 ? 419 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 14.645 14.991  26.304 1.00 41.42 ? 420 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 17.607 1.002   20.349 1.00 21.09 ? 421 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 16.893 21.313  19.077 1.00 27.13 ? 422 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? -1.415 12.283  22.428 1.00 39.83 ? 423 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 7.272  13.588  4.623  1.00 22.30 ? 424 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 33.891 5.211   16.855 1.00 34.77 ? 425 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 0.680  -1.087  16.707 1.00 24.44 ? 426 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 5.662  27.377  19.311 1.00 40.23 ? 427 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 17.811 24.381  10.513 1.00 35.81 ? 428 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 22.715 3.523   20.890 1.00 24.33 ? 429 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 23.363 8.503   21.778 1.00 28.02 ? 430 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 23.338 19.180  6.340  1.00 21.66 ? 431 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 15.219 21.879  8.024  1.00 35.64 ? 432 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 27.366 -1.257  16.206 1.00 30.85 ? 433 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 34.204 7.823   16.820 1.00 35.29 ? 434 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 23.554 -6.804  12.196 1.00 36.12 ? 435 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 1.397  -4.957  17.494 1.00 39.96 ? 436 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 6.657  24.071  9.926  1.00 34.11 ? 437 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 15.806 -4.911  0.473  1.00 45.89 ? 438 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 3.438  -0.809  20.900 1.00 36.71 ? 439 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 20.948 10.139  21.949 1.00 19.55 ? 440 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 9.453  19.573  26.155 1.00 57.06 ? 441 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 17.288 -2.368  19.700 1.00 24.65 ? 442 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 17.839 24.155  16.909 1.00 51.11 ? 443 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? -1.457 -3.017  15.357 1.00 32.30 ? 444 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 2.928  16.608  19.099 1.00 30.60 ? 445 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 2.318  14.477  16.675 1.00 56.10 ? 446 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 19.889 9.429   -0.883 1.00 29.68 ? 447 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 7.830  -4.929  3.031  1.00 36.47 ? 448 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 14.357 13.457  28.395 1.00 39.34 ? 449 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? -0.034 10.220  30.080 1.00 53.77 ? 450 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 31.968 7.109   5.575  1.00 32.22 ? 451 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 1.477  10.683  27.656 1.00 32.19 ? 452 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 18.355 3.649   26.084 1.00 47.67 ? 453 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 33.386 -4.180  6.177  1.00 41.21 ? 454 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 0.722  13.078  26.828 1.00 44.42 ? 455 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 2.544  -5.588  14.543 1.00 49.78 ? 456 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? 12.115 24.432  13.703 1.00 40.38 ? 457 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 2.787  -0.677  26.641 1.00 30.74 ? 458 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 27.828 0.167   5.192  1.00 49.07 ? 459 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? 15.837 13.117  26.042 1.00 30.92 ? 460 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 22.151 14.645  1.368  1.00 46.54 ? 461 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 29.800 0.833   16.660 1.00 35.17 ? 462 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 10.478 17.224  26.032 1.00 38.50 ? 463 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 18.084 14.359  27.354 1.00 37.48 ? 464 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 18.584 2.184   22.975 1.00 40.60 ? 465 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 8.312  11.864  31.678 1.00 53.33 ? 466 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 5 .   ? 1.193  26.795  17.704 1.00 43.06 ? 467 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 5 .   ? 12.432 15.807  25.483 1.00 50.09 ? 468 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 5 .   ? 13.825 25.240  15.316 1.00 45.02 ? 469 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 5 .   ? 30.293 7.205   17.987 1.00 32.51 ? 470 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 5 .   ? 23.836 1.005   19.990 1.00 36.76 ? 471 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 5 .   ? 20.940 11.634  24.466 1.00 39.03 ? 472 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 5 .   ? 10.959 16.040  30.156 1.00 46.49 ? 473 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 5 .   ? 21.155 -0.935  19.186 1.00 31.23 ? 474 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 5 .   ? 39.187 -2.424  10.828 1.00 41.20 ? 475 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 5 .   ? 12.307 -5.093  32.941 1.00 31.47 ? 476 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 5 .   ? 31.193 4.779   17.226 1.00 25.06 ? 477 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 5 .   ? 8.020  16.893  25.931 1.00 47.11 ? 478 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 5 .   ? 37.934 -4.698  6.869  1.00 30.56 ? 479 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 5 .   ? 2.570  -1.708  22.774 1.00 29.32 ? 480 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 5 .   ? 5.951  11.396  29.667 1.00 34.71 ? 481 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 5 .   ? 19.688 12.181  26.431 1.00 40.41 ? 482 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 5 .   ? 4.165  -6.829  23.506 1.00 38.42 ? 483 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 5 .   ? 26.443 0.619   20.309 1.00 45.81 ? 484 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 5 .   ? 6.234  14.227  29.831 1.00 50.25 ? 485 HOH   A O   1 
HETATM 2392 O  O   . HOH   G 5 .   ? 36.421 -0.481  17.722 1.00 46.88 ? 486 HOH   A O   1 
HETATM 2393 O  O   . HOH   G 5 .   ? 6.988  16.221  28.315 1.00 47.62 ? 487 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 38.541 -7.413  7.146  1.00 23.71 ? 301 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 31.398 -18.013 -0.068 1.00 41.94 ? 302 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 7.389  -29.786 21.361 1.00 38.26 ? 303 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 17.835 -33.331 24.120 1.00 38.37 ? 304 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 10.506 -20.143 29.103 1.00 37.67 ? 305 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 38.910 -18.913 21.529 1.00 31.05 ? 306 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 29.454 -26.017 -1.163 1.00 27.29 ? 307 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 15.148 -18.814 32.120 1.00 44.15 ? 308 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 20.025 -4.298  20.295 1.00 25.77 ? 309 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 26.690 -5.607  10.201 1.00 26.37 ? 310 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 18.076 -5.923  24.102 1.00 32.83 ? 311 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 24.233 -8.165  9.622  1.00 25.26 ? 312 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 6.740  -18.776 25.233 1.00 46.33 ? 313 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 20.985 -18.799 12.985 1.00 17.24 ? 314 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 26.886 -15.402 30.840 1.00 30.27 ? 315 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 31.123 -18.389 26.936 1.00 20.98 ? 316 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 38.608 -16.926 10.193 1.00 37.99 ? 317 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 37.268 -32.232 10.897 1.00 25.37 ? 318 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 23.333 -6.005  21.200 1.00 23.35 ? 319 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 37.327 -18.955 28.279 1.00 29.28 ? 320 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 24.844 -5.973  15.354 1.00 25.76 ? 321 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 15.127 -23.689 12.558 1.00 38.00 ? 322 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 22.049 -26.390 34.536 1.00 28.71 ? 323 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 18.022 -27.533 16.630 1.00 21.56 ? 324 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 24.761 -9.616  27.057 1.00 42.06 ? 325 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 32.232 -10.494 13.856 1.00 20.98 ? 326 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 37.265 -10.506 4.834  1.00 37.27 ? 327 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 21.457 -24.853 4.309  1.00 49.58 ? 328 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 18.988 -8.776  13.948 1.00 27.07 ? 329 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 40.099 -29.898 11.917 1.00 30.44 ? 330 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 19.413 -32.291 19.895 1.00 48.35 ? 331 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 31.360 -21.725 28.417 1.00 17.55 ? 332 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 31.099 -23.986 -1.299 1.00 23.92 ? 333 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 10.276 -8.866  24.091 1.00 30.01 ? 334 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 21.817 -28.469 4.937  1.00 30.15 ? 335 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 23.740 -33.689 29.077 1.00 32.57 ? 336 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 36.519 -26.517 34.304 1.00 31.41 ? 337 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 10.828 -16.801 12.637 1.00 35.89 ? 338 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 11.023 -6.486  13.339 1.00 30.43 ? 339 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 17.777 -24.290 8.694  1.00 48.30 ? 340 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 40.658 -27.567 15.122 1.00 15.62 ? 341 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 9.459  -7.963  21.444 1.00 38.11 ? 342 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 36.292 -17.859 11.514 1.00 38.00 ? 343 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 26.144 -25.338 8.931  1.00 17.42 ? 344 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 31.745 -35.328 31.825 1.00 41.69 ? 345 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 10.506 -17.616 18.501 1.00 32.63 ? 346 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 7.348  -9.334  22.992 1.00 39.87 ? 347 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 14.263 -24.336 29.514 1.00 32.37 ? 348 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 24.975 -15.885 7.438  1.00 23.21 ? 349 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 4.654  -10.311 20.208 1.00 35.17 ? 350 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 35.928 -28.751 2.868  1.00 45.73 ? 351 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 10.700 -16.759 15.359 1.00 37.00 ? 352 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 41.917 -12.780 13.451 1.00 43.43 ? 353 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 10.513 -30.947 24.991 1.00 42.27 ? 354 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 12.240 -24.252 21.914 1.00 19.21 ? 355 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 36.464 -21.508 6.805  1.00 30.28 ? 356 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 22.922 -32.778 20.952 1.00 39.38 ? 357 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 30.206 -15.404 19.637 1.00 19.27 ? 358 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 35.370 -13.275 8.788  1.00 21.60 ? 359 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 6.163  -16.583 22.656 1.00 47.94 ? 360 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 25.816 -37.972 24.286 1.00 36.26 ? 361 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 31.162 -6.130  5.926  1.00 40.79 ? 362 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 23.258 -8.506  14.234 1.00 19.25 ? 363 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 38.995 -14.683 13.440 1.00 34.82 ? 364 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 32.815 -23.921 29.233 1.00 16.83 ? 365 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 28.507 -16.573 22.212 1.00 17.34 ? 366 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 20.820 -25.638 13.993 1.00 28.20 ? 367 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 44.643 -20.644 6.277  1.00 40.54 ? 368 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 42.876 -11.548 11.196 1.00 29.30 ? 369 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 27.508 -7.188  2.524  1.00 51.06 ? 370 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 19.412 -27.798 28.339 1.00 21.10 ? 371 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 14.697 -28.860 25.695 1.00 37.28 ? 372 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 22.363 -23.634 6.236  1.00 49.94 ? 373 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 16.402 -28.011 31.493 1.00 56.93 ? 374 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 31.168 -37.494 9.106  1.00 47.39 ? 375 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 29.984 -13.235 13.090 1.00 18.77 ? 376 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 14.952 -18.136 10.651 1.00 41.12 ? 377 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 38.746 -13.670 10.898 1.00 33.86 ? 378 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 24.332 -3.397  19.252 1.00 43.58 ? 379 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 35.854 -24.925 24.719 1.00 19.87 ? 380 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 38.140 -31.656 25.732 1.00 28.23 ? 381 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 31.520 -12.293 10.784 1.00 17.75 ? 382 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 27.105 -12.265 27.773 1.00 29.83 ? 383 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 42.042 -12.479 17.885 1.00 25.35 ? 384 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 23.475 -31.186 13.390 1.00 38.05 ? 385 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 21.912 -18.917 6.053  1.00 33.58 ? 386 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 26.448 -31.443 14.966 1.00 26.72 ? 387 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 41.587 -25.305 7.103  1.00 45.70 ? 388 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 35.513 -4.363  17.738 1.00 31.93 ? 389 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 33.202 -9.880  11.232 1.00 17.59 ? 390 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 34.317 -2.496  13.923 1.00 46.88 ? 391 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 10.984 -11.965 9.280  1.00 35.34 ? 392 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 22.557 -11.171 7.669  1.00 45.97 ? 393 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 23.033 -28.264 12.706 1.00 23.36 ? 394 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 10.373 -24.851 20.029 1.00 24.84 ? 395 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 7.013  -17.157 19.076 1.00 47.77 ? 396 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 20.607 -19.626 36.231 1.00 42.36 ? 397 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 34.841 -35.338 18.032 1.00 34.55 ? 398 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 18.951 -11.798 8.000  1.00 46.51 ? 399 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 34.724 -13.666 25.607 1.00 20.82 ? 400 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 4.066  -8.396  14.898 1.00 34.68 ? 401 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 27.121 -35.899 20.801 1.00 28.26 ? 402 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 11.862 -22.558 28.972 1.00 27.18 ? 403 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 36.675 -25.201 27.257 1.00 37.06 ? 404 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 23.284 -25.504 9.034  1.00 23.05 ? 405 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 23.092 -7.549  25.873 1.00 46.33 ? 406 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 5.382  -28.620 22.945 1.00 52.29 ? 407 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 27.012 -6.168  22.226 1.00 30.56 ? 408 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 20.673 -23.791 35.081 1.00 33.93 ? 409 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 10.298 -18.456 26.974 1.00 32.25 ? 410 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 10.054 -24.675 29.464 1.00 37.67 ? 411 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 23.031 -13.879 29.883 1.00 33.90 ? 412 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 8.988  -13.351 11.009 1.00 26.57 ? 413 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 39.239 -13.290 25.855 1.00 30.52 ? 414 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 35.770 -28.885 7.808  1.00 21.48 ? 415 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 36.409 -32.922 25.196 1.00 41.86 ? 416 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 24.779 -34.542 22.478 1.00 48.90 ? 417 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 30.560 -10.580 27.719 1.00 40.65 ? 418 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 31.584 -13.616 4.547  1.00 36.48 ? 419 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 19.033 -8.312  25.707 1.00 24.30 ? 420 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 22.890 -33.583 5.440  1.00 37.62 ? 421 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 43.525 -26.163 23.648 1.00 25.51 ? 422 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 36.990 -16.293 12.504 1.00 32.86 ? 423 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 30.389 -18.188 8.425  1.00 30.52 ? 424 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 36.977 -29.537 10.040 1.00 29.12 ? 425 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 28.825 -36.591 7.872  1.00 24.64 ? 426 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 33.242 -30.710 31.713 1.00 21.28 ? 427 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 38.055 -20.711 4.671  1.00 34.52 ? 428 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 26.175 -31.206 30.889 1.00 18.26 ? 429 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 17.353 -25.356 13.018 1.00 26.86 ? 430 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 6.821  -22.733 18.594 1.00 35.16 ? 431 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 30.719 -16.324 30.489 1.00 33.32 ? 432 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 40.099 -30.241 14.518 1.00 21.40 ? 433 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 42.382 -12.284 20.352 1.00 48.47 ? 434 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 33.359 -34.245 24.044 1.00 47.25 ? 435 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 35.707 -30.380 33.681 1.00 42.42 ? 436 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 16.579 -20.634 11.704 1.00 28.83 ? 437 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 35.398 -14.017 6.101  1.00 34.43 ? 438 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 15.558 -29.830 17.809 1.00 54.19 ? 439 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 37.447 -14.653 9.626  1.00 33.98 ? 440 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 37.264 -31.458 29.194 1.00 43.35 ? 441 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? 18.969 -19.045 11.061 1.00 21.75 ? 442 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? 32.961 -14.491 9.484  1.00 18.06 ? 443 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? 6.713  -20.103 18.423 1.00 30.68 ? 444 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? 20.654 -32.293 22.405 1.00 32.44 ? 445 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? 33.541 -20.726 -1.921 1.00 39.55 ? 446 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? 3.574  -22.064 25.845 1.00 53.51 ? 447 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? 23.903 -17.754 33.496 1.00 24.95 ? 448 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? 31.637 -15.877 7.241  1.00 34.94 ? 449 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? 34.401 -15.857 27.321 1.00 38.16 ? 450 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? 44.220 -18.908 4.323  1.00 51.43 ? 451 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? 34.374 -32.068 29.487 1.00 26.54 ? 452 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 5 .   ? 43.810 -25.863 26.111 1.00 37.88 ? 453 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 5 .   ? 24.160 -15.899 31.622 1.00 31.29 ? 454 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 5 .   ? 26.292 -35.732 7.482  1.00 27.57 ? 455 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 5 .   ? 21.613 -17.585 34.888 1.00 29.33 ? 456 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 5 .   ? 10.612 -27.072 18.512 1.00 32.90 ? 457 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 5 .   ? 21.506 -27.031 10.511 1.00 32.46 ? 458 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 5 .   ? 14.429 -27.080 29.281 1.00 53.81 ? 459 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 5 .   ? 16.496 -27.549 14.453 1.00 38.09 ? 460 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 5 .   ? 34.132 -11.501 27.052 1.00 47.21 ? 461 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 5 .   ? 18.138 -17.573 8.584  1.00 45.27 ? 462 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 5 .   ? 34.143 -34.512 30.432 1.00 51.55 ? 463 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 5 .   ? 25.530 -13.328 29.824 1.00 41.56 ? 464 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 5 .   ? 32.913 -19.640 28.994 1.00 28.82 ? 465 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 5 .   ? 27.563 -4.252  8.159  1.00 41.11 ? 466 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 5 .   ? 43.353 -21.306 3.808  1.00 41.78 ? 467 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 5 .   ? 28.478 -12.631 30.482 1.00 46.59 ? 468 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 5 .   ? 18.664 -26.090 10.571 1.00 39.54 ? 469 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 5 .   ? 43.677 -28.829 23.161 1.00 29.76 ? 470 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 5 .   ? 41.741 -15.483 13.492 1.00 37.84 ? 471 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 5 .   ? 10.231 -21.185 16.617 1.00 36.00 ? 472 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 5 .   ? 17.113 -28.903 28.977 1.00 38.28 ? 473 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 5 .   ? 27.636 -15.621 33.767 1.00 43.55 ? 474 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 5 .   ? 9.438  -23.312 17.916 1.00 32.16 ? 475 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 5 .   ? 35.461 -23.360 29.039 1.00 33.44 ? 476 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 5 .   ? 3.322  -8.712  21.931 1.00 42.99 ? 477 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 5 .   ? 3.731  -9.790  17.143 1.00 41.26 ? 478 HOH   C O   1 
HETATM 2572 O  O   . HOH   H 5 .   ? 20.085 -15.224 34.911 1.00 37.50 ? 479 HOH   C O   1 
HETATM 2573 O  O   . HOH   H 5 .   ? 13.682 -28.063 14.696 1.00 48.81 ? 480 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   ? 0.2439 0.2250 0.2155 0.0010  -0.0100 -0.0111 7   SER   A N   
2    C  CA  . SER   A 1   ? 0.2474 0.2289 0.2242 0.0020  -0.0125 -0.0097 7   SER   A CA  
3    C  C   . SER   A 1   ? 0.2431 0.2255 0.2243 0.0043  -0.0136 -0.0062 7   SER   A C   
4    O  O   . SER   A 1   ? 0.2462 0.2285 0.2255 0.0046  -0.0134 -0.0045 7   SER   A O   
