data_7I79
# 
_entry.id   7I79 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I79         pdb_00007i79 10.2210/pdb7i79/pdb 
WWPDB D_1001408404 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I79 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-{[4-(methylsulfanyl)pyridin-3-yl]sulfamoyl}piperidine-3-carboxamide' 330.426   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    214 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-{[4-(methylsulfanyl)pyridin-3-yl]sulfamoyl}piperidine-3-carboxamide' A1B5X 
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 
A1B5X non-polymer         . '(3S)-1-{[4-(methylsulfanyl)pyridin-3-yl]sulfamoyl}piperidine-3-carboxamide' ? 'C12 H18 N4 O3 S2' 
330.426 
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 140 146 146 GLU GLU 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        A1B5X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B5X 
_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 A1B5X 1   201 201 A1B5X 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   301 211 HOH   HOH A . 
G 5 HOH   2   302 103 HOH   HOH A . 
G 5 HOH   3   303 193 HOH   HOH A . 
G 5 HOH   4   304 161 HOH   HOH A . 
G 5 HOH   5   305 143 HOH   HOH A . 
G 5 HOH   6   306 101 HOH   HOH A . 
G 5 HOH   7   307 109 HOH   HOH A . 
G 5 HOH   8   308 106 HOH   HOH A . 
G 5 HOH   9   309 175 HOH   HOH A . 
G 5 HOH   10  310 189 HOH   HOH A . 
G 5 HOH   11  311 70  HOH   HOH A . 
G 5 HOH   12  312 87  HOH   HOH A . 
G 5 HOH   13  313 174 HOH   HOH A . 
G 5 HOH   14  314 113 HOH   HOH A . 
G 5 HOH   15  315 57  HOH   HOH A . 
G 5 HOH   16  316 97  HOH   HOH A . 
G 5 HOH   17  317 53  HOH   HOH A . 
G 5 HOH   18  318 19  HOH   HOH A . 
G 5 HOH   19  319 198 HOH   HOH A . 
G 5 HOH   20  320 132 HOH   HOH A . 
G 5 HOH   21  321 114 HOH   HOH A . 
G 5 HOH   22  322 13  HOH   HOH A . 
G 5 HOH   23  323 83  HOH   HOH A . 
G 5 HOH   24  324 17  HOH   HOH A . 
G 5 HOH   25  325 201 HOH   HOH A . 
G 5 HOH   26  326 124 HOH   HOH A . 
G 5 HOH   27  327 75  HOH   HOH A . 
G 5 HOH   28  328 43  HOH   HOH A . 
G 5 HOH   29  329 27  HOH   HOH A . 
G 5 HOH   30  330 29  HOH   HOH A . 
G 5 HOH   31  331 42  HOH   HOH A . 
G 5 HOH   32  332 22  HOH   HOH A . 
G 5 HOH   33  333 37  HOH   HOH A . 
G 5 HOH   34  334 34  HOH   HOH A . 
G 5 HOH   35  335 23  HOH   HOH A . 
G 5 HOH   36  336 71  HOH   HOH A . 
G 5 HOH   37  337 45  HOH   HOH A . 
G 5 HOH   38  338 55  HOH   HOH A . 
G 5 HOH   39  339 137 HOH   HOH A . 
G 5 HOH   40  340 49  HOH   HOH A . 
G 5 HOH   41  341 194 HOH   HOH A . 
G 5 HOH   42  342 171 HOH   HOH A . 
G 5 HOH   43  343 41  HOH   HOH A . 
G 5 HOH   44  344 31  HOH   HOH A . 
G 5 HOH   45  345 78  HOH   HOH A . 
G 5 HOH   46  346 32  HOH   HOH A . 
G 5 HOH   47  347 61  HOH   HOH A . 
G 5 HOH   48  348 3   HOH   HOH A . 
G 5 HOH   49  349 117 HOH   HOH A . 
G 5 HOH   50  350 162 HOH   HOH A . 
G 5 HOH   51  351 80  HOH   HOH A . 
G 5 HOH   52  352 5   HOH   HOH A . 
G 5 HOH   53  353 62  HOH   HOH A . 
G 5 HOH   54  354 38  HOH   HOH A . 
G 5 HOH   55  355 131 HOH   HOH A . 
G 5 HOH   56  356 108 HOH   HOH A . 
G 5 HOH   57  357 147 HOH   HOH A . 
G 5 HOH   58  358 125 HOH   HOH A . 
G 5 HOH   59  359 48  HOH   HOH A . 
G 5 HOH   60  360 169 HOH   HOH A . 