5    C  CB  . SER   A 1   ? 0.2905 0.2739 0.2644 -0.0012 -0.0160 -0.0094 7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.3130 0.2987 0.2843 -0.0022 -0.0190 -0.0057 7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.2216 0.2047 0.2085 0.0056  -0.0144 -0.0057 8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.2071 0.1907 0.1986 0.0075  -0.0146 -0.0036 8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.2039 0.1880 0.2004 0.0085  -0.0131 -0.0045 8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.2104 0.1940 0.2067 0.0081  -0.0116 -0.0060 8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.1829 0.1681 0.1843 0.0096  -0.0131 -0.0036 9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.1866 0.1731 0.1920 0.0097  -0.0112 -0.0048 9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.1833 0.1695 0.1916 0.0106  -0.0092 -0.0051 9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.1927 0.1771 0.2014 0.0115  -0.0097 -0.0040 9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.1948 0.1843 0.2048 0.0094  -0.0127 -0.0049 9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1731 0.1606 0.1828 0.0096  -0.0067 -0.0066 10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1686 0.1560 0.1810 0.0095  -0.0038 -0.0082 10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1737 0.1644 0.1931 0.0101  -0.0031 -0.0092 10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1795 0.1730 0.1994 0.0088  -0.0035 -0.0093 10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1830 0.1712 0.1914 0.0068  -0.0013 -0.0093 10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.2026 0.1894 0.2054 0.0061  -0.0023 -0.0077 10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.1810 0.1688 0.1911 0.0057  0.0023  -0.0121 10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.2054 0.1948 0.2051 0.0031  -0.0011 -0.0072 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1701 0.1604 0.1959 0.0120  -0.0018 -0.0100 11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.1747 0.1692 0.2093 0.0129  -0.0005 -0.0111 11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.1900 0.1840 0.2272 0.0122  0.0050  -0.0152 11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.1967 0.1871 0.2376 0.0141  0.0067  -0.0161 11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.1733 0.1686 0.2156 0.0161  -0.0037 -0.0083 11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.1783 0.1752 0.2172 0.0155  -0.0088 -0.0051 11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.1846 0.1861 0.2252 0.0141  -0.0102 -0.0050 11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.1907 0.1841 0.2233 0.0154  -0.0117 -0.0027 11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.1952 0.1975 0.2317 0.0126  -0.0144 -0.0030 11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2016 0.1963 0.2298 0.0139  -0.0156 -0.0008 11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2088 0.2076 0.2387 0.0124  -0.0168 -0.0013 11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.2415 0.2412 0.2665 0.0101  -0.0202 -0.0004 11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.1868 0.1840 0.2212 0.0088  0.0079  -0.0176 12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.1943 0.1919 0.2289 0.0065  0.0136  -0.0222 12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2099 0.2136 0.2502 0.0054  0.0163  -0.0242 12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2068 0.2141 0.2449 0.0035  0.0142  -0.0222 12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2088 0.2053 0.2325 0.0018  0.0146  -0.0229 12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2150 0.2144 0.2330 -0.0004 0.0113  -0.0194 12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2194 0.2172 0.2417 -0.0021 0.0207  -0.0282 12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2139 0.2187 0.2630 0.0068  0.0212  -0.0282 13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2046 0.2165 0.2608 0.0058  0.0245  -0.0304 13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2072 0.2235 0.2687 0.0078  0.0194  -0.0260 13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.1990 0.2135 0.2650 0.0118  0.0150  -0.0225 13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.1939 0.2157 0.2534 0.0042  0.0195  -0.0257 14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.1846 0.2101 0.2476 0.0048  0.0146  -0.0218 14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.1842 0.2062 0.2362 0.0022  0.0101  -0.0185 14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.1951 0.2201 0.2468 0.0000  0.0079  -0.0167 14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2013 0.2352 0.2724 0.0031  0.0173  -0.0233 14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.2456 0.2837 0.3316 0.0074  0.0204  -0.0253 14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.2744 0.3160 0.3700 0.0107  0.0167  -0.0222 14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.2419 0.2798 0.3304 0.0072  0.0274  -0.0305 14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.1786 0.1944 0.2230 0.0028  0.0087  -0.0177 15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1817 0.1940 0.2174 0.0012  0.0051  -0.0148 15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1886 0.1961 0.2224 0.0044  0.0013  -0.0128 15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1884 0.1935 0.2239 0.0069  0.0019  -0.0134 15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.1814 0.1921 0.2088 -0.0022 0.0072  -0.0152 15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.1980 0.2137 0.2245 -0.0069 0.0108  -0.0167 15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2160 0.2351 0.2436 -0.0094 0.0097  -0.0149 15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2093 0.2264 0.2334 -0.0095 0.0154  -0.0201 15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2239 0.2480 0.2500 -0.0145 0.0130  -0.0158 15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2192 0.2416 0.2411 -0.0148 0.0190  -0.0216 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2391 0.2652 0.2619 -0.0173 0.0176  -0.0191 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.2841 0.3159 0.3042 -0.0233 0.0211  -0.0201 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1743 0.1800 0.2042 0.0038  -0.0022 -0.0105 16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1635 0.1649 0.1897 0.0056  -0.0054 -0.0089 16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1725 0.1705 0.1918 0.0040  -0.0055 -0.0081 16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1830 0.1813 0.2017 0.0019  -0.0058 -0.0074 16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1560 0.1589 0.1845 0.0057  -0.0090 -0.0078 16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.1750 0.1738 0.1977 0.0059  -0.0118 -0.0068 16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.1968 0.1980 0.2212 0.0050  -0.0155 -0.0059 16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2044 0.2020 0.2223 0.0029  -0.0168 -0.0067 16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2367 0.2317 0.2491 0.0029  -0.0183 -0.0066 16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2366 0.2320 0.2490 0.0048  -0.0191 -0.0049 16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2305 0.2220 0.2376 0.0007  -0.0184 -0.0084 16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1589 0.1540 0.1740 0.0049  -0.0050 -0.0078 17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1653 0.1583 0.1757 0.0040  -0.0051 -0.0064 17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1821 0.1718 0.1902 0.0057  -0.0069 -0.0059 17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1769 0.1656 0.1839 0.0071  -0.0074 -0.0062 17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1687 0.1622 0.1763 0.0029  -0.0031 -0.0064 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1820 0.1753 0.1867 0.0017  -0.0037 -0.0038 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.1751 0.1720 0.1843 0.0007  -0.0004 -0.0082 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1775 0.1653 0.1849 0.0053  -0.0077 -0.0054 18  VAL   A N   
86   C  CA  A VAL   A 12  ? 0.1689 0.1536 0.1737 0.0063  -0.0085 -0.0061 18  VAL   A CA  
87   C  CA  B VAL   A 12  ? 0.1955 0.1801 0.2004 0.0062  -0.0086 -0.0061 18  VAL   A CA  
88   C  C   . VAL   A 12  ? 0.1854 0.1678 0.1901 0.0066  -0.0074 -0.0051 18  VAL   A C   
89   O  O   . VAL   A 12  ? 0.1953 0.1783 0.2021 0.0057  -0.0070 -0.0031 18  VAL   A O   
90   C  CB  A VAL   A 12  ? 0.1518 0.1359 0.1569 0.0053  -0.0101 -0.0075 18  VAL   A CB  
91   C  CB  B VAL   A 12  ? 0.2267 0.2106 0.2324 0.0049  -0.0101 -0.0075 18  VAL   A CB  
92   C  CG1 A VAL   A 12  ? 0.1431 0.1301 0.1494 0.0056  -0.0119 -0.0074 18  VAL   A CG1 
93   C  CG1 B VAL   A 12  ? 0.2323 0.2142 0.2341 0.0049  -0.0110 -0.0091 18  VAL   A CG1 
94   C  CG2 A VAL   A 12  ? 0.1311 0.1148 0.1388 0.0035  -0.0101 -0.0075 18  VAL   A CG2 
95   C  CG2 B VAL   A 12  ? 0.2516 0.2394 0.2609 0.0041  -0.0112 -0.0075 18  VAL   A CG2 
96   N  N   . ASN   A 13  ? 0.1774 0.1572 0.1801 0.0077  -0.0069 -0.0062 19  ASN   A N   
97   C  CA  . ASN   A 13  ? 0.1760 0.1535 0.1809 0.0087  -0.0054 -0.0056 19  ASN   A CA  
98   C  C   . ASN   A 13  ? 0.1783 0.1525 0.1856 0.0075  -0.0055 -0.0065 19  ASN   A C   
99   O  O   . ASN   A 13  ? 0.1912 0.1640 0.1963 0.0060  -0.0063 -0.0092 19  ASN   A O   
100  C  CB  . ASN   A 13  ? 0.1788 0.1545 0.1814 0.0097  -0.0040 -0.0079 19  ASN   A CB  
101  C  CG  . ASN   A 13  ? 0.1996 0.1783 0.1999 0.0104  -0.0038 -0.0070 19  ASN   A CG  
102  O  OD1 . ASN   A 13  ? 0.2123 0.1918 0.2086 0.0097  -0.0048 -0.0078 19  ASN   A OD1 
103  N  ND2 . ASN   A 13  ? 0.1834 0.1639 0.1866 0.0116  -0.0027 -0.0047 19  ASN   A ND2 
104  N  N   . ARG   A 14  ? 0.1655 0.1384 0.1771 0.0076  -0.0051 -0.0038 20  ARG   A N   
105  C  CA  . ARG   A 14  ? 0.1739 0.1426 0.1879 0.0060  -0.0051 -0.0043 20  ARG   A CA  
106  C  C   . ARG   A 14  ? 0.2032 0.1665 0.2162 0.0061  -0.0036 -0.0089 20  ARG   A C   
107  O  O   . ARG   A 14  ? 0.2225 0.1832 0.2342 0.0037  -0.0040 -0.0113 20  ARG   A O   
108  C  CB  . ARG   A 14  ? 0.1881 0.1555 0.2076 0.0065  -0.0050 0.0003  20  ARG   A CB  
109  C  CG  . ARG   A 14  ? 0.2059 0.1689 0.2286 0.0044  -0.0052 0.0011  20  ARG   A CG  
110  C  CD  . ARG   A 14  ? 0.2216 0.1829 0.2505 0.0052  -0.0054 0.0068  20  ARG   A CD  
111  N  NE  . ARG   A 14  ? 0.2731 0.2300 0.3052 0.0027  -0.0060 0.0088  20  ARG   A NE  
112  C  CZ  . ARG   A 14  ? 0.2912 0.2397 0.3270 0.0031  -0.0044 0.0067  20  ARG   A CZ  
113  N  NH1 . ARG   A 14  ? 0.2664 0.2104 0.3026 0.0056  -0.0018 0.0016  20  ARG   A NH1 
114  N  NH2 . ARG   A 14  ? 0.2780 0.2222 0.3169 0.0004  -0.0051 0.0093  20  ARG   A NH2 
115  N  N   . HIS   A 15  ? 0.1976 0.1595 0.2106 0.0085  -0.0014 -0.0103 21  HIS   A N   
116  C  CA  . HIS   A 15  ? 0.2044 0.1610 0.2159 0.0080  0.0012  -0.0156 21  HIS   A CA  
117  C  C   . HIS   A 15  ? 0.2218 0.1798 0.2255 0.0050  0.0000  -0.0195 21  HIS   A C   
118  O  O   . HIS   A 15  ? 0.2386 0.1925 0.2393 0.0029  0.0017  -0.0244 21  HIS   A O   
119  C  CB  . HIS   A 15  ? 0.2154 0.1708 0.2302 0.0112  0.0046  -0.0165 21  HIS   A CB  
120  C  CG  . HIS   A 15  ? 0.2099 0.1704 0.2201 0.0118  0.0048  -0.0170 21  HIS   A CG  
121  N  ND1 . HIS   A 15  ? 0.2150 0.1811 0.2267 0.0133  0.0033  -0.0124 21  HIS   A ND1 
122  C  CD2 . HIS   A 15  ? 0.2208 0.1814 0.2248 0.0104  0.0063  -0.0214 21  HIS   A CD2 
123  C  CE1 . HIS   A 15  ? 0.2210 0.1898 0.2277 0.0131  0.0040  -0.0141 21  HIS   A CE1 
124  N  NE2 . HIS   A 15  ? 0.2274 0.1933 0.2296 0.0114  0.0059  -0.0192 21  HIS   A NE2 
125  N  N   . LEU   A 16  ? 0.2117 0.1755 0.2125 0.0044  -0.0030 -0.0173 22  LEU   A N   
126  C  CA  . LEU   A 16  ? 0.2169 0.1832 0.2117 0.0017  -0.0052 -0.0192 22  LEU   A CA  
127  C  C   . LEU   A 16  ? 0.2221 0.1913 0.2183 -0.0003 -0.0083 -0.0177 22  LEU   A C   
128  O  O   . LEU   A 16  ? 0.2284 0.2013 0.2218 -0.0022 -0.0110 -0.0177 22  LEU   A O   
129  C  CB  . LEU   A 16  ? 0.2228 0.1931 0.2144 0.0030  -0.0059 -0.0177 22  LEU   A CB  
130  C  CG  . LEU   A 16  ? 0.2446 0.2136 0.2346 0.0044  -0.0028 -0.0193 22  LEU   A CG  
131  C  CD1 . LEU   A 16  ? 0.2501 0.2230 0.2365 0.0047  -0.0040 -0.0173 22  LEU   A CD1 
132  C  CD2 . LEU   A 16  ? 0.2567 0.2221 0.2421 0.0017  -0.0004 -0.0247 22  LEU   A CD2 
133  N  N   . ALA   A 17  ? 0.2128 0.1812 0.2140 -0.0001 -0.0082 -0.0158 23  ALA   A N   
134  C  CA  . ALA   A 17  ? 0.2110 0.1829 0.2143 -0.0023 -0.0105 -0.0146 23  ALA   A CA  
135  C  C   . ALA   A 17  ? 0.2303 0.2013 0.2313 -0.0062 -0.0118 -0.0176 23  ALA   A C   
136  O  O   . ALA   A 17  ? 0.2413 0.2063 0.2400 -0.0079 -0.0100 -0.0210 23  ALA   A O   
137  C  CB  . ALA   A 17  ? 0.2076 0.1787 0.2157 -0.0022 -0.0097 -0.0120 23  ALA   A CB  
138  N  N   . THR   A 18  ? 0.2257 0.2027 0.2274 -0.0079 -0.0148 -0.0165 24  THR   A N   
139  C  CA  . THR   A 18  ? 0.2321 0.2106 0.2317 -0.0125 -0.0172 -0.0185 24  THR   A CA  
140  C  C   . THR   A 18  ? 0.2257 0.2038 0.2296 -0.0153 -0.0172 -0.0184 24  THR   A C   
141  O  O   . THR   A 18  ? 0.2205 0.1986 0.2289 -0.0135 -0.0158 -0.0161 24  THR   A O   
142  C  CB  . THR   A 18  ? 0.2514 0.2381 0.2518 -0.0128 -0.0210 -0.0161 24  THR   A CB  
143  O  OG1 . THR   A 18  ? 0.2583 0.2503 0.2663 -0.0109 -0.0214 -0.0131 24  THR   A OG1 
144  C  CG2 . THR   A 18  ? 0.2645 0.2519 0.2612 -0.0104 -0.0214 -0.0151 24  THR   A CG2 
145  N  N   . HIS   A 19  ? 0.2251 0.2036 0.2271 -0.0204 -0.0190 -0.0206 25  HIS   A N   
146  C  CA  . HIS   A 19  ? 0.2391 0.2182 0.2452 -0.0238 -0.0194 -0.0203 25  HIS   A CA  
147  C  C   . HIS   A 19  ? 0.2348 0.2230 0.2478 -0.0222 -0.0209 -0.0163 25  HIS   A C   
148  O  O   . HIS   A 19  ? 0.2326 0.2206 0.2496 -0.0226 -0.0194 -0.0148 25  HIS   A O   
149  C  CB  . HIS   A 19  ? 0.2775 0.2569 0.2800 -0.0304 -0.0217 -0.0234 25  HIS   A CB  
150  C  CG  . HIS   A 19  ? 0.3777 0.3607 0.3852 -0.0344 -0.0230 -0.0223 25  HIS   A CG  
151  N  ND1 . HIS   A 19  ? 0.4323 0.4076 0.4411 -0.0364 -0.0205 -0.0232 25  HIS   A ND1 
152  C  CD2 . HIS   A 19  ? 0.4119 0.4056 0.4242 -0.0365 -0.0264 -0.0197 25  HIS   A CD2 
153  C  CE1 . HIS   A 19  ? 0.4388 0.4202 0.4519 -0.0404 -0.0224 -0.0217 25  HIS   A CE1 
154  N  NE2 . HIS   A 19  ? 0.4443 0.4373 0.4600 -0.0405 -0.0259 -0.0197 25  HIS   A NE2 
155  N  N   . ASN   A 20  ? 0.2202 0.2162 0.2349 -0.0204 -0.0234 -0.0144 26  ASN   A N   
156  C  CA  . ASN   A 20  ? 0.2221 0.2264 0.2449 -0.0184 -0.0237 -0.0114 26  ASN   A CA  
157  C  C   . ASN   A 20  ? 0.2019 0.2037 0.2261 -0.0147 -0.0201 -0.0104 26  ASN   A C   
158  O  O   . ASN   A 20  ? 0.2067 0.2128 0.2363 -0.0150 -0.0187 -0.0092 26  ASN   A O   
159  C  CB  . ASN   A 20  ? 0.2423 0.2541 0.2682 -0.0164 -0.0267 -0.0092 26  ASN   A CB  
160  C  CG  . ASN   A 20  ? 0.3314 0.3517 0.3676 -0.0145 -0.0263 -0.0069 26  ASN   A CG  
161  O  OD1 . ASN   A 20  ? 0.3704 0.3970 0.4121 -0.0176 -0.0276 -0.0064 26  ASN   A OD1 
162  N  ND2 . ASN   A 20  ? 0.3546 0.3751 0.3937 -0.0098 -0.0239 -0.0060 26  ASN   A ND2 
163  N  N   . ASP   A 21  ? 0.1933 0.1889 0.2128 -0.0118 -0.0184 -0.0109 27  ASP   A N   
164  C  CA  . ASP   A 21  ? 0.1849 0.1789 0.2052 -0.0092 -0.0155 -0.0096 27  ASP   A CA  
165  C  C   . ASP   A 21  ? 0.1985 0.1895 0.2198 -0.0119 -0.0140 -0.0088 27  ASP   A C   
166  O  O   . ASP   A 21  ? 0.2012 0.1956 0.2252 -0.0122 -0.0125 -0.0071 27  ASP   A O   
167  C  CB  . ASP   A 21  ? 0.1926 0.1811 0.2082 -0.0062 -0.0144 -0.0099 27  ASP   A CB  
168  C  CG  . ASP   A 21  ? 0.2255 0.2166 0.2401 -0.0035 -0.0154 -0.0096 27  ASP   A CG  
169  O  OD1 . ASP   A 21  ? 0.2004 0.1971 0.2195 -0.0023 -0.0156 -0.0084 27  ASP   A OD1 
170  O  OD2 . ASP   A 21  ? 0.2188 0.2063 0.2286 -0.0028 -0.0155 -0.0106 27  ASP   A OD2 
171  N  N   . TRP   A 22  ? 0.2041 0.1885 0.2230 -0.0142 -0.0142 -0.0102 28  TRP   A N   
172  C  CA  . TRP   A 22  ? 0.2135 0.1938 0.2339 -0.0168 -0.0131 -0.0089 28  TRP   A CA  
173  C  C   . TRP   A 22  ? 0.2194 0.2057 0.2437 -0.0209 -0.0138 -0.0080 28  TRP   A C   
174  O  O   . TRP   A 22  ? 0.2216 0.2079 0.2478 -0.0228 -0.0127 -0.0055 28  TRP   A O   
175  C  CB  . TRP   A 22  ? 0.2227 0.1933 0.2407 -0.0183 -0.0126 -0.0113 28  TRP   A CB  
176  C  CG  . TRP   A 22  ? 0.2299 0.1943 0.2465 -0.0144 -0.0107 -0.0113 28  TRP   A CG  
177  C  CD1 . TRP   A 22  ? 0.2432 0.2052 0.2563 -0.0122 -0.0101 -0.0142 28  TRP   A CD1 
178  C  CD2 . TRP   A 22  ? 0.2320 0.1931 0.2514 -0.0125 -0.0093 -0.0075 28  TRP   A CD2 
179  N  NE1 . TRP   A 22  ? 0.2431 0.2003 0.2574 -0.0088 -0.0080 -0.0130 28  TRP   A NE1 
180  C  CE2 . TRP   A 22  ? 0.2444 0.2014 0.2630 -0.0087 -0.0078 -0.0085 28  TRP   A CE2 
181  C  CE3 . TRP   A 22  ? 0.2414 0.2035 0.2639 -0.0141 -0.0094 -0.0029 28  TRP   A CE3 
182  C  CZ2 . TRP   A 22  ? 0.2526 0.2067 0.2746 -0.0061 -0.0067 -0.0047 28  TRP   A CZ2 
183  C  CZ3 . TRP   A 22  ? 0.2497 0.2089 0.2745 -0.0120 -0.0087 0.0011  28  TRP   A CZ3 
184  C  CH2 . TRP   A 22  ? 0.2525 0.2078 0.2777 -0.0079 -0.0075 0.0005  28  TRP   A CH2 
185  N  N   . ALA   A 23  ? 0.2115 0.2039 0.2374 -0.0224 -0.0159 -0.0096 29  ALA   A N   
186  C  CA  . ALA   A 23  ? 0.2227 0.2226 0.2537 -0.0262 -0.0166 -0.0088 29  ALA   A CA  
187  C  C   . ALA   A 23  ? 0.2274 0.2360 0.2633 -0.0242 -0.0149 -0.0071 29  ALA   A C   
188  O  O   . ALA   A 23  ? 0.2311 0.2463 0.2719 -0.0273 -0.0143 -0.0064 29  ALA   A O   
189  C  CB  . ALA   A 23  ? 0.2385 0.2430 0.2704 -0.0287 -0.0199 -0.0104 29  ALA   A CB  
190  N  N   . ASN   A 24  ? 0.2124 0.2209 0.2472 -0.0196 -0.0136 -0.0069 30  ASN   A N   
191  C  CA  . ASN   A 24  ? 0.2066 0.2220 0.2455 -0.0178 -0.0111 -0.0065 30  ASN   A CA  
192  C  C   . ASN   A 24  ? 0.2041 0.2150 0.2382 -0.0162 -0.0088 -0.0055 30  ASN   A C   
193  O  O   . ASN   A 24  ? 0.2017 0.2146 0.2360 -0.0133 -0.0072 -0.0061 30  ASN   A O   
194  C  CB  . ASN   A 24  ? 0.2100 0.2307 0.2533 -0.0142 -0.0122 -0.0073 30  ASN   A CB  
195  C  CG  . ASN   A 24  ? 0.2534 0.2809 0.3028 -0.0163 -0.0149 -0.0071 30  ASN   A CG  
196  O  OD1 . ASN   A 24  ? 0.2574 0.2927 0.3138 -0.0179 -0.0134 -0.0070 30  ASN   A OD1 
197  N  ND2 . ASN   A 24  ? 0.2521 0.2775 0.2987 -0.0172 -0.0187 -0.0072 30  ASN   A ND2 
198  N  N   . LEU   A 25  ? 0.2012 0.2060 0.2316 -0.0183 -0.0088 -0.0037 31  LEU   A N   
199  C  CA  . LEU   A 25  ? 0.1981 0.1989 0.2245 -0.0171 -0.0077 -0.0017 31  LEU   A CA  
200  C  C   . LEU   A 25  ? 0.2064 0.2128 0.2326 -0.0190 -0.0051 -0.0005 31  LEU   A C   
201  O  O   . LEU   A 25  ? 0.2219 0.2325 0.2498 -0.0232 -0.0041 0.0005  31  LEU   A O   
202  C  CB  . LEU   A 25  ? 0.1912 0.1842 0.2161 -0.0189 -0.0087 0.0007  31  LEU   A CB  
203  C  CG  . LEU   A 25  ? 0.2185 0.2077 0.2410 -0.0174 -0.0083 0.0040  31  LEU   A CG  
204  C  CD1 . LEU   A 25  ? 0.2259 0.2130 0.2464 -0.0126 -0.0085 0.0021  31  LEU   A CD1 
205  C  CD2 . LEU   A 25  ? 0.2503 0.2318 0.2738 -0.0187 -0.0092 0.0069  31  LEU   A CD2 
206  N  N   . VAL   A 26  ? 0.1917 0.1982 0.2151 -0.0168 -0.0040 -0.0005 32  VAL   A N   
207  C  CA  . VAL   A 26  ? 0.1964 0.2078 0.2176 -0.0196 -0.0014 0.0003  32  VAL   A CA  
208  C  C   . VAL   A 26  ? 0.2088 0.2165 0.2256 -0.0211 -0.0027 0.0049  32  VAL   A C   
209  O  O   . VAL   A 26  ? 0.2233 0.2337 0.2382 -0.0258 -0.0022 0.0081  32  VAL   A O   
210  C  CB  . VAL   A 26  ? 0.2011 0.2155 0.2223 -0.0171 0.0010  -0.0032 32  VAL   A CB  
211  C  CG1 . VAL   A 26  ? 0.2082 0.2267 0.2252 -0.0209 0.0040  -0.0030 32  VAL   A CG1 
212  C  CG2 . VAL   A 26  ? 0.2168 0.2356 0.2446 -0.0154 0.0022  -0.0067 32  VAL   A CG2 
213  N  N   . TRP   A 27  ? 0.1935 0.1958 0.2092 -0.0172 -0.0044 0.0057  33  TRP   A N   
214  C  CA  . TRP   A 27  ? 0.2108 0.2107 0.2244 -0.0178 -0.0057 0.0105  33  TRP   A CA  
215  C  C   . TRP   A 27  ? 0.2140 0.2076 0.2289 -0.0130 -0.0072 0.0103  33  TRP   A C   
216  O  O   . TRP   A 27  ? 0.2059 0.1986 0.2205 -0.0098 -0.0068 0.0064  33  TRP   A O   
217  C  CB  . TRP   A 27  ? 0.2196 0.2248 0.2289 -0.0196 -0.0044 0.0109  33  TRP   A CB  
218  C  CG  . TRP   A 27  ? 0.2346 0.2393 0.2421 -0.0199 -0.0063 0.0160  33  TRP   A CG  
219  C  CD1 . TRP   A 27  ? 0.2603 0.2669 0.2669 -0.0240 -0.0080 0.0224  33  TRP   A CD1 
220  C  CD2 . TRP   A 27  ? 0.2306 0.2340 0.2374 -0.0165 -0.0069 0.0158  33  TRP   A CD2 
221  N  NE1 . TRP   A 27  ? 0.2692 0.2763 0.2755 -0.0230 -0.0099 0.0264  33  TRP   A NE1 
222  C  CE2 . TRP   A 27  ? 0.2505 0.2556 0.2570 -0.0183 -0.0091 0.0221  33  TRP   A CE2 
223  C  CE3 . TRP   A 27  ? 0.2393 0.2406 0.2461 -0.0123 -0.0061 0.0114  33  TRP   A CE3 
224  C  CZ2 . TRP   A 27  ? 0.2491 0.2548 0.2557 -0.0161 -0.0102 0.0237  33  TRP   A CZ2 
225  C  CZ3 . TRP   A 27  ? 0.2457 0.2468 0.2517 -0.0104 -0.0070 0.0128  33  TRP   A CZ3 
226  C  CH2 . TRP   A 27  ? 0.2445 0.2480 0.2506 -0.0122 -0.0088 0.0187  33  TRP   A CH2 
227  N  N   . GLU   A 28  ? 0.2118 0.2011 0.2286 -0.0126 -0.0087 0.0146  34  GLU   A N   
228  C  CA  . GLU   A 28  ? 0.2070 0.1909 0.2257 -0.0081 -0.0091 0.0141  34  GLU   A CA  
229  C  C   . GLU   A 28  ? 0.2179 0.2012 0.2392 -0.0077 -0.0103 0.0202  34  GLU   A C   
230  O  O   . GLU   A 28  ? 0.2226 0.2069 0.2452 -0.0111 -0.0116 0.0255  34  GLU   A O   
231  C  CB  . GLU   A 28  ? 0.2162 0.1933 0.2374 -0.0068 -0.0089 0.0110  34  GLU   A CB  
232  C  CG  . GLU   A 28  ? 0.2286 0.2021 0.2528 -0.0099 -0.0095 0.0137  34  GLU   A CG  
233  C  CD  . GLU   A 28  ? 0.2867 0.2541 0.3159 -0.0088 -0.0101 0.0186  34  GLU   A CD  
234  O  OE1 . GLU   A 28  ? 0.2942 0.2600 0.3256 -0.0120 -0.0110 0.0232  34  GLU   A OE1 
235  O  OE2 . GLU   A 28  ? 0.2771 0.2417 0.3086 -0.0047 -0.0095 0.0184  34  GLU   A OE2 
236  N  N   . ASP   A 29  ? 0.2052 0.1872 0.2280 -0.0039 -0.0102 0.0200  35  ASP   A N   
237  C  CA  . ASP   A 29  ? 0.2003 0.1827 0.2277 -0.0029 -0.0116 0.0264  35  ASP   A CA  
238  C  C   . ASP   A 29  ? 0.2133 0.1912 0.2452 0.0023  -0.0103 0.0243  35  ASP   A C   
239  O  O   . ASP   A 29  ? 0.2081 0.1885 0.2374 0.0041  -0.0095 0.0213  35  ASP   A O   
240  C  CB  . ASP   A 29  ? 0.2363 0.2272 0.2600 -0.0056 -0.0128 0.0299  35  ASP   A CB  
241  C  CG  . ASP   A 29  ? 0.3105 0.3042 0.3391 -0.0058 -0.0153 0.0380  35  ASP   A CG  
242  O  OD1 . ASP   A 29  ? 0.3296 0.3192 0.3658 -0.0014 -0.0153 0.0397  35  ASP   A OD1 
243  O  OD2 . ASP   A 29  ? 0.3478 0.3485 0.3730 -0.0105 -0.0172 0.0427  35  ASP   A OD2 
244  N  N   . SER   A 30  ? 0.2258 0.1967 0.2646 0.0044  -0.0098 0.0255  36  SER   A N   
245  C  CA  A SER   A 30  ? 0.2257 0.1919 0.2697 0.0092  -0.0075 0.0228  36  SER   A CA  
246  C  CA  B SER   A 30  ? 0.2288 0.1952 0.2725 0.0092  -0.0075 0.0226  36  SER   A CA  
247  C  C   . SER   A 30  ? 0.2232 0.1950 0.2711 0.0117  -0.0080 0.0267  36  SER   A C   
248  O  O   . SER   A 30  ? 0.2226 0.1946 0.2708 0.0147  -0.0058 0.0228  36  SER   A O   
249  C  CB  A SER   A 30  ? 0.2483 0.2054 0.3003 0.0107  -0.0063 0.0237  36  SER   A CB  
250  C  CB  B SER   A 30  ? 0.2597 0.2166 0.3107 0.0107  -0.0060 0.0226  36  SER   A CB  
251  O  OG  A SER   A 30  ? 0.2699 0.2229 0.3283 0.0154  -0.0033 0.0211  36  SER   A OG  
252  O  OG  B SER   A 30  ? 0.2931 0.2502 0.3513 0.0102  -0.0083 0.0312  36  SER   A OG  
253  N  N   . SER   A 31  ? 0.2137 0.1910 0.2647 0.0099  -0.0110 0.0349  37  SER   A N   
254  C  CA  . SER   A 31  ? 0.2170 0.2011 0.2724 0.0116  -0.0122 0.0397  37  SER   A CA  
255  C  C   . SER   A 31  ? 0.2160 0.2063 0.2632 0.0104  -0.0118 0.0357  37  SER   A C   
256  O  O   . SER   A 31  ? 0.2253 0.2202 0.2758 0.0123  -0.0118 0.0374  37  SER   A O   
257  C  CB  . SER   A 31  ? 0.2437 0.2335 0.3031 0.0087  -0.0163 0.0500  37  SER   A CB  
258  O  OG  . SER   A 31  ? 0.2982 0.2945 0.3476 0.0026  -0.0184 0.0511  37  SER   A OG  
259  N  N   . ARG   A 32  ? 0.1964 0.1868 0.2339 0.0074  -0.0113 0.0308  38  ARG   A N   
260  C  CA  . ARG   A 32  ? 0.1854 0.1800 0.2156 0.0064  -0.0106 0.0268  38  ARG   A CA  
261  C  C   . ARG   A 32  ? 0.1838 0.1733 0.2107 0.0088  -0.0080 0.0191  38  ARG   A C   
262  O  O   . ARG   A 32  ? 0.1809 0.1726 0.2026 0.0084  -0.0074 0.0161  38  ARG   A O   
263  C  CB  . ARG   A 32  ? 0.1929 0.1915 0.2154 0.0011  -0.0116 0.0267  38  ARG   A CB  
264  C  CG  . ARG   A 32  ? 0.2028 0.2083 0.2256 -0.0030 -0.0144 0.0340  38  ARG   A CG  
265  C  CD  . ARG   A 32  ? 0.2112 0.2207 0.2257 -0.0089 -0.0143 0.0327  38  ARG   A CD  
266  N  NE  . ARG   A 32  ? 0.2089 0.2205 0.2173 -0.0098 -0.0127 0.0277  38  ARG   A NE  
267  C  CZ  . ARG   A 32  ? 0.2192 0.2360 0.2209 -0.0152 -0.0124 0.0269  38  ARG   A CZ  
268  N  NH1 . ARG   A 32  ? 0.2373 0.2588 0.2364 -0.0207 -0.0138 0.0312  38  ARG   A NH1 
269  N  NH2 . ARG   A 32  ? 0.2172 0.2342 0.2143 -0.0157 -0.0105 0.0220  38  ARG   A NH2 
270  N  N   . ASP   A 33  ? 0.1639 0.1465 0.1934 0.0107  -0.0066 0.0162  39  ASP   A N   
271  C  CA  . ASP   A 33  ? 0.1638 0.1425 0.1890 0.0116  -0.0048 0.0095  39  ASP   A CA  
272  C  C   . ASP   A 33  ? 0.1680 0.1488 0.1863 0.0089  -0.0057 0.0071  39  ASP   A C   
273  O  O   . ASP   A 33  ? 0.1818 0.1623 0.1960 0.0094  -0.0051 0.0032  39  ASP   A O   
274  C  CB  . ASP   A 33  ? 0.1774 0.1564 0.2025 0.0142  -0.0027 0.0068  39  ASP   A CB  
275  C  CG  . ASP   A 33  ? 0.1955 0.1707 0.2156 0.0142  -0.0012 0.0006  39  ASP   A CG  
276  O  OD1 . ASP   A 33  ? 0.2024 0.1725 0.2226 0.0136  -0.0007 -0.0020 39  ASP   A OD1 
277  O  OD2 . ASP   A 33  ? 0.1958 0.1732 0.2116 0.0143  -0.0006 -0.0014 39  ASP   A OD2 
278  N  N   . LEU   A 34  ? 0.1647 0.1476 0.1824 0.0060  -0.0070 0.0095  40  LEU   A N   
279  C  CA  . LEU   A 34  ? 0.1646 0.1497 0.1776 0.0038  -0.0070 0.0067  40  LEU   A CA  
280  C  C   . LEU   A 34  ? 0.1785 0.1619 0.1923 0.0020  -0.0073 0.0058  40  LEU   A C   
281  O  O   . LEU   A 34  ? 0.1870 0.1689 0.2038 0.0007  -0.0079 0.0089  40  LEU   A O   
282  C  CB  . LEU   A 34  ? 0.1650 0.1558 0.1753 0.0011  -0.0073 0.0088  40  LEU   A CB  
283  C  CG  . LEU   A 34  ? 0.1819 0.1754 0.1900 0.0017  -0.0070 0.0089  40  LEU   A CG  
284  C  CD1 . LEU   A 34  ? 0.2016 0.2005 0.2064 -0.0023 -0.0071 0.0105  40  LEU   A CD1 
285  C  CD2 . LEU   A 34  ? 0.1896 0.1811 0.1952 0.0037  -0.0061 0.0044  40  LEU   A CD2 
286  N  N   . LEU   A 35  ? 0.1666 0.1509 0.1784 0.0015  -0.0072 0.0022  41  LEU   A N   
287  C  CA  . LEU   A 35  ? 0.1710 0.1557 0.1840 -0.0007 -0.0075 0.0013  41  LEU   A CA  
288  C  C   . LEU   A 35  ? 0.1820 0.1712 0.1942 -0.0012 -0.0069 -0.0009 41  LEU   A C   
289  O  O   . LEU   A 35  ? 0.1920 0.1814 0.2030 0.0009  -0.0069 -0.0028 41  LEU   A O   
290  C  CB  . LEU   A 35  ? 0.1675 0.1473 0.1813 -0.0003 -0.0080 -0.0012 41  LEU   A CB  
291  C  CG  . LEU   A 35  ? 0.1827 0.1634 0.1982 -0.0032 -0.0086 -0.0020 41  LEU   A CG  
292  C  CD1 . LEU   A 35  ? 0.1951 0.1695 0.2117 -0.0042 -0.0088 -0.0029 41  LEU   A CD1 
293  C  CD2 . LEU   A 35  ? 0.1978 0.1826 0.2131 -0.0032 -0.0094 -0.0048 41  LEU   A CD2 
294  N  N   . VAL   A 36  ? 0.1772 0.1702 0.1907 -0.0040 -0.0062 -0.0006 42  VAL   A N   
295  C  CA  . VAL   A 36  ? 0.1749 0.1724 0.1898 -0.0042 -0.0049 -0.0031 42  VAL   A CA  
296  C  C   . VAL   A 36  ? 0.1792 0.1790 0.1980 -0.0057 -0.0053 -0.0041 42  VAL   A C   
297  O  O   . VAL   A 36  ? 0.1844 0.1846 0.2037 -0.0087 -0.0052 -0.0024 42  VAL   A O   
298  C  CB  . VAL   A 36  ? 0.1734 0.1749 0.1864 -0.0067 -0.0025 -0.0028 42  VAL   A CB  
299  C  CG1 . VAL   A 36  ? 0.1906 0.1962 0.2066 -0.0066 -0.0001 -0.0063 42  VAL   A CG1 
300  C  CG2 . VAL   A 36  ? 0.1795 0.1797 0.1887 -0.0059 -0.0026 -0.0016 42  VAL   A CG2 
301  N  N   . SER   A 37  ? 0.1684 0.1701 0.1904 -0.0039 -0.0059 -0.0062 43  SER   A N   
302  C  CA  . SER   A 37  ? 0.1741 0.1799 0.2010 -0.0055 -0.0065 -0.0068 43  SER   A CA  
303  C  C   . SER   A 37  ? 0.1909 0.2029 0.2236 -0.0045 -0.0043 -0.0085 43  SER   A C   
304  O  O   . SER   A 37  ? 0.1920 0.2036 0.2244 -0.0023 -0.0026 -0.0095 43  SER   A O   
305  C  CB  . SER   A 37  ? 0.1812 0.1849 0.2083 -0.0048 -0.0097 -0.0072 43  SER   A CB  
306  O  OG  . SER   A 37  ? 0.1863 0.1895 0.2129 -0.0017 -0.0108 -0.0076 43  SER   A OG  
307  N  N   . SER   A 38  ? 0.1830 0.2007 0.2216 -0.0063 -0.0039 -0.0089 44  SER   A N   
308  C  CA  . SER   A 38  ? 0.1984 0.2226 0.2448 -0.0049 -0.0012 -0.0108 44  SER   A CA  
309  C  C   . SER   A 38  ? 0.2166 0.2430 0.2698 -0.0014 -0.0040 -0.0102 44  SER   A C   
310  O  O   . SER   A 38  ? 0.2271 0.2527 0.2792 -0.0020 -0.0082 -0.0086 44  SER   A O   
311  C  CB  . SER   A 38  ? 0.2229 0.2538 0.2736 -0.0087 0.0012  -0.0114 44  SER   A CB  
312  O  OG  . SER   A 38  ? 0.2530 0.2853 0.3058 -0.0105 -0.0023 -0.0098 44  SER   A OG  
313  N  N   . THR   A 39  ? 0.2140 0.2431 0.2741 0.0019  -0.0017 -0.0114 45  THR   A N   
314  C  CA  . THR   A 39  ? 0.2230 0.2545 0.2909 0.0054  -0.0047 -0.0097 45  THR   A CA  
315  C  C   . THR   A 39  ? 0.2453 0.2852 0.3269 0.0070  -0.0020 -0.0105 45  THR   A C   
316  O  O   . THR   A 39  ? 0.2432 0.2855 0.3273 0.0061  0.0035  -0.0138 45  THR   A O   
317  C  CB  . THR   A 39  ? 0.2328 0.2583 0.2983 0.0090  -0.0048 -0.0093 45  THR   A CB  
318  O  OG1 . THR   A 39  ? 0.2558 0.2804 0.3238 0.0102  0.0008  -0.0125 45  THR   A OG1 
319  C  CG2 . THR   A 39  ? 0.2307 0.2489 0.2840 0.0079  -0.0068 -0.0086 45  THR   A CG2 
320  N  N   . THR   A 40  ? 0.2590 0.3040 0.3498 0.0091  -0.0060 -0.0075 46  THR   A N   
321  C  CA  . THR   A 40  ? 0.2732 0.3271 0.3799 0.0115  -0.0037 -0.0077 46  THR   A CA  
322  C  C   . THR   A 40  ? 0.2739 0.3247 0.3876 0.0167  -0.0004 -0.0087 46  THR   A C   
323  O  O   . THR   A 40  ? 0.2887 0.3427 0.4114 0.0182  0.0058  -0.0122 46  THR   A O   
324  C  CB  . THR   A 40  ? 0.3105 0.3725 0.4251 0.0110  -0.0097 -0.0032 46  THR   A CB  
325  O  OG1 . THR   A 40  ? 0.3590 0.4173 0.4706 0.0128  -0.0154 0.0008  46  THR   A OG1 
326  C  CG2 . THR   A 40  ? 0.3153 0.3795 0.4231 0.0050  -0.0120 -0.0032 46  THR   A CG2 
327  N  N   . ALA   A 41  ? 0.2696 0.3137 0.3788 0.0191  -0.0039 -0.0060 47  ALA   A N   
328  C  CA  . ALA   A 41  ? 0.2701 0.3097 0.3857 0.0238  -0.0011 -0.0066 47  ALA   A CA  
329  C  C   . ALA   A 41  ? 0.2619 0.2929 0.3664 0.0225  0.0040  -0.0113 47  ALA   A C   
330  O  O   . ALA   A 41  ? 0.2569 0.2840 0.3475 0.0189  0.0026  -0.0117 47  ALA   A O   
331  C  CB  . ALA   A 41  ? 0.2857 0.3227 0.4020 0.0263  -0.0076 -0.0007 47  ALA   A CB  
332  N  N   . GLN   A 42  ? 0.2455 0.2737 0.3569 0.0253  0.0098  -0.0148 48  GLN   A N   
333  C  CA  . GLN   A 42  ? 0.2580 0.2786 0.3596 0.0234  0.0146  -0.0194 48  GLN   A CA  
334  C  C   . GLN   A 42  ? 0.2572 0.2693 0.3513 0.0246  0.0109  -0.0165 48  GLN   A C   
335  O  O   . GLN   A 42  ? 0.2599 0.2707 0.3614 0.0284  0.0074  -0.0123 48  GLN   A O   
336  C  CB  . GLN   A 42  ? 0.2975 0.3178 0.4092 0.0253  0.0228  -0.0252 48  GLN   A CB  
337  C  CG  . GLN   A 42  ? 0.3622 0.3902 0.4765 0.0220  0.0285  -0.0300 48  GLN   A CG  
338  C  CD  . GLN   A 42  ? 0.4352 0.4624 0.5581 0.0232  0.0377  -0.0369 48  GLN   A CD  
339  O  OE1 . GLN   A 42  ? 0.4288 0.4571 0.5684 0.0286  0.0398  -0.0370 48  GLN   A OE1 
340  N  NE2 . GLN   A 42  ? 0.4739 0.4992 0.5860 0.0178  0.0434  -0.0429 48  GLN   A NE2 
341  N  N   . GLY   A 43  ? 0.2304 0.2376 0.3101 0.0210  0.0112  -0.0180 49  GLY   A N   
342  C  CA  . GLY   A 43  ? 0.2282 0.2282 0.2999 0.0214  0.0083  -0.0157 49  GLY   A CA  
343  C  C   . GLY   A 43  ? 0.2141 0.2074 0.2862 0.0219  0.0131  -0.0192 49  GLY   A C   
344  O  O   . GLY   A 43  ? 0.2191 0.2128 0.2952 0.0212  0.0194  -0.0246 49  GLY   A O   
345  N  N   . CYS   A 44  ? 0.2084 0.1952 0.2759 0.0228  0.0103  -0.0164 50  CYS   A N   
346  C  CA  . CYS   A 44  ? 0.2182 0.1973 0.2862 0.0231  0.0143  -0.0192 50  CYS   A CA  
347  C  C   . CYS   A 44  ? 0.2260 0.2009 0.2802 0.0187  0.0152  -0.0211 50  CYS   A C   
348  O  O   . CYS   A 44  ? 0.2379 0.2065 0.2914 0.0178  0.0190  -0.0243 50  CYS   A O   
349  C  CB  . CYS   A 44  ? 0.2306 0.2051 0.3068 0.0274  0.0112  -0.0143 50  CYS   A CB  
350  S  SG  . CYS   A 44  ? 0.2615 0.2409 0.3580 0.0331  0.0110  -0.0119 50  CYS   A SG  
351  N  N   . ASP   A 45  ? 0.2080 0.1862 0.2521 0.0159  0.0119  -0.0192 51  ASP   A N   
352  C  CA  . ASP   A 45  ? 0.2135 0.1893 0.2461 0.0119  0.0124  -0.0203 51  ASP   A CA  
353  C  C   . ASP   A 45  ? 0.2259 0.2035 0.2550 0.0076  0.0178  -0.0258 51  ASP   A C   
354  O  O   . ASP   A 45  ? 0.2245 0.2070 0.2570 0.0071  0.0200  -0.0279 51  ASP   A O   
355  C  CB  . ASP   A 45  ? 0.2120 0.1909 0.2371 0.0109  0.0076  -0.0164 51  ASP   A CB  
356  C  CG  . ASP   A 45  ? 0.2311 0.2085 0.2570 0.0136  0.0026  -0.0116 51  ASP   A CG  
357  O  OD1 . ASP   A 45  ? 0.2393 0.2118 0.2668 0.0149  0.0023  -0.0103 51  ASP   A OD1 
358  O  OD2 . ASP   A 45  ? 0.2179 0.1987 0.2421 0.0138  -0.0008 -0.0093 51  ASP   A OD2 
359  N  N   . THR   A 46  ? 0.2355 0.2098 0.2570 0.0038  0.0198  -0.0280 52  THR   A N   
360  C  CA  . THR   A 46  ? 0.2464 0.2233 0.2619 -0.0020 0.0242  -0.0327 52  THR   A CA  
361  C  C   . THR   A 46  ? 0.2401 0.2196 0.2449 -0.0060 0.0209  -0.0296 52  THR   A C   
362  O  O   . THR   A 46  ? 0.2632 0.2399 0.2654 -0.0050 0.0176  -0.0264 52  THR   A O   
363  C  CB  . THR   A 46  ? 0.2868 0.2579 0.3028 -0.0041 0.0299  -0.0386 52  THR   A CB  
364  O  OG1 . THR   A 46  ? 0.3316 0.2969 0.3445 -0.0040 0.0278  -0.0365 52  THR   A OG1 
365  C  CG2 . THR   A 46  ? 0.2991 0.2675 0.3280 0.0005  0.0339  -0.0417 52  THR   A CG2 
366  N  N   . ILE   A 47  ? 0.2259 0.2113 0.2253 -0.0107 0.0217  -0.0303 53  ILE   A N   
367  C  CA  . ILE   A 47  ? 0.2115 0.2003 0.2029 -0.0141 0.0182  -0.0264 53  ILE   A CA  
368  C  C   . ILE   A 47  ? 0.2258 0.2141 0.2098 -0.0203 0.0205  -0.0291 53  ILE   A C   
369  O  O   . ILE   A 47  ? 0.2402 0.2289 0.2218 -0.0249 0.0254  -0.0345 53  ILE   A O   
370  C  CB  . ILE   A 47  ? 0.2097 0.2052 0.1993 -0.0163 0.0168  -0.0239 53  ILE   A CB  
371  C  CG1 . ILE   A 47  ? 0.2085 0.2046 0.2055 -0.0112 0.0150  -0.0220 53  ILE   A CG1 
372  C  CG2 . ILE   A 47  ? 0.2195 0.2187 0.2036 -0.0187 0.0125  -0.0185 53  ILE   A CG2 
373  C  CD1 . ILE   A 47  ? 0.2174 0.2103 0.2167 -0.0061 0.0104  -0.0179 53  ILE   A CD1 
374  N  N   . ALA   A 48  ? 0.2142 0.2025 0.1942 -0.0212 0.0173  -0.0256 54  ALA   A N   
375  C  CA  . ALA   A 48  ? 0.2230 0.2123 0.1955 -0.0278 0.0184  -0.0272 54  ALA   A CA  
376  C  C   . ALA   A 48  ? 0.2354 0.2331 0.2016 -0.0344 0.0178  -0.0259 54  ALA   A C   
377  O  O   . ALA   A 48  ? 0.2300 0.2328 0.1975 -0.0330 0.0143  -0.0207 54  ALA   A O   
378  C  CB  . ALA   A 48  ? 0.2106 0.1997 0.1817 -0.0268 0.0143  -0.0226 54  ALA   A CB  
379  N  N   . ARG   A 49  ? 0.2448 0.2438 0.2040 -0.0422 0.0214  -0.0305 55  ARG   A N   
380  C  CA  . ARG   A 49  ? 0.2550 0.2628 0.2067 -0.0499 0.0205  -0.0287 55  ARG   A CA  
381  C  C   . ARG   A 49  ? 0.2871 0.2969 0.2309 -0.0573 0.0198  -0.0290 55  ARG   A C   
382  O  O   . ARG   A 49  ? 0.3039 0.3120 0.2415 -0.0640 0.0245  -0.0357 55  ARG   A O   
383  C  CB  . ARG   A 49  ? 0.2540 0.2631 0.2037 -0.0539 0.0261  -0.0348 55  ARG   A CB  
384  C  CG  . ARG   A 49  ? 0.2620 0.2694 0.2206 -0.0469 0.0272  -0.0350 55  ARG   A CG  
385  C  CD  . ARG   A 49  ? 0.2632 0.2760 0.2238 -0.0445 0.0217  -0.0271 55  ARG   A CD  
386  N  NE  . ARG   A 49  ? 0.2532 0.2644 0.2218 -0.0388 0.0229  -0.0279 55  ARG   A NE  
387  C  CZ  . ARG   A 49  ? 0.2746 0.2871 0.2478 -0.0344 0.0186  -0.0223 55  ARG   A CZ  
388  N  NH1 . ARG   A 49  ? 0.2598 0.2749 0.2311 -0.0345 0.0134  -0.0154 55  ARG   A NH1 
389  N  NH2 . ARG   A 49  ? 0.2740 0.2853 0.2541 -0.0300 0.0198  -0.0235 55  ARG   A NH2 
390  N  N   . CYS   A 50  ? 0.2888 0.3025 0.2334 -0.0561 0.0143  -0.0220 56  CYS   A N   
391  C  CA  . CYS   A 50  ? 0.3033 0.3188 0.2427 -0.0616 0.0129  -0.0214 56  CYS   A CA  
392  C  C   . CYS   A 50  ? 0.3150 0.3389 0.2564 -0.0609 0.0063  -0.0121 56  CYS   A C   
393  O  O   . CYS   A 50  ? 0.3144 0.3411 0.2614 -0.0557 0.0032  -0.0065 56  CYS   A O   
394  C  CB  . CYS   A 50  ? 0.2931 0.2985 0.2361 -0.0570 0.0153  -0.0253 56  CYS   A CB  
395  S  SG  . CYS   A 50  ? 0.2874 0.2901 0.2401 -0.0459 0.0112  -0.0193 56  CYS   A SG  
396  N  N   . ASP   A 51  ? 0.3363 0.3636 0.2743 -0.0656 0.0044  -0.0104 57  ASP   A N   
397  C  CA  . ASP   A 51  ? 0.3546 0.3901 0.2970 -0.0641 -0.0013 -0.0017 57  ASP   A CA  
398  C  C   . ASP   A 51  ? 0.3449 0.3766 0.2907 -0.0606 -0.0016 -0.0017 57  ASP   A C   
399  O  O   . ASP   A 51  ? 0.3529 0.3923 0.3002 -0.0627 -0.0051 0.0036  57  ASP   A O   
400  C  CB  . ASP   A 51  ? 0.4378 0.4853 0.3742 -0.0738 -0.0048 0.0030  57  ASP   A CB  
401  C  CG  . ASP   A 51  ? 0.5727 0.6211 0.4999 -0.0836 -0.0030 -0.0018 57  ASP   A CG  
402  O  OD1 . ASP   A 51  ? 0.5895 0.6277 0.5151 -0.0828 0.0016  -0.0093 57  ASP   A OD1 
403  O  OD2 . ASP   A 51  ? 0.6485 0.7077 0.5702 -0.0926 -0.0064 0.0023  57  ASP   A OD2 
404  N  N   . CYS   A 52  ? 0.3194 0.3402 0.2674 -0.0553 0.0019  -0.0068 58  CYS   A N   
405  C  CA  . CYS   A 52  ? 0.2887 0.3055 0.2398 -0.0519 0.0016  -0.0062 58  CYS   A CA  
406  C  C   . CYS   A 52  ? 0.2722 0.2952 0.2303 -0.0465 -0.0023 0.0009  58  CYS   A C   
407  O  O   . CYS   A 52  ? 0.2823 0.3070 0.2452 -0.0415 -0.0037 0.0038  58  CYS   A O   
408  C  CB  . CYS   A 52  ? 0.2701 0.2748 0.2237 -0.0461 0.0051  -0.0111 58  CYS   A CB  
409  S  SG  . CYS   A 52  ? 0.2973 0.2920 0.2456 -0.0513 0.0109  -0.0201 58  CYS   A SG  
410  N  N   . GLN   A 53  ? 0.2460 0.2720 0.2052 -0.0475 -0.0036 0.0032  59  GLN   A N   
411  C  CA  . GLN   A 53  ? 0.2396 0.2708 0.2065 -0.0420 -0.0060 0.0087  59  GLN   A CA  
412  C  C   . GLN   A 53  ? 0.2210 0.2465 0.1891 -0.0390 -0.0044 0.0072  59  GLN   A C   
413  O  O   . GLN   A 53  ? 0.2220 0.2524 0.1952 -0.0363 -0.0056 0.0108  59  GLN   A O   
414  C  CB  . GLN   A 53  ? 0.2684 0.3128 0.2383 -0.0457 -0.0097 0.0152  59  GLN   A CB  
415  C  CG  . GLN   A 53  ? 0.3238 0.3744 0.2941 -0.0474 -0.0122 0.0189  59  GLN   A CG  
416  C  CD  . GLN   A 53  ? 0.4201 0.4660 0.3943 -0.0408 -0.0117 0.0189  59  GLN   A CD  
417  O  OE1 . GLN   A 53  ? 0.3972 0.4413 0.3677 -0.0427 -0.0111 0.0173  59  GLN   A OE1 
418  N  NE2 . GLN   A 53  ? 0.4281 0.4722 0.4099 -0.0333 -0.0117 0.0207  59  GLN   A NE2 
419  N  N   . THR   A 54  ? 0.2065 0.2215 0.1704 -0.0394 -0.0016 0.0020  60  THR   A N   
420  C  CA  . THR   A 54  ? 0.2151 0.2230 0.1797 -0.0364 -0.0003 0.0010  60  THR   A CA  
421  C  C   . THR   A 54  ? 0.2064 0.2039 0.1714 -0.0318 0.0016  -0.0027 60  THR   A C   
422  O  O   . THR   A 54  ? 0.2319 0.2260 0.1949 -0.0334 0.0033  -0.0062 60  THR   A O   
423  C  CB  . THR   A 54  ? 0.2674 0.2733 0.2277 -0.0424 0.0006  -0.0004 60  THR   A CB  
424  O  OG1 . THR   A 54  ? 0.3243 0.3234 0.2795 -0.0471 0.0030  -0.0055 60  THR   A OG1 
425  C  CG2 . THR   A 54  ? 0.2698 0.2872 0.2305 -0.0475 -0.0015 0.0034  60  THR   A CG2 
426  N  N   . GLY   A 55  ? 0.1898 0.1836 0.1575 -0.0265 0.0014  -0.0015 61  GLY   A N   
427  C  CA  . GLY   A 55  ? 0.1957 0.1811 0.1650 -0.0221 0.0024  -0.0037 61  GLY   A CA  
428  C  C   . GLY   A 55  ? 0.2008 0.1832 0.1715 -0.0183 0.0015  -0.0016 61  GLY   A C   
429  O  O   . GLY   A 55  ? 0.2140 0.1991 0.1835 -0.0200 0.0011  0.0006  61  GLY   A O   
430  N  N   . VAL   A 56  ? 0.1864 0.1643 0.1595 -0.0138 0.0012  -0.0019 62  VAL   A N   
431  C  CA  . VAL   A 56  ? 0.1792 0.1545 0.1526 -0.0110 0.0000  0.0003  62  VAL   A CA  
432  C  C   . VAL   A 56  ? 0.1775 0.1545 0.1535 -0.0066 -0.0011 0.0005  62  VAL   A C   
433  O  O   . VAL   A 56  ? 0.1901 0.1660 0.1686 -0.0051 -0.0008 -0.0013 62  VAL   A O   
434  C  CB  . VAL   A 56  ? 0.2039 0.1701 0.1777 -0.0110 0.0004  -0.0001 62  VAL   A CB  
435  C  CG1 . VAL   A 56  ? 0.2279 0.1919 0.2021 -0.0083 -0.0017 0.0031  62  VAL   A CG1 
436  C  CG2 . VAL   A 56  ? 0.2128 0.1758 0.1837 -0.0160 0.0018  -0.0006 62  VAL   A CG2 
437  N  N   . TYR   A 57  ? 0.1711 0.1510 0.1465 -0.0050 -0.0020 0.0022  63  TYR   A N   
438  C  CA  . TYR   A 57  ? 0.1683 0.1492 0.1456 -0.0015 -0.0030 0.0019  63  TYR   A CA  
439  C  C   . TYR   A 57  ? 0.1739 0.1523 0.1492 -0.0007 -0.0044 0.0033  63  TYR   A C   
440  O  O   . TYR   A 57  ? 0.1847 0.1628 0.1567 -0.0027 -0.0044 0.0050  63  TYR   A O   
441  C  CB  . TYR   A 57  ? 0.1667 0.1537 0.1457 -0.0006 -0.0023 0.0018  63  TYR   A CB  
442  C  CG  . TYR   A 57  ? 0.1675 0.1578 0.1451 -0.0008 -0.0015 0.0026  63  TYR   A CG  
443  C  CD1 . TYR   A 57  ? 0.1869 0.1806 0.1635 -0.0034 -0.0005 0.0038  63  TYR   A CD1 
444  C  CD2 . TYR   A 57  ? 0.1710 0.1616 0.1484 0.0011  -0.0012 0.0016  63  TYR   A CD2 
445  C  CE1 . TYR   A 57  ? 0.1869 0.1845 0.1629 -0.0037 0.0010  0.0041  63  TYR   A CE1 
446  C  CE2 . TYR   A 57  ? 0.1710 0.1649 0.1472 0.0006  0.0006  0.0013  63  TYR   A CE2 
447  C  CZ  . TYR   A 57  ? 0.1824 0.1801 0.1582 -0.0016 0.0018  0.0026  63  TYR   A CZ  
448  O  OH  . TYR   A 57  ? 0.2075 0.2093 0.1825 -0.0024 0.0043  0.0021  63  TYR   A OH  
449  N  N   . TYR   A 58  ? 0.1814 0.1590 0.1582 0.0016  -0.0057 0.0029  64  TYR   A N   
450  C  CA  . TYR   A 58  ? 0.1840 0.1606 0.1582 0.0016  -0.0077 0.0046  64  TYR   A CA  
451  C  C   . TYR   A 58  ? 0.1851 0.1657 0.1567 0.0015  -0.0068 0.0033  64  TYR   A C   
452  O  O   . TYR   A 58  ? 0.1902 0.1724 0.1642 0.0031  -0.0060 0.0011  64  TYR   A O   
453  C  CB  . TYR   A 58  ? 0.1827 0.1571 0.1605 0.0037  -0.0099 0.0051  64  TYR   A CB  
454  C  CG  . TYR   A 58  ? 0.1898 0.1643 0.1647 0.0027  -0.0128 0.0078  64  TYR   A CG  
455  C  CD1 . TYR   A 58  ? 0.1927 0.1650 0.1647 0.0008  -0.0142 0.0114  64  TYR   A CD1 
456  C  CD2 . TYR   A 58  ? 0.1982 0.1751 0.1722 0.0030  -0.0142 0.0070  64  TYR   A CD2 
457  C  CE1 . TYR   A 58  ? 0.2122 0.1856 0.1803 -0.0011 -0.0173 0.0147  64  TYR   A CE1 
458  C  CE2 . TYR   A 58  ? 0.2086 0.1867 0.1783 0.0008  -0.0171 0.0095  64  TYR   A CE2 
459  C  CZ  . TYR   A 58  ? 0.2258 0.2024 0.1927 -0.0011 -0.0189 0.0138  64  TYR   A CZ  
460  O  OH  . TYR   A 58  ? 0.2531 0.2317 0.2150 -0.0041 -0.0222 0.0171  64  TYR   A OH  
461  N  N   . CYS   A 59  ? 0.1737 0.1552 0.1401 -0.0008 -0.0068 0.0045  65  CYS   A N   
462  C  CA  . CYS   A 59  ? 0.1857 0.1708 0.1489 -0.0017 -0.0049 0.0023  65  CYS   A CA  
463  C  C   . CYS   A 59  ? 0.1998 0.1844 0.1578 -0.0037 -0.0073 0.0033  65  CYS   A C   
464  O  O   . CYS   A 59  ? 0.2103 0.1946 0.1635 -0.0066 -0.0087 0.0063  65  CYS   A O   
465  C  CB  . CYS   A 59  ? 0.1867 0.1750 0.1478 -0.0038 -0.0023 0.0027  65  CYS   A CB  
466  S  SG  . CYS   A 59  ? 0.2042 0.1970 0.1615 -0.0053 0.0013  -0.0007 65  CYS   A SG  
467  N  N   . SER   A 60  ? 0.1855 0.1700 0.1442 -0.0028 -0.0082 0.0012  66  SER   A N   
468  C  CA  . SER   A 60  ? 0.1963 0.1813 0.1497 -0.0055 -0.0111 0.0024  66  SER   A CA  
469  C  C   . SER   A 60  ? 0.2088 0.1965 0.1537 -0.0098 -0.0093 0.0012  66  SER   A C   
470  O  O   . SER   A 60  ? 0.2235 0.2122 0.1624 -0.0135 -0.0124 0.0044  66  SER   A O   
471  C  CB  . SER   A 60  ? 0.2241 0.2090 0.1798 -0.0044 -0.0122 0.0000  66  SER   A CB  
472  O  OG  . SER   A 60  ? 0.2600 0.2454 0.2151 -0.0043 -0.0084 -0.0051 66  SER   A OG  
473  N  N   . SER   A 61  ? 0.1922 0.1818 0.1370 -0.0096 -0.0043 -0.0030 67  SER   A N   
474  C  CA  . SER   A 61  ? 0.1875 0.1803 0.1247 -0.0138 -0.0011 -0.0053 67  SER   A CA  
475  C  C   . SER   A 61  ? 0.1880 0.1824 0.1208 -0.0169 -0.0018 -0.0010 67  SER   A C   
476  O  O   . SER   A 61  ? 0.2099 0.2076 0.1355 -0.0213 0.0007  -0.0023 67  SER   A O   
477  C  CB  . SER   A 61  ? 0.1988 0.1933 0.1398 -0.0118 0.0050  -0.0110 67  SER   A CB  
478  O  OG  . SER   A 61  ? 0.2173 0.2130 0.1654 -0.0087 0.0067  -0.0097 67  SER   A OG  
479  N  N   . ARG   A 62  ? 0.1888 0.1807 0.1256 -0.0152 -0.0045 0.0036  68  ARG   A N   
480  C  CA  . ARG   A 62  ? 0.2025 0.1944 0.1354 -0.0185 -0.0057 0.0083  68  ARG   A CA  
481  C  C   . ARG   A 62  ? 0.2349 0.2222 0.1692 -0.0183 -0.0114 0.0145  68  ARG   A C   
482  O  O   . ARG   A 62  ? 0.2518 0.2374 0.1840 -0.0207 -0.0129 0.0192  68  ARG   A O   
483  C  CB  . ARG   A 62  ? 0.2040 0.1966 0.1417 -0.0171 -0.0027 0.0079  68  ARG   A CB  
484  C  CG  . ARG   A 62  ? 0.2187 0.2169 0.1573 -0.0171 0.0030  0.0031  68  ARG   A CG  
485  C  CD  . ARG   A 62  ? 0.2129 0.2151 0.1434 -0.0225 0.0052  0.0034  68  ARG   A CD  
486  N  NE  . ARG   A 62  ? 0.2180 0.2262 0.1507 -0.0223 0.0114  -0.0016 68  ARG   A NE  
487  C  CZ  . ARG   A 62  ? 0.2400 0.2501 0.1711 -0.0224 0.0151  -0.0070 68  ARG   A CZ  
488  N  NH1 . ARG   A 62  ? 0.2537 0.2608 0.1797 -0.0235 0.0126  -0.0081 68  ARG   A NH1 
489  N  NH2 . ARG   A 62  ? 0.2473 0.2626 0.1824 -0.0217 0.0214  -0.0116 68  ARG   A NH2 
490  N  N   . ARG   A 63  ? 0.2472 0.2322 0.1867 -0.0149 -0.0142 0.0145  69  ARG   A N   
491  C  CA  . ARG   A 63  ? 0.2580 0.2389 0.2021 -0.0135 -0.0188 0.0199  69  ARG   A CA  
492  C  C   . ARG   A 63  ? 0.2663 0.2427 0.2146 -0.0123 -0.0179 0.0218  69  ARG   A C   
493  O  O   . ARG   A 63  ? 0.2869 0.2597 0.2355 -0.0135 -0.0207 0.0273  69  ARG   A O   
494  C  CB  . ARG   A 63  ? 0.2939 0.2759 0.2323 -0.0176 -0.0235 0.0257  69  ARG   A CB  
495  C  CG  . ARG   A 63  ? 0.3199 0.3050 0.2572 -0.0182 -0.0264 0.0253  69  ARG   A CG  
496  C  CD  . ARG   A 63  ? 0.3324 0.3187 0.2665 -0.0219 -0.0325 0.0332  69  ARG   A CD  
497  N  NE  . ARG   A 63  ? 0.3471 0.3383 0.2764 -0.0248 -0.0346 0.0317  69  ARG   A NE  
498  C  CZ  . ARG   A 63  ? 0.3165 0.3123 0.2341 -0.0314 -0.0346 0.0309  69  ARG   A CZ  
499  N  NH1 . ARG   A 63  ? 0.3206 0.3171 0.2304 -0.0357 -0.0329 0.0325  69  ARG   A NH1 
500  N  NH2 . ARG   A 63  ? 0.3018 0.3017 0.2150 -0.0345 -0.0362 0.0286  69  ARG   A NH2 
501  N  N   . LYS   A 64  ? 0.2397 0.2166 0.1908 -0.0105 -0.0140 0.0176  70  LYS   A N   
502  C  CA  . LYS   A 64  ? 0.2456 0.2191 0.1993 -0.0107 -0.0126 0.0185  70  LYS   A CA  
503  C  C   . LYS   A 64  ? 0.2346 0.2077 0.1941 -0.0076 -0.0103 0.0146  70  LYS   A C   
504  O  O   . LYS   A 64  ? 0.2292 0.2062 0.1900 -0.0059 -0.0086 0.0111  70  LYS   A O   
505  C  CB  . LYS   A 64  ? 0.2998 0.2769 0.2481 -0.0145 -0.0100 0.0185  70  LYS   A CB  
506  C  CG  . LYS   A 64  ? 0.4178 0.3936 0.3600 -0.0190 -0.0122 0.0238  70  LYS   A CG  
507  C  CD  . LYS   A 64  ? 0.5235 0.5017 0.4619 -0.0230 -0.0094 0.0242  70  LYS   A CD  
508  C  CE  . LYS   A 64  ? 0.6067 0.5848 0.5377 -0.0282 -0.0115 0.0295  70  LYS   A CE  
509  N  NZ  . LYS   A 64  ? 0.6586 0.6415 0.5833 -0.0301 -0.0124 0.0294  70  LYS   A NZ  
510  N  N   . HIS   A 65  ? 0.2255 0.1939 0.1884 -0.0076 -0.0100 0.0153  71  HIS   A N   
511  C  CA  . HIS   A 65  ? 0.2129 0.1812 0.1797 -0.0063 -0.0077 0.0117  71  HIS   A CA  
512  C  C   . HIS   A 65  ? 0.2348 0.2056 0.1990 -0.0097 -0.0055 0.0114  71  HIS   A C   
513  O  O   . HIS   A 65  ? 0.2616 0.2294 0.2231 -0.0128 -0.0058 0.0141  71  HIS   A O   
514  C  CB  . HIS   A 65  ? 0.2078 0.1693 0.1797 -0.0049 -0.0080 0.0118  71  HIS   A CB  
515  C  CG  . HIS   A 65  ? 0.2250 0.1852 0.2015 -0.0014 -0.0101 0.0123  71  HIS   A CG  
516  N  ND1 . HIS   A 65  ? 0.2731 0.2347 0.2540 0.0012  -0.0090 0.0089  71  HIS   A ND1 
517  C  CD2 . HIS   A 65  ? 0.2379 0.1963 0.2157 -0.0005 -0.0133 0.0164  71  HIS   A CD2 
518  C  CE1 . HIS   A 65  ? 0.2614 0.2222 0.2465 0.0036  -0.0113 0.0106  71  HIS   A CE1 
519  N  NE2 . HIS   A 65  ? 0.2696 0.2288 0.2533 0.0028  -0.0142 0.0153  71  HIS   A NE2 
520  N  N   . TYR   A 66  ? 0.2098 0.1864 0.1752 -0.0095 -0.0036 0.0089  72  TYR   A N   
521  C  CA  . TYR   A 66  ? 0.2021 0.1831 0.1663 -0.0127 -0.0018 0.0090  72  TYR   A CA  
522  C  C   . TYR   A 66  ? 0.1975 0.1793 0.1642 -0.0138 -0.0009 0.0072  72  TYR   A C   
523  O  O   . TYR   A 66  ? 0.1888 0.1727 0.1585 -0.0114 -0.0009 0.0055  72  TYR   A O   
524  C  CB  . TYR   A 66  ? 0.1973 0.1866 0.1620 -0.0119 -0.0002 0.0083  72  TYR   A CB  
525  C  CG  . TYR   A 66  ? 0.1988 0.1889 0.1592 -0.0126 -0.0001 0.0093  72  TYR   A CG  
526  C  CD1 . TYR   A 66  ? 0.2009 0.1915 0.1570 -0.0167 0.0004  0.0115  72  TYR   A CD1 
527  C  CD2 . TYR   A 66  ? 0.2054 0.1959 0.1654 -0.0102 -0.0003 0.0078  72  TYR   A CD2 
528  C  CE1 . TYR   A 66  ? 0.2158 0.2083 0.1668 -0.0184 0.0008  0.0124  72  TYR   A CE1 
529  C  CE2 . TYR   A 66  ? 0.2155 0.2075 0.1703 -0.0120 0.0001  0.0081  72  TYR   A CE2 
530  C  CZ  . TYR   A 66  ? 0.2292 0.2224 0.1791 -0.0162 0.0007  0.0105  72  TYR   A CZ  
531  O  OH  . TYR   A 66  ? 0.2601 0.2554 0.2037 -0.0189 0.0012  0.0108  72  TYR   A OH  
532  N  N   . PRO   A 67  ? 0.2045 0.1857 0.1696 -0.0181 -0.0002 0.0076  73  PRO   A N   
533  C  CA  . PRO   A 67  ? 0.2125 0.1964 0.1786 -0.0205 0.0005  0.0059  73  PRO   A CA  
534  C  C   . PRO   A 67  ? 0.2318 0.2266 0.2006 -0.0203 0.0007  0.0068  73  PRO   A C   
535  O  O   . PRO   A 67  ? 0.2671 0.2670 0.2363 -0.0204 0.0013  0.0084  73  PRO   A O   
536  C  CB  . PRO   A 67  ? 0.2418 0.2225 0.2048 -0.0261 0.0012  0.0063  73  PRO   A CB  
537  C  CG  . PRO   A 67  ? 0.2479 0.2280 0.2088 -0.0266 0.0009  0.0092  73  PRO   A CG  
538  C  CD  . PRO   A 67  ? 0.2132 0.1919 0.1747 -0.0217 -0.0002 0.0100  73  PRO   A CD  
539  N  N   . VAL   A 68  ? 0.2021 0.2006 0.1733 -0.0201 0.0003  0.0060  74  VAL   A N   
540  C  CA  . VAL   A 68  ? 0.2085 0.2173 0.1841 -0.0195 0.0000  0.0079  74  VAL   A CA  
541  C  C   . VAL   A 68  ? 0.2042 0.2177 0.1802 -0.0232 -0.0010 0.0084  74  VAL   A C   
542  O  O   . VAL   A 68  ? 0.2039 0.2125 0.1770 -0.0248 -0.0010 0.0060  74  VAL   A O   
543  C  CB  . VAL   A 68  ? 0.2348 0.2448 0.2146 -0.0138 0.0000  0.0079  74  VAL   A CB  
544  C  CG1 . VAL   A 68  ? 0.2681 0.2769 0.2475 -0.0113 0.0012  0.0077  74  VAL   A CG1 
545  C  CG2 . VAL   A 68  ? 0.2357 0.2396 0.2147 -0.0119 -0.0007 0.0059  74  VAL   A CG2 
546  N  N   . SER   A 69  ? 0.2006 0.2246 0.1808 -0.0246 -0.0018 0.0115  75  SER   A N   
547  C  CA  . SER   A 69  ? 0.2075 0.2389 0.1892 -0.0280 -0.0037 0.0136  75  SER   A CA  
548  C  C   . SER   A 69  ? 0.1983 0.2338 0.1870 -0.0226 -0.0046 0.0159  75  SER   A C   
549  O  O   . SER   A 69  ? 0.2040 0.2420 0.1985 -0.0180 -0.0035 0.0170  75  SER   A O   
550  C  CB  . SER   A 69  ? 0.2557 0.2976 0.2399 -0.0325 -0.0046 0.0169  75  SER   A CB  
551  O  OG  . SER   A 69  ? 0.3468 0.3845 0.3242 -0.0384 -0.0038 0.0147  75  SER   A OG  
552  N  N   . PHE   A 70  ? 0.1880 0.2238 0.1762 -0.0232 -0.0060 0.0163  76  PHE   A N   
553  C  CA  . PHE   A 70  ? 0.1855 0.2237 0.1804 -0.0184 -0.0069 0.0188  76  PHE   A CA  
554  C  C   . PHE   A 70  ? 0.1981 0.2449 0.1954 -0.0217 -0.0099 0.0236  76  PHE   A C   
555  O  O   . PHE   A 70  ? 0.2192 0.2682 0.2105 -0.0284 -0.0111 0.0233  76  PHE   A O   
556  C  CB  . PHE   A 70  ? 0.1834 0.2119 0.1759 -0.0145 -0.0057 0.0152  76  PHE   A CB  
557  C  CG  . PHE   A 70  ? 0.1923 0.2152 0.1777 -0.0181 -0.0053 0.0117  76  PHE   A CG  
558  C  CD1 . PHE   A 70  ? 0.1966 0.2121 0.1769 -0.0193 -0.0036 0.0077  76  PHE   A CD1 
559  C  CD2 . PHE   A 70  ? 0.2006 0.2251 0.1852 -0.0199 -0.0064 0.0124  76  PHE   A CD2 
560  C  CE1 . PHE   A 70  ? 0.2140 0.2239 0.1896 -0.0219 -0.0024 0.0040  76  PHE   A CE1 
561  C  CE2 . PHE   A 70  ? 0.2167 0.2364 0.1952 -0.0233 -0.0050 0.0084  76  PHE   A CE2 
562  C  CZ  . PHE   A 70  ? 0.2176 0.2299 0.1923 -0.0239 -0.0027 0.0039  76  PHE   A CZ  
563  N  N   . SER   A 71  ? 0.1902 0.2423 0.1969 -0.0176 -0.0112 0.0281  77  SER   A N   
564  C  CA  . SER   A 71  ? 0.1905 0.2514 0.2013 -0.0202 -0.0148 0.0344  77  SER   A CA  
565  C  C   . SER   A 71  ? 0.1968 0.2539 0.2018 -0.0226 -0.0158 0.0336  77  SER   A C   
566  O  O   . SER   A 71  ? 0.2071 0.2547 0.2076 -0.0204 -0.0135 0.0284  77  SER   A O   
567  C  CB  . SER   A 71  ? 0.2070 0.2735 0.2313 -0.0143 -0.0155 0.0398  77  SER   A CB  
568  O  OG  . SER   A 71  ? 0.2259 0.2842 0.2533 -0.0080 -0.0136 0.0376  77  SER   A OG  
569  N  N   . LYS   A 72  ? 0.1939 0.2592 0.1992 -0.0274 -0.0194 0.0392  78  LYS   A N   
570  C  CA  . LYS   A 72  ? 0.2047 0.2678 0.2044 -0.0305 -0.0202 0.0389  78  LYS   A CA  
571  C  C   . LYS   A 72  ? 0.2152 0.2741 0.2222 -0.0238 -0.0202 0.0410  78  LYS   A C   
572  O  O   . LYS   A 72  ? 0.2166 0.2779 0.2345 -0.0183 -0.0209 0.0451  78  LYS   A O   
573  C  CB  . LYS   A 72  ? 0.2308 0.3051 0.2277 -0.0388 -0.0244 0.0450  78  LYS   A CB  
574  C  CG  . LYS   A 72  ? 0.2757 0.3523 0.2629 -0.0468 -0.0237 0.0411  78  LYS   A CG  
575  C  CD  . LYS   A 72  ? 0.3668 0.4528 0.3472 -0.0569 -0.0271 0.0450  78  LYS   A CD  
576  C  CE  . LYS   A 72  ? 0.4454 0.5337 0.4160 -0.0658 -0.0263 0.0408  78  LYS   A CE  
577  N  NZ  . LYS   A 72  ? 0.4930 0.5883 0.4536 -0.0768 -0.0284 0.0421  78  LYS   A NZ  
578  N  N   . PRO   A 73  ? 0.2176 0.2701 0.2195 -0.0242 -0.0191 0.0379  79  PRO   A N   
579  C  CA  . PRO   A 73  ? 0.2247 0.2727 0.2331 -0.0186 -0.0191 0.0397  79  PRO   A CA  
580  C  C   . PRO   A 73  ? 0.2270 0.2828 0.2451 -0.0181 -0.0231 0.0493  79  PRO   A C   
581  O  O   . PRO   A 73  ? 0.2366 0.3008 0.2523 -0.0244 -0.0266 0.0548  79  PRO   A O   
582  C  CB  . PRO   A 73  ? 0.2564 0.2997 0.2569 -0.0217 -0.0178 0.0358  79  PRO   A CB  
583  C  CG  . PRO   A 73  ? 0.2817 0.3251 0.2721 -0.0276 -0.0161 0.0306  79  PRO   A CG  
584  C  CD  . PRO   A 73  ? 0.2353 0.2849 0.2259 -0.0301 -0.0173 0.0324  79  PRO   A CD  
585  N  N   . SER   A 74  ? 0.2212 0.2744 0.2503 -0.0109 -0.0225 0.0512  80  SER   A N   
586  C  CA  . SER   A 74  ? 0.2304 0.2900 0.2715 -0.0091 -0.0258 0.0606  80  SER   A CA  
587  C  C   . SER   A 74  ? 0.2154 0.2672 0.2669 -0.0014 -0.0239 0.0605  80  SER   A C   
588  O  O   . SER   A 74  ? 0.2064 0.2486 0.2543 0.0018  -0.0202 0.0531  80  SER   A O   
589  C  CB  . SER   A 74  ? 0.2919 0.3618 0.3395 -0.0096 -0.0275 0.0649  80  SER   A CB  
590  O  OG  . SER   A 74  ? 0.3594 0.4255 0.4123 -0.0034 -0.0235 0.0600  80  SER   A OG  
591  N  N   . LEU   A 75  ? 0.2197 0.2757 0.2839 0.0010  -0.0267 0.0693  81  LEU   A N   
592  C  CA  . LEU   A 75  ? 0.2306 0.2793 0.3064 0.0079  -0.0249 0.0704  81  LEU   A CA  
593  C  C   . LEU   A 75  ? 0.2401 0.2897 0.3272 0.0143  -0.0216 0.0685  81  LEU   A C   
594  O  O   . LEU   A 75  ? 0.2503 0.3099 0.3466 0.0148  -0.0236 0.0747  81  LEU   A O   
595  C  CB  . LEU   A 75  ? 0.2368 0.2900 0.3213 0.0066  -0.0299 0.0818  81  LEU   A CB  
596  C  CG  . LEU   A 75  ? 0.2763 0.3206 0.3720 0.0122  -0.0289 0.0842  81  LEU   A CG  
597  C  CD1 . LEU   A 75  ? 0.2881 0.3210 0.3737 0.0112  -0.0263 0.0768  81  LEU   A CD1 
598  C  CD2 . LEU   A 75  ? 0.2900 0.3409 0.3954 0.0103  -0.0349 0.0978  81  LEU   A CD2 
599  N  N   . ILE   A 76  ? 0.2254 0.2654 0.3113 0.0187  -0.0163 0.0598  82  ILE   A N   
600  C  CA  . ILE   A 76  ? 0.2360 0.2765 0.3301 0.0240  -0.0119 0.0560  82  ILE   A CA  
601  C  C   . ILE   A 76  ? 0.2473 0.2776 0.3498 0.0301  -0.0073 0.0520  82  ILE   A C   
602  O  O   . ILE   A 76  ? 0.2398 0.2603 0.3355 0.0297  -0.0062 0.0474  82  ILE   A O   
603  C  CB  . ILE   A 76  ? 0.2568 0.2962 0.3377 0.0215  -0.0093 0.0476  82  ILE   A CB  
604  C  CG1 . ILE   A 76  ? 0.2927 0.3410 0.3651 0.0148  -0.0131 0.0506  82  ILE   A CG1 
605  C  CG2 . ILE   A 76  ? 0.2608 0.3001 0.3477 0.0259  -0.0040 0.0426  82  ILE   A CG2 
606  C  CD1 . ILE   A 76  ? 0.3227 0.3698 0.3839 0.0123  -0.0110 0.0438  82  ILE   A CD1 
607  N  N   . PHE   A 77  ? 0.2472 0.2799 0.3647 0.0356  -0.0044 0.0533  83  PHE   A N   
608  C  CA  . PHE   A 77  ? 0.2658 0.2886 0.3922 0.0413  0.0010  0.0486  83  PHE   A CA  
609  C  C   . PHE   A 77  ? 0.2788 0.2946 0.3940 0.0411  0.0065  0.0368  83  PHE   A C   
610  O  O   . PHE   A 77  ? 0.2838 0.3051 0.3944 0.0400  0.0082  0.0334  83  PHE   A O   
611  C  CB  . PHE   A 77  ? 0.2752 0.3032 0.4225 0.0475  0.0034  0.0529  83  PHE   A CB  
612  C  CG  . PHE   A 77  ? 0.3137 0.3301 0.4718 0.0531  0.0085  0.0495  83  PHE   A CG  
613  C  CD1 . PHE   A 77  ? 0.3401 0.3495 0.5027 0.0535  0.0056  0.0546  83  PHE   A CD1 
614  C  CD2 . PHE   A 77  ? 0.3407 0.3527 0.5033 0.0571  0.0163  0.0404  83  PHE   A CD2 
615  C  CE1 . PHE   A 77  ? 0.3686 0.3659 0.5408 0.0581  0.0105  0.0509  83  PHE   A CE1 
616  C  CE2 . PHE   A 77  ? 0.3541 0.3543 0.5258 0.0615  0.0217  0.0360  83  PHE   A CE2 
617  C  CZ  . PHE   A 77  ? 0.3644 0.3570 0.5413 0.0621  0.0187  0.0413  83  PHE   A CZ  
618  N  N   . VAL   A 78  ? 0.2703 0.2744 0.3805 0.0414  0.0087  0.0310  84  VAL   A N   
619  C  CA  . VAL   A 78  ? 0.2747 0.2723 0.3747 0.0406  0.0135  0.0204  84  VAL   A CA  
620  C  C   . VAL   A 78  ? 0.2918 0.2805 0.4013 0.0450  0.0197  0.0149  84  VAL   A C   
621  O  O   . VAL   A 78  ? 0.2976 0.2791 0.4132 0.0464  0.0192  0.0171  84  VAL   A O   
622  C  CB  . VAL   A 78  ? 0.2752 0.2677 0.3594 0.0358  0.0107  0.0174  84  VAL   A CB  
623  C  CG1 . VAL   A 78  ? 0.2756 0.2622 0.3496 0.0347  0.0148  0.0076  84  VAL   A CG1 
624  C  CG2 . VAL   A 78  ? 0.2750 0.2755 0.3506 0.0315  0.0057  0.0217  84  VAL   A CG2 
625  N  N   . GLU   A 79  ? 0.3127 0.3016 0.4224 0.0465  0.0258  0.0077  85  GLU   A N   
626  C  CA  . GLU   A 79  ? 0.3419 0.3225 0.4598 0.0500  0.0329  0.0010  85  GLU   A CA  
627  C  C   . GLU   A 79  ? 0.3595 0.3279 0.4676 0.0473  0.0338  -0.0055 85  GLU   A C   
628  O  O   . GLU   A 79  ? 0.3682 0.3360 0.4615 0.0425  0.0300  -0.0065 85  GLU   A O   
629  C  CB  . GLU   A 79  ? 0.3911 0.3759 0.5099 0.0511  0.0396  -0.0058 85  GLU   A CB  
630  C  CG  . GLU   A 79  ? 0.4976 0.4881 0.6376 0.0573  0.0434  -0.0023 85  GLU   A CG  
631  C  CD  . GLU   A 79  ? 0.6134 0.5939 0.7684 0.0621  0.0467  -0.0025 85  GLU   A CD  
632  O  OE1 . GLU   A 79  ? 0.6256 0.5952 0.7759 0.0614  0.0524  -0.0121 85  GLU   A OE1 
633  O  OE2 . GLU   A 79  ? 0.6676 0.6506 0.8380 0.0659  0.0432  0.0072  85  GLU   A OE2 
634  N  N   . ALA   A 80  ? 0.3630 0.3218 0.4802 0.0502  0.0394  -0.0102 86  ALA   A N   
635  C  CA  . ALA   A 80  ? 0.3674 0.3144 0.4761 0.0471  0.0410  -0.0170 86  ALA   A CA  
636  C  C   . ALA   A 80  ? 0.3654 0.3128 0.4567 0.0420  0.0429  -0.0259 86  ALA   A C   
637  O  O   . ALA   A 80  ? 0.3651 0.3179 0.4547 0.0421  0.0469  -0.0299 86  ALA   A O   
638  C  CB  . ALA   A 80  ? 0.3737 0.3105 0.4960 0.0510  0.0481  -0.0219 86  ALA   A CB  
639  N  N   . SER   A 81  ? 0.3554 0.2982 0.4338 0.0372  0.0395  -0.0278 87  SER   A N   
640  C  CA  . SER   A 81  ? 0.3580 0.3008 0.4199 0.0317  0.0401  -0.0351 87  SER   A CA  
641  C  C   . SER   A 81  ? 0.3617 0.2940 0.4183 0.0282  0.0408  -0.0406 87  SER   A C   
642  O  O   . SER   A 81  ? 0.3707 0.2958 0.4368 0.0302  0.0411  -0.0385 87  SER   A O   
643  C  CB  . SER   A 81  ? 0.3530 0.3036 0.4042 0.0288  0.0332  -0.0299 87  SER   A CB  
644  O  OG  . SER   A 81  ? 0.3442 0.2926 0.3940 0.0274  0.0277  -0.0251 87  SER   A OG  
645  N  N   . GLU   A 82  ? 0.3642 0.2959 0.4060 0.0224  0.0407  -0.0468 88  GLU   A N   
646  C  CA  . GLU   A 82  ? 0.3669 0.2902 0.4027 0.0180  0.0405  -0.0515 88  GLU   A CA  
647  C  C   . GLU   A 82  ? 0.3454 0.2689 0.3803 0.0169  0.0333  -0.0444 88  GLU   A C   
648  O  O   . GLU   A 82  ? 0.3415 0.2586 0.3736 0.0135  0.0326  -0.0469 88  GLU   A O   
649  C  CB  . GLU   A 82  ? 0.4178 0.3421 0.4378 0.0113  0.0415  -0.0591 88  GLU   A CB  
650  C  CG  . GLU   A 82  ? 0.5258 0.4598 0.5355 0.0091  0.0356  -0.0547 88  GLU   A CG  
651  C  CD  . GLU   A 82  ? 0.6518 0.5878 0.6463 0.0021  0.0350  -0.0600 88  GLU   A CD  
652  O  OE1 . GLU   A 82  ? 0.6640 0.6057 0.6524 0.0008  0.0363  -0.0612 88  GLU   A OE1 
653  O  OE2 . GLU   A 82  ? 0.6942 0.6264 0.6827 -0.0026 0.0327  -0.0623 88  GLU   A OE2 
654  N  N   . TYR   A 83  ? 0.3237 0.2549 0.3609 0.0193  0.0282  -0.0359 89  TYR   A N   
655  C  CA  . TYR   A 83  ? 0.3116 0.2445 0.3475 0.0179  0.0221  -0.0297 89  TYR   A CA  
656  C  C   . TYR   A 83  ? 0.3098 0.2415 0.3576 0.0214  0.0205  -0.0222 89  TYR   A C   
657  O  O   . TYR   A 83  ? 0.3070 0.2365 0.3547 0.0195  0.0171  -0.0188 89  TYR   A O   
658  C  CB  . TYR   A 83  ? 0.3004 0.2426 0.3283 0.0165  0.0175  -0.0262 89  TYR   A CB  
659  C  CG  . TYR   A 83  ? 0.3179 0.2615 0.3337 0.0123  0.0175  -0.0318 89  TYR   A CG  
660  C  CD1 . TYR   A 83  ? 0.3381 0.2797 0.3471 0.0078  0.0150  -0.0339 89  TYR   A CD1 
661  C  CD2 . TYR   A 83  ? 0.3500 0.2977 0.3615 0.0124  0.0198  -0.0343 89  TYR   A CD2 
662  C  CE1 . TYR   A 83  ? 0.3547 0.2988 0.3531 0.0036  0.0140  -0.0377 89  TYR   A CE1 
663  C  CE2 . TYR   A 83  ? 0.3736 0.3231 0.3737 0.0079  0.0192  -0.0384 89  TYR   A CE2 
664  C  CZ  . TYR   A 83  ? 0.3857 0.3336 0.3794 0.0035  0.0160  -0.0397 89  TYR   A CZ  
665  O  OH  . TYR   A 83  ? 0.4210 0.3718 0.4039 -0.0013 0.0145  -0.0424 89  TYR   A OH  
666  N  N   . TYR   A 84  ? 0.3035 0.2371 0.3620 0.0263  0.0229  -0.0192 90  TYR   A N   
667  C  CA  . TYR   A 84  ? 0.2951 0.2289 0.3658 0.0295  0.0206  -0.0105 90  TYR   A CA  
668  C  C   . TYR   A 84  ? 0.3169 0.2479 0.4021 0.0349  0.0257  -0.0108 90  TYR   A C   
669  O  O   . TYR   A 84  ? 0.3179 0.2521 0.4033 0.0366  0.0298  -0.0153 90  TYR   A O   
670  C  CB  . TYR   A 84  ? 0.2725 0.2175 0.3419 0.0296  0.0156  -0.0026 90  TYR   A CB  
671  C  CG  . TYR   A 84  ? 0.2454 0.1944 0.3030 0.0251  0.0108  -0.0014 90  TYR   A CG  
672  C  CD1 . TYR   A 84  ? 0.2438 0.1906 0.3008 0.0226  0.0075  0.0023  90  TYR   A CD1 
673  C  CD2 . TYR   A 84  ? 0.2405 0.1957 0.2884 0.0234  0.0099  -0.0037 90  TYR   A CD2 
674  C  CE1 . TYR   A 84  ? 0.2333 0.1845 0.2810 0.0187  0.0040  0.0030  90  TYR   A CE1 
675  C  CE2 . TYR   A 84  ? 0.2395 0.1983 0.2788 0.0200  0.0061  -0.0026 90  TYR   A CE2 
676  C  CZ  . TYR   A 84  ? 0.2298 0.1867 0.2693 0.0178  0.0034  0.0003  90  TYR   A CZ  
677  O  OH  . TYR   A 84  ? 0.2151 0.1758 0.2472 0.0146  0.0005  0.0008  90  TYR   A OH  
678  N  N   . PRO   A 85  ? 0.3429 0.2696 0.4414 0.0378  0.0251  -0.0045 91  PRO   A N   
679  C  CA  . PRO   A 85  ? 0.3659 0.2922 0.4814 0.0441  0.0292  -0.0024 91  PRO   A CA  
680  C  C   . PRO   A 85  ? 0.3775 0.3174 0.4969 0.0463  0.0261  0.0050  91  PRO   A C   
681  O  O   . PRO   A 85  ? 0.3751 0.3230 0.4844 0.0428  0.0206  0.0089  91  PRO   A O   
682  C  CB  . PRO   A 85  ? 0.3731 0.2918 0.5009 0.0458  0.0275  0.0045  91  PRO   A CB  
683  C  CG  . PRO   A 85  ? 0.3767 0.2991 0.4945 0.0408  0.0201  0.0108  91  PRO   A CG  
684  C  CD  . PRO   A 85  ? 0.3515 0.2752 0.4511 0.0357  0.0202  0.0024  91  PRO   A CD  
685  N  N   . ALA   A 86  ? 0.3769 0.3196 0.5121 0.0520  0.0294  0.0073  92  ALA   A N   
686  C  CA  . ALA   A 86  ? 0.3754 0.3318 0.5156 0.0537  0.0261  0.0150  92  ALA   A CA  
687  C  C   . ALA   A 86  ? 0.3578 0.3185 0.5007 0.0521  0.0182  0.0271  92  ALA   A C   
688  O  O   . ALA   A 86  ? 0.3720 0.3256 0.5239 0.0535  0.0171  0.0318  92  ALA   A O   
689  C  CB  . ALA   A 86  ? 0.3855 0.3441 0.5447 0.0602  0.0314  0.0155  92  ALA   A CB  
690  N  N   . ARG   A 87  ? 0.3225 0.2935 0.4549 0.0481  0.0128  0.0312  93  ARG   A N   
691  C  CA  . ARG   A 87  ? 0.2916 0.2668 0.4229 0.0450  0.0056  0.0414  93  ARG   A CA  
692  C  C   . ARG   A 87  ? 0.2758 0.2642 0.3993 0.0414  0.0012  0.0454  93  ARG   A C   
693  O  O   . ARG   A 87  ? 0.2835 0.2760 0.4011 0.0413  0.0037  0.0398  93  ARG   A O   
694  C  CB  . ARG   A 87  ? 0.2899 0.2569 0.4087 0.0403  0.0042  0.0380  93  ARG   A CB  
695  C  CG  . ARG   A 87  ? 0.2860 0.2560 0.3864 0.0356  0.0037  0.0312  93  ARG   A CG  
696  C  CD  . ARG   A 87  ? 0.2794 0.2413 0.3687 0.0322  0.0043  0.0248  93  ARG   A CD  
697  N  NE  . ARG   A 87  ? 0.2523 0.2191 0.3272 0.0273  0.0014  0.0232  93  ARG   A NE  
698  C  CZ  . ARG   A 87  ? 0.2517 0.2223 0.3175 0.0262  0.0023  0.0181  93  ARG   A CZ  
699  N  NH1 . ARG   A 87  ? 0.2615 0.2332 0.3297 0.0291  0.0059  0.0142  93  ARG   A NH1 
700  N  NH2 . ARG   A 87  ? 0.2269 0.2006 0.2817 0.0222  -0.0002 0.0173  93  ARG   A NH2 
701  N  N   . TYR   A 88  ? 0.2635 0.2576 0.3851 0.0376  -0.0051 0.0545  94  TYR   A N   
702  C  CA  . TYR   A 88  ? 0.2524 0.2578 0.3647 0.0328  -0.0092 0.0577  94  TYR   A CA  
703  C  C   . TYR   A 88  ? 0.2315 0.2340 0.3261 0.0273  -0.0102 0.0524  94  TYR   A C   
704  O  O   . TYR   A 88  ? 0.2475 0.2449 0.3387 0.0248  -0.0118 0.0536  94  TYR   A O   
705  C  CB  . TYR   A 88  ? 0.2541 0.2687 0.3739 0.0309  -0.0154 0.0705  94  TYR   A CB  
706  C  CG  . TYR   A 88  ? 0.2651 0.2872 0.4020 0.0358  -0.0151 0.0761  94  TYR   A CG  
707  C  CD1 . TYR   A 88  ? 0.2745 0.3078 0.4100 0.0346  -0.0157 0.0765  94  TYR   A CD1 
708  C  CD2 . TYR   A 88  ? 0.2778 0.2952 0.4330 0.0420  -0.0136 0.0804  94  TYR   A CD2 
709  C  CE1 . TYR   A 88  ? 0.2858 0.3269 0.4379 0.0393  -0.0151 0.0813  94  TYR   A CE1 
710  C  CE2 . TYR   A 88  ? 0.2870 0.3118 0.4601 0.0472  -0.0128 0.0855  94  TYR   A CE2 
711  C  CZ  . TYR   A 88  ? 0.2922 0.3293 0.4636 0.0459  -0.0135 0.0858  94  TYR   A CZ  
712  O  OH  . TYR   A 88  ? 0.3226 0.3683 0.5128 0.0510  -0.0126 0.0909  94  TYR   A OH  
713  N  N   . GLN   A 89  ? 0.2150 0.2209 0.2992 0.0254  -0.0089 0.0464  95  GLN   A N   
714  C  CA  . GLN   A 89  ? 0.1957 0.1997 0.2648 0.0206  -0.0096 0.0416  95  GLN   A CA  
715  C  C   . GLN   A 89  ? 0.1982 0.2119 0.2615 0.0154  -0.0136 0.0466  95  GLN   A C   
716  O  O   . GLN   A 89  ? 0.1895 0.2110 0.2551 0.0153  -0.0143 0.0489  95  GLN   A O   
717  C  CB  . GLN   A 89  ? 0.1829 0.1831 0.2443 0.0216  -0.0057 0.0320  95  GLN   A CB  
718  C  CG  . GLN   A 89  ? 0.1827 0.1814 0.2309 0.0173  -0.0065 0.0277  95  GLN   A CG  
719  C  CD  . GLN   A 89  ? 0.1980 0.1913 0.2398 0.0183  -0.0034 0.0194  95  GLN   A CD  
720  O  OE1 . GLN   A 89  ? 0.2261 0.2136 0.2711 0.0211  -0.0005 0.0155  95  GLN   A OE1 
721  N  NE2 . GLN   A 89  ? 0.1885 0.1835 0.2209 0.0156  -0.0039 0.0165  95  GLN   A NE2 
722  N  N   . SER   A 90  ? 0.1914 0.2051 0.2467 0.0105  -0.0160 0.0478  96  SER   A N   
723  C  CA  . SER   A 90  ? 0.1913 0.2138 0.2397 0.0044  -0.0191 0.0515  96  SER   A CA  
724  C  C   . SER   A 90  ? 0.1915 0.2132 0.2274 0.0015  -0.0172 0.0438  96  SER   A C   
725  O  O   . SER   A 90  ? 0.1939 0.2085 0.2265 0.0038  -0.0142 0.0367  96  SER   A O   
726  C  CB  . SER   A 90  ? 0.2200 0.2440 0.2670 -0.0001 -0.0224 0.0577  96  SER   A CB  
727  O  OG  . SER   A 90  ? 0.2584 0.2751 0.2989 -0.0010 -0.0203 0.0519  96  SER   A OG  
728  N  N   . HIS   A 91  ? 0.1855 0.2149 0.2152 -0.0040 -0.0190 0.0456  97  HIS   A N   
729  C  CA  . HIS   A 91  ? 0.1905 0.2193 0.2094 -0.0073 -0.0172 0.0389  97  HIS   A CA  
730  C  C   . HIS   A 91  ? 0.1857 0.2103 0.2046 -0.0031 -0.0142 0.0330  97  HIS   A C   
731  O  O   . HIS   A 91  ? 0.1879 0.2080 0.2001 -0.0035 -0.0121 0.0267  97  HIS   A O   
732  C  CB  . HIS   A 91  ? 0.2103 0.2346 0.2227 -0.0098 -0.0159 0.0351  97  HIS   A CB  
733  C  CG  . HIS   A 91  ? 0.2414 0.2705 0.2520 -0.0152 -0.0185 0.0408  97  HIS   A CG  
734  N  ND1 . HIS   A 91  ? 0.2707 0.3058 0.2728 -0.0224 -0.0190 0.0408  97  HIS   A ND1 
735  C  CD2 . HIS   A 91  ? 0.2575 0.2861 0.2736 -0.0148 -0.0206 0.0467  97  HIS   A CD2 
736  C  CE1 . HIS   A 91  ? 0.2695 0.3084 0.2713 -0.0266 -0.0215 0.0467  97  HIS   A CE1 
737  N  NE2 . HIS   A 91  ? 0.2666 0.3017 0.2771 -0.0221 -0.0228 0.0510  97  HIS   A NE2 
738  N  N   . LEU   A 92  ? 0.1779 0.2049 0.2046 0.0005  -0.0141 0.0353  98  LEU   A N   
739  C  CA  . LEU   A 92  ? 0.1833 0.2074 0.2101 0.0039  -0.0112 0.0303  98  LEU   A CA  
740  C  C   . LEU   A 92  ? 0.1774 0.2083 0.2021 0.0011  -0.0117 0.0312  98  LEU   A C   
741  O  O   . LEU   A 92  ? 0.1879 0.2272 0.2170 -0.0010 -0.0143 0.0372  98  LEU   A O   
742  C  CB  . LEU   A 92  ? 0.1911 0.2129 0.2285 0.0099  -0.0095 0.0311  98  LEU   A CB  
743  C  CG  . LEU   A 92  ? 0.2204 0.2389 0.2576 0.0131  -0.0058 0.0254  98  LEU   A CG  
744  C  CD1 . LEU   A 92  ? 0.2211 0.2318 0.2497 0.0129  -0.0042 0.0189  98  LEU   A CD1 
745  C  CD2 . LEU   A 92  ? 0.2168 0.2340 0.2658 0.0185  -0.0033 0.0261  98  LEU   A CD2 
746  N  N   . MET   A 93  ? 0.1687 0.1964 0.1870 0.0007  -0.0095 0.0257  99  MET   A N   
747  C  CA  . MET   A 93  ? 0.1690 0.2020 0.1848 -0.0024 -0.0096 0.0258  99  MET   A CA  
748  C  C   . MET   A 93  ? 0.1844 0.2157 0.2026 0.0012  -0.0069 0.0231  99  MET   A C   
749  O  O   . MET   A 93  ? 0.1865 0.2106 0.2021 0.0039  -0.0048 0.0185  99  MET   A O   
750  C  CB  . MET   A 93  ? 0.1814 0.2110 0.1867 -0.0070 -0.0092 0.0217  99  MET   A CB  
751  C  CG  . MET   A 93  ? 0.1973 0.2282 0.1988 -0.0113 -0.0109 0.0231  99  MET   A CG  
752  S  SD  . MET   A 93  ? 0.2432 0.2688 0.2340 -0.0160 -0.0089 0.0168  99  MET   A SD  
753  C  CE  . MET   A 93  ? 0.2638 0.2797 0.2553 -0.0102 -0.0066 0.0119  99  MET   A CE  
754  N  N   . LEU   A 94  ? 0.1714 0.2103 0.1946 0.0008  -0.0069 0.0259  100 LEU   A N   
755  C  CA  . LEU   A 94  ? 0.1804 0.2189 0.2059 0.0036  -0.0037 0.0232  100 LEU   A CA  
756  C  C   . LEU   A 94  ? 0.1887 0.2288 0.2075 -0.0005 -0.0033 0.0215  100 LEU   A C   
757  O  O   . LEU   A 94  ? 0.1846 0.2298 0.2010 -0.0054 -0.0055 0.0240  100 LEU   A O   
758  C  CB  . LEU   A 94  ? 0.1988 0.2449 0.2372 0.0071  -0.0029 0.0271  100 LEU   A CB  
759  C  CG  . LEU   A 94  ? 0.2387 0.2824 0.2863 0.0120  -0.0025 0.0288  100 LEU   A CG  
760  C  CD1 . LEU   A 94  ? 0.2586 0.3098 0.3210 0.0161  -0.0009 0.0324  100 LEU   A CD1 
761  C  CD2 . LEU   A 94  ? 0.2562 0.2892 0.2997 0.0151  0.0007  0.0224  100 LEU   A CD2 
762  N  N   . ALA   A 95  ? 0.1889 0.2250 0.2047 0.0009  -0.0004 0.0176  101 ALA   A N   
763  C  CA  . ALA   A 95  ? 0.1910 0.2279 0.2010 -0.0029 0.0003  0.0164  101 ALA   A CA  
764  C  C   . ALA   A 95  ? 0.1849 0.2231 0.1972 -0.0007 0.0037  0.0146  101 ALA   A C   
765  O  O   . ALA   A 95  ? 0.1854 0.2210 0.2010 0.0035  0.0060  0.0125  101 ALA   A O   
766  C  CB  . ALA   A 95  ? 0.2004 0.2279 0.2003 -0.0051 -0.0002 0.0130  101 ALA   A CB  
767  N  N   . VAL   A 96  ? 0.1654 0.2072 0.1750 -0.0043 0.0045  0.0149  102 VAL   A N   
768  C  CA  . VAL   A 96  ? 0.1706 0.2135 0.1801 -0.0036 0.0081  0.0128  102 VAL   A CA  
769  C  C   . VAL   A 96  ? 0.2025 0.2355 0.2011 -0.0050 0.0081  0.0096  102 VAL   A C   
770  O  O   . VAL   A 96  ? 0.2192 0.2479 0.2113 -0.0084 0.0060  0.0100  102 VAL   A O   
771  C  CB  . VAL   A 96  ? 0.1686 0.2205 0.1802 -0.0074 0.0087  0.0151  102 VAL   A CB  
772  C  CG1 . VAL   A 96  ? 0.1833 0.2363 0.1932 -0.0076 0.0128  0.0126  102 VAL   A CG1 
773  C  CG2 . VAL   A 96  ? 0.1673 0.2303 0.1915 -0.0057 0.0081  0.0193  102 VAL   A CG2 
774  N  N   . GLY   A 97  ? 0.2056 0.2350 0.2032 -0.0022 0.0102  0.0066  103 GLY   A N   
775  C  CA  . GLY   A 97  ? 0.2219 0.2432 0.2101 -0.0034 0.0097  0.0046  103 GLY   A CA  
776  C  C   . GLY   A 97  ? 0.2165 0.2357 0.2041 -0.0010 0.0122  0.0011  103 GLY   A C   
777  O  O   . GLY   A 97  ? 0.2228 0.2443 0.2175 0.0024  0.0144  -0.0003 103 GLY   A O   
778  N  N   . HIS   A 98  ? 0.2114 0.2263 0.1904 -0.0033 0.0121  -0.0002 104 HIS   A N   
779  C  CA  . HIS   A 98  ? 0.2143 0.2273 0.1905 -0.0024 0.0144  -0.0039 104 HIS   A CA  
780  C  C   . HIS   A 98  ? 0.2026 0.2099 0.1798 0.0004  0.0122  -0.0052 104 HIS   A C   
781  O  O   . HIS   A 98  ? 0.2044 0.2074 0.1796 0.0002  0.0084  -0.0032 104 HIS   A O   
782  C  CB  . HIS   A 98  ? 0.2237 0.2348 0.1896 -0.0068 0.0140  -0.0040 104 HIS   A CB  
783  C  CG  . HIS   A 98  ? 0.2322 0.2425 0.1940 -0.0073 0.0167  -0.0083 104 HIS   A CG  
784  N  ND1 . HIS   A 98  ? 0.2471 0.2622 0.2118 -0.0070 0.0224  -0.0123 104 HIS   A ND1 
785  C  CD2 . HIS   A 98  ? 0.2333 0.2389 0.1889 -0.0083 0.0144  -0.0094 104 HIS   A CD2 
786  C  CE1 . HIS   A 98  ? 0.2492 0.2614 0.2086 -0.0081 0.0238  -0.0165 104 HIS   A CE1 
787  N  NE2 . HIS   A 98  ? 0.2403 0.2472 0.1939 -0.0092 0.0187  -0.0145 104 HIS   A NE2 
788  N  N   . SER   A 99  ? 0.2109 0.2179 0.1910 0.0025  0.0151  -0.0088 105 SER   A N   
789  C  CA  . SER   A 99  ? 0.2038 0.2055 0.1838 0.0042  0.0135  -0.0106 105 SER   A CA  
790  C  C   . SER   A 99  ? 0.2340 0.2347 0.2136 0.0045  0.0178  -0.0159 105 SER   A C   
791  O  O   . SER   A 99  ? 0.2498 0.2544 0.2332 0.0050  0.0226  -0.0183 105 SER   A O   
792  C  CB  . SER   A 99  ? 0.2259 0.2267 0.2135 0.0074  0.0115  -0.0083 105 SER   A CB  
793  O  OG  . SER   A 99  ? 0.2331 0.2378 0.2301 0.0103  0.0145  -0.0084 105 SER   A OG  
794  N  N   . GLU   A 100 ? 0.2308 0.2264 0.2055 0.0035  0.0161  -0.0180 106 GLU   A N   
795  C  CA  . GLU   A 100 ? 0.2440 0.2368 0.2168 0.0027  0.0193  -0.0237 106 GLU   A CA  
796  C  C   . GLU   A 100 ? 0.2556 0.2434 0.2315 0.0046  0.0166  -0.0238 106 GLU   A C   
797  O  O   . GLU   A 100 ? 0.2531 0.2401 0.2303 0.0056  0.0121  -0.0196 106 GLU   A O   
798  C  CB  . GLU   A 100 ? 0.2590 0.2519 0.2195 -0.0029 0.0188  -0.0256 106 GLU   A CB  
799  C  CG  . GLU   A 100 ? 0.2770 0.2750 0.2335 -0.0055 0.0207  -0.0244 106 GLU   A CG  
800  C  CD  . GLU   A 100 ? 0.3040 0.3035 0.2482 -0.0118 0.0209  -0.0257 106 GLU   A CD  
801  O  OE1 . GLU   A 100 ? 0.3394 0.3367 0.2771 -0.0149 0.0208  -0.0292 106 GLU   A OE1 
802  O  OE2 . GLU   A 100 ? 0.2914 0.2948 0.2321 -0.0143 0.0212  -0.0231 106 GLU   A OE2 
803  N  N   . PRO   A 101 ? 0.2755 0.2597 0.2533 0.0050  0.0198  -0.0287 107 PRO   A N   
804  C  CA  . PRO   A 101 ? 0.2834 0.2628 0.2650 0.0067  0.0175  -0.0284 107 PRO   A CA  
805  C  C   . PRO   A 101 ? 0.2778 0.2564 0.2539 0.0045  0.0116  -0.0255 107 PRO   A C   
806  O  O   . PRO   A 101 ? 0.2841 0.2618 0.2649 0.0066  0.0085  -0.0222 107 PRO   A O   
807  C  CB  . PRO   A 101 ? 0.3052 0.2801 0.2865 0.0056  0.0223  -0.0353 107 PRO   A CB  
808  C  CG  . PRO   A 101 ? 0.3064 0.2842 0.2905 0.0064  0.0283  -0.0384 107 PRO   A CG  
809  C  CD  . PRO   A 101 ? 0.2841 0.2679 0.2619 0.0042  0.0264  -0.0351 107 PRO   A CD  
810  N  N   . GLY   A 102 ? 0.2495 0.2292 0.2162 0.0003  0.0099  -0.0262 108 GLY   A N   
811  C  CA  . GLY   A 102 ? 0.2435 0.2234 0.2060 -0.0017 0.0043  -0.0231 108 GLY   A CA  
812  C  C   . GLY   A 102 ? 0.2200 0.2017 0.1849 0.0001  0.0008  -0.0174 108 GLY   A C   
813  O  O   . GLY   A 102 ? 0.2305 0.2123 0.1948 -0.0005 -0.0034 -0.0146 108 GLY   A O   
814  N  N   . ASP   A 103 ? 0.2016 0.1852 0.1700 0.0022  0.0027  -0.0157 109 ASP   A N   
815  C  CA  . ASP   A 103 ? 0.1941 0.1787 0.1649 0.0035  0.0001  -0.0112 109 ASP   A CA  
816  C  C   . ASP   A 103 ? 0.2020 0.1854 0.1794 0.0062  -0.0011 -0.0099 109 ASP   A C   
817  O  O   . ASP   A 103 ? 0.1951 0.1788 0.1740 0.0066  -0.0031 -0.0071 109 ASP   A O   
818  C  CB  . ASP   A 103 ? 0.1937 0.1813 0.1652 0.0037  0.0024  -0.0100 109 ASP   A CB  
819  C  CG  . ASP   A 103 ? 0.2147 0.2038 0.1787 0.0002  0.0028  -0.0099 109 ASP   A CG  
820  O  OD1 . ASP   A 103 ? 0.2133 0.2012 0.1722 -0.0021 -0.0005 -0.0081 109 ASP   A OD1 
821  O  OD2 . ASP   A 103 ? 0.2247 0.2167 0.1884 -0.0005 0.0063  -0.0111 109 ASP   A OD2 
822  N  N   . CYS   A 104 ? 0.1998 0.1816 0.1812 0.0075  0.0003  -0.0121 110 CYS   A N   
823  C  CA  . CYS   A 104 ? 0.1981 0.1793 0.1851 0.0092  -0.0009 -0.0104 110 CYS   A CA  
824  C  C   . CYS   A 104 ? 0.1943 0.1752 0.1800 0.0083  -0.0043 -0.0090 110 CYS   A C   
825  O  O   . CYS   A 104 ? 0.2040 0.1842 0.1861 0.0066  -0.0060 -0.0098 110 CYS   A O   
826  C  CB  . CYS   A 104 ? 0.2145 0.1930 0.2054 0.0101  0.0007  -0.0125 110 CYS   A CB  
827  S  SG  . CYS   A 104 ? 0.2291 0.2084 0.2265 0.0127  0.0048  -0.0128 110 CYS   A SG  
828  N  N   . GLY   A 105 ? 0.1891 0.1709 0.1779 0.0091  -0.0051 -0.0068 111 GLY   A N   
829  C  CA  . GLY   A 105 ? 0.1924 0.1743 0.1820 0.0088  -0.0073 -0.0059 111 GLY   A CA  
830  C  C   . GLY   A 105 ? 0.1971 0.1792 0.1855 0.0086  -0.0079 -0.0042 111 GLY   A C   
831  O  O   . GLY   A 105 ? 0.1942 0.1761 0.1851 0.0089  -0.0088 -0.0036 111 GLY   A O   
832  N  N   . GLY   A 106 ? 0.1931 0.1753 0.1781 0.0080  -0.0071 -0.0037 112 GLY   A N   
833  C  CA  . GLY   A 106 ? 0.1959 0.1773 0.1798 0.0074  -0.0076 -0.0019 112 GLY   A CA  
834  C  C   . GLY   A 106 ? 0.1780 0.1597 0.1646 0.0073  -0.0064 -0.0019 112 GLY   A C   
835  O  O   . GLY   A 106 ? 0.1811 0.1651 0.1689 0.0072  -0.0051 -0.0021 112 GLY   A O   
836  N  N   . ILE   A 107 ? 0.1689 0.1485 0.1569 0.0072  -0.0067 -0.0015 113 ILE   A N   
837  C  CA  . ILE   A 107 ? 0.1617 0.1414 0.1511 0.0062  -0.0049 -0.0025 113 ILE   A CA  
838  C  C   . ILE   A 107 ? 0.1756 0.1557 0.1620 0.0039  -0.0037 -0.0020 113 ILE   A C   
839  O  O   . ILE   A 107 ? 0.1758 0.1540 0.1600 0.0032  -0.0041 -0.0009 113 ILE   A O   
840  C  CB  . ILE   A 107 ? 0.1708 0.1475 0.1639 0.0069  -0.0047 -0.0034 113 ILE   A CB  
841  C  CG1 . ILE   A 107 ? 0.1782 0.1567 0.1753 0.0084  -0.0051 -0.0043 113 ILE   A CG1 
842  C  CG2 . ILE   A 107 ? 0.1798 0.1549 0.1728 0.0048  -0.0020 -0.0053 113 ILE   A CG2 
843  C  CD1 . ILE   A 107 ? 0.2068 0.1837 0.2097 0.0098  -0.0046 -0.0050 113 ILE   A CD1 
844  N  N   . LEU   A 108 ? 0.1644 0.1475 0.1507 0.0021  -0.0026 -0.0025 114 LEU   A N   
845  C  CA  . LEU   A 108 ? 0.1680 0.1525 0.1519 -0.0011 -0.0017 -0.0022 114 LEU   A CA  
846  C  C   . LEU   A 108 ? 0.1690 0.1508 0.1526 -0.0033 0.0001  -0.0048 114 LEU   A C   
847  O  O   . LEU   A 108 ? 0.1797 0.1630 0.1650 -0.0033 0.0007  -0.0061 114 LEU   A O   
848  C  CB  . LEU   A 108 ? 0.1785 0.1693 0.1628 -0.0024 -0.0019 -0.0005 114 LEU   A CB  
849  C  CG  . LEU   A 108 ? 0.2000 0.1941 0.1819 -0.0067 -0.0015 0.0002  114 LEU   A CG  
850  C  CD1 . LEU   A 108 ? 0.1950 0.1886 0.1751 -0.0077 -0.0013 0.0010  114 LEU   A CD1 
851  C  CD2 . LEU   A 108 ? 0.2022 0.2038 0.1865 -0.0077 -0.0026 0.0032  114 LEU   A CD2 
852  N  N   . ARG   A 109 ? 0.1682 0.1463 0.1500 -0.0056 0.0013  -0.0059 115 ARG   A N   
853  C  CA  . ARG   A 109 ? 0.1644 0.1392 0.1464 -0.0078 0.0040  -0.0095 115 ARG   A CA  
854  C  C   . ARG   A 109 ? 0.1990 0.1730 0.1765 -0.0129 0.0054  -0.0106 115 ARG   A C   
855  O  O   . ARG   A 109 ? 0.2061 0.1804 0.1817 -0.0140 0.0042  -0.0084 115 ARG   A O   
856  C  CB  . ARG   A 109 ? 0.1968 0.1648 0.1833 -0.0045 0.0047  -0.0106 115 ARG   A CB  
857  C  CG  . ARG   A 109 ? 0.2159 0.1789 0.2019 -0.0041 0.0036  -0.0083 115 ARG   A CG  
858  C  CD  . ARG   A 109 ? 0.2326 0.1897 0.2250 -0.0004 0.0036  -0.0081 115 ARG   A CD  
859  N  NE  . ARG   A 109 ? 0.2493 0.2093 0.2446 0.0034  0.0007  -0.0054 115 ARG   A NE  
860  C  CZ  . ARG   A 109 ? 0.2500 0.2102 0.2518 0.0064  0.0007  -0.0062 115 ARG   A CZ  
861  N  NH1 . ARG   A 109 ? 0.2361 0.1941 0.2422 0.0064  0.0043  -0.0100 115 ARG   A NH1 
862  N  NH2 . ARG   A 109 ? 0.2385 0.2018 0.2421 0.0089  -0.0024 -0.0036 115 ARG   A NH2 
863  N  N   . CYS   A 110 ? 0.2085 0.1814 0.1845 -0.0167 0.0082  -0.0146 116 CYS   A N   
864  C  CA  . CYS   A 110 ? 0.2389 0.2104 0.2100 -0.0228 0.0100  -0.0168 116 CYS   A CA  
865  C  C   . CYS   A 110 ? 0.2809 0.2436 0.2537 -0.0236 0.0144  -0.0223 116 CYS   A C   
866  O  O   . CYS   A 110 ? 0.2757 0.2344 0.2545 -0.0187 0.0154  -0.0232 116 CYS   A O   
867  C  CB  . CYS   A 110 ? 0.2518 0.2318 0.2182 -0.0282 0.0096  -0.0165 116 CYS   A CB  
868  S  SG  . CYS   A 110 ? 0.2482 0.2300 0.2140 -0.0301 0.0124  -0.0207 116 CYS   A SG  
869  N  N   . GLN   A 111 ? 0.3099 0.2696 0.2779 -0.0300 0.0173  -0.0263 117 GLN   A N   
870  C  CA  . GLN   A 111 ? 0.3468 0.2972 0.3173 -0.0307 0.0224  -0.0324 117 GLN   A CA  
871  C  C   . GLN   A 111 ? 0.3582 0.3101 0.3314 -0.0297 0.0258  -0.0368 117 GLN   A C   
872  O  O   . GLN   A 111 ? 0.3816 0.3262 0.3609 -0.0272 0.0300  -0.0411 117 GLN   A O   
873  C  CB  . GLN   A 111 ? 0.4016 0.3486 0.3654 -0.0389 0.0254  -0.0367 117 GLN   A CB  
874  C  CG  . GLN   A 111 ? 0.4800 0.4361 0.4355 -0.0467 0.0257  -0.0387 117 GLN   A CG  
875  C  CD  . GLN   A 111 ? 0.5774 0.5314 0.5252 -0.0560 0.0282  -0.0430 117 GLN   A CD  
876  O  OE1 . GLN   A 111 ? 0.6043 0.5638 0.5473 -0.0604 0.0248  -0.0393 117 GLN   A OE1 
877  N  NE2 . GLN   A 111 ? 0.5847 0.5310 0.5314 -0.0596 0.0344  -0.0511 117 GLN   A NE2 
878  N  N   . HIS   A 112 ? 0.3289 0.2905 0.2987 -0.0314 0.0241  -0.0353 118 HIS   A N   
879  C  CA  . HIS   A 112 ? 0.3034 0.2677 0.2745 -0.0318 0.0273  -0.0392 118 HIS   A CA  
880  C  C   . HIS   A 112 ? 0.2910 0.2567 0.2702 -0.0243 0.0256  -0.0364 118 HIS   A C   
881  O  O   . HIS   A 112 ? 0.3117 0.2793 0.2937 -0.0240 0.0287  -0.0397 118 HIS   A O   
882  C  CB  . HIS   A 112 ? 0.2889 0.2630 0.2516 -0.0389 0.0263  -0.0386 118 HIS   A CB  
883  C  CG  . HIS   A 112 ? 0.3208 0.2953 0.2748 -0.0475 0.0273  -0.0409 118 HIS   A CG  
884  N  ND1 . HIS   A 112 ? 0.3340 0.3145 0.2839 -0.0501 0.0224  -0.0353 118 HIS   A ND1 
885  C  CD2 . HIS   A 112 ? 0.3485 0.3189 0.2976 -0.0542 0.0328  -0.0485 118 HIS   A CD2 
886  C  CE1 . HIS   A 112 ? 0.3691 0.3493 0.3117 -0.0585 0.0245  -0.0390 118 HIS   A CE1 
887  N  NE2 . HIS   A 112 ? 0.3707 0.3442 0.3120 -0.0615 0.0309  -0.0473 118 HIS   A NE2 
888  N  N   . GLY   A 113 ? 0.2638 0.2295 0.2463 -0.0190 0.0208  -0.0305 119 GLY   A N   
889  C  CA  . GLY   A 113 ? 0.2482 0.2158 0.2372 -0.0129 0.0187  -0.0278 119 GLY   A CA  
890  C  C   . GLY   A 113 ? 0.2146 0.1873 0.2019 -0.0110 0.0134  -0.0218 119 GLY   A C   
891  O  O   . GLY   A 113 ? 0.2207 0.1943 0.2039 -0.0125 0.0113  -0.0191 119 GLY   A O   
892  N  N   . VAL   A 114 ? 0.1983 0.1744 0.1893 -0.0076 0.0117  -0.0200 120 VAL   A N   
893  C  CA  . VAL   A 114 ? 0.1820 0.1618 0.1722 -0.0055 0.0075  -0.0152 120 VAL   A CA  
894  C  C   . VAL   A 114 ? 0.1790 0.1650 0.1646 -0.0094 0.0066  -0.0135 120 VAL   A C   
895  O  O   . VAL   A 114 ? 0.1735 0.1630 0.1579 -0.0123 0.0081  -0.0149 120 VAL   A O   
896  C  CB  . VAL   A 114 ? 0.1936 0.1743 0.1894 -0.0013 0.0062  -0.0142 120 VAL   A CB  
897  C  CG1 . VAL   A 114 ? 0.1956 0.1793 0.1903 0.0002  0.0027  -0.0105 120 VAL   A CG1 
898  C  CG2 . VAL   A 114 ? 0.2003 0.1762 0.2017 0.0026  0.0059  -0.0143 120 VAL   A CG2 
899  N  N   . VAL   A 115 ? 0.1752 0.1633 0.1588 -0.0093 0.0040  -0.0100 121 VAL   A N   
900  C  CA  . VAL   A 115 ? 0.1829 0.1774 0.1640 -0.0124 0.0024  -0.0069 121 VAL   A CA  
901  C  C   . VAL   A 115 ? 0.1787 0.1758 0.1634 -0.0091 0.0001  -0.0035 121 VAL   A C   
902  O  O   . VAL   A 115 ? 0.1876 0.1893 0.1723 -0.0110 -0.0010 -0.0010 121 VAL   A O   
903  C  CB  . VAL   A 115 ? 0.1987 0.1946 0.1774 -0.0143 0.0014  -0.0050 121 VAL   A CB  
904  C  CG1 . VAL   A 115 ? 0.1988 0.2027 0.1775 -0.0164 -0.0009 -0.0005 121 VAL   A CG1 
905  C  CG2 . VAL   A 115 ? 0.2099 0.2031 0.1845 -0.0188 0.0038  -0.0086 121 VAL   A CG2 
906  N  N   . GLY   A 116 ? 0.1799 0.1739 0.1674 -0.0046 -0.0009 -0.0030 122 GLY   A N   
907  C  CA  . GLY   A 116 ? 0.1772 0.1722 0.1678 -0.0017 -0.0025 -0.0008 122 GLY   A CA  
908  C  C   . GLY   A 116 ? 0.1755 0.1669 0.1674 0.0020  -0.0031 -0.0014 122 GLY   A C   
909  O  O   . GLY   A 116 ? 0.1686 0.1567 0.1594 0.0026  -0.0027 -0.0029 122 GLY   A O   
910  N  N   . ILE   A 117 ? 0.1733 0.1649 0.1674 0.0042  -0.0039 -0.0002 123 ILE   A N   
911  C  CA  . ILE   A 117 ? 0.1621 0.1508 0.1559 0.0065  -0.0042 -0.0013 123 ILE   A CA  
912  C  C   . ILE   A 117 ? 0.1629 0.1530 0.1579 0.0077  -0.0038 -0.0003 123 ILE   A C   
913  O  O   . ILE   A 117 ? 0.1722 0.1648 0.1705 0.0078  -0.0037 0.0017  123 ILE   A O   
914  C  CB  . ILE   A 117 ? 0.1734 0.1601 0.1688 0.0077  -0.0050 -0.0025 123 ILE   A CB  
915  C  CG1 . ILE   A 117 ? 0.1772 0.1651 0.1756 0.0075  -0.0050 -0.0014 123 ILE   A CG1 
916  C  CG2 . ILE   A 117 ? 0.1755 0.1613 0.1714 0.0073  -0.0052 -0.0037 123 ILE   A CG2 
917  C  CD1 . ILE   A 117 ? 0.1891 0.1748 0.1889 0.0081  -0.0058 -0.0030 123 ILE   A CD1 
918  N  N   . VAL   A 118 ? 0.1565 0.1452 0.1492 0.0084  -0.0033 -0.0014 124 VAL   A N   
919  C  CA  . VAL   A 118 ? 0.1586 0.1486 0.1529 0.0096  -0.0018 -0.0015 124 VAL   A CA  
920  C  C   . VAL   A 118 ? 0.1662 0.1548 0.1646 0.0113  -0.0013 -0.0022 124 VAL   A C   
921  O  O   . VAL   A 118 ? 0.1730 0.1585 0.1702 0.0111  -0.0021 -0.0039 124 VAL   A O   
922  C  CB  . VAL   A 118 ? 0.1787 0.1674 0.1684 0.0092  -0.0011 -0.0033 124 VAL   A CB  
923  C  CG1 . VAL   A 118 ? 0.1870 0.1772 0.1786 0.0102  0.0016  -0.0047 124 VAL   A CG1 
924  C  CG2 . VAL   A 118 ? 0.1951 0.1845 0.1814 0.0073  -0.0016 -0.0019 124 VAL   A CG2 
925  N  N   . SER   A 119 ? 0.1634 0.1541 0.1674 0.0127  0.0000  -0.0006 125 SER   A N   
926  C  CA  . SER   A 119 ? 0.1854 0.1736 0.1946 0.0144  0.0008  -0.0008 125 SER   A CA  
927  C  C   . SER   A 119 ? 0.2045 0.1930 0.2189 0.0168  0.0039  -0.0018 125 SER   A C   
928  O  O   . SER   A 119 ? 0.2188 0.2030 0.2361 0.0181  0.0056  -0.0042 125 SER   A O   
929  C  CB  . SER   A 119 ? 0.2197 0.2098 0.2330 0.0140  -0.0011 0.0034  125 SER   A CB  
930  O  OG  . SER   A 119 ? 0.2197 0.2071 0.2391 0.0156  -0.0006 0.0043  125 SER   A OG  
931  N  N   . THR   A 120 ? 0.1763 0.1698 0.1924 0.0172  0.0051  -0.0005 126 THR   A N   
932  C  CA  . THR   A 120 ? 0.1898 0.1845 0.2128 0.0198  0.0089  -0.0017 126 THR   A CA  
933  C  C   . THR   A 120 ? 0.2088 0.2078 0.2280 0.0185  0.0106  -0.0031 126 THR   A C   
934  O  O   . THR   A 120 ? 0.2070 0.2078 0.2197 0.0158  0.0084  -0.0019 126 THR   A O   
935  C  CB  . THR   A 120 ? 0.2070 0.2061 0.2415 0.0222  0.0083  0.0037  126 THR   A CB  
936  O  OG1 . THR   A 120 ? 0.2098 0.2164 0.2442 0.0205  0.0063  0.0079  126 THR   A OG1 
937  C  CG2 . THR   A 120 ? 0.2151 0.2111 0.2530 0.0225  0.0058  0.0069  126 THR   A CG2 
938  N  N   . GLY   A 121 ? 0.2066 0.2073 0.2307 0.0203  0.0149  -0.0054 127 GLY   A N   
939  C  CA  . GLY   A 121 ? 0.2258 0.2317 0.2472 0.0188  0.0170  -0.0063 127 GLY   A CA  
940  C  C   . GLY   A 121 ? 0.2574 0.2666 0.2876 0.0214  0.0224  -0.0085 127 GLY   A C   
941  O  O   . GLY   A 121 ? 0.2841 0.2899 0.3217 0.0246  0.0252  -0.0105 127 GLY   A O   
942  N  N   . GLY   A 122 ? 0.2708 0.2867 0.3007 0.0200  0.0241  -0.0080 128 GLY   A N   
943  C  CA  . GLY   A 122 ? 0.2869 0.3081 0.3261 0.0223  0.0299  -0.0101 128 GLY   A CA  
944  C  C   . GLY   A 122 ? 0.2985 0.3244 0.3307 0.0187  0.0324  -0.0121 128 GLY   A C   
945  O  O   . GLY   A 122 ? 0.3198 0.3430 0.3391 0.0145  0.0299  -0.0126 128 GLY   A O   
946  N  N   . ASN   A 123 ? 0.2967 0.3299 0.3378 0.0202  0.0373  -0.0130 129 ASN   A N   
947  C  CA  . ASN   A 123 ? 0.2857 0.3248 0.3211 0.0164  0.0401  -0.0145 129 ASN   A CA  
948  C  C   . ASN   A 123 ? 0.2556 0.2997 0.2878 0.0132  0.0350  -0.0084 129 ASN   A C   
949  O  O   . ASN   A 123 ? 0.2443 0.2973 0.2865 0.0142  0.0348  -0.0043 129 ASN   A O   
950  C  CB  . ASN   A 123 ? 0.3147 0.3612 0.3621 0.0189  0.0475  -0.0174 129 ASN   A CB  
951  C  CG  . ASN   A 123 ? 0.3740 0.4241 0.4122 0.0141  0.0522  -0.0218 129 ASN   A CG  
952  O  OD1 . ASN   A 123 ? 0.3983 0.4456 0.4214 0.0086  0.0492  -0.0215 129 ASN   A OD1 
953  N  ND2 . ASN   A 123 ? 0.3796 0.4364 0.4274 0.0158  0.0598  -0.0255 129 ASN   A ND2 
954  N  N   . GLY   A 124 ? 0.2246 0.2632 0.2434 0.0092  0.0309  -0.0079 130 GLY   A N   
955  C  CA  . GLY   A 124 ? 0.2166 0.2578 0.2313 0.0057  0.0264  -0.0030 130 GLY   A CA  
956  C  C   . GLY   A 124 ? 0.2027 0.2427 0.2212 0.0071  0.0213  0.0013  130 GLY   A C   
957  O  O   . GLY   A 124 ? 0.2196 0.2622 0.2357 0.0040  0.0181  0.0050  130 GLY   A O   
958  N  N   . LEU   A 125 ? 0.1945 0.2300 0.2175 0.0110  0.0207  0.0008  131 LEU   A N   
959  C  CA  . LEU   A 125 ? 0.1938 0.2278 0.2186 0.0114  0.0158  0.0047  131 LEU   A CA  
960  C  C   . LEU   A 125 ? 0.2029 0.2271 0.2197 0.0114  0.0138  0.0024  131 LEU   A C   
961  O  O   . LEU   A 125 ? 0.2184 0.2375 0.2323 0.0125  0.0162  -0.0020 131 LEU   A O   
962  C  CB  . LEU   A 125 ? 0.2039 0.2420 0.2423 0.0156  0.0161  0.0077  131 LEU   A CB  
963  C  CG  . LEU   A 125 ? 0.2207 0.2701 0.2695 0.0160  0.0174  0.0112  131 LEU   A CG  
964  C  CD1 . LEU   A 125 ? 0.2313 0.2841 0.2961 0.0216  0.0191  0.0134  131 LEU   A CD1 
965  C  CD2 . LEU   A 125 ? 0.2228 0.2780 0.2685 0.0114  0.0126  0.0164  131 LEU   A CD2 
966  N  N   . VAL   A 126 ? 0.1726 0.1948 0.1861 0.0098  0.0096  0.0050  132 VAL   A N   
967  C  CA  . VAL   A 126 ? 0.1790 0.1935 0.1874 0.0100  0.0076  0.0034  132 VAL   A CA  
968  C  C   . VAL   A 126 ? 0.1692 0.1850 0.1817 0.0103  0.0046  0.0070  132 VAL   A C   
969  O  O   . VAL   A 126 ? 0.1735 0.1945 0.1871 0.0080  0.0029  0.0103  132 VAL   A O   
970  C  CB  . VAL   A 126 ? 0.1955 0.2055 0.1936 0.0069  0.0062  0.0020  132 VAL   A CB  
971  C  CG1 . VAL   A 126 ? 0.2056 0.2184 0.2015 0.0035  0.0044  0.0047  132 VAL   A CG1 
972  C  CG2 . VAL   A 126 ? 0.2016 0.2050 0.1963 0.0075  0.0041  0.0007  132 VAL   A CG2 
973  N  N   . GLY   A 127 ? 0.1722 0.1835 0.1863 0.0122  0.0040  0.0063  133 GLY   A N   
974  C  CA  . GLY   A 127 ? 0.1710 0.1835 0.1881 0.0118  0.0012  0.0099  133 GLY   A CA  
975  C  C   . GLY   A 127 ? 0.1754 0.1823 0.1861 0.0104  -0.0004 0.0081  133 GLY   A C   
976  O  O   . GLY   A 127 ? 0.1843 0.1857 0.1918 0.0114  0.0004  0.0046  133 GLY   A O   
977  N  N   . PHE   A 128 ? 0.1674 0.1763 0.1761 0.0075  -0.0027 0.0104  134 PHE   A N   
978  C  CA  . PHE   A 128 ? 0.1735 0.1780 0.1770 0.0060  -0.0036 0.0084  134 PHE   A CA  
979  C  C   . PHE   A 128 ? 0.1753 0.1811 0.1814 0.0051  -0.0051 0.0110  134 PHE   A C   
980  O  O   . PHE   A 128 ? 0.1797 0.1911 0.1884 0.0033  -0.0065 0.0152  134 PHE   A O   
981  C  CB  . PHE   A 128 ? 0.1714 0.1765 0.1692 0.0024  -0.0039 0.0076  134 PHE   A CB  
982  C  CG  . PHE   A 128 ? 0.1664 0.1705 0.1615 0.0023  -0.0027 0.0061  134 PHE   A CG  
983  C  CD1 . PHE   A 128 ? 0.1665 0.1651 0.1582 0.0035  -0.0022 0.0034  134 PHE   A CD1 
984  C  CD2 . PHE   A 128 ? 0.1785 0.1879 0.1745 0.0005  -0.0026 0.0081  134 PHE   A CD2 
985  C  CE1 . PHE   A 128 ? 0.1782 0.1760 0.1668 0.0027  -0.0015 0.0029  134 PHE   A CE1 
986  C  CE2 . PHE   A 128 ? 0.1869 0.1955 0.1800 -0.0002 -0.0015 0.0070  134 PHE   A CE2 
987  C  CZ  . PHE   A 128 ? 0.1831 0.1856 0.1722 0.0008  -0.0009 0.0045  134 PHE   A CZ  
988  N  N   . ALA   A 129 ? 0.1634 0.1647 0.1686 0.0058  -0.0051 0.0091  135 ALA   A N   
989  C  CA  . ALA   A 129 ? 0.1757 0.1781 0.1822 0.0042  -0.0064 0.0115  135 ALA   A CA  
990  C  C   . ALA   A 129 ? 0.1766 0.1807 0.1775 0.0001  -0.0064 0.0103  135 ALA   A C   
991  O  O   . ALA   A 129 ? 0.1749 0.1754 0.1725 0.0001  -0.0053 0.0063  135 ALA   A O   
992  C  CB  . ALA   A 129 ? 0.1813 0.1785 0.1890 0.0060  -0.0060 0.0093  135 ALA   A CB  
993  N  N   . ASP   A 130 ? 0.1800 0.1897 0.1799 -0.0038 -0.0076 0.0137  136 ASP   A N   
994  C  CA  . ASP   A 130 ? 0.1885 0.1999 0.1825 -0.0087 -0.0069 0.0117  136 ASP   A CA  
995  C  C   . ASP   A 130 ? 0.1917 0.2011 0.1844 -0.0097 -0.0059 0.0097  136 ASP   A C   
996  O  O   . ASP   A 130 ? 0.1978 0.2073 0.1939 -0.0089 -0.0071 0.0124  136 ASP   A O   
997  C  CB  . ASP   A 130 ? 0.2064 0.2254 0.1989 -0.0138 -0.0088 0.0163  136 ASP   A CB  
998  C  CG  . ASP   A 130 ? 0.3057 0.3268 0.2907 -0.0201 -0.0075 0.0135  136 ASP   A CG  
999  O  OD1 . ASP   A 130 ? 0.2477 0.2649 0.2294 -0.0204 -0.0051 0.0085  136 ASP   A OD1 
1000 O  OD2 . ASP   A 130 ? 0.3997 0.4257 0.3820 -0.0251 -0.0085 0.0161  136 ASP   A OD2 
1001 N  N   . VAL   A 131 ? 0.1779 0.1856 0.1668 -0.0117 -0.0036 0.0049  137 VAL   A N   
1002 C  CA  . VAL   A 131 ? 0.1760 0.1835 0.1643 -0.0134 -0.0020 0.0028  137 VAL   A CA  
1003 C  C   . VAL   A 131 ? 0.1926 0.2035 0.1753 -0.0196 0.0002  0.0003  137 VAL   A C   
1004 O  O   . VAL   A 131 ? 0.1998 0.2112 0.1818 -0.0216 0.0025  -0.0023 137 VAL   A O   
1005 C  CB  . VAL   A 131 ? 0.1845 0.1869 0.1757 -0.0094 -0.0005 -0.0013 137 VAL   A CB  
1006 C  CG1 . VAL   A 131 ? 0.1774 0.1768 0.1727 -0.0047 -0.0026 0.0004  137 VAL   A CG1 
1007 C  CG2 . VAL   A 131 ? 0.1925 0.1917 0.1826 -0.0086 0.0015  -0.0053 137 VAL   A CG2 
1008 N  N   . ARG   A 132 ? 0.1904 0.2035 0.1688 -0.0232 0.0001  0.0005  138 ARG   A N   
1009 C  CA  . ARG   A 132 ? 0.1866 0.2020 0.1587 -0.0298 0.0030  -0.0032 138 ARG   A CA  
1010 C  C   . ARG   A 132 ? 0.2093 0.2311 0.1774 -0.0360 0.0028  -0.0011 138 ARG   A C   
1011 O  O   . ARG   A 132 ? 0.2244 0.2477 0.1871 -0.0417 0.0064  -0.0058 138 ARG   A O   
1012 C  CB  . ARG   A 132 ? 0.1921 0.2088 0.1602 -0.0331 0.0025  -0.0032 138 ARG   A CB  
1013 C  CG  . ARG   A 132 ? 0.1905 0.2003 0.1611 -0.0284 0.0036  -0.0062 138 ARG   A CG  
1014 C  CD  . ARG   A 132 ? 0.1948 0.2067 0.1614 -0.0324 0.0028  -0.0054 138 ARG   A CD  
1015 N  NE  . ARG   A 132 ? 0.2095 0.2274 0.1789 -0.0313 -0.0015 0.0015  138 ARG   A NE  
1016 C  CZ  . ARG   A 132 ? 0.2387 0.2602 0.2068 -0.0338 -0.0030 0.0038  138 ARG   A CZ  
1017 N  NH1 . ARG   A 132 ? 0.2456 0.2650 0.2084 -0.0384 -0.0009 -0.0003 138 ARG   A NH1 
1018 N  NH2 . ARG   A 132 ? 0.2276 0.2548 0.2006 -0.0318 -0.0064 0.0100  138 ARG   A NH2 
1019 N  N   . ASP   A 133 ? 0.1974 0.2231 0.1680 -0.0356 -0.0012 0.0059  139 ASP   A N   
1020 C  CA  . ASP   A 133 ? 0.2087 0.2406 0.1755 -0.0419 -0.0021 0.0094  139 ASP   A CA  
1021 C  C   . ASP   A 133 ? 0.2118 0.2419 0.1806 -0.0410 0.0002  0.0072  139 ASP   A C   
1022 O  O   . ASP   A 133 ? 0.2212 0.2565 0.1861 -0.0470 0.0002  0.0094  139 ASP   A O   
1023 C  CB  . ASP   A 133 ? 0.2245 0.2613 0.1945 -0.0420 -0.0076 0.0190  139 ASP   A CB  
1024 C  CG  . ASP   A 133 ? 0.2783 0.3099 0.2575 -0.0340 -0.0093 0.0218  139 ASP   A CG  
1025 O  OD1 . ASP   A 133 ? 0.2719 0.2975 0.2547 -0.0279 -0.0079 0.0178  139 ASP   A OD1 
1026 O  OD2 . ASP   A 133 ? 0.2980 0.3314 0.2803 -0.0344 -0.0119 0.0278  139 ASP   A OD2 
1027 N  N   . LEU   A 134 ? 0.2089 0.2326 0.1836 -0.0341 0.0017  0.0035  140 LEU   A N   
1028 C  CA  . LEU   A 134 ? 0.2025 0.2251 0.1806 -0.0328 0.0034  0.0018  140 LEU   A CA  
1029 C  C   . LEU   A 134 ? 0.2094 0.2326 0.1851 -0.0356 0.0089  -0.0056 140 LEU   A C   
1030 O  O   . LEU   A 134 ? 0.2204 0.2392 0.2007 -0.0310 0.0114  -0.0105 140 LEU   A O   
1031 C  CB  . LEU   A 134 ? 0.2050 0.2216 0.1905 -0.0249 0.0021  0.0017  140 LEU   A CB  
1032 C  CG  . LEU   A 134 ? 0.2116 0.2267 0.2004 -0.0217 -0.0022 0.0078  140 LEU   A CG  
1033 C  CD1 . LEU   A 134 ? 0.2079 0.2171 0.2022 -0.0152 -0.0027 0.0062  140 LEU   A CD1 
1034 C  CD2 . LEU   A 134 ? 0.2377 0.2561 0.2269 -0.0249 -0.0047 0.0141  140 LEU   A CD2 
1035 N  N   . LEU   A 135 ? 0.2114 0.2403 0.1800 -0.0436 0.0110  -0.0063 141 LEU   A N   
1036 C  CA  . LEU   A 135 ? 0.2179 0.2474 0.1838 -0.0471 0.0174  -0.0145 141 LEU   A CA  
1037 C  C   . LEU   A 135 ? 0.2179 0.2466 0.1905 -0.0440 0.0209  -0.0185 141 LEU   A C   
1038 O  O   . LEU   A 135 ? 0.2261 0.2527 0.2016 -0.0429 0.0263  -0.0258 141 LEU   A O   
1039 C  CB  . LEU   A 135 ? 0.2369 0.2735 0.1923 -0.0577 0.0192  -0.0150 141 LEU   A CB  
1040 C  CG  . LEU   A 135 ? 0.2737 0.3133 0.2227 -0.0620 0.0149  -0.0100 141 LEU   A CG  
1041 C  CD1 . LEU   A 135 ? 0.3025 0.3497 0.2399 -0.0737 0.0168  -0.0111 141 LEU   A CD1 
1042 C  CD2 . LEU   A 135 ? 0.2784 0.3120 0.2289 -0.0578 0.0151  -0.0131 141 LEU   A CD2 
1043 N  N   . TRP   A 136 ? 0.2138 0.2442 0.1897 -0.0429 0.0181  -0.0137 142 TRP   A N   
1044 C  CA  . TRP   A 136 ? 0.2139 0.2450 0.1965 -0.0407 0.0208  -0.0165 142 TRP   A CA  
1045 C  C   . TRP   A 136 ? 0.2235 0.2491 0.2153 -0.0323 0.0212  -0.0196 142 TRP   A C   
1046 O  O   . TRP   A 136 ? 0.2266 0.2536 0.2252 -0.0305 0.0243  -0.0231 142 TRP   A O   
1047 C  CB  . TRP   A 136 ? 0.2130 0.2466 0.1964 -0.0422 0.0172  -0.0100 142 TRP   A CB  
1048 C  CG  . TRP   A 136 ? 0.2057 0.2347 0.1915 -0.0375 0.0111  -0.0037 142 TRP   A CG  
1049 C  CD1 . TRP   A 136 ? 0.2196 0.2491 0.2016 -0.0396 0.0068  0.0029  142 TRP   A CD1 
1050 C  CD2 . TRP   A 136 ? 0.2119 0.2356 0.2051 -0.0304 0.0089  -0.0034 142 TRP   A CD2 
1051 N  NE1 . TRP   A 136 ? 0.2229 0.2471 0.2102 -0.0336 0.0029  0.0066  142 TRP   A NE1 
1052 C  CE2 . TRP   A 136 ? 0.2193 0.2398 0.2125 -0.0284 0.0041  0.0025  142 TRP   A CE2 
1053 C  CE3 . TRP   A 136 ? 0.2220 0.2440 0.2221 -0.0259 0.0104  -0.0074 142 TRP   A CE3 
1054 C  CZ2 . TRP   A 136 ? 0.2332 0.2482 0.2317 -0.0225 0.0016  0.0033  142 TRP   A CZ2 
1055 C  CZ3 . TRP   A 136 ? 0.2272 0.2445 0.2320 -0.0206 0.0070  -0.0056 142 TRP   A CZ3 
1056 C  CH2 . TRP   A 136 ? 0.2271 0.2406 0.2304 -0.0192 0.0030  -0.0008 142 TRP   A CH2 
1057 N  N   . LEU   A 137 ? 0.2130 0.2332 0.2056 -0.0277 0.0181  -0.0182 143 LEU   A N   
1058 C  CA  . LEU   A 137 ? 0.2300 0.2455 0.2304 -0.0206 0.0181  -0.0205 143 LEU   A CA  
1059 C  C   . LEU   A 137 ? 0.2625 0.2773 0.2665 -0.0202 0.0240  -0.0274 143 LEU   A C   
1060 O  O   . LEU   A 137 ? 0.2551 0.2680 0.2679 -0.0149 0.0245  -0.0289 143 LEU   A O   
1061 C  CB  . LEU   A 137 ? 0.2143 0.2246 0.2134 -0.0169 0.0143  -0.0177 143 LEU   A CB  
1062 C  CG  . LEU   A 137 ? 0.2111 0.2205 0.2099 -0.0152 0.0091  -0.0119 143 LEU   A CG  
1063 C  CD1 . LEU   A 137 ? 0.2132 0.2187 0.2101 -0.0125 0.0066  -0.0101 143 LEU   A CD1 
1064 C  CD2 . LEU   A 137 ? 0.2067 0.2150 0.2122 -0.0111 0.0075  -0.0114 143 LEU   A CD2 
1065 N  N   . ASP   A 138 ? 0.2951 0.3116 0.2929 -0.0260 0.0284  -0.0314 144 ASP   A N   
1066 C  CA  . ASP   A 138 ? 0.3381 0.3531 0.3392 -0.0263 0.0353  -0.0391 144 ASP   A CA  
1067 C  C   . ASP   A 138 ? 0.3846 0.4047 0.3911 -0.0278 0.0409  -0.0436 144 ASP   A C   
1068 O  O   . ASP   A 138 ? 0.3874 0.4063 0.3980 -0.0278 0.0475  -0.0506 144 ASP   A O   
1069 C  CB  . ASP   A 138 ? 0.3602 0.3747 0.3510 -0.0332 0.0383  -0.0426 144 ASP   A CB  
1070 C  CG  . ASP   A 138 ? 0.4312 0.4410 0.4175 -0.0323 0.0342  -0.0397 144 ASP   A CG  
1071 O  OD1 . ASP   A 138 ? 0.4583 0.4639 0.4498 -0.0257 0.0301  -0.0361 144 ASP   A OD1 
1072 O  OD2 . ASP   A 138 ? 0.4877 0.4987 0.4646 -0.0390 0.0352  -0.0409 144 ASP   A OD2 
1073 N  N   . GLU   A 139 ? 0.4084 0.4344 0.4153 -0.0295 0.0390  -0.0401 145 GLU   A N   
1074 C  CA  . GLU   A 139 ? 0.4353 0.4674 0.4478 -0.0315 0.0448  -0.0445 145 GLU   A CA  
1075 C  C   . GLU   A 139 ? 0.4349 0.4710 0.4538 -0.0292 0.0413  -0.0400 145 GLU   A C   
1076 O  O   . GLU   A 139 ? 0.4411 0.4747 0.4591 -0.0267 0.0346  -0.0337 145 GLU   A O   
1077 C  CB  . GLU   A 139 ? 0.4963 0.5340 0.4984 -0.0412 0.0496  -0.0478 145 GLU   A CB  
1078 C  CG  . GLU   A 139 ? 0.5951 0.6367 0.5873 -0.0470 0.0443  -0.0405 145 GLU   A CG  
1079 C  CD  . GLU   A 139 ? 0.7170 0.7573 0.6973 -0.0521 0.0415  -0.0379 145 GLU   A CD  
1080 O  OE1 . GLU   A 139 ? 0.7486 0.7937 0.7206 -0.0585 0.0385  -0.0325 145 GLU   A OE1 
1081 O  OE2 . GLU   A 139 ? 0.7628 0.7977 0.7424 -0.0498 0.0421  -0.0408 145 GLU   A OE2 
1082 N  N   . SER   B 1   ? 0.3130 0.3094 0.3191 -0.0176 -0.0294 0.0620  7   SER   C N   
1083 C  CA  . SER   B 1   ? 0.3116 0.3118 0.3296 -0.0180 -0.0297 0.0647  7   SER   C CA  
1084 C  C   . SER   B 1   ? 0.2994 0.2969 0.3133 -0.0169 -0.0294 0.0604  7   SER   C C   
1085 O  O   . SER   B 1   ? 0.3192 0.3112 0.3204 -0.0165 -0.0303 0.0563  7   SER   C O   
1086 C  CB  . SER   B 1   ? 0.3431 0.3445 0.3640 -0.0222 -0.0354 0.0722  7   SER   C CB  
1087 O  OG  . SER   B 1   ? 0.4016 0.3969 0.4092 -0.0251 -0.0406 0.0718  7   SER   C OG  
1088 N  N   . GLY   B 2   ? 0.2691 0.2702 0.2937 -0.0161 -0.0276 0.0616  8   GLY   C N   
1089 C  CA  . GLY   B 2   ? 0.2512 0.2501 0.2726 -0.0153 -0.0272 0.0584  8   GLY   C CA  
1090 C  C   . GLY   B 2   ? 0.2276 0.2302 0.2597 -0.0127 -0.0221 0.0571  8   GLY   C C   
1091 O  O   . GLY   B 2   ? 0.2277 0.2333 0.2670 -0.0105 -0.0181 0.0559  8   GLY   C O   
1092 N  N   . ALA   B 3   ? 0.2149 0.2168 0.2472 -0.0130 -0.0222 0.0571  9   ALA   C N   
1093 C  CA  . ALA   B 3   ? 0.2097 0.2142 0.2504 -0.0106 -0.0171 0.0558  9   ALA   C CA  
1094 C  C   . ALA   B 3   ? 0.2038 0.2046 0.2368 -0.0100 -0.0167 0.0523  9   ALA   C C   
1095 O  O   . ALA   B 3   ? 0.2148 0.2115 0.2384 -0.0118 -0.0209 0.0522  9   ALA   C O   
1096 C  CB  . ALA   B 3   ? 0.2227 0.2324 0.2774 -0.0119 -0.0165 0.0625  9   ALA   C CB  
1097 N  N   . ILE   B 4   ? 0.1949 0.1965 0.2313 -0.0074 -0.0118 0.0495  10  ILE   C N   
1098 C  CA  . ILE   B 4   ? 0.2003 0.1989 0.2308 -0.0069 -0.0109 0.0472  10  ILE   C CA  
1099 C  C   . ILE   B 4   ? 0.2030 0.2052 0.2440 -0.0077 -0.0083 0.0520  10  ILE   C C   
1100 O  O   . ILE   B 4   ? 0.2106 0.2166 0.2624 -0.0064 -0.0042 0.0536  10  ILE   C O   
1101 C  CB  . ILE   B 4   ? 0.2055 0.2023 0.2317 -0.0036 -0.0071 0.0408  10  ILE   C CB  
1102 C  CG1 . ILE   B 4   ? 0.2193 0.2146 0.2389 -0.0024 -0.0086 0.0365  10  ILE   C CG1 
1103 C  CG2 . ILE   B 4   ? 0.2190 0.2125 0.2382 -0.0032 -0.0065 0.0390  10  ILE   C CG2 
1104 C  CD1 . ILE   B 4   ? 0.2341 0.2291 0.2525 0.0004  -0.0051 0.0309  10  ILE   C CD1 
1105 N  N   . TYR   B 5   ? 0.1902 0.1909 0.2287 -0.0097 -0.0102 0.0544  11  TYR   C N   
1106 C  CA  . TYR   B 5   ? 0.2026 0.2072 0.2515 -0.0106 -0.0075 0.0595  11  TYR   C CA  
1107 C  C   . TYR   B 5   ? 0.2169 0.2182 0.2593 -0.0093 -0.0042 0.0566  11  TYR   C C   
1108 O  O   . TYR   B 5   ? 0.2308 0.2283 0.2648 -0.0110 -0.0077 0.0564  11  TYR   C O   
1109 C  CB  . TYR   B 5   ? 0.2023 0.2088 0.2551 -0.0150 -0.0133 0.0663  11  TYR   C CB  
1110 C  CG  . TYR   B 5   ? 0.2096 0.2197 0.2692 -0.0165 -0.0166 0.0701  11  TYR   C CG  
1111 C  CD1 . TYR   B 5   ? 0.2040 0.2207 0.2791 -0.0158 -0.0135 0.0750  11  TYR   C CD1 
1112 C  CD2 . TYR   B 5   ? 0.2334 0.2398 0.2833 -0.0182 -0.0221 0.0687  11  TYR   C CD2 
1113 C  CE1 . TYR   B 5   ? 0.2247 0.2446 0.3059 -0.0171 -0.0167 0.0789  11  TYR   C CE1 
1114 C  CE2 . TYR   B 5   ? 0.2472 0.2564 0.3019 -0.0196 -0.0250 0.0723  11  TYR   C CE2 
1115 C  CZ  . TYR   B 5   ? 0.2533 0.2694 0.3238 -0.0192 -0.0226 0.0776  11  TYR   C CZ  
1116 O  OH  . TYR   B 5   ? 0.2779 0.2968 0.3533 -0.0205 -0.0256 0.0816  11  TYR   C OH  
1117 N  N   . VAL   B 6   ? 0.2123 0.2142 0.2575 -0.0062 0.0024  0.0539  12  VAL   C N   
1118 C  CA  . VAL   B 6   ? 0.2186 0.2169 0.2564 -0.0050 0.0058  0.0510  12  VAL   C CA  
1119 C  C   . VAL   B 6   ? 0.2268 0.2286 0.2749 -0.0039 0.0127  0.0542  12  VAL   C C   
1120 O  O   . VAL   B 6   ? 0.2264 0.2309 0.2834 -0.0020 0.0170  0.0544  12  VAL   C O   
1121 C  CB  . VAL   B 6   ? 0.2351 0.2291 0.2623 -0.0022 0.0069  0.0434  12  VAL   C CB  
1122 C  CG1 . VAL   B 6   ? 0.2331 0.2290 0.2664 -0.0001 0.0103  0.0409  12  VAL   C CG1 
1123 C  CG2 . VAL   B 6   ? 0.2429 0.2331 0.2622 -0.0010 0.0105  0.0409  12  VAL   C CG2 
1124 N  N   . GLY   B 7   ? 0.2287 0.2304 0.2767 -0.0052 0.0142  0.0574  13  GLY   C N   
1125 C  CA  . GLY   B 7   ? 0.2212 0.2266 0.2797 -0.0041 0.0216  0.0611  13  GLY   C CA  
1126 C  C   . GLY   B 7   ? 0.2280 0.2406 0.3037 -0.0045 0.0221  0.0670  13  GLY   C C   
1127 O  O   . GLY   B 7   ? 0.2468 0.2622 0.3268 -0.0076 0.0155  0.0713  13  GLY   C O   
1128 N  N   . ASN   B 8   ? 0.2226 0.2373 0.3074 -0.0013 0.0296  0.0669  14  ASN   C N   
1129 C  CA  . ASN   B 8   ? 0.2139 0.2352 0.3157 -0.0011 0.0301  0.0727  14  ASN   C CA  
1130 C  C   . ASN   B 8   ? 0.2052 0.2250 0.3066 0.0008  0.0295  0.0686  14  ASN   C C   
1131 O  O   . ASN   B 8   ? 0.2006 0.2234 0.3142 0.0029  0.0337  0.0709  14  ASN   C O   
1132 C  CB  . ASN   B 8   ? 0.2393 0.2652 0.3552 0.0010  0.0387  0.0774  14  ASN   C CB  
1133 C  CG  . ASN   B 8   ? 0.3120 0.3422 0.4335 -0.0019 0.0378  0.0841  14  ASN   C CG  
1134 O  OD1 . ASN   B 8   ? 0.3201 0.3575 0.4555 -0.0044 0.0342  0.0920  14  ASN   C OD1 
1135 N  ND2 . ASN   B 8   ? 0.3271 0.3530 0.4378 -0.0019 0.0406  0.0815  14  ASN   C ND2 
1136 N  N   . TYR   B 9   ? 0.2000 0.2153 0.2883 -0.0001 0.0241  0.0634  15  TYR   C N   
1137 C  CA  . TYR   B 9   ? 0.2030 0.2169 0.2904 0.0011  0.0230  0.0597  15  TYR   C CA  
1138 C  C   . TYR   B 9   ? 0.1966 0.2114 0.2806 -0.0018 0.0145  0.0612  15  TYR   C C   
1139 O  O   . TYR   B 9   ? 0.2016 0.2143 0.2764 -0.0042 0.0093  0.0610  15  TYR   C O   
1140 C  CB  . TYR   B 9   ? 0.2184 0.2258 0.2927 0.0032  0.0254  0.0511  15  TYR   C CB  
1141 C  CG  . TYR   B 9   ? 0.2422 0.2468 0.3162 0.0060  0.0339  0.0483  15  TYR   C CG  
1142 C  CD1 . TYR   B 9   ? 0.2633 0.2690 0.3485 0.0085  0.0405  0.0495  15  TYR   C CD1 
1143 C  CD2 . TYR   B 9   ? 0.2681 0.2680 0.3295 0.0063  0.0353  0.0442  15  TYR   C CD2 
1144 C  CE1 . TYR   B 9   ? 0.2793 0.2810 0.3625 0.0112  0.0488  0.0463  15  TYR   C CE1 
1145 C  CE2 . TYR   B 9   ? 0.2911 0.2873 0.3500 0.0087  0.0432  0.0413  15  TYR   C CE2 
1146 C  CZ  . TYR   B 9   ? 0.3148 0.3115 0.3840 0.0111  0.0501  0.0419  15  TYR   C CZ  
1147 O  OH  . TYR   B 9   ? 0.3556 0.3474 0.4208 0.0136  0.0584  0.0386  15  TYR   C OH  
1148 N  N   . ARG   B 10  ? 0.1661 0.1828 0.2562 -0.0014 0.0134  0.0623  16  ARG   C N   
1149 C  CA  . ARG   B 10  ? 0.1664 0.1832 0.2525 -0.0037 0.0065  0.0631  16  ARG   C CA  
1150 C  C   . ARG   B 10  ? 0.1776 0.1914 0.2591 -0.0016 0.0081  0.0571  16  ARG   C C   
1151 O  O   . ARG   B 10  ? 0.1814 0.1962 0.2713 0.0005  0.0129  0.0570  16  ARG   C O   
1152 C  CB  . ARG   B 10  ? 0.1814 0.2040 0.2805 -0.0056 0.0036  0.0712  16  ARG   C CB  
1153 C  CG  . ARG   B 10  ? 0.2010 0.2233 0.2964 -0.0075 -0.0023 0.0720  16  ARG   C CG  
1154 C  CD  . ARG   B 10  ? 0.2142 0.2420 0.3208 -0.0102 -0.0065 0.0808  16  ARG   C CD  
1155 N  NE  . ARG   B 10  ? 0.2219 0.2507 0.3315 -0.0101 -0.0080 0.0823  16  ARG   C NE  
1156 C  CZ  . ARG   B 10  ? 0.2430 0.2701 0.3443 -0.0127 -0.0141 0.0830  16  ARG   C CZ  
1157 N  NH1 . ARG   B 10  ? 0.2284 0.2519 0.3169 -0.0155 -0.0192 0.0814  16  ARG   C NH1 
1158 N  NH2 . ARG   B 10  ? 0.2454 0.2736 0.3503 -0.0126 -0.0147 0.0850  16  ARG   C NH2 
1159 N  N   . VAL   B 11  ? 0.1686 0.1788 0.2373 -0.0021 0.0046  0.0523  17  VAL   C N   
1160 C  CA  . VAL   B 11  ? 0.1652 0.1732 0.2296 -0.0005 0.0057  0.0468  17  VAL   C CA  
1161 C  C   . VAL   B 11  ? 0.1743 0.1834 0.2374 -0.0022 0.0009  0.0487  17  VAL   C C   
1162 O  O   . VAL   B 11  ? 0.1815 0.1892 0.2364 -0.0040 -0.0039 0.0493  17  VAL   C O   
1163 C  CB  . VAL   B 11  ? 0.1752 0.1788 0.2268 0.0005  0.0055  0.0401  17  VAL   C CB  
1164 C  CG1 . VAL   B 11  ? 0.2019 0.2043 0.2516 0.0020  0.0070  0.0348  17  VAL   C CG1 
1165 C  CG2 . VAL   B 11  ? 0.1901 0.1919 0.2399 0.0015  0.0092  0.0388  17  VAL   C CG2 
1166 N  N   . VAL   B 12  ? 0.1716 0.1824 0.2420 -0.0016 0.0026  0.0497  18  VAL   C N   
1167 C  CA  A VAL   B 12  ? 0.1651 0.1770 0.2342 -0.0032 -0.0013 0.0520  18  VAL   C CA  
1168 C  CA  B VAL   B 12  ? 0.1834 0.1956 0.2537 -0.0032 -0.0011 0.0525  18  VAL   C CA  
1169 C  C   . VAL   B 12  ? 0.1796 0.1908 0.2492 -0.0018 0.0011  0.0482  18  VAL   C C   
1170 O  O   . VAL   B 12  ? 0.1741 0.1842 0.2475 0.0001  0.0057  0.0447  18  VAL   C O   
1171 C  CB  A VAL   B 12  ? 0.1569 0.1727 0.2368 -0.0048 -0.0030 0.0600  18  VAL   C CB  
1172 C  CB  B VAL   B 12  ? 0.2088 0.2252 0.2922 -0.0042 -0.0016 0.0603  18  VAL   C CB  
1173 C  CG1 A VAL   B 12  ? 0.1650 0.1819 0.2438 -0.0073 -0.0072 0.0644  18  VAL   C CG1 
1174 C  CG1 B VAL   B 12  ? 0.2146 0.2320 0.2951 -0.0070 -0.0072 0.0646  18  VAL   C CG1 
1175 C  CG2 A VAL   B 12  ? 0.1370 0.1550 0.2309 -0.0027 0.0025  0.0619  18  VAL   C CG2 
1176 C  CG2 B VAL   B 12  ? 0.2317 0.2506 0.3225 -0.0046 -0.0008 0.0646  18  VAL   C CG2 
1177 N  N   . ASN   B 13  ? 0.1597 0.1712 0.2257 -0.0030 -0.0018 0.0492  19  ASN   C N   
1178 C  CA  . ASN   B 13  ? 0.1604 0.1720 0.2286 -0.0022 0.0004  0.0468  19  ASN   C CA  
1179 C  C   . ASN   B 13  ? 0.1622 0.1757 0.2440 -0.0018 0.0034  0.0510  19  ASN   C C   
1180 O  O   . ASN   B 13  ? 0.1641 0.1799 0.2518 -0.0029 0.0015  0.0574  19  ASN   C O   
1181 C  CB  . ASN   B 13  ? 0.1634 0.1754 0.2261 -0.0036 -0.0027 0.0485  19  ASN   C CB  
1182 C  CG  . ASN   B 13  ? 0.1913 0.2010 0.2411 -0.0036 -0.0051 0.0446  19  ASN   C CG  
1183 O  OD1 . ASN   B 13  ? 0.2028 0.2108 0.2456 -0.0050 -0.0087 0.0465  19  ASN   C OD1 
1184 N  ND2 . ASN   B 13  ? 0.1768 0.1861 0.2236 -0.0020 -0.0032 0.0393  19  ASN   C ND2 
1185 N  N   . ARG   B 14  ? 0.1597 0.1719 0.2465 -0.0002 0.0079  0.0475  20  ARG   C N   
1186 C  CA  . ARG   B 14  ? 0.1597 0.1724 0.2594 0.0007  0.0114  0.0511  20  ARG   C CA  
1187 C  C   . ARG   B 14  ? 0.1763 0.1916 0.2811 -0.0008 0.0089  0.0575  20  ARG   C C   
1188 O  O   . ARG   B 14  ? 0.1874 0.2047 0.3025 -0.0006 0.0093  0.0636  20  ARG   C O   
1189 C  CB  . ARG   B 14  ? 0.1751 0.1844 0.2769 0.0021  0.0159  0.0455  20  ARG   C CB  
1190 C  CG  . ARG   B 14  ? 0.1888 0.1968 0.3032 0.0036  0.0207  0.0480  20  ARG   C CG  
1191 C  CD  . ARG   B 14  ? 0.1987 0.2020 0.3132 0.0043  0.0244  0.0420  20  ARG   C CD  
1192 N  NE  . ARG   B 14  ? 0.1914 0.1913 0.3165 0.0061  0.0298  0.0430  20  ARG   C NE  
1193 C  CZ  . ARG   B 14  ? 0.2077 0.2078 0.3427 0.0061  0.0308  0.0475  20  ARG   C CZ  
1194 N  NH1 . ARG   B 14  ? 0.2142 0.2180 0.3497 0.0042  0.0267  0.0519  20  ARG   C NH1 
1195 N  NH2 . ARG   B 14  ? 0.1882 0.1840 0.3323 0.0082  0.0362  0.0477  20  ARG   C NH2 
1196 N  N   . HIS   B 15  ? 0.1683 0.1837 0.2658 -0.0022 0.0063  0.0565  21  HIS   C N   
1197 C  CA  . HIS   B 15  ? 0.1635 0.1807 0.2641 -0.0038 0.0041  0.0626  21  HIS   C CA  
1198 C  C   . HIS   B 15  ? 0.1861 0.2055 0.2852 -0.0058 -0.0009 0.0692  21  HIS   C C   
1199 O  O   . HIS   B 15  ? 0.2047 0.2256 0.3074 -0.0073 -0.0031 0.0754  21  HIS   C O   
1200 C  CB  . HIS   B 15  ? 0.1672 0.1840 0.2608 -0.0047 0.0036  0.0601  21  HIS   C CB  
1201 C  CG  . HIS   B 15  ? 0.1881 0.2044 0.2683 -0.0057 0.0002  0.0582  21  HIS   C CG  
1202 N  ND1 . HIS   B 15  ? 0.2189 0.2338 0.2916 -0.0045 0.0007  0.0516  21  HIS   C ND1 
1203 C  CD2 . HIS   B 15  ? 0.2086 0.2250 0.2816 -0.0076 -0.0035 0.0620  21  HIS   C CD2 
1204 C  CE1 . HIS   B 15  ? 0.2363 0.2504 0.2982 -0.0054 -0.0023 0.0516  21  HIS   C CE1 
1205 N  NE2 . HIS   B 15  ? 0.2280 0.2427 0.2890 -0.0073 -0.0048 0.0574  21  HIS   C NE2 
1206 N  N   . LEU   B 16  ? 0.1823 0.2015 0.2763 -0.0061 -0.0030 0.0683  22  LEU   C N   
1207 C  CA  . LEU   B 16  ? 0.2002 0.2212 0.2930 -0.0085 -0.0083 0.0743  22  LEU   C CA  
1208 C  C   . LEU   B 16  ? 0.2027 0.2264 0.3068 -0.0079 -0.0073 0.0782  22  LEU   C C   
1209 O  O   . LEU   B 16  ? 0.2092 0.2348 0.3133 -0.0101 -0.0119 0.0830  22  LEU   C O   
1210 C  CB  . LEU   B 16  ? 0.2103 0.2285 0.2879 -0.0100 -0.0120 0.0710  22  LEU   C CB  
1211 C  CG  . LEU   B 16  ? 0.2270 0.2428 0.2934 -0.0105 -0.0127 0.0679  22  LEU   C CG  
1212 C  CD1 . LEU   B 16  ? 0.2340 0.2461 0.2857 -0.0114 -0.0158 0.0645  22  LEU   C CD1 
1213 C  CD2 . LEU   B 16  ? 0.2240 0.2408 0.2915 -0.0126 -0.0152 0.0741  22  LEU   C CD2 
1214 N  N   . ALA   B 17  ? 0.1956 0.2193 0.3088 -0.0049 -0.0014 0.0759  23  ALA   C N   
1215 C  CA  . ALA   B 17  ? 0.2044 0.2307 0.3286 -0.0038 0.0008  0.0793  23  ALA   C CA  
1216 C  C   . ALA   B 17  ? 0.2203 0.2512 0.3571 -0.0048 -0.0017 0.0888  23  ALA   C C   
1217 O  O   . ALA   B 17  ? 0.2252 0.2564 0.3660 -0.0050 -0.0023 0.0920  23  ALA   C O   
1218 C  CB  . ALA   B 17  ? 0.2125 0.2364 0.3425 -0.0002 0.0083  0.0747  23  ALA   C CB  
1219 N  N   . THR   B 18  ? 0.2153 0.2499 0.3580 -0.0058 -0.0038 0.0938  24  THR   C N   
1220 C  CA  . THR   B 18  ? 0.2101 0.2503 0.3661 -0.0070 -0.0070 0.1037  24  THR   C CA  
1221 C  C   . THR   B 18  ? 0.2143 0.2571 0.3883 -0.0031 -0.0001 0.1066  24  THR   C C   
1222 O  O   . THR   B 18  ? 0.2114 0.2511 0.3859 0.0002  0.0069  0.1007  24  THR   C O   
1223 C  CB  . THR   B 18  ? 0.2268 0.2701 0.3810 -0.0105 -0.0130 0.1080  24  THR   C CB  
1224 O  OG1 . THR   B 18  ? 0.2375 0.2818 0.3961 -0.0086 -0.0083 0.1059  24  THR   C OG1 
1225 C  CG2 . THR   B 18  ? 0.2455 0.2849 0.3810 -0.0142 -0.0193 0.1047  24  THR   C CG2 
1226 N  N   . HIS   B 19  ? 0.2053 0.2536 0.3945 -0.0033 -0.0022 0.1163  25  HIS   C N   
1227 C  CA  . HIS   B 19  ? 0.2103 0.2616 0.4181 0.0007  0.0044  0.1200  25  HIS   C CA  
1228 C  C   . HIS   B 19  ? 0.2018 0.2546 0.4121 0.0021  0.0084  0.1182  25  HIS   C C   
1229 O  O   . HIS   B 19  ? 0.2159 0.2664 0.4319 0.0063  0.0170  0.1147  25  HIS   C O   
1230 C  CB  . HIS   B 19  ? 0.2220 0.2804 0.4461 -0.0002 0.0001  0.1319  25  HIS   C CB  
1231 C  CG  . HIS   B 19  ? 0.2673 0.3302 0.5122 0.0040  0.0064  0.1371  25  HIS   C CG  
1232 N  ND1 . HIS   B 19  ? 0.2950 0.3548 0.5497 0.0089  0.0144  0.1360  25  HIS   C ND1 
1233 C  CD2 . HIS   B 19  ? 0.2918 0.3615 0.5486 0.0040  0.0064  0.1429  25  HIS   C CD2 
1234 C  CE1 . HIS   B 19  ? 0.3010 0.3659 0.5736 0.0120  0.0191  0.1415  25  HIS   C CE1 
1235 N  NE2 . HIS   B 19  ? 0.2999 0.3714 0.5750 0.0093  0.0147  0.1461  25  HIS   C NE2 
1236 N  N   . ASN   B 20  ? 0.1951 0.2509 0.4000 -0.0016 0.0026  0.1202  26  ASN   C N   
1237 C  CA  . ASN   B 20  ? 0.1983 0.2555 0.4054 -0.0007 0.0065  0.1189  26  ASN   C CA  
1238 C  C   . ASN   B 20  ? 0.2058 0.2556 0.4000 0.0018  0.0129  0.1080  26  ASN   C C   
1239 O  O   . ASN   B 20  ? 0.1958 0.2453 0.3947 0.0047  0.0201  0.1062  26  ASN   C O   
1240 C  CB  . ASN   B 20  ? 0.2257 0.2863 0.4280 -0.0057 -0.0014 0.1225  26  ASN   C CB  
1241 C  CG  . ASN   B 20  ? 0.3060 0.3691 0.5136 -0.0047 0.0030  0.1229  26  ASN   C CG  
1242 O  OD1 . ASN   B 20  ? 0.3220 0.3916 0.5477 -0.0030 0.0064  0.1297  26  ASN   C OD1 
1243 N  ND2 . ASN   B 20  ? 0.3298 0.3879 0.5223 -0.0055 0.0038  0.1157  26  ASN   C ND2 
1244 N  N   . ASP   B 21  ? 0.2025 0.2465 0.3804 0.0006  0.0104  0.1010  27  ASP   C N   
1245 C  CA  . ASP   B 21  ? 0.2000 0.2374 0.3661 0.0027  0.0156  0.0911  27  ASP   C CA  
1246 C  C   . ASP   B 21  ? 0.1977 0.2322 0.3720 0.0072  0.0244  0.0884  27  ASP   C C   
1247 O  O   . ASP   B 21  ? 0.2053 0.2364 0.3773 0.0096  0.0309  0.0835  27  ASP   C O   
1248 C  CB  . ASP   B 21  ? 0.2064 0.2391 0.3562 0.0008  0.0113  0.0851  27  ASP   C CB  
1249 C  CG  . ASP   B 21  ? 0.2115 0.2441 0.3490 -0.0030 0.0042  0.0850  27  ASP   C CG  
1250 O  OD1 . ASP   B 21  ? 0.2144 0.2477 0.3502 -0.0036 0.0043  0.0850  27  ASP   C OD1 
1251 O  OD2 . ASP   B 21  ? 0.2112 0.2426 0.3406 -0.0053 -0.0011 0.0848  27  ASP   C OD2 
1252 N  N   . TRP   B 22  ? 0.1943 0.2291 0.3770 0.0081  0.0247  0.0915  28  TRP   C N   
1253 C  CA  . TRP   B 22  ? 0.2013 0.2322 0.3921 0.0123  0.0329  0.0892  28  TRP   C CA  
1254 C  C   . TRP   B 22  ? 0.2078 0.2416 0.4138 0.0157  0.0396  0.0936  28  TRP   C C   
1255 O  O   . TRP   B 22  ? 0.2130 0.2417 0.4202 0.0193  0.0480  0.0889  28  TRP   C O   
1256 C  CB  . TRP   B 22  ? 0.1946 0.2251 0.3916 0.0123  0.0313  0.0924  28  TRP   C CB  
1257 C  CG  . TRP   B 22  ? 0.1960 0.2216 0.3790 0.0104  0.0286  0.0858  28  TRP   C CG  
1258 C  CD1 . TRP   B 22  ? 0.2059 0.2332 0.3808 0.0068  0.0213  0.0873  28  TRP   C CD1 
1259 C  CD2 . TRP   B 22  ? 0.1935 0.2119 0.3691 0.0118  0.0334  0.0769  28  TRP   C CD2 
1260 N  NE1 . TRP   B 22  ? 0.2124 0.2347 0.3769 0.0064  0.0217  0.0803  28  TRP   C NE1 
1261 C  CE2 . TRP   B 22  ? 0.1981 0.2152 0.3630 0.0091  0.0286  0.0739  28  TRP   C CE2 
1262 C  CE3 . TRP   B 22  ? 0.2005 0.2130 0.3773 0.0150  0.0413  0.0713  28  TRP   C CE3 
1263 C  CZ2 . TRP   B 22  ? 0.1986 0.2098 0.3557 0.0093  0.0310  0.0660  28  TRP   C CZ2 
1264 C  CZ3 . TRP   B 22  ? 0.2133 0.2189 0.3806 0.0149  0.0432  0.0630  28  TRP   C CZ3 
1265 C  CH2 . TRP   B 22  ? 0.2073 0.2128 0.3656 0.0119  0.0378  0.0607  28  TRP   C CH2 
1266 N  N   . ALA   B 23  ? 0.2033 0.2453 0.4206 0.0144  0.0360  0.1027  29  ALA   C N   
1267 C  CA  . ALA   B 23  ? 0.2152 0.2617 0.4488 0.0176  0.0423  0.1081  29  ALA   C CA  
1268 C  C   . ALA   B 23  ? 0.2237 0.2687 0.4502 0.0182  0.0469  0.1035  29  ALA   C C   
1269 O  O   . ALA   B 23  ? 0.2279 0.2751 0.4659 0.0215  0.0542  0.1063  29  ALA   C O   
1270 C  CB  . ALA   B 23  ? 0.2158 0.2723 0.4641 0.0154  0.0359  0.1198  29  ALA   C CB  
1271 N  N   . ASN   B 24  ? 0.2219 0.2630 0.4296 0.0153  0.0429  0.0968  30  ASN   C N   
1272 C  CA  . ASN   B 24  ? 0.2242 0.2633 0.4235 0.0155  0.0466  0.0926  30  ASN   C CA  
1273 C  C   . ASN   B 24  ? 0.2301 0.2601 0.4101 0.0156  0.0477  0.0815  30  ASN   C C   
1274 O  O   . ASN   B 24  ? 0.2238 0.2519 0.3902 0.0136  0.0450  0.0775  30  ASN   C O   
1275 C  CB  . ASN   B 24  ? 0.2416 0.2866 0.4390 0.0111  0.0389  0.0975  30  ASN   C CB  
1276 C  CG  . ASN   B 24  ? 0.2654 0.3200 0.4828 0.0107  0.0378  0.1086  30  ASN   C CG  
1277 O  OD1 . ASN   B 24  ? 0.2723 0.3301 0.5000 0.0130  0.0443  0.1116  30  ASN   C OD1 
1278 N  ND2 . ASN   B 24  ? 0.2557 0.3150 0.4786 0.0077  0.0295  0.1150  30  ASN   C ND2 
1279 N  N   . LEU   B 25  ? 0.2357 0.2601 0.4147 0.0178  0.0512  0.0769  31  LEU   C N   
1280 C  CA  . LEU   B 25  ? 0.2392 0.2557 0.4018 0.0174  0.0512  0.0672  31  LEU   C CA  
1281 C  C   . LEU   B 25  ? 0.2530 0.2635 0.4050 0.0190  0.0572  0.0603  31  LEU   C C   
1282 O  O   . LEU   B 25  ? 0.2733 0.2818 0.4317 0.0224  0.0656  0.0604  31  LEU   C O   
1283 C  CB  . LEU   B 25  ? 0.2353 0.2474 0.4019 0.0191  0.0537  0.0650  31  LEU   C CB  
1284 C  CG  . LEU   B 25  ? 0.2432 0.2480 0.3948 0.0181  0.0528  0.0558  31  LEU   C CG  
1285 C  CD1 . LEU   B 25  ? 0.2497 0.2572 0.3912 0.0143  0.0438  0.0553  31  LEU   C CD1 
1286 C  CD2 . LEU   B 25  ? 0.2461 0.2464 0.4034 0.0196  0.0558  0.0543  31  LEU   C CD2 
1287 N  N   . VAL   B 26  ? 0.2358 0.2431 0.3714 0.0168  0.0532  0.0543  32  VAL   C N   
1288 C  CA  . VAL   B 26  ? 0.2330 0.2339 0.3561 0.0179  0.0577  0.0473  32  VAL   C CA  
1289 C  C   . VAL   B 26  ? 0.2412 0.2346 0.3542 0.0180  0.0580  0.0390  32  VAL   C C   
1290 O  O   . VAL   B 26  ? 0.2543 0.2407 0.3634 0.0200  0.0646  0.0337  32  VAL   C O   
1291 C  CB  . VAL   B 26  ? 0.2430 0.2454 0.3547 0.0154  0.0530  0.0467  32  VAL   C CB  
1292 C  CG1 . VAL   B 26  ? 0.2468 0.2420 0.3437 0.0162  0.0566  0.0391  32  VAL   C CG1 
1293 C  CG2 . VAL   B 26  ? 0.2424 0.2517 0.3640 0.0149  0.0530  0.0547  32  VAL   C CG2 
1294 N  N   . TRP   B 27  ? 0.2202 0.2149 0.3287 0.0155  0.0508  0.0378  33  TRP   C N   
1295 C  CA  . TRP   B 27  ? 0.2200 0.2089 0.3198 0.0149  0.0500  0.0306  33  TRP   C CA  
1296 C  C   . TRP   B 27  ? 0.2181 0.2107 0.3193 0.0127  0.0432  0.0324  33  TRP   C C   
1297 O  O   . TRP   B 27  ? 0.2281 0.2261 0.3294 0.0110  0.0378  0.0368  33  TRP   C O   
1298 C  CB  . TRP   B 27  ? 0.2368 0.2217 0.3203 0.0140  0.0486  0.0241  33  TRP   C CB  
1299 C  CG  . TRP   B 27  ? 0.2471 0.2278 0.3208 0.0126  0.0455  0.0173  33  TRP   C CG  
1300 C  CD1 . TRP   B 27  ? 0.2671 0.2406 0.3364 0.0130  0.0490  0.0111  33  TRP   C CD1 
1301 C  CD2 . TRP   B 27  ? 0.2364 0.2201 0.3036 0.0104  0.0382  0.0162  33  TRP   C CD2 
1302 N  NE1 . TRP   B 27  ? 0.2720 0.2447 0.3335 0.0109  0.0437  0.0065  33  TRP   C NE1 
1303 C  CE2 . TRP   B 27  ? 0.2507 0.2298 0.3113 0.0096  0.0375  0.0097  33  TRP   C CE2 
1304 C  CE3 . TRP   B 27  ? 0.2398 0.2292 0.3064 0.0090  0.0323  0.0201  33  TRP   C CE3 
1305 C  CZ2 . TRP   B 27  ? 0.2555 0.2366 0.3101 0.0078  0.0314  0.0074  33  TRP   C CZ2 
1306 C  CZ3 . TRP   B 27  ? 0.2517 0.2419 0.3112 0.0076  0.0269  0.0173  33  TRP   C CZ3 
1307 C  CH2 . TRP   B 27  ? 0.2591 0.2457 0.3135 0.0072  0.0267  0.0113  33  TRP   C CH2 
1308 N  N   . GLU   B 28  ? 0.2039 0.1932 0.3060 0.0125  0.0436  0.0292  34  GLU   C N   
1309 C  CA  . GLU   B 28  ? 0.1944 0.1869 0.2969 0.0104  0.0378  0.0306  34  GLU   C CA  
1310 C  C   . GLU   B 28  ? 0.2108 0.1986 0.3075 0.0095  0.0376  0.0239  34  GLU   C C   
1311 O  O   . GLU   B 28  ? 0.2079 0.1893 0.3041 0.0105  0.0425  0.0195  34  GLU   C O   
1312 C  CB  . GLU   B 28  ? 0.2221 0.2185 0.3384 0.0106  0.0377  0.0380  34  GLU   C CB  
1313 C  CG  . GLU   B 28  ? 0.2430 0.2355 0.3699 0.0130  0.0443  0.0386  34  GLU   C CG  
1314 C  CD  . GLU   B 28  ? 0.2695 0.2571 0.3968 0.0125  0.0453  0.0347  34  GLU   C CD  
1315 O  OE1 . GLU   B 28  ? 0.2902 0.2715 0.4214 0.0144  0.0513  0.0322  34  GLU   C OE1 
1316 O  OE2 . GLU   B 28  ? 0.2671 0.2567 0.3905 0.0101  0.0403  0.0342  34  GLU   C OE2 
1317 N  N   . ASP   B 29  ? 0.2013 0.1919 0.2936 0.0074  0.0322  0.0232  35  ASP   C N   
1318 C  CA  . ASP   B 29  ? 0.2091 0.1965 0.2976 0.0061  0.0315  0.0177  35  ASP   C CA  
1319 C  C   . ASP   B 29  ? 0.1957 0.1879 0.2869 0.0044  0.0272  0.0207  35  ASP   C C   
1320 O  O   . ASP   B 29  ? 0.2040 0.2000 0.2892 0.0036  0.0229  0.0214  35  ASP   C O   
1321 C  CB  . ASP   B 29  ? 0.2223 0.2073 0.2983 0.0056  0.0298  0.0114  35  ASP   C CB  
1322 C  CG  . ASP   B 29  ? 0.3079 0.2897 0.3799 0.0040  0.0286  0.0054  35  ASP   C CG  
1323 O  OD1 . ASP   B 29  ? 0.3146 0.2987 0.3918 0.0026  0.0268  0.0066  35  ASP   C OD1 
1324 O  OD2 . ASP   B 29  ? 0.3317 0.3089 0.3952 0.0038  0.0291  -0.0001 35  ASP   C OD2 
1325 N  N   . SER   B 30  ? 0.1968 0.1882 0.2966 0.0039  0.0288  0.0226  36  SER   C N   
1326 C  CA  A SER   B 30  ? 0.1943 0.1899 0.2969 0.0023  0.0256  0.0258  36  SER   C CA  
1327 C  CA  B SER   B 30  ? 0.1995 0.1952 0.3019 0.0023  0.0255  0.0259  36  SER   C CA  
1328 C  C   . SER   B 30  ? 0.1944 0.1913 0.2893 0.0007  0.0223  0.0212  36  SER   C C   
1329 O  O   . SER   B 30  ? 0.1989 0.2003 0.2916 -0.0002 0.0191  0.0236  36  SER   C O   
1330 C  CB  A SER   B 30  ? 0.2016 0.1948 0.3146 0.0020  0.0284  0.0281  36  SER   C CB  
1331 C  CB  B SER   B 30  ? 0.2237 0.2177 0.3369 0.0021  0.0281  0.0290  36  SER   C CB  
1332 O  OG  A SER   B 30  ? 0.1903 0.1869 0.3048 0.0001  0.0258  0.0305  36  SER   C OG  
1333 O  OG  B SER   B 30  ? 0.2471 0.2348 0.3607 0.0018  0.0312  0.0234  36  SER   C OG  
1334 N  N   . SER   B 31  ? 0.2003 0.1930 0.2911 0.0002  0.0233  0.0147  37  SER   C N   
1335 C  CA  . SER   B 31  ? 0.2089 0.2037 0.2943 -0.0013 0.0199  0.0108  37  SER   C CA  
1336 C  C   . SER   B 31  ? 0.1985 0.1971 0.2753 -0.0006 0.0164  0.0106  37  SER   C C   
1337 O  O   . SER   B 31  ? 0.2030 0.2052 0.2772 -0.0013 0.0135  0.0095  37  SER   C O   
1338 C  CB  . SER   B 31  ? 0.2568 0.2462 0.3391 -0.0024 0.0208  0.0041  37  SER   C CB  
1339 O  OG  . SER   B 31  ? 0.3177 0.3039 0.3914 -0.0013 0.0210  0.0006  37  SER   C OG  
1340 N  N   . ARG   B 32  ? 0.1893 0.1871 0.2624 0.0010  0.0168  0.0120  38  ARG   C N   
1341 C  CA  . ARG   B 32  ? 0.1861 0.1865 0.2510 0.0016  0.0134  0.0123  38  ARG   C CA  
1342 C  C   . ARG   B 32  ? 0.1871 0.1910 0.2535 0.0017  0.0119  0.0184  38  ARG   C C   
1343 O  O   . ARG   B 32  ? 0.1822 0.1873 0.2416 0.0021  0.0091  0.0189  38  ARG   C O   
1344 C  CB  . ARG   B 32  ? 0.2031 0.2000 0.2618 0.0028  0.0146  0.0100  38  ARG   C CB  
1345 C  CG  . ARG   B 32  ? 0.2277 0.2203 0.2817 0.0024  0.0153  0.0037  38  ARG   C CG  
1346 C  CD  . ARG   B 32  ? 0.2388 0.2275 0.2856 0.0035  0.0170  0.0018  38  ARG   C CD  
1347 N  NE  . ARG   B 32  ? 0.2209 0.2118 0.2600 0.0041  0.0135  0.0024  38  ARG   C NE  
1348 C  CZ  . ARG   B 32  ? 0.2397 0.2276 0.2697 0.0046  0.0130  -0.0005 38  ARG   C CZ  
1349 N  NH1 . ARG   B 32  ? 0.2495 0.2321 0.2760 0.0045  0.0159  -0.0044 38  ARG   C NH1 
1350 N  NH2 . ARG   B 32  ? 0.2161 0.2057 0.2397 0.0051  0.0097  0.0005  38  ARG   C NH2 
1351 N  N   . ASP   B 33  ? 0.1767 0.1813 0.2517 0.0014  0.0136  0.0231  39  ASP   C N   
1352 C  CA  . ASP   B 33  ? 0.1626 0.1698 0.2388 0.0010  0.0117  0.0293  39  ASP   C CA  
1353 C  C   . ASP   B 33  ? 0.1596 0.1663 0.2326 0.0017  0.0110  0.0306  39  ASP   C C   
1354 O  O   . ASP   B 33  ? 0.1551 0.1634 0.2241 0.0010  0.0078  0.0338  39  ASP   C O   
1355 C  CB  . ASP   B 33  ? 0.1637 0.1737 0.2348 0.0001  0.0085  0.0305  39  ASP   C CB  
1356 C  CG  . ASP   B 33  ? 0.1930 0.2046 0.2641 -0.0008 0.0062  0.0368  39  ASP   C CG  
1357 O  OD1 . ASP   B 33  ? 0.2006 0.2128 0.2800 -0.0012 0.0072  0.0415  39  ASP   C OD1 
1358 O  OD2 . ASP   B 33  ? 0.1778 0.1898 0.2406 -0.0012 0.0033  0.0371  39  ASP   C OD2 
1359 N  N   . LEU   B 34  ? 0.1653 0.1692 0.2399 0.0029  0.0144  0.0285  40  LEU   C N   
1360 C  CA  . LEU   B 34  ? 0.1641 0.1679 0.2369 0.0034  0.0144  0.0304  40  LEU   C CA  
1361 C  C   . LEU   B 34  ? 0.1641 0.1678 0.2471 0.0044  0.0184  0.0341  40  LEU   C C   
1362 O  O   . LEU   B 34  ? 0.1766 0.1778 0.2652 0.0054  0.0226  0.0323  40  LEU   C O   
1363 C  CB  . LEU   B 34  ? 0.1675 0.1682 0.2310 0.0042  0.0149  0.0249  40  LEU   C CB  
1364 C  CG  . LEU   B 34  ? 0.1876 0.1886 0.2408 0.0038  0.0106  0.0219  40  LEU   C CG  
1365 C  CD1 . LEU   B 34  ? 0.2024 0.2002 0.2473 0.0046  0.0112  0.0170  40  LEU   C CD1 
1366 C  CD2 . LEU   B 34  ? 0.1979 0.2008 0.2476 0.0029  0.0067  0.0260  40  LEU   C CD2 
1367 N  N   . LEU   B 35  ? 0.1572 0.1633 0.2424 0.0041  0.0173  0.0389  41  LEU   C N   
1368 C  CA  . LEU   B 35  ? 0.1682 0.1751 0.2640 0.0054  0.0214  0.0431  41  LEU   C CA  
1369 C  C   . LEU   B 35  ? 0.1740 0.1822 0.2667 0.0051  0.0205  0.0450  41  LEU   C C   
1370 O  O   . LEU   B 35  ? 0.1818 0.1916 0.2685 0.0031  0.0152  0.0466  41  LEU   C O   
1371 C  CB  . LEU   B 35  ? 0.1698 0.1806 0.2773 0.0048  0.0202  0.0504  41  LEU   C CB  
1372 C  CG  . LEU   B 35  ? 0.1852 0.1979 0.3063 0.0065  0.0246  0.0556  41  LEU   C CG  
1373 C  CD1 . LEU   B 35  ? 0.2142 0.2280 0.3470 0.0072  0.0258  0.0598  41  LEU   C CD1 
1374 C  CD2 . LEU   B 35  ? 0.1949 0.2126 0.3192 0.0051  0.0212  0.0621  41  LEU   C CD2 
1375 N  N   . VAL   B 36  ? 0.1790 0.1859 0.2753 0.0069  0.0258  0.0446  42  VAL   C N   
1376 C  CA  . VAL   B 36  ? 0.1803 0.1886 0.2752 0.0065  0.0260  0.0470  42  VAL   C CA  
1377 C  C   . VAL   B 36  ? 0.1882 0.2002 0.2978 0.0077  0.0300  0.0535  42  VAL   C C   
1378 O  O   . VAL   B 36  ? 0.1986 0.2086 0.3152 0.0103  0.0364  0.0525  42  VAL   C O   
1379 C  CB  . VAL   B 36  ? 0.1823 0.1856 0.2662 0.0077  0.0291  0.0405  42  VAL   C CB  
1380 C  CG1 . VAL   B 36  ? 0.1940 0.1986 0.2768 0.0073  0.0298  0.0435  42  VAL   C CG1 
1381 C  CG2 . VAL   B 36  ? 0.1791 0.1796 0.2498 0.0066  0.0245  0.0348  42  VAL   C CG2 
1382 N  N   . SER   B 37  ? 0.1789 0.1959 0.2935 0.0058  0.0264  0.0601  43  SER   C N   
1383 C  CA  . SER   B 37  ? 0.1801 0.2021 0.3102 0.0068  0.0297  0.0673  43  SER   C CA  
1384 C  C   . SER   B 37  ? 0.2031 0.2267 0.3321 0.0060  0.0306  0.0693  43  SER   C C   
1385 O  O   . SER   B 37  ? 0.2037 0.2247 0.3198 0.0042  0.0271  0.0660  43  SER   C O   
1386 C  CB  . SER   B 37  ? 0.1969 0.2246 0.3371 0.0047  0.0241  0.0750  43  SER   C CB  
1387 O  OG  . SER   B 37  ? 0.2130 0.2420 0.3451 0.0008  0.0160  0.0767  43  SER   C OG  
1388 N  N   . SER   B 38  ? 0.1961 0.2240 0.3392 0.0076  0.0357  0.0749  44  SER   C N   
1389 C  CA  . SER   B 38  ? 0.2135 0.2437 0.3574 0.0067  0.0372  0.0777  44  SER   C CA  
1390 C  C   . SER   B 38  ? 0.2287 0.2658 0.3800 0.0027  0.0297  0.0861  44  SER   C C   
1391 O  O   . SER   B 38  ? 0.2247 0.2665 0.3862 0.0016  0.0258  0.0917  44  SER   C O   
1392 C  CB  . SER   B 38  ? 0.2438 0.2748 0.3984 0.0106  0.0475  0.0791  44  SER   C CB  
1393 O  OG  . SER   B 38  ? 0.2790 0.3160 0.4524 0.0120  0.0489  0.0863  44  SER   C OG  
1394 N  N   . THR   B 39  ? 0.2327 0.2702 0.3787 0.0002  0.0275  0.0873  45  THR   C N   
1395 C  CA  . THR   B 39  ? 0.2409 0.2839 0.3924 -0.0044 0.0198  0.0947  45  THR   C CA  
1396 C  C   . THR   B 39  ? 0.2707 0.3190 0.4332 -0.0048 0.0237  0.1007  45  THR   C C   
1397 O  O   . THR   B 39  ? 0.2686 0.3143 0.4282 -0.0021 0.0314  0.0975  45  THR   C O   
1398 C  CB  . THR   B 39  ? 0.2444 0.2822 0.3782 -0.0081 0.0118  0.0909  45  THR   C CB  
1399 O  OG1 . THR   B 39  ? 0.2456 0.2787 0.3686 -0.0073 0.0153  0.0861  45  THR   C OG1 
1400 C  CG2 . THR   B 39  ? 0.2493 0.2824 0.3722 -0.0077 0.0082  0.0853  45  THR   C CG2 
1401 N  N   . THR   B 40  ? 0.2916 0.3472 0.4662 -0.0084 0.0182  0.1096  46  THR   C N   
1402 C  CA  . THR   B 40  ? 0.3112 0.3729 0.4974 -0.0097 0.0208  0.1162  46  THR   C CA  
1403 C  C   . THR   B 40  ? 0.3194 0.3766 0.4913 -0.0136 0.0163  0.1141  46  THR   C C   
1404 O  O   . THR   B 40  ? 0.3341 0.3910 0.5054 -0.0128 0.0221  0.1138  46  THR   C O   
1405 C  CB  . THR   B 40  ? 0.3508 0.4227 0.5576 -0.0120 0.0164  0.1271  46  THR   C CB  
1406 O  OG1 . THR   B 40  ? 0.3964 0.4674 0.5961 -0.0174 0.0046  0.1288  46  THR   C OG1 
1407 C  CG2 . THR   B 40  ? 0.3402 0.4158 0.5613 -0.0075 0.0214  0.1294  46  THR   C CG2 
1408 N  N   . ALA   B 41  ? 0.3068 0.3600 0.4665 -0.0177 0.0066  0.1123  47  ALA   C N   
1409 C  CA  . ALA   B 41  ? 0.3067 0.3545 0.4525 -0.0214 0.0021  0.1101  47  ALA   C CA  
1410 C  C   . ALA   B 41  ? 0.2934 0.3317 0.4196 -0.0185 0.0048  0.1000  47  ALA   C C   
1411 O  O   . ALA   B 41  ? 0.2786 0.3137 0.3993 -0.0155 0.0062  0.0944  47  ALA   C O   
1412 C  CB  . ALA   B 41  ? 0.3171 0.3640 0.4583 -0.0271 -0.0095 0.1130  47  ALA   C CB  
1413 N  N   . GLN   B 42  ? 0.2981 0.3320 0.4145 -0.0197 0.0053  0.0980  48  GLN   C N   
1414 C  CA  . GLN   B 42  ? 0.3246 0.3496 0.4225 -0.0174 0.0069  0.0892  48  GLN   C CA  
1415 C  C   . GLN   B 42  ? 0.3218 0.3408 0.4058 -0.0196 -0.0017 0.0853  48  GLN   C C   
1416 O  O   . GLN   B 42  ? 0.3357 0.3547 0.4196 -0.0242 -0.0092 0.0892  48  GLN   C O   
1417 C  CB  . GLN   B 42  ? 0.3800 0.4024 0.4726 -0.0180 0.0101  0.0894  48  GLN   C CB  
1418 C  CG  . GLN   B 42  ? 0.4657 0.4913 0.5663 -0.0143 0.0208  0.0902  48  GLN   C CG  
1419 C  CD  . GLN   B 42  ? 0.5827 0.6047 0.6753 -0.0150 0.0239  0.0899  48  GLN   C CD  
1420 O  OE1 . GLN   B 42  ? 0.6250 0.6491 0.7217 -0.0189 0.0211  0.0957  48  GLN   C OE1 
1421 N  NE2 . GLN   B 42  ? 0.6105 0.6265 0.6910 -0.0114 0.0295  0.0834  48  GLN   C NE2 
1422 N  N   . GLY   B 43  ? 0.2950 0.3088 0.3677 -0.0164 -0.0005 0.0777  49  GLY   C N   
1423 C  CA  . GLY   B 43  ? 0.2881 0.2960 0.3474 -0.0175 -0.0071 0.0733  49  GLY   C CA  
1424 C  C   . GLY   B 43  ? 0.2833 0.2839 0.3279 -0.0178 -0.0086 0.0694  49  GLY   C C   
1425 O  O   . GLY   B 43  ? 0.3095 0.3092 0.3528 -0.0167 -0.0040 0.0691  49  GLY   C O   
1426 N  N   . CYS   B 44  ? 0.2642 0.2592 0.2972 -0.0190 -0.0146 0.0664  50  CYS   C N   
1427 C  CA  A CYS   B 44  ? 0.2756 0.2631 0.2951 -0.0193 -0.0166 0.0632  50  CYS   C CA  
1428 C  CA  B CYS   B 44  ? 0.2851 0.2727 0.3046 -0.0192 -0.0166 0.0633  50  CYS   C CA  
1429 C  C   . CYS   B 44  ? 0.2918 0.2742 0.2992 -0.0157 -0.0166 0.0559  50  CYS   C C   
1430 O  O   . CYS   B 44  ? 0.3244 0.3005 0.3208 -0.0154 -0.0183 0.0533  50  CYS   C O   
1431 C  CB  A CYS   B 44  ? 0.2754 0.2593 0.2913 -0.0241 -0.0238 0.0668  50  CYS   C CB  
1432 C  CB  B CYS   B 44  ? 0.3091 0.2930 0.3249 -0.0241 -0.0238 0.0667  50  CYS   C CB  
1433 S  SG  A CYS   B 44  ? 0.2724 0.2638 0.3046 -0.0290 -0.0253 0.0763  50  CYS   C SG  
1434 S  SG  B CYS   B 44  ? 0.3959 0.3780 0.4079 -0.0257 -0.0302 0.0660  50  CYS   C SG  
1435 N  N   . ASP   B 45  ? 0.2546 0.2396 0.2645 -0.0132 -0.0148 0.0530  51  ASP   C N   
1436 C  CA  . ASP   B 45  ? 0.2471 0.2284 0.2473 -0.0101 -0.0149 0.0465  51  ASP   C CA  
1437 C  C   . ASP   B 45  ? 0.2514 0.2319 0.2486 -0.0071 -0.0100 0.0430  51  ASP   C C   
1438 O  O   . ASP   B 45  ? 0.2704 0.2542 0.2747 -0.0067 -0.0051 0.0448  51  ASP   C O   
1439 C  CB  . ASP   B 45  ? 0.2543 0.2388 0.2586 -0.0087 -0.0145 0.0448  51  ASP   C CB  
1440 C  CG  . ASP   B 45  ? 0.3081 0.2924 0.3125 -0.0115 -0.0196 0.0476  51  ASP   C CG  
1441 O  OD1 . ASP   B 45  ? 0.3225 0.3015 0.3183 -0.0135 -0.0242 0.0479  51  ASP   C OD1 
1442 O  OD2 . ASP   B 45  ? 0.2897 0.2785 0.3021 -0.0117 -0.0191 0.0496  51  ASP   C OD2 
1443 N  N   . THR   B 46  ? 0.2312 0.2069 0.2175 -0.0051 -0.0114 0.0383  52  THR   C N   
1444 C  CA  . THR   B 46  ? 0.2248 0.1992 0.2064 -0.0025 -0.0078 0.0346  52  THR   C CA  
1445 C  C   . THR   B 46  ? 0.2241 0.1994 0.2041 0.0002  -0.0078 0.0295  52  THR   C C   
1446 O  O   . THR   B 46  ? 0.2291 0.2031 0.2056 0.0006  -0.0114 0.0280  52  THR   C O   
1447 C  CB  . THR   B 46  ? 0.2607 0.2290 0.2312 -0.0023 -0.0104 0.0338  52  THR   C CB  
1448 O  OG1 . THR   B 46  ? 0.2797 0.2468 0.2515 -0.0051 -0.0106 0.0387  52  THR   C OG1 
1449 C  CG2 . THR   B 46  ? 0.2772 0.2437 0.2409 0.0004  -0.0080 0.0297  52  THR   C CG2 
1450 N  N   . ILE   B 47  ? 0.2091 0.1862 0.1914 0.0018  -0.0036 0.0269  53  ILE   C N   
1451 C  CA  . ILE   B 47  ? 0.2085 0.1866 0.1899 0.0038  -0.0037 0.0222  53  ILE   C CA  
1452 C  C   . ILE   B 47  ? 0.1920 0.1665 0.1629 0.0055  -0.0058 0.0185  53  ILE   C C   
1453 O  O   . ILE   B 47  ? 0.2113 0.1830 0.1766 0.0056  -0.0045 0.0183  53  ILE   C O   
1454 C  CB  . ILE   B 47  ? 0.2220 0.2024 0.2095 0.0044  0.0014  0.0207  53  ILE   C CB  
1455 C  CG1 . ILE   B 47  ? 0.2098 0.1940 0.2090 0.0032  0.0041  0.0251  53  ILE   C CG1 
1456 C  CG2 . ILE   B 47  ? 0.2221 0.2036 0.2095 0.0058  0.0008  0.0161  53  ILE   C CG2 
1457 C  CD1 . ILE   B 47  ? 0.2341 0.2210 0.2381 0.0022  0.0004  0.0271  53  ILE   C CD1 
1458 N  N   . ALA   B 48  ? 0.1869 0.1617 0.1557 0.0068  -0.0088 0.0159  54  ALA   C N   
1459 C  CA  . ALA   B 48  ? 0.1957 0.1682 0.1565 0.0087  -0.0112 0.0128  54  ALA   C CA  
1460 C  C   . ALA   B 48  ? 0.2061 0.1793 0.1661 0.0092  -0.0088 0.0094  54  ALA   C C   
1461 O  O   . ALA   B 48  ? 0.2133 0.1894 0.1798 0.0088  -0.0063 0.0081  54  ALA   C O   
1462 C  CB  . ALA   B 48  ? 0.2013 0.1752 0.1626 0.0102  -0.0141 0.0112  54  ALA   C CB  
1463 N  N   . ARG   B 49  ? 0.1945 0.1644 0.1458 0.0100  -0.0099 0.0080  55  ARG   C N   
1464 C  CA  . ARG   B 49  ? 0.2071 0.1764 0.1550 0.0101  -0.0087 0.0045  55  ARG   C CA  
1465 C  C   . ARG   B 49  ? 0.2256 0.1943 0.1673 0.0117  -0.0137 0.0026  55  ARG   C C   
1466 O  O   . ARG   B 49  ? 0.2456 0.2107 0.1792 0.0123  -0.0158 0.0037  55  ARG   C O   
1467 C  CB  . ARG   B 49  ? 0.2044 0.1700 0.1471 0.0092  -0.0048 0.0054  55  ARG   C CB  
1468 C  CG  . ARG   B 49  ? 0.2142 0.1813 0.1649 0.0081  0.0003  0.0082  55  ARG   C CG  
1469 C  CD  . ARG   B 49  ? 0.2303 0.2001 0.1892 0.0080  0.0034  0.0061  55  ARG   C CD  
1470 N  NE  . ARG   B 49  ? 0.2380 0.2094 0.2053 0.0073  0.0081  0.0097  55  ARG   C NE  
1471 C  CZ  . ARG   B 49  ? 0.2551 0.2296 0.2324 0.0072  0.0105  0.0099  55  ARG   C CZ  
1472 N  NH1 . ARG   B 49  ? 0.2281 0.2040 0.2078 0.0075  0.0090  0.0067  55  ARG   C NH1 
1473 N  NH2 . ARG   B 49  ? 0.2602 0.2367 0.2460 0.0067  0.0143  0.0140  55  ARG   C NH2 
1474 N  N   . CYS   B 50  ? 0.2209 0.1936 0.1676 0.0124  -0.0156 0.0004  56  CYS   C N   
1475 C  CA  . CYS   B 50  ? 0.2049 0.1786 0.1491 0.0143  -0.0204 -0.0005 56  CYS   C CA  
1476 C  C   . CYS   B 50  ? 0.2088 0.1879 0.1603 0.0146  -0.0215 -0.0029 56  CYS   C C   
1477 O  O   . CYS   B 50  ? 0.2026 0.1839 0.1606 0.0132  -0.0186 -0.0037 56  CYS   C O   
1478 C  CB  . CYS   B 50  ? 0.2161 0.1885 0.1599 0.0158  -0.0220 0.0023  56  CYS   C CB  
1479 S  SG  . CYS   B 50  ? 0.2183 0.1944 0.1715 0.0156  -0.0204 0.0033  56  CYS   C SG  
1480 N  N   . ASP   B 51  ? 0.2162 0.1977 0.1678 0.0165  -0.0256 -0.0035 57  ASP   C N   
1481 C  CA  . ASP   B 51  ? 0.2198 0.2073 0.1797 0.0168  -0.0266 -0.0050 57  ASP   C CA  
1482 C  C   . ASP   B 51  ? 0.2294 0.2193 0.1930 0.0197  -0.0277 -0.0032 57  ASP   C C   
1483 O  O   . ASP   B 51  ? 0.2307 0.2256 0.1996 0.0210  -0.0296 -0.0039 57  ASP   C O   
1484 C  CB  . ASP   B 51  ? 0.2437 0.2332 0.2025 0.0162  -0.0301 -0.0074 57  ASP   C CB  
1485 C  CG  . ASP   B 51  ? 0.3069 0.2954 0.2597 0.0182  -0.0348 -0.0064 57  ASP   C CG  
1486 O  OD1 . ASP   B 51  ? 0.2989 0.2844 0.2480 0.0204  -0.0349 -0.0040 57  ASP   C OD1 
1487 O  OD2 . ASP   B 51  ? 0.3752 0.3659 0.3274 0.0176  -0.0386 -0.0079 57  ASP   C OD2 
1488 N  N   . CYS   B 52  ? 0.2238 0.2099 0.1844 0.0205  -0.0264 -0.0009 58  CYS   C N   
1489 C  CA  . CYS   B 52  ? 0.2051 0.1915 0.1672 0.0231  -0.0268 0.0004  58  CYS   C CA  
1490 C  C   . CYS   B 52  ? 0.2049 0.1972 0.1758 0.0233  -0.0251 -0.0003 58  CYS   C C   
1491 O  O   . CYS   B 52  ? 0.2011 0.1955 0.1766 0.0208  -0.0228 -0.0008 58  CYS   C O   
1492 C  CB  . CYS   B 52  ? 0.1995 0.1801 0.1568 0.0227  -0.0255 0.0025  58  CYS   C CB  
1493 S  SG  . CYS   B 52  ? 0.2318 0.2048 0.1787 0.0232  -0.0277 0.0042  58  CYS   C SG  
1494 N  N   . GLN   B 53  ? 0.1937 0.1881 0.1668 0.0263  -0.0259 0.0000  59  GLN   C N   
1495 C  CA  . GLN   B 53  ? 0.1914 0.1910 0.1723 0.0269  -0.0236 0.0000  59  GLN   C CA  
1496 C  C   . GLN   B 53  ? 0.1940 0.1903 0.1719 0.0294  -0.0219 0.0013  59  GLN   C C   
1497 O  O   . GLN   B 53  ? 0.1949 0.1951 0.1780 0.0308  -0.0199 0.0014  59  GLN   C O   
1498 C  CB  . GLN   B 53  ? 0.1919 0.1990 0.1808 0.0279  -0.0251 -0.0010 59  GLN   C CB  
1499 C  CG  . GLN   B 53  ? 0.2071 0.2173 0.1996 0.0245  -0.0262 -0.0028 59  GLN   C CG  
1500 C  CD  . GLN   B 53  ? 0.2653 0.2832 0.2666 0.0252  -0.0281 -0.0032 59  GLN   C CD  
1501 O  OE1 . GLN   B 53  ? 0.2943 0.3139 0.2953 0.0252  -0.0321 -0.0039 59  GLN   C OE1 
1502 N  NE2 . GLN   B 53  ? 0.2174 0.2404 0.2269 0.0257  -0.0254 -0.0025 59  GLN   C NE2 
1503 N  N   . THR   B 54  ? 0.1991 0.1878 0.1683 0.0298  -0.0226 0.0022  60  THR   C N   
1504 C  CA  . THR   B 54  ? 0.2145 0.1978 0.1786 0.0314  -0.0212 0.0031  60  THR   C CA  
1505 C  C   . THR   B 54  ? 0.2212 0.1981 0.1788 0.0281  -0.0214 0.0044  60  THR   C C   
1506 O  O   . THR   B 54  ? 0.2268 0.2018 0.1820 0.0262  -0.0229 0.0048  60  THR   C O   
1507 C  CB  . THR   B 54  ? 0.2672 0.2468 0.2272 0.0357  -0.0223 0.0030  60  THR   C CB  
1508 O  OG1 . THR   B 54  ? 0.3027 0.2774 0.2567 0.0354  -0.0252 0.0036  60  THR   C OG1 
1509 C  CG2 . THR   B 54  ? 0.2679 0.2550 0.2360 0.0392  -0.0224 0.0025  60  THR   C CG2 
1510 N  N   . GLY   B 55  ? 0.1992 0.1732 0.1544 0.0271  -0.0198 0.0052  61  GLY   C N   
1511 C  CA  . GLY   B 55  ? 0.2020 0.1709 0.1524 0.0235  -0.0205 0.0070  61  GLY   C CA  
1512 C  C   . GLY   B 55  ? 0.2081 0.1729 0.1540 0.0231  -0.0194 0.0077  61  GLY   C C   
1513 O  O   . GLY   B 55  ? 0.2139 0.1780 0.1582 0.0262  -0.0178 0.0065  61  GLY   C O   
1514 N  N   . VAL   B 56  ? 0.2054 0.1674 0.1491 0.0191  -0.0203 0.0098  62  VAL   C N   
1515 C  CA  . VAL   B 56  ? 0.2015 0.1588 0.1394 0.0176  -0.0202 0.0107  62  VAL   C CA  
1516 C  C   . VAL   B 56  ? 0.2036 0.1655 0.1474 0.0137  -0.0200 0.0133  62  VAL   C C   
1517 O  O   . VAL   B 56  ? 0.2083 0.1720 0.1563 0.0113  -0.0211 0.0149  62  VAL   C O   
1518 C  CB  . VAL   B 56  ? 0.2146 0.1618 0.1421 0.0163  -0.0230 0.0114  62  VAL   C CB  
1519 C  CG1 . VAL   B 56  ? 0.2410 0.1824 0.1612 0.0134  -0.0239 0.0127  62  VAL   C CG1 
1520 C  CG2 . VAL   B 56  ? 0.2195 0.1612 0.1411 0.0206  -0.0230 0.0091  62  VAL   C CG2 
1521 N  N   . TYR   B 57  ? 0.1984 0.1616 0.1424 0.0130  -0.0186 0.0140  63  TYR   C N   
1522 C  CA  . TYR   B 57  ? 0.1927 0.1600 0.1426 0.0093  -0.0187 0.0170  63  TYR   C CA  
1523 C  C   . TYR   B 57  ? 0.2082 0.1697 0.1498 0.0066  -0.0205 0.0191  63  TYR   C C   
1524 O  O   . TYR   B 57  ? 0.2227 0.1785 0.1551 0.0083  -0.0198 0.0174  63  TYR   C O   
1525 C  CB  . TYR   B 57  ? 0.1923 0.1679 0.1522 0.0103  -0.0156 0.0167  63  TYR   C CB  
1526 C  CG  . TYR   B 57  ? 0.1914 0.1676 0.1492 0.0114  -0.0132 0.0165  63  TYR   C CG  
1527 C  CD1 . TYR   B 57  ? 0.2027 0.1785 0.1578 0.0153  -0.0110 0.0138  63  TYR   C CD1 
1528 C  CD2 . TYR   B 57  ? 0.1855 0.1635 0.1453 0.0087  -0.0128 0.0195  63  TYR   C CD2 
1529 C  CE1 . TYR   B 57  ? 0.2106 0.1873 0.1642 0.0166  -0.0078 0.0138  63  TYR   C CE1 
1530 C  CE2 . TYR   B 57  ? 0.1959 0.1745 0.1535 0.0097  -0.0100 0.0196  63  TYR   C CE2 
1531 C  CZ  . TYR   B 57  ? 0.2154 0.1933 0.1696 0.0136  -0.0073 0.0166  63  TYR   C CZ  
1532 O  OH  . TYR   B 57  ? 0.2399 0.2187 0.1922 0.0147  -0.0037 0.0170  63  TYR   C OH  
1533 N  N   . TYR   B 58  ? 0.1986 0.1617 0.1439 0.0026  -0.0224 0.0228  64  TYR   C N   
1534 C  CA  . TYR   B 58  ? 0.2185 0.1767 0.1563 -0.0008 -0.0250 0.0255  64  TYR   C CA  
1535 C  C   . TYR   B 58  ? 0.2158 0.1788 0.1575 -0.0010 -0.0227 0.0270  64  TYR   C C   
1536 O  O   . TYR   B 58  ? 0.2080 0.1785 0.1613 -0.0016 -0.0214 0.0289  64  TYR   C O   
1537 C  CB  . TYR   B 58  ? 0.2250 0.1829 0.1654 -0.0053 -0.0291 0.0297  64  TYR   C CB  
1538 C  CG  . TYR   B 58  ? 0.2431 0.1954 0.1747 -0.0093 -0.0328 0.0325  64  TYR   C CG  
1539 C  CD1 . TYR   B 58  ? 0.2657 0.2077 0.1822 -0.0095 -0.0344 0.0302  64  TYR   C CD1 
1540 C  CD2 . TYR   B 58  ? 0.2404 0.1972 0.1782 -0.0128 -0.0346 0.0373  64  TYR   C CD2 
1541 C  CE1 . TYR   B 58  ? 0.2830 0.2189 0.1895 -0.0135 -0.0379 0.0324  64  TYR   C CE1 
1542 C  CE2 . TYR   B 58  ? 0.2638 0.2154 0.1928 -0.0168 -0.0387 0.0401  64  TYR   C CE2 
1543 C  CZ  . TYR   B 58  ? 0.2896 0.2305 0.2023 -0.0174 -0.0406 0.0375  64  TYR   C CZ  
1544 O  OH  . TYR   B 58  ? 0.3448 0.2792 0.2464 -0.0217 -0.0448 0.0398  64  TYR   C OH  
1545 N  N   . CYS   B 59  ? 0.2167 0.1743 0.1477 -0.0010 -0.0223 0.0264  65  CYS   C N   
1546 C  CA  . CYS   B 59  ? 0.2247 0.1854 0.1567 -0.0013 -0.0200 0.0280  65  CYS   C CA  
1547 C  C   . CYS   B 59  ? 0.2577 0.2128 0.1806 -0.0060 -0.0241 0.0316  65  CYS   C C   
1548 O  O   . CYS   B 59  ? 0.2659 0.2117 0.1740 -0.0064 -0.0251 0.0300  65  CYS   C O   
1549 C  CB  . CYS   B 59  ? 0.2302 0.1893 0.1566 0.0029  -0.0154 0.0243  65  CYS   C CB  
1550 S  SG  . CYS   B 59  ? 0.2567 0.2182 0.1818 0.0024  -0.0119 0.0265  65  CYS   C SG  
1551 N  N   . SER   B 60  ? 0.2522 0.2123 0.1834 -0.0095 -0.0266 0.0365  66  SER   C N   
1552 C  CA  A SER   B 60  ? 0.2667 0.2220 0.1901 -0.0144 -0.0316 0.0407  66  SER   C CA  
1553 C  CA  B SER   B 60  ? 0.2581 0.2135 0.1816 -0.0144 -0.0316 0.0407  66  SER   C CA  
1554 C  C   . SER   B 60  ? 0.2702 0.2209 0.1816 -0.0149 -0.0304 0.0408  66  SER   C C   
1555 O  O   . SER   B 60  ? 0.3054 0.2476 0.2028 -0.0182 -0.0343 0.0417  66  SER   C O   
1556 C  CB  A SER   B 60  ? 0.2948 0.2574 0.2315 -0.0176 -0.0344 0.0464  66  SER   C CB  
1557 C  CB  B SER   B 60  ? 0.2615 0.2243 0.1982 -0.0175 -0.0342 0.0465  66  SER   C CB  
1558 O  OG  A SER   B 60  ? 0.3208 0.2916 0.2699 -0.0155 -0.0302 0.0474  66  SER   C OG  
1559 O  OG  B SER   B 60  ? 0.2566 0.2150 0.1858 -0.0226 -0.0400 0.0510  66  SER   C OG  
1560 N  N   . SER   B 61  ? 0.2567 0.2123 0.1726 -0.0118 -0.0249 0.0398  67  SER   C N   
1561 C  CA  . SER   B 61  ? 0.2711 0.2228 0.1757 -0.0119 -0.0226 0.0401  67  SER   C CA  
1562 C  C   . SER   B 61  ? 0.3052 0.2466 0.1927 -0.0097 -0.0206 0.0352  67  SER   C C   
1563 O  O   . SER   B 61  ? 0.3293 0.2654 0.2045 -0.0099 -0.0185 0.0351  67  SER   C O   
1564 C  CB  . SER   B 61  ? 0.2863 0.2465 0.2017 -0.0094 -0.0170 0.0407  67  SER   C CB  
1565 O  OG  . SER   B 61  ? 0.3159 0.2798 0.2376 -0.0045 -0.0122 0.0361  67  SER   C OG  
1566 N  N   . ARG   B 62  ? 0.2936 0.2317 0.1800 -0.0073 -0.0208 0.0312  68  ARG   C N   
1567 C  CA  . ARG   B 62  ? 0.3020 0.2293 0.1726 -0.0049 -0.0189 0.0267  68  ARG   C CA  
1568 C  C   . ARG   B 62  ? 0.3176 0.2357 0.1795 -0.0078 -0.0248 0.0259  68  ARG   C C   
1569 O  O   . ARG   B 62  ? 0.3403 0.2482 0.1893 -0.0058 -0.0238 0.0219  68  ARG   C O   
1570 C  CB  . ARG   B 62  ? 0.3024 0.2333 0.1791 0.0015  -0.0130 0.0223  68  ARG   C CB  
1571 C  CG  . ARG   B 62  ? 0.3482 0.2876 0.2330 0.0044  -0.0068 0.0227  68  ARG   C CG  
1572 C  CD  . ARG   B 62  ? 0.3757 0.3080 0.2459 0.0055  -0.0027 0.0217  68  ARG   C CD  
1573 N  NE  . ARG   B 62  ? 0.3962 0.3370 0.2748 0.0079  0.0034  0.0227  68  ARG   C NE  
1574 C  CZ  . ARG   B 62  ? 0.4836 0.4286 0.3647 0.0050  0.0037  0.0269  68  ARG   C CZ  
1575 N  NH1 . ARG   B 62  ? 0.5213 0.4633 0.3977 -0.0004 -0.0021 0.0306  68  ARG   C NH1 
1576 N  NH2 . ARG   B 62  ? 0.4810 0.4332 0.3696 0.0073  0.0097  0.0277  68  ARG   C NH2 
1577 N  N   . ARG   B 63  ? 0.3247 0.2468 0.1952 -0.0117 -0.0303 0.0295  69  ARG   C N   
1578 C  CA  . ARG   B 63  ? 0.3504 0.2653 0.2153 -0.0148 -0.0360 0.0294  69  ARG   C CA  
1579 C  C   . ARG   B 63  ? 0.3527 0.2638 0.2162 -0.0103 -0.0334 0.0245  69  ARG   C C   
1580 O  O   . ARG   B 63  ? 0.3738 0.2734 0.2242 -0.0111 -0.0357 0.0222  69  ARG   C O   
1581 C  CB  . ARG   B 63  ? 0.4033 0.3054 0.2486 -0.0192 -0.0401 0.0297  69  ARG   C CB  
1582 C  CG  . ARG   B 63  ? 0.4842 0.3861 0.3300 -0.0263 -0.0480 0.0351  69  ARG   C CG  
1583 C  CD  . ARG   B 63  ? 0.4889 0.4034 0.3505 -0.0275 -0.0482 0.0404  69  ARG   C CD  
1584 N  NE  . ARG   B 63  ? 0.5268 0.4404 0.3859 -0.0341 -0.0554 0.0462  69  ARG   C NE  
1585 C  CZ  . ARG   B 63  ? 0.5392 0.4618 0.4090 -0.0359 -0.0565 0.0517  69  ARG   C CZ  
1586 N  NH1 . ARG   B 63  ? 0.5067 0.4392 0.3899 -0.0317 -0.0505 0.0518  69  ARG   C NH1 
1587 N  NH2 . ARG   B 63  ? 0.5321 0.4537 0.3994 -0.0421 -0.0637 0.0574  69  ARG   C NH2 
1588 N  N   . LYS   B 64  ? 0.3193 0.2393 0.1953 -0.0055 -0.0287 0.0229  70  LYS   C N   
1589 C  CA  . LYS   B 64  ? 0.3203 0.2371 0.1948 -0.0006 -0.0261 0.0185  70  LYS   C CA  
1590 C  C   . LYS   B 64  ? 0.2856 0.2123 0.1757 0.0017  -0.0249 0.0186  70  LYS   C C   
1591 O  O   . LYS   B 64  ? 0.2708 0.2078 0.1732 0.0016  -0.0233 0.0205  70  LYS   C O   
1592 C  CB  . LYS   B 64  ? 0.3712 0.2859 0.2400 0.0045  -0.0199 0.0151  70  LYS   C CB  
1593 C  CG  . LYS   B 64  ? 0.5070 0.4074 0.3561 0.0042  -0.0198 0.0127  70  LYS   C CG  
1594 C  CD  . LYS   B 64  ? 0.6081 0.5058 0.4528 0.0107  -0.0129 0.0087  70  LYS   C CD  
1595 C  CE  . LYS   B 64  ? 0.6845 0.5675 0.5087 0.0105  -0.0116 0.0063  70  LYS   C CE  
1596 N  NZ  . LYS   B 64  ? 0.7371 0.6190 0.5541 0.0057  -0.0130 0.0091  70  LYS   C NZ  
1597 N  N   . HIS   B 65  ? 0.2708 0.1937 0.1594 0.0039  -0.0254 0.0163  71  HIS   C N   
1598 C  CA  . HIS   B 65  ? 0.2682 0.1992 0.1691 0.0066  -0.0241 0.0156  71  HIS   C CA  
1599 C  C   . HIS   B 65  ? 0.2880 0.2195 0.1886 0.0126  -0.0196 0.0120  71  HIS   C C   
1600 O  O   . HIS   B 65  ? 0.3366 0.2588 0.2263 0.0149  -0.0188 0.0096  71  HIS   C O   
1601 C  CB  . HIS   B 65  ? 0.2596 0.1860 0.1590 0.0050  -0.0279 0.0161  71  HIS   C CB  
1602 C  CG  . HIS   B 65  ? 0.2565 0.1836 0.1584 -0.0008 -0.0322 0.0202  71  HIS   C CG  
1603 N  ND1 . HIS   B 65  ? 0.2807 0.2165 0.1953 -0.0021 -0.0325 0.0227  71  HIS   C ND1 
1604 C  CD2 . HIS   B 65  ? 0.2828 0.2028 0.1762 -0.0056 -0.0364 0.0224  71  HIS   C CD2 
1605 C  CE1 . HIS   B 65  ? 0.2798 0.2142 0.1944 -0.0072 -0.0365 0.0266  71  HIS   C CE1 
1606 N  NE2 . HIS   B 65  ? 0.3081 0.2335 0.2105 -0.0098 -0.0394 0.0267  71  HIS   C NE2 
1607 N  N   . TYR   B 66  ? 0.2450 0.1869 0.1576 0.0152  -0.0166 0.0116  72  TYR   C N   
1608 C  CA  . TYR   B 66  ? 0.2471 0.1911 0.1616 0.0207  -0.0126 0.0089  72  TYR   C CA  
1609 C  C   . TYR   B 66  ? 0.2298 0.1791 0.1528 0.0232  -0.0132 0.0079  72  TYR   C C   
1610 O  O   . TYR   B 66  ? 0.2299 0.1868 0.1626 0.0212  -0.0141 0.0091  72  TYR   C O   
1611 C  CB  . TYR   B 66  ? 0.2515 0.2039 0.1733 0.0215  -0.0086 0.0094  72  TYR   C CB  
1612 C  CG  . TYR   B 66  ? 0.2794 0.2268 0.1919 0.0201  -0.0069 0.0102  72  TYR   C CG  
1613 C  CD1 . TYR   B 66  ? 0.3022 0.2427 0.2048 0.0236  -0.0035 0.0080  72  TYR   C CD1 
1614 C  CD2 . TYR   B 66  ? 0.2971 0.2468 0.2109 0.0155  -0.0084 0.0134  72  TYR   C CD2 
1615 C  CE1 . TYR   B 66  ? 0.3246 0.2600 0.2172 0.0223  -0.0014 0.0086  72  TYR   C CE1 
1616 C  CE2 . TYR   B 66  ? 0.3157 0.2609 0.2202 0.0140  -0.0070 0.0144  72  TYR   C CE2 
1617 C  CZ  . TYR   B 66  ? 0.3406 0.2781 0.2334 0.0172  -0.0036 0.0118  72  TYR   C CZ  
1618 O  OH  . TYR   B 66  ? 0.3685 0.3010 0.2506 0.0155  -0.0019 0.0128  72  TYR   C OH  
1619 N  N   . PRO   B 67  ? 0.2307 0.1763 0.1505 0.0276  -0.0124 0.0057  73  PRO   C N   
1620 C  CA  . PRO   B 67  ? 0.2267 0.1782 0.1549 0.0301  -0.0130 0.0050  73  PRO   C CA  
1621 C  C   . PRO   B 67  ? 0.2262 0.1887 0.1659 0.0322  -0.0100 0.0047  73  PRO   C C   
1622 O  O   . PRO   B 67  ? 0.2539 0.2174 0.1933 0.0344  -0.0063 0.0042  73  PRO   C O   
1623 C  CB  . PRO   B 67  ? 0.2643 0.2081 0.1853 0.0346  -0.0129 0.0033  73  PRO   C CB  
1624 C  CG  . PRO   B 67  ? 0.2821 0.2188 0.1941 0.0359  -0.0098 0.0023  73  PRO   C CG  
1625 C  CD  . PRO   B 67  ? 0.2514 0.1871 0.1599 0.0308  -0.0105 0.0038  73  PRO   C CD  
1626 N  N   . VAL   B 68  ? 0.2020 0.1725 0.1513 0.0312  -0.0113 0.0050  74  VAL   C N   
1627 C  CA  . VAL   B 68  ? 0.2065 0.1870 0.1670 0.0321  -0.0091 0.0048  74  VAL   C CA  
1628 C  C   . VAL   B 68  ? 0.1978 0.1839 0.1654 0.0329  -0.0113 0.0040  74  VAL   C C   
1629 O  O   . VAL   B 68  ? 0.2069 0.1901 0.1716 0.0315  -0.0143 0.0040  74  VAL   C O   
1630 C  CB  . VAL   B 68  ? 0.2277 0.2128 0.1935 0.0279  -0.0082 0.0063  74  VAL   C CB  
1631 C  CG1 . VAL   B 68  ? 0.2596 0.2418 0.2203 0.0271  -0.0056 0.0074  74  VAL   C CG1 
1632 C  CG2 . VAL   B 68  ? 0.2244 0.2080 0.1899 0.0240  -0.0111 0.0073  74  VAL   C CG2 
1633 N  N   . SER   B 69  ? 0.1916 0.1858 0.1684 0.0351  -0.0099 0.0035  75  SER   C N   
1634 C  CA  . SER   B 69  ? 0.1895 0.1906 0.1745 0.0348  -0.0122 0.0029  75  SER   C CA  
1635 C  C   . SER   B 69  ? 0.1740 0.1807 0.1664 0.0309  -0.0112 0.0032  75  SER   C C   
1636 O  O   . SER   B 69  ? 0.1749 0.1837 0.1701 0.0302  -0.0081 0.0041  75  SER   C O   
1637 C  CB  . SER   B 69  ? 0.2159 0.2231 0.2081 0.0390  -0.0115 0.0027  75  SER   C CB  
1638 O  OG  . SER   B 69  ? 0.2749 0.2765 0.2609 0.0429  -0.0124 0.0026  75  SER   C OG  
1639 N  N   . PHE   B 70  ? 0.1687 0.1768 0.1634 0.0282  -0.0136 0.0024  76  PHE   C N   
1640 C  CA  . PHE   B 70  ? 0.1661 0.1781 0.1674 0.0246  -0.0125 0.0025  76  PHE   C CA  
1641 C  C   . PHE   B 70  ? 0.1784 0.1951 0.1858 0.0234  -0.0147 0.0008  76  PHE   C C   
1642 O  O   . PHE   B 70  ? 0.1807 0.1963 0.1850 0.0245  -0.0177 -0.0002 76  PHE   C O   
1643 C  CB  . PHE   B 70  ? 0.1780 0.1849 0.1749 0.0216  -0.0120 0.0037  76  PHE   C CB  
1644 C  CG  . PHE   B 70  ? 0.1728 0.1745 0.1629 0.0212  -0.0144 0.0033  76  PHE   C CG  
1645 C  CD1 . PHE   B 70  ? 0.1754 0.1707 0.1568 0.0224  -0.0154 0.0041  76  PHE   C CD1 
1646 C  CD2 . PHE   B 70  ? 0.1754 0.1776 0.1672 0.0191  -0.0152 0.0022  76  PHE   C CD2 
1647 C  CE1 . PHE   B 70  ? 0.1870 0.1776 0.1626 0.0217  -0.0173 0.0042  76  PHE   C CE1 
1648 C  CE2 . PHE   B 70  ? 0.1823 0.1797 0.1677 0.0187  -0.0167 0.0022  76  PHE   C CE2 
1649 C  CZ  . PHE   B 70  ? 0.1879 0.1799 0.1657 0.0199  -0.0178 0.0034  76  PHE   C CZ  
1650 N  N   . SER   B 71  ? 0.1592 0.1809 0.1751 0.0211  -0.0134 0.0007  77  SER   C N   
1651 C  CA  . SER   B 71  ? 0.1659 0.1917 0.1875 0.0193  -0.0157 -0.0012 77  SER   C CA  
1652 C  C   . SER   B 71  ? 0.1899 0.2108 0.2066 0.0168  -0.0171 -0.0029 77  SER   C C   
1653 O  O   . SER   B 71  ? 0.2058 0.2214 0.2166 0.0163  -0.0158 -0.0021 77  SER   C O   
1654 C  CB  . SER   B 71  ? 0.1783 0.2102 0.2104 0.0175  -0.0138 -0.0008 77  SER   C CB  
1655 O  OG  . SER   B 71  ? 0.1904 0.2199 0.2233 0.0149  -0.0110 0.0001  77  SER   C OG  
1656 N  N   . LYS   B 72  ? 0.1801 0.2028 0.1992 0.0150  -0.0195 -0.0051 78  LYS   C N   
1657 C  CA  . LYS   B 72  ? 0.1899 0.2074 0.2035 0.0126  -0.0200 -0.0070 78  LYS   C CA  
1658 C  C   . LYS   B 72  ? 0.1822 0.1986 0.2006 0.0099  -0.0166 -0.0072 78  LYS   C C   
1659 O  O   . LYS   B 72  ? 0.1856 0.2065 0.2125 0.0089  -0.0153 -0.0066 78  LYS   C O   
1660 C  CB  . LYS   B 72  ? 0.2440 0.2628 0.2570 0.0115  -0.0242 -0.0095 78  LYS   C CB  
1661 C  CG  . LYS   B 72  ? 0.3060 0.3254 0.3143 0.0145  -0.0279 -0.0088 78  LYS   C CG  
1662 C  CD  . LYS   B 72  ? 0.4283 0.4463 0.4316 0.0128  -0.0323 -0.0111 78  LYS   C CD  
1663 C  CE  . LYS   B 72  ? 0.5174 0.5359 0.5164 0.0159  -0.0362 -0.0097 78  LYS   C CE  
1664 N  NZ  . LYS   B 72  ? 0.5647 0.5818 0.5580 0.0141  -0.0412 -0.0115 78  LYS   C NZ  
1665 N  N   . PRO   B 73  ? 0.1829 0.1937 0.1966 0.0087  -0.0148 -0.0077 79  PRO   C N   
1666 C  CA  . PRO   B 73  ? 0.1877 0.1973 0.2068 0.0066  -0.0111 -0.0073 79  PRO   C CA  
1667 C  C   . PRO   B 73  ? 0.2010 0.2125 0.2263 0.0041  -0.0116 -0.0098 79  PRO   C C   
1668 O  O   . PRO   B 73  ? 0.2169 0.2270 0.2388 0.0030  -0.0143 -0.0130 79  PRO   C O   
1669 C  CB  . PRO   B 73  ? 0.2142 0.2177 0.2273 0.0062  -0.0093 -0.0078 79  PRO   C CB  
1670 C  CG  . PRO   B 73  ? 0.2288 0.2303 0.2331 0.0080  -0.0116 -0.0076 79  PRO   C CG  
1671 C  CD  . PRO   B 73  ? 0.1884 0.1940 0.1925 0.0094  -0.0155 -0.0082 79  PRO   C CD  
1672 N  N   . SER   B 74  ? 0.1827 0.1972 0.2167 0.0031  -0.0095 -0.0083 80  SER   C N   
1673 C  CA  . SER   B 74  ? 0.1965 0.2129 0.2373 0.0004  -0.0102 -0.0103 80  SER   C CA  
1674 C  C   . SER   B 74  ? 0.1979 0.2144 0.2470 -0.0012 -0.0065 -0.0083 80  SER   C C   
1675 O  O   . SER   B 74  ? 0.1935 0.2090 0.2428 0.0000  -0.0037 -0.0052 80  SER   C O   
1676 C  CB  . SER   B 74  ? 0.2507 0.2741 0.2956 0.0008  -0.0136 -0.0102 80  SER   C CB  
1677 O  OG  . SER   B 74  ? 0.3175 0.3459 0.3676 0.0025  -0.0117 -0.0067 80  SER   C OG  
1678 N  N   . LEU   B 75  ? 0.2068 0.2241 0.2625 -0.0040 -0.0067 -0.0100 81  LEU   C N   
1679 C  CA  . LEU   B 75  ? 0.2201 0.2372 0.2842 -0.0058 -0.0035 -0.0081 81  LEU   C CA  
1680 C  C   . LEU   B 75  ? 0.2212 0.2462 0.2927 -0.0055 -0.0037 -0.0049 81  LEU   C C   
1681 O  O   . LEU   B 75  ? 0.2242 0.2541 0.2995 -0.0066 -0.0064 -0.0060 81  LEU   C O   
1682 C  CB  . LEU   B 75  ? 0.2363 0.2493 0.3029 -0.0093 -0.0041 -0.0119 81  LEU   C CB  
1683 C  CG  . LEU   B 75  ? 0.2565 0.2667 0.3311 -0.0114 -0.0006 -0.0107 81  LEU   C CG  
1684 C  CD1 . LEU   B 75  ? 0.2595 0.2643 0.3324 -0.0096 0.0036  -0.0088 81  LEU   C CD1 
1685 C  CD2 . LEU   B 75  ? 0.2814 0.2866 0.3569 -0.0152 -0.0020 -0.0153 81  LEU   C CD2 
1686 N  N   . ILE   B 76  ? 0.2051 0.2314 0.2778 -0.0040 -0.0009 -0.0008 82  ILE   C N   
1687 C  CA  . ILE   B 76  ? 0.1971 0.2299 0.2744 -0.0032 -0.0001 0.0025  82  ILE   C CA  
1688 C  C   . ILE   B 76  ? 0.1989 0.2319 0.2831 -0.0048 0.0033  0.0061  82  ILE   C C   
1689 O  O   . ILE   B 76  ? 0.1967 0.2251 0.2794 -0.0048 0.0051  0.0077  82  ILE   C O   
1690 C  CB  . ILE   B 76  ? 0.2207 0.2537 0.2901 0.0002  -0.0001 0.0043  82  ILE   C CB  
1691 C  CG1 . ILE   B 76  ? 0.2565 0.2891 0.3188 0.0022  -0.0034 0.0014  82  ILE   C CG1 
1692 C  CG2 . ILE   B 76  ? 0.2279 0.2660 0.3000 0.0014  0.0020  0.0079  82  ILE   C CG2 
1693 C  CD1 . ILE   B 76  ? 0.2896 0.3286 0.3555 0.0032  -0.0053 0.0009  82  ILE   C CD1 
1694 N  N   . PHE   B 77  ? 0.1882 0.2268 0.2805 -0.0061 0.0041  0.0078  83  PHE   C N   
1695 C  CA  . PHE   B 77  ? 0.1989 0.2379 0.2971 -0.0076 0.0074  0.0119  83  PHE   C CA  
1696 C  C   . PHE   B 77  ? 0.2064 0.2461 0.2989 -0.0051 0.0092  0.0158  83  PHE   C C   
1697 O  O   . PHE   B 77  ? 0.2226 0.2661 0.3116 -0.0028 0.0090  0.0161  83  PHE   C O   
1698 C  CB  . PHE   B 77  ? 0.1981 0.2430 0.3065 -0.0100 0.0080  0.0129  83  PHE   C CB  
1699 C  CG  . PHE   B 77  ? 0.2090 0.2530 0.3236 -0.0120 0.0113  0.0171  83  PHE   C CG  
1700 C  CD1 . PHE   B 77  ? 0.2228 0.2608 0.3409 -0.0143 0.0118  0.0165  83  PHE   C CD1 
1701 C  CD2 . PHE   B 77  ? 0.2265 0.2748 0.3425 -0.0113 0.0142  0.0218  83  PHE   C CD2 
1702 C  CE1 . PHE   B 77  ? 0.2392 0.2760 0.3631 -0.0160 0.0147  0.0209  83  PHE   C CE1 
1703 C  CE2 . PHE   B 77  ? 0.2353 0.2825 0.3563 -0.0132 0.0170  0.0262  83  PHE   C CE2 
1704 C  CZ  . PHE   B 77  ? 0.2375 0.2792 0.3630 -0.0155 0.0170  0.0258  83  PHE   C CZ  
1705 N  N   . VAL   B 78  ? 0.1775 0.2132 0.2688 -0.0054 0.0107  0.0189  84  VAL   C N   
1706 C  CA  . VAL   B 78  ? 0.1827 0.2181 0.2676 -0.0038 0.0117  0.0227  84  VAL   C CA  
1707 C  C   . VAL   B 78  ? 0.1774 0.2142 0.2676 -0.0055 0.0144  0.0277  84  VAL   C C   
1708 O  O   . VAL   B 78  ? 0.1836 0.2180 0.2803 -0.0075 0.0153  0.0291  84  VAL   C O   
1709 C  CB  . VAL   B 78  ? 0.2013 0.2313 0.2800 -0.0030 0.0104  0.0230  84  VAL   C CB  
1710 C  CG1 . VAL   B 78  ? 0.2134 0.2426 0.2848 -0.0020 0.0105  0.0270  84  VAL   C CG1 
1711 C  CG2 . VAL   B 78  ? 0.2141 0.2423 0.2875 -0.0015 0.0081  0.0184  84  VAL   C CG2 
1712 N  N   . GLU   B 79  ? 0.1571 0.1968 0.2440 -0.0047 0.0161  0.0305  85  GLU   C N   
1713 C  CA  . GLU   B 79  ? 0.1761 0.2168 0.2663 -0.0063 0.0188  0.0357  85  GLU   C CA  
1714 C  C   . GLU   B 79  ? 0.1816 0.2174 0.2686 -0.0070 0.0181  0.0396  85  GLU   C C   
1715 O  O   . GLU   B 79  ? 0.1799 0.2123 0.2606 -0.0059 0.0158  0.0387  85  GLU   C O   
1716 C  CB  . GLU   B 79  ? 0.2057 0.2498 0.2908 -0.0049 0.0213  0.0378  85  GLU   C CB  
1717 C  CG  . GLU   B 79  ? 0.2451 0.2958 0.3372 -0.0046 0.0231  0.0359  85  GLU   C CG  
1718 C  CD  . GLU   B 79  ? 0.3734 0.4274 0.4786 -0.0078 0.0243  0.0369  85  GLU   C CD  
1719 O  OE1 . GLU   B 79  ? 0.4276 0.4803 0.5361 -0.0100 0.0262  0.0412  85  GLU   C OE1 
1720 O  OE2 . GLU   B 79  ? 0.3735 0.4310 0.4857 -0.0084 0.0229  0.0335  85  GLU   C OE2 
1721 N  N   . ALA   B 80  ? 0.1963 0.2320 0.2880 -0.0090 0.0199  0.0446  86  ALA   C N   
1722 C  CA  . ALA   B 80  ? 0.2013 0.2332 0.2915 -0.0097 0.0189  0.0493  86  ALA   C CA  
1723 C  C   . ALA   B 80  ? 0.2076 0.2376 0.2853 -0.0085 0.0170  0.0509  86  ALA   C C   
1724 O  O   . ALA   B 80  ? 0.2194 0.2507 0.2893 -0.0075 0.0180  0.0505  86  ALA   C O   
1725 C  CB  . ALA   B 80  ? 0.2015 0.2341 0.2976 -0.0119 0.0213  0.0550  86  ALA   C CB  
1726 N  N   . SER   B 81  ? 0.2082 0.2349 0.2844 -0.0085 0.0144  0.0523  87  SER   C N   
1727 C  CA  . SER   B 81  ? 0.2257 0.2501 0.2907 -0.0081 0.0117  0.0543  87  SER   C CA  
1728 C  C   . SER   B 81  ? 0.2473 0.2699 0.3145 -0.0100 0.0101  0.0612  87  SER   C C   
1729 O  O   . SER   B 81  ? 0.2516 0.2749 0.3292 -0.0110 0.0116  0.0640  87  SER   C O   
1730 C  CB  . SER   B 81  ? 0.2164 0.2389 0.2778 -0.0066 0.0092  0.0501  87  SER   C CB  
1731 O  OG  . SER   B 81  ? 0.2095 0.2310 0.2793 -0.0070 0.0086  0.0510  87  SER   C OG  
1732 N  N   . GLU   B 82  ? 0.2682 0.2885 0.3262 -0.0106 0.0067  0.0641  88  GLU   C N   
1733 C  CA  . GLU   B 82  ? 0.2759 0.2953 0.3370 -0.0125 0.0045  0.0713  88  GLU   C CA  
1734 C  C   . GLU   B 82  ? 0.2688 0.2884 0.3418 -0.0120 0.0036  0.0722  88  GLU   C C   
1735 O  O   . GLU   B 82  ? 0.2933 0.3130 0.3732 -0.0131 0.0027  0.0782  88  GLU   C O   
1736 C  CB  . GLU   B 82  ? 0.3336 0.3503 0.3815 -0.0141 0.0005  0.0748  88  GLU   C CB  
1737 C  CG  . GLU   B 82  ? 0.4350 0.4496 0.4767 -0.0137 -0.0032 0.0725  88  GLU   C CG  
1738 C  CD  . GLU   B 82  ? 0.5217 0.5327 0.5495 -0.0160 -0.0075 0.0760  88  GLU   C CD  
1739 O  OE1 . GLU   B 82  ? 0.5134 0.5227 0.5315 -0.0167 -0.0063 0.0770  88  GLU   C OE1 
1740 O  OE2 . GLU   B 82  ? 0.5607 0.5705 0.5874 -0.0172 -0.0121 0.0779  88  GLU   C OE2 
1741 N  N   . TYR   B 83  ? 0.2271 0.2467 0.3029 -0.0102 0.0045  0.0663  89  TYR   C N   
1742 C  CA  . TYR   B 83  ? 0.2253 0.2445 0.3109 -0.0094 0.0046  0.0667  89  TYR   C CA  
1743 C  C   . TYR   B 83  ? 0.2192 0.2380 0.3141 -0.0082 0.0085  0.0620  89  TYR   C C   
1744 O  O   . TYR   B 83  ? 0.2383 0.2558 0.3418 -0.0074 0.0096  0.0626  89  TYR   C O   
1745 C  CB  . TYR   B 83  ? 0.2232 0.2415 0.3031 -0.0088 0.0017  0.0650  89  TYR   C CB  
1746 C  CG  . TYR   B 83  ? 0.2315 0.2490 0.3007 -0.0078 0.0014  0.0588  89  TYR   C CG  
1747 C  CD1 . TYR   B 83  ? 0.2457 0.2621 0.3026 -0.0086 -0.0008 0.0593  89  TYR   C CD1 
1748 C  CD2 . TYR   B 83  ? 0.2260 0.2433 0.2968 -0.0061 0.0033  0.0525  89  TYR   C CD2 
1749 C  CE1 . TYR   B 83  ? 0.2513 0.2667 0.2992 -0.0072 -0.0006 0.0537  89  TYR   C CE1 
1750 C  CE2 . TYR   B 83  ? 0.2434 0.2602 0.3052 -0.0050 0.0028  0.0474  89  TYR   C CE2 
1751 C  CZ  . TYR   B 83  ? 0.2585 0.2745 0.3095 -0.0054 0.0010  0.0481  89  TYR   C CZ  
1752 O  OH  . TYR   B 83  ? 0.2649 0.2801 0.3079 -0.0038 0.0009  0.0432  89  TYR   C OH  
1753 N  N   . TYR   B 84  ? 0.1925 0.2120 0.2858 -0.0081 0.0106  0.0573  90  TYR   C N   
1754 C  CA  . TYR   B 84  ? 0.1854 0.2040 0.2869 -0.0079 0.0135  0.0531  90  TYR   C CA  
1755 C  C   . TYR   B 84  ? 0.1888 0.2095 0.2923 -0.0093 0.0154  0.0531  90  TYR   C C   
1756 O  O   . TYR   B 84  ? 0.1936 0.2167 0.2899 -0.0095 0.0150  0.0533  90  TYR   C O   
1757 C  CB  . TYR   B 84  ? 0.1737 0.1917 0.2711 -0.0065 0.0134  0.0456  90  TYR   C CB  
1758 C  CG  . TYR   B 84  ? 0.1638 0.1795 0.2607 -0.0051 0.0127  0.0446  90  TYR   C CG  
1759 C  CD1 . TYR   B 84  ? 0.1663 0.1793 0.2720 -0.0046 0.0149  0.0457  90  TYR   C CD1 
1760 C  CD2 . TYR   B 84  ? 0.1631 0.1790 0.2512 -0.0042 0.0104  0.0425  90  TYR   C CD2 
1761 C  CE1 . TYR   B 84  ? 0.1677 0.1791 0.2735 -0.0031 0.0151  0.0450  90  TYR   C CE1 
1762 C  CE2 . TYR   B 84  ? 0.1601 0.1743 0.2482 -0.0031 0.0101  0.0421  90  TYR   C CE2 
1763 C  CZ  . TYR   B 84  ? 0.1733 0.1855 0.2704 -0.0025 0.0127  0.0432  90  TYR   C CZ  
1764 O  OH  . TYR   B 84  ? 0.1840 0.1948 0.2813 -0.0012 0.0131  0.0429  90  TYR   C OH  
1765 N  N   . PRO   B 85  ? 0.1892 0.2085 0.3021 -0.0101 0.0178  0.0519  91  PRO   C N   
1766 C  CA  . PRO   B 85  ? 0.1879 0.2095 0.3037 -0.0118 0.0195  0.0511  91  PRO   C CA  
1767 C  C   . PRO   B 85  ? 0.1898 0.2138 0.3016 -0.0112 0.0190  0.0444  91  PRO   C C   
1768 O  O   . PRO   B 85  ? 0.1873 0.2101 0.2939 -0.0096 0.0174  0.0402  91  PRO   C O   
1769 C  CB  . PRO   B 85  ? 0.1989 0.2169 0.3258 -0.0130 0.0217  0.0513  91  PRO   C CB  
1770 C  CG  . PRO   B 85  ? 0.2047 0.2186 0.3323 -0.0113 0.0215  0.0477  91  PRO   C CG  
1771 C  CD  . PRO   B 85  ? 0.1879 0.2029 0.3090 -0.0096 0.0193  0.0508  91  PRO   C CD  
1772 N  N   . ALA   B 86  ? 0.1882 0.2157 0.3032 -0.0126 0.0203  0.0436  92  ALA   C N   
1773 C  CA  . ALA   B 86  ? 0.1930 0.2235 0.3066 -0.0123 0.0196  0.0380  92  ALA   C CA  
1774 C  C   . ALA   B 86  ? 0.2051 0.2316 0.3227 -0.0130 0.0188  0.0329  92  ALA   C C   
1775 O  O   . ALA   B 86  ? 0.2277 0.2507 0.3529 -0.0147 0.0202  0.0336  92  ALA   C O   
1776 C  CB  . ALA   B 86  ? 0.1891 0.2246 0.3084 -0.0142 0.0214  0.0393  92  ALA   C CB  
1777 N  N   . ARG   B 87  ? 0.1848 0.2107 0.2964 -0.0114 0.0168  0.0279  93  ARG   C N   
1778 C  CA  . ARG   B 87  ? 0.1895 0.2106 0.3023 -0.0119 0.0162  0.0230  93  ARG   C CA  
1779 C  C   . ARG   B 87  ? 0.1911 0.2134 0.2968 -0.0106 0.0136  0.0178  93  ARG   C C   
1780 O  O   . ARG   B 87  ? 0.1851 0.2114 0.2851 -0.0088 0.0124  0.0185  93  ARG   C O   
1781 C  CB  . ARG   B 87  ? 0.2038 0.2194 0.3163 -0.0106 0.0174  0.0248  93  ARG   C CB  
1782 C  CG  . ARG   B 87  ? 0.1960 0.2120 0.2999 -0.0081 0.0159  0.0252  93  ARG   C CG  
1783 C  CD  . ARG   B 87  ? 0.2093 0.2218 0.3147 -0.0069 0.0171  0.0287  93  ARG   C CD  
1784 N  NE  . ARG   B 87  ? 0.2057 0.2184 0.3030 -0.0051 0.0153  0.0281  93  ARG   C NE  
1785 C  CZ  . ARG   B 87  ? 0.2314 0.2409 0.3275 -0.0037 0.0158  0.0270  93  ARG   C CZ  
1786 N  NH1 . ARG   B 87  ? 0.2202 0.2253 0.3227 -0.0036 0.0187  0.0265  93  ARG   C NH1 
1787 N  NH2 . ARG   B 87  ? 0.2353 0.2454 0.3238 -0.0025 0.0139  0.0265  93  ARG   C NH2 
1788 N  N   . TYR   B 88  ? 0.1980 0.2162 0.3031 -0.0113 0.0127  0.0128  94  TYR   C N   
1789 C  CA  . TYR   B 88  ? 0.2201 0.2384 0.3173 -0.0100 0.0100  0.0084  94  TYR   C CA  
1790 C  C   . TYR   B 88  ? 0.2034 0.2178 0.2941 -0.0076 0.0106  0.0089  94  TYR   C C   
1791 O  O   . TYR   B 88  ? 0.2141 0.2236 0.3072 -0.0075 0.0130  0.0099  94  TYR   C O   
1792 C  CB  . TYR   B 88  ? 0.2449 0.2592 0.3423 -0.0122 0.0086  0.0027  94  TYR   C CB  
1793 C  CG  . TYR   B 88  ? 0.2824 0.3015 0.3858 -0.0148 0.0067  0.0018  94  TYR   C CG  
1794 C  CD1 . TYR   B 88  ? 0.3053 0.3304 0.4065 -0.0142 0.0035  0.0004  94  TYR   C CD1 
1795 C  CD2 . TYR   B 88  ? 0.3068 0.3250 0.4192 -0.0179 0.0082  0.0029  94  TYR   C CD2 
1796 C  CE1 . TYR   B 88  ? 0.3236 0.3547 0.4323 -0.0166 0.0018  0.0005  94  TYR   C CE1 
1797 C  CE2 . TYR   B 88  ? 0.3270 0.3506 0.4463 -0.0207 0.0064  0.0027  94  TYR   C CE2 
1798 C  CZ  . TYR   B 88  ? 0.3453 0.3757 0.4631 -0.0201 0.0032  0.0015  94  TYR   C CZ  
1799 O  OH  . TYR   B 88  ? 0.3935 0.4302 0.5198 -0.0228 0.0017  0.0021  94  TYR   C OH  
1800 N  N   . GLN   B 89  ? 0.1854 0.2018 0.2683 -0.0055 0.0086  0.0083  95  GLN   C N   
1801 C  CA  . GLN   B 89  ? 0.1811 0.1940 0.2577 -0.0036 0.0088  0.0085  95  GLN   C CA  
1802 C  C   . GLN   B 89  ? 0.1895 0.2008 0.2587 -0.0030 0.0065  0.0036  95  GLN   C C   
1803 O  O   . GLN   B 89  ? 0.2019 0.2170 0.2690 -0.0028 0.0039  0.0019  95  GLN   C O   
1804 C  CB  . GLN   B 89  ? 0.1948 0.2104 0.2678 -0.0021 0.0082  0.0129  95  GLN   C CB  
1805 C  CG  . GLN   B 89  ? 0.2172 0.2297 0.2846 -0.0006 0.0080  0.0138  95  GLN   C CG  
1806 C  CD  . GLN   B 89  ? 0.2126 0.2264 0.2781 -0.0002 0.0074  0.0190  95  GLN   C CD  
1807 O  OE1 . GLN   B 89  ? 0.2162 0.2315 0.2864 -0.0011 0.0083  0.0230  95  GLN   C OE1 
1808 N  NE2 . GLN   B 89  ? 0.2057 0.2184 0.2638 0.0010  0.0056  0.0190  95  GLN   C NE2 
1809 N  N   . SER   B 90  ? 0.1695 0.1755 0.2350 -0.0025 0.0077  0.0016  96  SER   C N   
1810 C  CA  . SER   B 90  ? 0.1831 0.1868 0.2405 -0.0021 0.0057  -0.0029 96  SER   C CA  
1811 C  C   . SER   B 90  ? 0.1856 0.1895 0.2352 0.0001  0.0045  -0.0017 96  SER   C C   
1812 O  O   . SER   B 90  ? 0.1825 0.1871 0.2330 0.0011  0.0056  0.0024  96  SER   C O   
1813 C  CB  . SER   B 90  ? 0.2092 0.2059 0.2656 -0.0031 0.0080  -0.0065 96  SER   C CB  
1814 O  OG  . SER   B 90  ? 0.2166 0.2101 0.2739 -0.0017 0.0117  -0.0040 96  SER   C OG  
1815 N  N   . HIS   B 91  ? 0.1766 0.1796 0.2183 0.0007  0.0018  -0.0050 97  HIS   C N   
1816 C  CA  . HIS   B 91  ? 0.1809 0.1832 0.2146 0.0026  0.0004  -0.0042 97  HIS   C CA  
1817 C  C   . HIS   B 91  ? 0.1732 0.1795 0.2074 0.0039  -0.0007 -0.0003 97  HIS   C C   
1818 O  O   . HIS   B 91  ? 0.1839 0.1888 0.2140 0.0049  -0.0006 0.0021  97  HIS   C O   
1819 C  CB  . HIS   B 91  ? 0.2032 0.2006 0.2342 0.0030  0.0035  -0.0035 97  HIS   C CB  
1820 C  CG  . HIS   B 91  ? 0.2355 0.2275 0.2638 0.0020  0.0053  -0.0078 97  HIS   C CG  
1821 N  ND1 . HIS   B 91  ? 0.2585 0.2472 0.2771 0.0023  0.0039  -0.0109 97  HIS   C ND1 
1822 C  CD2 . HIS   B 91  ? 0.2541 0.2428 0.2873 0.0008  0.0084  -0.0094 97  HIS   C CD2 
1823 C  CE1 . HIS   B 91  ? 0.2699 0.2532 0.2869 0.0011  0.0064  -0.0145 97  HIS   C CE1 
1824 N  NE2 . HIS   B 91  ? 0.2669 0.2497 0.2927 0.0003  0.0092  -0.0139 97  HIS   C NE2 
1825 N  N   . LEU   B 92  ? 0.1637 0.1746 0.2024 0.0036  -0.0016 0.0002  98  LEU   C N   
1826 C  CA  . LEU   B 92  ? 0.1656 0.1796 0.2040 0.0049  -0.0020 0.0034  98  LEU   C CA  
1827 C  C   . LEU   B 92  ? 0.1653 0.1817 0.1994 0.0067  -0.0047 0.0020  98  LEU   C C   
1828 O  O   . LEU   B 92  ? 0.1741 0.1927 0.2100 0.0065  -0.0064 -0.0008 98  LEU   C O   
1829 C  CB  . LEU   B 92  ? 0.1673 0.1846 0.2139 0.0036  -0.0001 0.0057  98  LEU   C CB  
1830 C  CG  . LEU   B 92  ? 0.1912 0.2107 0.2368 0.0045  0.0003  0.0093  98  LEU   C CG  
1831 C  CD1 . LEU   B 92  ? 0.2063 0.2225 0.2479 0.0045  0.0006  0.0126  98  LEU   C CD1 
1832 C  CD2 . LEU   B 92  ? 0.1886 0.2119 0.2422 0.0031  0.0023  0.0114  98  LEU   C CD2 
1833 N  N   . MET   B 93  ? 0.1559 0.1714 0.1842 0.0086  -0.0054 0.0038  99  MET   C N   
1834 C  CA  . MET   B 93  ? 0.1469 0.1639 0.1711 0.0110  -0.0074 0.0029  99  MET   C CA  
1835 C  C   . MET   B 93  ? 0.1590 0.1778 0.1834 0.0122  -0.0059 0.0054  99  MET   C C   
1836 O  O   . MET   B 93  ? 0.1654 0.1816 0.1873 0.0115  -0.0047 0.0079  99  MET   C O   
1837 C  CB  . MET   B 93  ? 0.1719 0.1840 0.1867 0.0124  -0.0092 0.0026  99  MET   C CB  
1838 C  CG  . MET   B 93  ? 0.1921 0.2016 0.2052 0.0112  -0.0100 0.0004  99  MET   C CG  
1839 S  SD  . MET   B 93  ? 0.2254 0.2290 0.2283 0.0122  -0.0114 0.0010  99  MET   C SD  
1840 C  CE  . MET   B 93  ? 0.2254 0.2269 0.2289 0.0109  -0.0093 0.0047  99  MET   C CE  
1841 N  N   . LEU   B 94  ? 0.1486 0.1717 0.1756 0.0140  -0.0059 0.0049  100 LEU   C N   
1842 C  CA  . LEU   B 94  ? 0.1647 0.1892 0.1913 0.0154  -0.0035 0.0070  100 LEU   C CA  
1843 C  C   . LEU   B 94  ? 0.1707 0.1931 0.1902 0.0190  -0.0041 0.0066  100 LEU   C C   
1844 O  O   . LEU   B 94  ? 0.1727 0.1957 0.1915 0.0208  -0.0064 0.0048  100 LEU   C O   
1845 C  CB  . LEU   B 94  ? 0.1780 0.2097 0.2148 0.0151  -0.0016 0.0074  100 LEU   C CB  
1846 C  CG  . LEU   B 94  ? 0.1898 0.2237 0.2347 0.0117  -0.0004 0.0082  100 LEU   C CG  
1847 C  CD1 . LEU   B 94  ? 0.2122 0.2534 0.2669 0.0115  0.0013  0.0088  100 LEU   C CD1 
1848 C  CD2 . LEU   B 94  ? 0.2120 0.2422 0.2543 0.0101  0.0014  0.0111  100 LEU   C CD2 
1849 N  N   . ALA   B 95  ? 0.1655 0.1847 0.1791 0.0200  -0.0021 0.0083  101 ALA   C N   
1850 C  CA  . ALA   B 95  ? 0.1675 0.1838 0.1741 0.0237  -0.0017 0.0078  101 ALA   C CA  
1851 C  C   . ALA   B 95  ? 0.1722 0.1894 0.1781 0.0247  0.0024  0.0095  101 ALA   C C   
1852 O  O   . ALA   B 95  ? 0.1790 0.1974 0.1872 0.0221  0.0041  0.0114  101 ALA   C O   
1853 C  CB  . ALA   B 95  ? 0.1783 0.1859 0.1735 0.0236  -0.0038 0.0078  101 ALA   C CB  
1854 N  N   . VAL   B 96  ? 0.1634 0.1797 0.1659 0.0287  0.0044  0.0089  102 VAL   C N   
1855 C  CA  . VAL   B 96  ? 0.1868 0.2024 0.1861 0.0301  0.0090  0.0102  102 VAL   C CA  
1856 C  C   . VAL   B 96  ? 0.2143 0.2195 0.1992 0.0291  0.0084  0.0105  102 VAL   C C   
1857 O  O   . VAL   B 96  ? 0.2251 0.2237 0.2018 0.0308  0.0064  0.0090  102 VAL   C O   
1858 C  CB  . VAL   B 96  ? 0.2123 0.2306 0.2140 0.0353  0.0118  0.0093  102 VAL   C CB  
1859 C  CG1 . VAL   B 96  ? 0.2327 0.2487 0.2288 0.0372  0.0176  0.0104  102 VAL   C CG1 
1860 C  CG2 . VAL   B 96  ? 0.2127 0.2421 0.2298 0.0355  0.0116  0.0095  102 VAL   C CG2 
1861 N  N   . GLY   B 97  ? 0.2441 0.2479 0.2263 0.0259  0.0094  0.0128  103 GLY   C N   
1862 C  CA  . GLY   B 97  ? 0.2589 0.2533 0.2277 0.0241  0.0078  0.0135  103 GLY   C CA  
1863 C  C   . GLY   B 97  ? 0.2695 0.2640 0.2375 0.0202  0.0082  0.0167  103 GLY   C C   
1864 O  O   . GLY   B 97  ? 0.2745 0.2762 0.2531 0.0187  0.0097  0.0184  103 GLY   C O   
1865 N  N   . HIS   B 98  ? 0.2698 0.2560 0.2253 0.0182  0.0065  0.0178  104 HIS   C N   
1866 C  CA  . HIS   B 98  ? 0.2769 0.2623 0.2300 0.0144  0.0063  0.0214  104 HIS   C CA  
1867 C  C   . HIS   B 98  ? 0.2601 0.2475 0.2197 0.0105  0.0019  0.0239  104 HIS   C C   
1868 O  O   . HIS   B 98  ? 0.2571 0.2415 0.2151 0.0098  -0.0018 0.0230  104 HIS   C O   
1869 C  CB  . HIS   B 98  ? 0.3183 0.2933 0.2541 0.0137  0.0059  0.0216  104 HIS   C CB  
1870 C  CG  . HIS   B 98  ? 0.3989 0.3731 0.3310 0.0100  0.0057  0.0256  104 HIS   C CG  
1871 N  ND1 . HIS   B 98  ? 0.4198 0.3991 0.3561 0.0104  0.0104  0.0275  104 HIS   C ND1 
1872 C  CD2 . HIS   B 98  ? 0.4304 0.3997 0.3557 0.0056  0.0010  0.0285  104 HIS   C CD2 
1873 C  CE1 . HIS   B 98  ? 0.4460 0.4229 0.3772 0.0064  0.0084  0.0314  104 HIS   C CE1 
1874 N  NE2 . HIS   B 98  ? 0.4491 0.4201 0.3736 0.0034  0.0025  0.0323  104 HIS   C NE2 
1875 N  N   . SER   B 99  ? 0.2508 0.2431 0.2180 0.0080  0.0027  0.0273  105 SER   C N   
1876 C  CA  . SER   B 99  ? 0.2474 0.2418 0.2220 0.0046  -0.0006 0.0302  105 SER   C CA  
1877 C  C   . SER   B 99  ? 0.2661 0.2628 0.2437 0.0018  0.0003  0.0350  105 SER   C C   
1878 O  O   . SER   B 99  ? 0.2831 0.2853 0.2689 0.0025  0.0038  0.0355  105 SER   C O   
1879 C  CB  . SER   B 99  ? 0.2501 0.2507 0.2378 0.0056  -0.0002 0.0283  105 SER   C CB  
1880 O  OG  . SER   B 99  ? 0.2783 0.2810 0.2743 0.0031  -0.0020 0.0308  105 SER   C OG  
1881 N  N   . GLU   B 100 ? 0.2673 0.2597 0.2385 -0.0014 -0.0033 0.0387  106 GLU   C N   
1882 C  CA  . GLU   B 100 ? 0.2604 0.2544 0.2341 -0.0043 -0.0036 0.0441  106 GLU   C CA  
1883 C  C   . GLU   B 100 ? 0.2406 0.2383 0.2268 -0.0062 -0.0063 0.0468  106 GLU   C C   
1884 O  O   . GLU   B 100 ? 0.2321 0.2292 0.2204 -0.0058 -0.0085 0.0450  106 GLU   C O   
1885 C  CB  . GLU   B 100 ? 0.3138 0.3006 0.2724 -0.0071 -0.0067 0.0470  106 GLU   C CB  
1886 C  CG  . GLU   B 100 ? 0.4106 0.3906 0.3532 -0.0054 -0.0047 0.0439  106 GLU   C CG  
1887 C  CD  . GLU   B 100 ? 0.4823 0.4619 0.4189 -0.0051 -0.0003 0.0453  106 GLU   C CD  
1888 O  OE1 . GLU   B 100 ? 0.5272 0.5128 0.4738 -0.0060 0.0017  0.0487  106 GLU   C OE1 
1889 O  OE2 . GLU   B 100 ? 0.5068 0.4797 0.4290 -0.0037 0.0019  0.0429  106 GLU   C OE2 
1890 N  N   . PRO   B 101 ? 0.2444 0.2453 0.2383 -0.0082 -0.0062 0.0517  107 PRO   C N   
1891 C  CA  . PRO   B 101 ? 0.2430 0.2470 0.2491 -0.0094 -0.0081 0.0544  107 PRO   C CA  
1892 C  C   . PRO   B 101 ? 0.2409 0.2419 0.2438 -0.0110 -0.0131 0.0559  107 PRO   C C   
1893 O  O   . PRO   B 101 ? 0.2433 0.2464 0.2547 -0.0104 -0.0134 0.0551  107 PRO   C O   
1894 C  CB  . PRO   B 101 ? 0.2705 0.2766 0.2820 -0.0115 -0.0079 0.0605  107 PRO   C CB  
1895 C  CG  . PRO   B 101 ? 0.2848 0.2908 0.2907 -0.0107 -0.0042 0.0596  107 PRO   C CG  
1896 C  CD  . PRO   B 101 ? 0.2558 0.2578 0.2486 -0.0090 -0.0036 0.0548  107 PRO   C CD  
1897 N  N   . GLY   B 102 ? 0.2291 0.2251 0.2193 -0.0133 -0.0168 0.0579  108 GLY   C N   
1898 C  CA  . GLY   B 102 ? 0.2331 0.2262 0.2201 -0.0156 -0.0221 0.0597  108 GLY   C CA  
1899 C  C   . GLY   B 102 ? 0.2293 0.2200 0.2130 -0.0138 -0.0222 0.0545  108 GLY   C C   
1900 O  O   . GLY   B 102 ? 0.2459 0.2351 0.2295 -0.0156 -0.0260 0.0559  108 GLY   C O   
1901 N  N   . ASP   B 103 ? 0.2141 0.2045 0.1953 -0.0104 -0.0182 0.0489  109 ASP   C N   
1902 C  CA  . ASP   B 103 ? 0.2082 0.1963 0.1865 -0.0083 -0.0182 0.0441  109 ASP   C CA  
1903 C  C   . ASP   B 103 ? 0.2069 0.1999 0.1980 -0.0071 -0.0170 0.0432  109 ASP   C C   
1904 O  O   . ASP   B 103 ? 0.2119 0.2031 0.2011 -0.0060 -0.0176 0.0403  109 ASP   C O   
1905 C  CB  . ASP   B 103 ? 0.2293 0.2157 0.2010 -0.0048 -0.0146 0.0389  109 ASP   C CB  
1906 C  CG  . ASP   B 103 ? 0.2573 0.2369 0.2137 -0.0055 -0.0154 0.0388  109 ASP   C CG  
1907 O  OD1 . ASP   B 103 ? 0.2653 0.2391 0.2131 -0.0082 -0.0197 0.0404  109 ASP   C OD1 
1908 O  OD2 . ASP   B 103 ? 0.2609 0.2405 0.2138 -0.0033 -0.0115 0.0370  109 ASP   C OD2 
1909 N  N   . CYS   B 104 ? 0.1946 0.1930 0.1983 -0.0074 -0.0150 0.0458  110 CYS   C N   
1910 C  CA  . CYS   B 104 ? 0.1985 0.2003 0.2132 -0.0061 -0.0132 0.0445  110 CYS   C CA  
1911 C  C   . CYS   B 104 ? 0.2074 0.2078 0.2224 -0.0075 -0.0161 0.0464  110 CYS   C C   
1912 O  O   . CYS   B 104 ? 0.2232 0.2225 0.2365 -0.0103 -0.0198 0.0511  110 CYS   C O   
1913 C  CB  . CYS   B 104 ? 0.2053 0.2115 0.2324 -0.0064 -0.0108 0.0474  110 CYS   C CB  
1914 S  SG  . CYS   B 104 ? 0.2273 0.2360 0.2574 -0.0047 -0.0065 0.0444  110 CYS   C SG  
1915 N  N   . GLY   B 105 ? 0.1711 0.1715 0.1876 -0.0058 -0.0147 0.0429  111 GLY   C N   
1916 C  CA  . GLY   B 105 ? 0.1920 0.1913 0.2091 -0.0070 -0.0167 0.0446  111 GLY   C CA  
1917 C  C   . GLY   B 105 ? 0.1964 0.1905 0.2018 -0.0069 -0.0192 0.0419  111 GLY   C C   
1918 O  O   . GLY   B 105 ? 0.2046 0.1975 0.2103 -0.0076 -0.0203 0.0425  111 GLY   C O   
1919 N  N   . GLY   B 106 ? 0.1984 0.1889 0.1935 -0.0061 -0.0198 0.0392  112 GLY   C N   
1920 C  CA  . GLY   B 106 ? 0.1988 0.1833 0.1823 -0.0054 -0.0216 0.0362  112 GLY   C CA  
1921 C  C   . GLY   B 106 ? 0.1939 0.1789 0.1790 -0.0027 -0.0196 0.0322  112 GLY   C C   
1922 O  O   . GLY   B 106 ? 0.1857 0.1747 0.1769 -0.0005 -0.0164 0.0298  112 GLY   C O   
1923 N  N   . ILE   B 107 ? 0.1944 0.1753 0.1742 -0.0033 -0.0218 0.0320  113 ILE   C N   
1924 C  CA  . ILE   B 107 ? 0.1922 0.1731 0.1726 -0.0010 -0.0202 0.0289  113 ILE   C CA  
1925 C  C   . ILE   B 107 ? 0.1918 0.1702 0.1652 0.0023  -0.0195 0.0243  113 ILE   C C   
1926 O  O   . ILE   B 107 ? 0.1923 0.1655 0.1565 0.0026  -0.0211 0.0234  113 ILE   C O   
1927 C  CB  . ILE   B 107 ? 0.2238 0.2017 0.2025 -0.0031 -0.0224 0.0311  113 ILE   C CB  
1928 C  CG1 . ILE   B 107 ? 0.2496 0.2328 0.2400 -0.0050 -0.0211 0.0352  113 ILE   C CG1 
1929 C  CG2 . ILE   B 107 ? 0.2330 0.2080 0.2068 -0.0008 -0.0218 0.0278  113 ILE   C CG2 
1930 C  CD1 . ILE   B 107 ? 0.2932 0.2751 0.2848 -0.0074 -0.0226 0.0386  113 ILE   C CD1 
1931 N  N   . LEU   B 108 ? 0.1744 0.1560 0.1518 0.0047  -0.0172 0.0213  114 LEU   C N   
1932 C  CA  . LEU   B 108 ? 0.1701 0.1501 0.1424 0.0079  -0.0172 0.0175  114 LEU   C CA  
1933 C  C   . LEU   B 108 ? 0.1806 0.1578 0.1500 0.0080  -0.0182 0.0170  114 LEU   C C   
1934 O  O   . LEU   B 108 ? 0.1708 0.1505 0.1455 0.0071  -0.0169 0.0176  114 LEU   C O   
1935 C  CB  . LEU   B 108 ? 0.1638 0.1496 0.1428 0.0098  -0.0147 0.0149  114 LEU   C CB  
1936 C  CG  . LEU   B 108 ? 0.1928 0.1786 0.1692 0.0130  -0.0150 0.0115  114 LEU   C CG  
1937 C  CD1 . LEU   B 108 ? 0.1991 0.1819 0.1691 0.0153  -0.0154 0.0107  114 LEU   C CD1 
1938 C  CD2 . LEU   B 108 ? 0.2011 0.1931 0.1855 0.0137  -0.0132 0.0095  114 LEU   C CD2 
1939 N  N   . ARG   B 109 ? 0.1947 0.1661 0.1554 0.0093  -0.0202 0.0161  115 ARG   C N   
1940 C  CA  . ARG   B 109 ? 0.2051 0.1731 0.1620 0.0093  -0.0214 0.0162  115 ARG   C CA  
1941 C  C   . ARG   B 109 ? 0.2171 0.1825 0.1684 0.0128  -0.0222 0.0134  115 ARG   C C   
1942 O  O   . ARG   B 109 ? 0.2159 0.1794 0.1638 0.0151  -0.0225 0.0120  115 ARG   C O   
1943 C  CB  . ARG   B 109 ? 0.2409 0.2030 0.1927 0.0064  -0.0239 0.0193  115 ARG   C CB  
1944 C  CG  . ARG   B 109 ? 0.3473 0.3031 0.2905 0.0070  -0.0258 0.0185  115 ARG   C CG  
1945 C  CD  . ARG   B 109 ? 0.4670 0.4152 0.4032 0.0040  -0.0290 0.0209  115 ARG   C CD  
1946 N  NE  . ARG   B 109 ? 0.5651 0.5137 0.5029 0.0001  -0.0305 0.0240  115 ARG   C NE  
1947 C  CZ  . ARG   B 109 ? 0.6253 0.5771 0.5695 -0.0036 -0.0313 0.0279  115 ARG   C CZ  
1948 N  NH1 . ARG   B 109 ? 0.6338 0.5882 0.5828 -0.0037 -0.0301 0.0289  115 ARG   C NH1 
1949 N  NH2 . ARG   B 109 ? 0.6333 0.5858 0.5792 -0.0070 -0.0333 0.0310  115 ARG   C NH2 
1950 N  N   . CYS   B 110 ? 0.2027 0.1678 0.1531 0.0134  -0.0224 0.0129  116 CYS   C N   
1951 C  CA  . CYS   B 110 ? 0.2123 0.1747 0.1574 0.0166  -0.0239 0.0110  116 CYS   C CA  
1952 C  C   . CYS   B 110 ? 0.2324 0.1885 0.1710 0.0155  -0.0256 0.0129  116 CYS   C C   
1953 O  O   . CYS   B 110 ? 0.2377 0.1920 0.1764 0.0122  -0.0256 0.0155  116 CYS   C O   
1954 C  CB  . CYS   B 110 ? 0.2113 0.1794 0.1608 0.0181  -0.0232 0.0088  116 CYS   C CB  
1955 S  SG  . CYS   B 110 ? 0.2106 0.1799 0.1615 0.0156  -0.0218 0.0093  116 CYS   C SG  
1956 N  N   . GLN   B 111 ? 0.2427 0.1957 0.1761 0.0180  -0.0272 0.0120  117 GLN   C N   
1957 C  CA  . GLN   B 111 ? 0.2782 0.2248 0.2052 0.0168  -0.0286 0.0142  117 GLN   C CA  
1958 C  C   . GLN   B 111 ? 0.2721 0.2210 0.2015 0.0138  -0.0269 0.0159  117 GLN   C C   
1959 O  O   . GLN   B 111 ? 0.2973 0.2419 0.2232 0.0117  -0.0274 0.0186  117 GLN   C O   
1960 C  CB  . GLN   B 111 ? 0.3178 0.2609 0.2392 0.0203  -0.0307 0.0134  117 GLN   C CB  
1961 C  CG  . GLN   B 111 ? 0.3774 0.3263 0.3015 0.0218  -0.0305 0.0117  117 GLN   C CG  
1962 C  CD  . GLN   B 111 ? 0.5109 0.4573 0.4304 0.0252  -0.0333 0.0115  117 GLN   C CD  
1963 O  OE1 . GLN   B 111 ? 0.5535 0.5029 0.4758 0.0285  -0.0342 0.0100  117 GLN   C OE1 
1964 N  NE2 . GLN   B 111 ? 0.5088 0.4503 0.4218 0.0245  -0.0345 0.0134  117 GLN   C NE2 
1965 N  N   . HIS   B 112 ? 0.2489 0.2042 0.1841 0.0137  -0.0246 0.0144  118 HIS   C N   
1966 C  CA  . HIS   B 112 ? 0.2294 0.1864 0.1664 0.0116  -0.0220 0.0155  118 HIS   C CA  
1967 C  C   . HIS   B 112 ? 0.2485 0.2084 0.1928 0.0087  -0.0196 0.0179  118 HIS   C C   
1968 O  O   . HIS   B 112 ? 0.2656 0.2264 0.2120 0.0070  -0.0168 0.0195  118 HIS   C O   
1969 C  CB  . HIS   B 112 ? 0.2323 0.1933 0.1706 0.0129  -0.0208 0.0124  118 HIS   C CB  
1970 C  CG  . HIS   B 112 ? 0.2418 0.2012 0.1743 0.0156  -0.0238 0.0107  118 HIS   C CG  
1971 N  ND1 . HIS   B 112 ? 0.2391 0.2020 0.1745 0.0179  -0.0254 0.0083  118 HIS   C ND1 
1972 C  CD2 . HIS   B 112 ? 0.2545 0.2098 0.1793 0.0162  -0.0253 0.0114  118 HIS   C CD2 
1973 C  CE1 . HIS   B 112 ? 0.2565 0.2174 0.1865 0.0200  -0.0283 0.0078  118 HIS   C CE1 
1974 N  NE2 . HIS   B 112 ? 0.2588 0.2148 0.1818 0.0191  -0.0285 0.0097  118 HIS   C NE2 
1975 N  N   . GLY   B 113 ? 0.2400 0.2013 0.1880 0.0082  -0.0204 0.0182  119 GLY   C N   
1976 C  CA  . GLY   B 113 ? 0.2265 0.1909 0.1819 0.0054  -0.0188 0.0209  119 GLY   C CA  
1977 C  C   . GLY   B 113 ? 0.1957 0.1647 0.1572 0.0059  -0.0180 0.0197  119 GLY   C C   
1978 O  O   . GLY   B 113 ? 0.1975 0.1663 0.1567 0.0079  -0.0193 0.0173  119 GLY   C O   
1979 N  N   . VAL   B 114 ? 0.1807 0.1538 0.1506 0.0041  -0.0157 0.0218  120 VAL   C N   
1980 C  CA  . VAL   B 114 ? 0.1866 0.1639 0.1629 0.0041  -0.0149 0.0214  120 VAL   C CA  
1981 C  C   . VAL   B 114 ? 0.1773 0.1578 0.1562 0.0062  -0.0126 0.0175  120 VAL   C C   
1982 O  O   . VAL   B 114 ? 0.1897 0.1709 0.1704 0.0064  -0.0100 0.0165  120 VAL   C O   
1983 C  CB  . VAL   B 114 ? 0.2014 0.1820 0.1865 0.0016  -0.0134 0.0256  120 VAL   C CB  
1984 C  CG1 . VAL   B 114 ? 0.2091 0.1938 0.2011 0.0017  -0.0123 0.0255  120 VAL   C CG1 
1985 C  CG2 . VAL   B 114 ? 0.2170 0.1949 0.2001 -0.0012 -0.0167 0.0298  120 VAL   C CG2 
1986 N  N   . VAL   B 115 ? 0.1719 0.1540 0.1510 0.0076  -0.0134 0.0154  121 VAL   C N   
1987 C  CA  . VAL   B 115 ? 0.1756 0.1609 0.1578 0.0091  -0.0121 0.0119  121 VAL   C CA  
1988 C  C   . VAL   B 115 ? 0.1936 0.1830 0.1849 0.0080  -0.0095 0.0126  121 VAL   C C   
1989 O  O   . VAL   B 115 ? 0.2023 0.1934 0.1977 0.0081  -0.0074 0.0104  121 VAL   C O   
1990 C  CB  . VAL   B 115 ? 0.1912 0.1767 0.1698 0.0113  -0.0142 0.0098  121 VAL   C CB  
1991 C  CG1 . VAL   B 115 ? 0.1873 0.1772 0.1709 0.0122  -0.0133 0.0068  121 VAL   C CG1 
1992 C  CG2 . VAL   B 115 ? 0.2105 0.1917 0.1807 0.0128  -0.0166 0.0091  121 VAL   C CG2 
1993 N  N   . GLY   B 116 ? 0.1828 0.1731 0.1768 0.0068  -0.0100 0.0155  122 GLY   C N   
1994 C  CA  . GLY   B 116 ? 0.1882 0.1820 0.1908 0.0058  -0.0079 0.0170  122 GLY   C CA  
1995 C  C   . GLY   B 116 ? 0.1833 0.1773 0.1864 0.0044  -0.0094 0.0207  122 GLY   C C   
1996 O  O   . GLY   B 116 ? 0.1799 0.1706 0.1766 0.0037  -0.0120 0.0222  122 GLY   C O   
1997 N  N   . ILE   B 117 ? 0.1763 0.1735 0.1866 0.0036  -0.0079 0.0223  123 ILE   C N   
1998 C  CA  . ILE   B 117 ? 0.1762 0.1735 0.1863 0.0020  -0.0096 0.0261  123 ILE   C CA  
1999 C  C   . ILE   B 117 ? 0.1589 0.1587 0.1712 0.0025  -0.0084 0.0255  123 ILE   C C   
2000 O  O   . ILE   B 117 ? 0.1640 0.1665 0.1822 0.0033  -0.0060 0.0233  123 ILE   C O   
2001 C  CB  . ILE   B 117 ? 0.1915 0.1905 0.2095 -0.0001 -0.0092 0.0310  123 ILE   C CB  
2002 C  CG1 . ILE   B 117 ? 0.1941 0.1962 0.2224 0.0005  -0.0053 0.0305  123 ILE   C CG1 
2003 C  CG2 . ILE   B 117 ? 0.2110 0.2079 0.2270 -0.0013 -0.0108 0.0332  123 ILE   C CG2 
2004 C  CD1 . ILE   B 117 ? 0.2191 0.2235 0.2574 -0.0010 -0.0046 0.0363  123 ILE   C CD1 
2005 N  N   . VAL   B 118 ? 0.1569 0.1552 0.1638 0.0018  -0.0101 0.0273  124 VAL   C N   
2006 C  CA  . VAL   B 118 ? 0.1590 0.1597 0.1676 0.0021  -0.0085 0.0275  124 VAL   C CA  
2007 C  C   . VAL   B 118 ? 0.1702 0.1748 0.1898 0.0009  -0.0065 0.0299  124 VAL   C C   
2008 O  O   . VAL   B 118 ? 0.1692 0.1739 0.1929 -0.0009 -0.0073 0.0338  124 VAL   C O   
2009 C  CB  . VAL   B 118 ? 0.1769 0.1744 0.1768 0.0010  -0.0104 0.0297  124 VAL   C CB  
2010 C  CG1 . VAL   B 118 ? 0.1852 0.1852 0.1867 0.0012  -0.0081 0.0306  124 VAL   C CG1 
2011 C  CG2 . VAL   B 118 ? 0.1872 0.1798 0.1760 0.0026  -0.0118 0.0268  124 VAL   C CG2 
2012 N  N   . SER   B 119 ? 0.1635 0.1712 0.1883 0.0017  -0.0039 0.0280  125 SER   C N   
2013 C  CA  . SER   B 119 ? 0.1660 0.1764 0.2012 0.0007  -0.0018 0.0300  125 SER   C CA  
2014 C  C   . SER   B 119 ? 0.1692 0.1822 0.2067 0.0004  -0.0001 0.0308  125 SER   C C   
2015 O  O   . SER   B 119 ? 0.1785 0.1928 0.2226 -0.0010 0.0010  0.0343  125 SER   C O   
2016 C  CB  . SER   B 119 ? 0.1813 0.1923 0.2223 0.0014  0.0001  0.0265  125 SER   C CB  
2017 O  OG  . SER   B 119 ? 0.1880 0.2003 0.2388 0.0005  0.0025  0.0279  125 SER   C OG  
2018 N  N   . THR   B 120 ? 0.1543 0.1681 0.1870 0.0019  0.0004  0.0279  126 THR   C N   
2019 C  CA  . THR   B 120 ? 0.1638 0.1808 0.1996 0.0018  0.0027  0.0288  126 THR   C CA  
2020 C  C   . THR   B 120 ? 0.1756 0.1914 0.2016 0.0032  0.0027  0.0285  126 THR   C C   
2021 O  O   . THR   B 120 ? 0.1784 0.1910 0.1962 0.0046  0.0010  0.0266  126 THR   C O   
2022 C  CB  . THR   B 120 ? 0.1628 0.1835 0.2067 0.0023  0.0044  0.0253  126 THR   C CB  
2023 O  OG1 . THR   B 120 ? 0.1741 0.1955 0.2138 0.0045  0.0036  0.0213  126 THR   C OG1 
2024 C  CG2 . THR   B 120 ? 0.1773 0.1974 0.2285 0.0013  0.0046  0.0243  126 THR   C CG2 
2025 N  N   . GLY   B 121 ? 0.1916 0.2096 0.2186 0.0029  0.0052  0.0304  127 GLY   C N   
2026 C  CA  . GLY   B 121 ? 0.2241 0.2408 0.2420 0.0046  0.0066  0.0299  127 GLY   C CA  
2027 C  C   . GLY   B 121 ? 0.2781 0.2991 0.3007 0.0046  0.0105  0.0315  127 GLY   C C   
2028 O  O   . GLY   B 121 ? 0.2824 0.3065 0.3141 0.0026  0.0115  0.0338  127 GLY   C O   
2029 N  N   . GLY   B 122 ? 0.3084 0.3289 0.3241 0.0066  0.0129  0.0310  128 GLY   C N   
2030 C  CA  . GLY   B 122 ? 0.3239 0.3487 0.3435 0.0068  0.0175  0.0328  128 GLY   C CA  
2031 C  C   . GLY   B 122 ? 0.3275 0.3573 0.3520 0.0100  0.0201  0.0297  128 GLY   C C   
2032 O  O   . GLY   B 122 ? 0.3300 0.3609 0.3575 0.0114  0.0179  0.0263  128 GLY   C O   
2033 N  N   . ASN   B 123 ? 0.3241 0.3573 0.3498 0.0110  0.0249  0.0312  129 ASN   C N   
2034 C  CA  . ASN   B 123 ? 0.3208 0.3599 0.3527 0.0143  0.0279  0.0291  129 ASN   C CA  
2035 C  C   . ASN   B 123 ? 0.2987 0.3345 0.3232 0.0181  0.0266  0.0255  129 ASN   C C   
2036 O  O   . ASN   B 123 ? 0.2996 0.3406 0.3315 0.0207  0.0270  0.0235  129 ASN   C O   
2037 C  CB  . ASN   B 123 ? 0.3602 0.4073 0.4084 0.0129  0.0270  0.0285  129 ASN   C CB  
2038 C  CG  . ASN   B 123 ? 0.4498 0.5035 0.5077 0.0115  0.0314  0.0316  129 ASN   C CG  
2039 O  OD1 . ASN   B 123 ? 0.4763 0.5287 0.5291 0.0112  0.0353  0.0349  129 ASN   C OD1 
2040 N  ND2 . ASN   B 123 ? 0.4657 0.5266 0.5378 0.0103  0.0308  0.0310  129 ASN   C ND2 
2041 N  N   . GLY   B 124 ? 0.2845 0.3114 0.2947 0.0184  0.0249  0.0250  130 GLY   C N   
2042 C  CA  . GLY   B 124 ? 0.2716 0.2939 0.2738 0.0220  0.0238  0.0217  130 GLY   C CA  
2043 C  C   . GLY   B 124 ? 0.2482 0.2705 0.2539 0.0218  0.0186  0.0192  130 GLY   C C   
2044 O  O   . GLY   B 124 ? 0.2453 0.2649 0.2468 0.0249  0.0175  0.0166  130 GLY   C O   
2045 N  N   . LEU   B 125 ? 0.2203 0.2447 0.2330 0.0183  0.0157  0.0200  131 LEU   C N   
2046 C  CA  . LEU   B 125 ? 0.2128 0.2369 0.2282 0.0179  0.0114  0.0176  131 LEU   C CA  
2047 C  C   . LEU   B 125 ? 0.2103 0.2288 0.2205 0.0149  0.0082  0.0189  131 LEU   C C   
2048 O  O   . LEU   B 125 ? 0.2392 0.2564 0.2481 0.0124  0.0089  0.0220  131 LEU   C O   
2049 C  CB  . LEU   B 125 ? 0.2286 0.2603 0.2580 0.0165  0.0110  0.0171  131 LEU   C CB  
2050 C  CG  . LEU   B 125 ? 0.2701 0.3091 0.3078 0.0189  0.0134  0.0164  131 LEU   C CG  
2051 C  CD1 . LEU   B 125 ? 0.2992 0.3450 0.3503 0.0163  0.0125  0.0162  131 LEU   C CD1 
2052 C  CD2 . LEU   B 125 ? 0.2804 0.3187 0.3149 0.0226  0.0119  0.0139  131 LEU   C CD2 
2053 N  N   . VAL   B 126 ? 0.1775 0.1928 0.1849 0.0151  0.0048  0.0169  132 VAL   C N   
2054 C  CA  . VAL   B 126 ? 0.1770 0.1884 0.1820 0.0124  0.0019  0.0183  132 VAL   C CA  
2055 C  C   . VAL   B 126 ? 0.1614 0.1754 0.1737 0.0119  0.0003  0.0163  132 VAL   C C   
2056 O  O   . VAL   B 126 ? 0.1595 0.1747 0.1723 0.0140  -0.0006 0.0134  132 VAL   C O   
2057 C  CB  . VAL   B 126 ? 0.1908 0.1946 0.1834 0.0128  -0.0004 0.0182  132 VAL   C CB  
2058 C  CG1 . VAL   B 126 ? 0.2192 0.2210 0.2076 0.0161  -0.0012 0.0149  132 VAL   C CG1 
2059 C  CG2 . VAL   B 126 ? 0.1952 0.1963 0.1876 0.0099  -0.0035 0.0200  132 VAL   C CG2 
2060 N  N   . GLY   B 127 ? 0.1591 0.1738 0.1772 0.0092  0.0000  0.0178  133 GLY   C N   
2061 C  CA  . GLY   B 127 ? 0.1584 0.1742 0.1822 0.0086  -0.0009 0.0157  133 GLY   C CA  
2062 C  C   . GLY   B 127 ? 0.1709 0.1825 0.1914 0.0075  -0.0026 0.0166  133 GLY   C C   
2063 O  O   . GLY   B 127 ? 0.1773 0.1871 0.1968 0.0059  -0.0028 0.0201  133 GLY   C O   
2064 N  N   . PHE   B 128 ? 0.1585 0.1687 0.1774 0.0083  -0.0039 0.0139  134 PHE   C N   
2065 C  CA  . PHE   B 128 ? 0.1568 0.1634 0.1729 0.0074  -0.0050 0.0147  134 PHE   C CA  
2066 C  C   . PHE   B 128 ? 0.1641 0.1713 0.1863 0.0066  -0.0037 0.0131  134 PHE   C C   
2067 O  O   . PHE   B 128 ? 0.1656 0.1742 0.1892 0.0072  -0.0037 0.0097  134 PHE   C O   
2068 C  CB  . PHE   B 128 ? 0.1556 0.1588 0.1630 0.0091  -0.0072 0.0129  134 PHE   C CB  
2069 C  CG  . PHE   B 128 ? 0.1657 0.1669 0.1660 0.0105  -0.0082 0.0135  134 PHE   C CG  
2070 C  CD1 . PHE   B 128 ? 0.1647 0.1619 0.1593 0.0092  -0.0094 0.0163  134 PHE   C CD1 
2071 C  CD2 . PHE   B 128 ? 0.1783 0.1811 0.1774 0.0130  -0.0079 0.0112  134 PHE   C CD2 
2072 C  CE1 . PHE   B 128 ? 0.1807 0.1744 0.1671 0.0103  -0.0100 0.0163  134 PHE   C CE1 
2073 C  CE2 . PHE   B 128 ? 0.1896 0.1896 0.1817 0.0148  -0.0080 0.0114  134 PHE   C CE2 
2074 C  CZ  . PHE   B 128 ? 0.1834 0.1782 0.1683 0.0134  -0.0089 0.0137  134 PHE   C CZ  
2075 N  N   . ALA   B 129 ? 0.1561 0.1620 0.1814 0.0052  -0.0027 0.0156  135 ALA   C N   
2076 C  CA  . ALA   B 129 ? 0.1605 0.1656 0.1903 0.0048  -0.0007 0.0140  135 ALA   C CA  
2077 C  C   . ALA   B 129 ? 0.1632 0.1651 0.1860 0.0057  -0.0016 0.0121  135 ALA   C C   
2078 O  O   . ALA   B 129 ? 0.1581 0.1583 0.1774 0.0054  -0.0026 0.0147  135 ALA   C O   
2079 C  CB  . ALA   B 129 ? 0.1610 0.1660 0.1977 0.0036  0.0013  0.0180  135 ALA   C CB  
2080 N  N   . ASP   B 130 ? 0.1680 0.1692 0.1885 0.0063  -0.0017 0.0079  136 ASP   C N   
2081 C  CA  . ASP   B 130 ? 0.1706 0.1686 0.1836 0.0070  -0.0026 0.0062  136 ASP   C CA  
2082 C  C   . ASP   B 130 ? 0.1824 0.1778 0.1968 0.0064  0.0004  0.0075  136 ASP   C C   
2083 O  O   . ASP   B 130 ? 0.1896 0.1851 0.2108 0.0058  0.0035  0.0076  136 ASP   C O   
2084 C  CB  . ASP   B 130 ? 0.1723 0.1702 0.1826 0.0074  -0.0037 0.0016  136 ASP   C CB  
2085 C  CG  . ASP   B 130 ? 0.2273 0.2217 0.2287 0.0081  -0.0051 0.0000  136 ASP   C CG  
2086 O  OD1 . ASP   B 130 ? 0.2431 0.2365 0.2394 0.0091  -0.0069 0.0017  136 ASP   C OD1 
2087 O  OD2 . ASP   B 130 ? 0.2543 0.2463 0.2533 0.0076  -0.0041 -0.0029 136 ASP   C OD2 
2088 N  N   . VAL   B 131 ? 0.1735 0.1664 0.1821 0.0067  -0.0001 0.0086  137 VAL   C N   
2089 C  CA  . VAL   B 131 ? 0.1730 0.1638 0.1828 0.0064  0.0033  0.0097  137 VAL   C CA  
2090 C  C   . VAL   B 131 ? 0.1865 0.1735 0.1871 0.0070  0.0033  0.0070  137 VAL   C C   
2091 O  O   . VAL   B 131 ? 0.2004 0.1852 0.2004 0.0069  0.0066  0.0078  137 VAL   C O   
2092 C  CB  . VAL   B 131 ? 0.1853 0.1771 0.1990 0.0055  0.0036  0.0152  137 VAL   C CB  
2093 C  CG1 . VAL   B 131 ? 0.1903 0.1854 0.2129 0.0047  0.0036  0.0183  137 VAL   C CG1 
2094 C  CG2 . VAL   B 131 ? 0.1868 0.1773 0.1931 0.0053  -0.0004 0.0166  137 VAL   C CG2 
2095 N  N   . ARG   B 132 ? 0.1819 0.1684 0.1754 0.0077  -0.0004 0.0043  138 ARG   C N   
2096 C  CA  . ARG   B 132 ? 0.1823 0.1651 0.1662 0.0082  -0.0012 0.0026  138 ARG   C CA  
2097 C  C   . ARG   B 132 ? 0.2124 0.1921 0.1933 0.0078  0.0019  -0.0009 138 ARG   C C   
2098 O  O   . ARG   B 132 ? 0.2310 0.2070 0.2038 0.0080  0.0025  -0.0014 138 ARG   C O   
2099 C  CB  . ARG   B 132 ? 0.1831 0.1664 0.1613 0.0093  -0.0060 0.0010  138 ARG   C CB  
2100 C  CG  . ARG   B 132 ? 0.1755 0.1596 0.1538 0.0098  -0.0085 0.0041  138 ARG   C CG  
2101 C  CD  . ARG   B 132 ? 0.1877 0.1724 0.1616 0.0116  -0.0124 0.0023  138 ARG   C CD  
2102 N  NE  . ARG   B 132 ? 0.1946 0.1836 0.1744 0.0119  -0.0129 0.0003  138 ARG   C NE  
2103 C  CZ  . ARG   B 132 ? 0.2203 0.2115 0.1997 0.0135  -0.0157 -0.0008 138 ARG   C CZ  
2104 N  NH1 . ARG   B 132 ? 0.2069 0.1959 0.1797 0.0153  -0.0185 -0.0005 138 ARG   C NH1 
2105 N  NH2 . ARG   B 132 ? 0.2006 0.1965 0.1868 0.0135  -0.0157 -0.0020 138 ARG   C NH2 
2106 N  N   . ASP   B 133 ? 0.2016 0.1820 0.1879 0.0073  0.0036  -0.0032 139 ASP   C N   
2107 C  CA  . ASP   B 133 ? 0.2123 0.1883 0.1949 0.0067  0.0067  -0.0071 139 ASP   C CA  
2108 C  C   . ASP   B 133 ? 0.2209 0.1943 0.2069 0.0070  0.0132  -0.0054 139 ASP   C C   
2109 O  O   . ASP   B 133 ? 0.2348 0.2033 0.2163 0.0068  0.0169  -0.0085 139 ASP   C O   
2110 C  CB  . ASP   B 133 ? 0.2288 0.2057 0.2159 0.0057  0.0059  -0.0105 139 ASP   C CB  
2111 C  CG  . ASP   B 133 ? 0.2584 0.2381 0.2574 0.0055  0.0086  -0.0081 139 ASP   C CG  
2112 O  OD1 . ASP   B 133 ? 0.2305 0.2142 0.2346 0.0060  0.0077  -0.0039 139 ASP   C OD1 
2113 O  OD2 . ASP   B 133 ? 0.2970 0.2741 0.2997 0.0047  0.0117  -0.0105 139 ASP   C OD2 
2114 N  N   . LEU   B 134 ? 0.1994 0.1762 0.1936 0.0073  0.0146  -0.0004 140 LEU   C N   
2115 C  CA  . LEU   B 134 ? 0.1977 0.1736 0.1983 0.0078  0.0208  0.0023  140 LEU   C CA  
2116 C  C   . LEU   B 134 ? 0.2093 0.1832 0.2039 0.0081  0.0227  0.0042  140 LEU   C C   
2117 O  O   . LEU   B 134 ? 0.2142 0.1911 0.2128 0.0079  0.0220  0.0092  140 LEU   C O   
2118 C  CB  . LEU   B 134 ? 0.1887 0.1698 0.2016 0.0076  0.0205  0.0074  140 LEU   C CB  
2119 C  CG  . LEU   B 134 ? 0.2087 0.1920 0.2278 0.0071  0.0187  0.0063  140 LEU   C CG  
2120 C  CD1 . LEU   B 134 ? 0.2145 0.2025 0.2440 0.0068  0.0181  0.0119  140 LEU   C CD1 
2121 C  CD2 . LEU   B 134 ? 0.2247 0.2042 0.2459 0.0074  0.0231  0.0024  140 LEU   C CD2 
2122 N  N   . LEU   B 135 ? 0.2171 0.1856 0.2009 0.0083  0.0245  0.0003  141 LEU   C N   
2123 C  CA  . LEU   B 135 ? 0.2349 0.2010 0.2109 0.0085  0.0259  0.0020  141 LEU   C CA  
2124 C  C   . LEU   B 135 ? 0.2475 0.2146 0.2309 0.0091  0.0323  0.0065  141 LEU   C C   
2125 O  O   . LEU   B 135 ? 0.2541 0.2219 0.2356 0.0088  0.0325  0.0102  141 LEU   C O   
2126 C  CB  . LEU   B 135 ? 0.2462 0.2060 0.2079 0.0084  0.0263  -0.0029 141 LEU   C CB  
2127 C  CG  . LEU   B 135 ? 0.2708 0.2301 0.2261 0.0076  0.0197  -0.0072 141 LEU   C CG  
2128 C  CD1 . LEU   B 135 ? 0.2770 0.2299 0.2175 0.0071  0.0195  -0.0115 141 LEU   C CD1 
2129 C  CD2 . LEU   B 135 ? 0.2686 0.2324 0.2249 0.0077  0.0131  -0.0046 141 LEU   C CD2 
2130 N  N   . TRP   B 136 ? 0.2435 0.2109 0.2362 0.0100  0.0375  0.0064  142 TRP   C N   
2131 C  CA  . TRP   B 136 ? 0.2475 0.2166 0.2497 0.0111  0.0442  0.0111  142 TRP   C CA  
2132 C  C   . TRP   B 136 ? 0.2475 0.2237 0.2605 0.0102  0.0412  0.0182  142 TRP   C C   
2133 O  O   . TRP   B 136 ? 0.2687 0.2473 0.2890 0.0106  0.0456  0.0231  142 TRP   C O   
2134 C  CB  . TRP   B 136 ? 0.2487 0.2159 0.2588 0.0126  0.0502  0.0094  142 TRP   C CB  
2135 C  CG  . TRP   B 136 ? 0.2423 0.2124 0.2603 0.0121  0.0463  0.0089  142 TRP   C CG  
2136 C  CD1 . TRP   B 136 ? 0.2647 0.2317 0.2778 0.0114  0.0436  0.0034  142 TRP   C CD1 
2137 C  CD2 . TRP   B 136 ? 0.2428 0.2194 0.2751 0.0120  0.0448  0.0146  142 TRP   C CD2 
2138 N  NE1 . TRP   B 136 ? 0.2651 0.2364 0.2889 0.0110  0.0410  0.0054  142 TRP   C NE1 
2139 C  CE2 . TRP   B 136 ? 0.2539 0.2309 0.2889 0.0114  0.0416  0.0122  142 TRP   C CE2 
2140 C  CE3 . TRP   B 136 ? 0.2419 0.2243 0.2851 0.0120  0.0455  0.0218  142 TRP   C CE3 
2141 C  CZ2 . TRP   B 136 ? 0.2541 0.2364 0.3012 0.0110  0.0395  0.0167  142 TRP   C CZ2 
2142 C  CZ3 . TRP   B 136 ? 0.2479 0.2356 0.3032 0.0114  0.0429  0.0262  142 TRP   C CZ3 
2143 C  CH2 . TRP   B 136 ? 0.2491 0.2365 0.3057 0.0110  0.0400  0.0236  142 TRP   C CH2 
2144 N  N   . LEU   B 137 ? 0.2332 0.2125 0.2466 0.0088  0.0338  0.0190  143 LEU   C N   
2145 C  CA  . LEU   B 137 ? 0.2386 0.2232 0.2597 0.0074  0.0303  0.0253  143 LEU   C CA  
2146 C  C   . LEU   B 137 ? 0.2722 0.2562 0.2880 0.0063  0.0298  0.0283  143 LEU   C C   
2147 O  O   . LEU   B 137 ? 0.2894 0.2773 0.3128 0.0049  0.0287  0.0342  143 LEU   C O   
2148 C  CB  . LEU   B 137 ? 0.2372 0.2236 0.2570 0.0062  0.0230  0.0248  143 LEU   C CB  
2149 C  CG  . LEU   B 137 ? 0.2511 0.2397 0.2787 0.0065  0.0227  0.0239  143 LEU   C CG  
2150 C  CD1 . LEU   B 137 ? 0.2559 0.2455 0.2795 0.0056  0.0162  0.0227  143 LEU   C CD1 
2151 C  CD2 . LEU   B 137 ? 0.2576 0.2508 0.2994 0.0062  0.0246  0.0301  143 LEU   C CD2 
2152 N  N   . ASP   B 138 ? 0.2822 0.2611 0.2849 0.0068  0.0303  0.0245  144 ASP   C N   
2153 C  CA  . ASP   B 138 ? 0.3000 0.2772 0.2961 0.0058  0.0299  0.0271  144 ASP   C CA  
2154 C  C   . ASP   B 138 ? 0.3408 0.3181 0.3405 0.0063  0.0376  0.0302  144 ASP   C C   
2155 O  O   . ASP   B 138 ? 0.3457 0.3217 0.3404 0.0053  0.0377  0.0328  144 ASP   C O   
2156 C  CB  . ASP   B 138 ? 0.3050 0.2767 0.2853 0.0061  0.0270  0.0222  144 ASP   C CB  
2157 C  CG  . ASP   B 138 ? 0.3232 0.2950 0.2994 0.0058  0.0193  0.0200  144 ASP   C CG  
2158 O  OD1 . ASP   B 138 ? 0.3151 0.2906 0.2989 0.0050  0.0160  0.0224  144 ASP   C OD1 
2159 O  OD2 . ASP   B 138 ? 0.3263 0.2944 0.2915 0.0064  0.0167  0.0159  144 ASP   C OD2 
2160 N  N   . GLU   B 139 ? 0.3684 0.3465 0.3761 0.0081  0.0444  0.0299  145 GLU   C N   
2161 C  CA  . GLU   B 139 ? 0.4253 0.4035 0.4369 0.0091  0.0529  0.0329  145 GLU   C CA  
2162 C  C   . GLU   B 139 ? 0.4547 0.4373 0.4830 0.0108  0.0589  0.0362  145 GLU   C C   
2163 O  O   . GLU   B 139 ? 0.4493 0.4346 0.4855 0.0109  0.0561  0.0360  145 GLU   C O   
2164 C  CB  . GLU   B 139 ? 0.4992 0.4696 0.4959 0.0105  0.0579  0.0272  145 GLU   C CB  
2165 C  CG  . GLU   B 139 ? 0.6122 0.5783 0.6066 0.0123  0.0608  0.0209  145 GLU   C CG  
2166 C  CD  . GLU   B 139 ? 0.7632 0.7245 0.7437 0.0116  0.0547  0.0143  145 GLU   C CD  
2167 O  OE1 . GLU   B 139 ? 0.7983 0.7543 0.7731 0.0125  0.0573  0.0086  145 GLU   C OE1 
2168 O  OE2 . GLU   B 139 ? 0.8094 0.7721 0.7850 0.0100  0.0471  0.0150  145 GLU   C OE2 
2169 N  N   . GLU   B 140 ? 0.4853 0.4686 0.5191 0.0122  0.0676  0.0394  146 GLU   C N   
2170 C  CA  . GLU   B 140 ? 0.5054 0.4920 0.5546 0.0148  0.0753  0.0424  146 GLU   C CA  
2171 C  C   . GLU   B 140 ? 0.5194 0.5134 0.5850 0.0140  0.0706  0.0472  146 GLU   C C   
2172 O  O   . GLU   B 140 ? 0.5307 0.5308 0.6127 0.0149  0.0747  0.0535  146 GLU   C O   
2173 C  CB  . GLU   B 140 ? 0.5474 0.5261 0.5893 0.0178  0.0822  0.0351  146 GLU   C CB  
2174 C  CG  . GLU   B 140 ? 0.6267 0.6059 0.6799 0.0198  0.0844  0.0342  146 GLU   C CG  
2175 C  CD  . GLU   B 140 ? 0.7155 0.6992 0.7867 0.0226  0.0929  0.0399  146 GLU   C CD  
2176 O  OE1 . GLU   B 140 ? 0.7482 0.7335 0.8309 0.0241  0.0936  0.0406  146 GLU   C OE1 
2177 O  OE2 . GLU   B 140 ? 0.7358 0.7218 0.8106 0.0234  0.0989  0.0442  146 GLU   C OE2 
2178 N  N1  . A1BON C .   ? 0.2673 0.2415 0.2967 0.0234  0.0199  -0.0176 201 A1BON A N1  
2179 C  C4  . A1BON C .   ? 0.2708 0.2378 0.2948 0.0211  0.0212  -0.0234 201 A1BON A C4  
2180 C  C5  . A1BON C .   ? 0.2728 0.2530 0.2988 0.0226  0.0208  -0.0177 201 A1BON A C5  
2181 C  C6  . A1BON C .   ? 0.3038 0.2829 0.3189 0.0191  0.0229  -0.0235 201 A1BON A C6  
2182 C  C7  . A1BON C .   ? 0.3287 0.3145 0.3407 0.0180  0.0238  -0.0227 201 A1BON A C7  
2183 C  C8  . A1BON C .   ? 0.3440 0.3324 0.3592 0.0187  0.0296  -0.0264 201 A1BON A C8  
2184 C  C10 . A1BON C .   ? 0.4242 0.4219 0.4380 0.0168  0.0379  -0.0312 201 A1BON A C10 
2185 C  C13 . A1BON C .   ? 0.3423 0.3315 0.3479 0.0158  0.0194  -0.0187 201 A1BON A C13 
2186 CL CL  . A1BON C .   ? 0.3709 0.3576 0.3736 0.0150  0.0133  -0.0148 201 A1BON A CL  
2187 C  C12 . A1BON C .   ? 0.3457 0.3402 0.3478 0.0141  0.0203  -0.0181 201 A1BON A C12 
2188 C  C11 . A1BON C .   ? 0.3575 0.3550 0.3622 0.0144  0.0258  -0.0214 201 A1BON A C11 
2189 C  C9  . A1BON C .   ? 0.3736 0.3682 0.3849 0.0168  0.0308  -0.0260 201 A1BON A C9  
2190 F  F2  . A1BON C .   ? 0.4454 0.4376 0.4548 0.0151  0.0418  -0.0381 201 A1BON A F2  
2191 F  F1  . A1BON C .   ? 0.4475 0.4501 0.4534 0.0132  0.0382  -0.0311 201 A1BON A F1  
2192 F  F   . A1BON C .   ? 0.4254 0.4266 0.4537 0.0215  0.0412  -0.0299 201 A1BON A F   
2193 O  O1  . A1BON C .   ? 0.2551 0.2415 0.2860 0.0240  0.0197  -0.0129 201 A1BON A O1  
2194 C  C3  . A1BON C .   ? 0.2612 0.2265 0.2801 0.0187  0.0160  -0.0209 201 A1BON A C3  
2195 C  C2  . A1BON C .   ? 0.2545 0.2201 0.2820 0.0210  0.0135  -0.0146 201 A1BON A C2  
2196 C  C14 . A1BON C .   ? 0.2517 0.2270 0.2898 0.0255  0.0169  -0.0110 201 A1BON A C14 
2197 C  C1  . A1BON C .   ? 0.2431 0.2163 0.2749 0.0228  0.0122  -0.0090 201 A1BON A C1  
2198 C  C   . A1BON C .   ? 0.2369 0.2118 0.2757 0.0238  0.0091  -0.0021 201 A1BON A C   
2199 O  O   . A1BON C .   ? 0.2360 0.2084 0.2848 0.0264  0.0103  0.0002  201 A1BON A O   
2200 N  N   . A1BON C .   ? 0.2277 0.2071 0.2616 0.0215  0.0052  0.0014  201 A1BON A N   
# 