G 5 HOH   61  361 139 HOH   HOH A . 
G 5 HOH   62  362 95  HOH   HOH A . 
G 5 HOH   63  363 127 HOH   HOH A . 
G 5 HOH   64  364 12  HOH   HOH A . 
G 5 HOH   65  365 102 HOH   HOH A . 
G 5 HOH   66  366 185 HOH   HOH A . 
G 5 HOH   67  367 120 HOH   HOH A . 
G 5 HOH   68  368 188 HOH   HOH A . 
G 5 HOH   69  369 122 HOH   HOH A . 
G 5 HOH   70  370 7   HOH   HOH A . 
G 5 HOH   71  371 82  HOH   HOH A . 
G 5 HOH   72  372 186 HOH   HOH A . 
G 5 HOH   73  373 176 HOH   HOH A . 
G 5 HOH   74  374 133 HOH   HOH A . 
G 5 HOH   75  375 212 HOH   HOH A . 
G 5 HOH   76  376 46  HOH   HOH A . 
G 5 HOH   77  377 107 HOH   HOH A . 
G 5 HOH   78  378 112 HOH   HOH A . 
G 5 HOH   79  379 58  HOH   HOH A . 
G 5 HOH   80  380 21  HOH   HOH A . 
G 5 HOH   81  381 208 HOH   HOH A . 
G 5 HOH   82  382 121 HOH   HOH A . 
G 5 HOH   83  383 111 HOH   HOH A . 
G 5 HOH   84  384 199 HOH   HOH A . 
G 5 HOH   85  385 181 HOH   HOH A . 
G 5 HOH   86  386 9   HOH   HOH A . 
G 5 HOH   87  387 180 HOH   HOH A . 
G 5 HOH   88  388 204 HOH   HOH A . 
G 5 HOH   89  389 81  HOH   HOH A . 
G 5 HOH   90  390 100 HOH   HOH A . 
G 5 HOH   91  391 93  HOH   HOH A . 
G 5 HOH   92  392 136 HOH   HOH A . 
G 5 HOH   93  393 203 HOH   HOH A . 
G 5 HOH   94  394 159 HOH   HOH A . 
G 5 HOH   95  395 207 HOH   HOH A . 
G 5 HOH   96  396 67  HOH   HOH A . 
G 5 HOH   97  397 197 HOH   HOH A . 
G 5 HOH   98  398 179 HOH   HOH A . 
G 5 HOH   99  399 116 HOH   HOH A . 
G 5 HOH   100 400 205 HOH   HOH A . 
G 5 HOH   101 401 153 HOH   HOH A . 
G 5 HOH   102 402 151 HOH   HOH A . 
G 5 HOH   103 403 155 HOH   HOH A . 
G 5 HOH   104 404 173 HOH   HOH A . 
G 5 HOH   105 405 118 HOH   HOH A . 
G 5 HOH   106 406 146 HOH   HOH A . 
H 5 HOH   1   301 213 HOH   HOH C . 
H 5 HOH   2   302 215 HOH   HOH C . 
H 5 HOH   3   303 96  HOH   HOH C . 
H 5 HOH   4   304 20  HOH   HOH C . 
H 5 HOH   5   305 92  HOH   HOH C . 
H 5 HOH   6   306 202 HOH   HOH C . 
H 5 HOH   7   307 128 HOH   HOH C . 
H 5 HOH   8   308 6   HOH   HOH C . 
H 5 HOH   9   309 25  HOH   HOH C . 
H 5 HOH   10  310 59  HOH   HOH C . 
H 5 HOH   11  311 68  HOH   HOH C . 
H 5 HOH   12  312 69  HOH   HOH C . 
H 5 HOH   13  313 130 HOH   HOH C . 
H 5 HOH   14  314 183 HOH   HOH C . 
H 5 HOH   15  315 167 HOH   HOH C . 
H 5 HOH   16  316 8   HOH   HOH C . 
H 5 HOH   17  317 214 HOH   HOH C . 
H 5 HOH   18  318 86  HOH   HOH C . 
H 5 HOH   19  319 115 HOH   HOH C . 
H 5 HOH   20  320 2   HOH   HOH C . 
H 5 HOH   21  321 30  HOH   HOH C . 
H 5 HOH   22  322 73  HOH   HOH C . 
H 5 HOH   23  323 170 HOH   HOH C . 
H 5 HOH   24  324 184 HOH   HOH C . 
H 5 HOH   25  325 166 HOH   HOH C . 
H 5 HOH   26  326 16  HOH   HOH C . 
H 5 HOH   27  327 35  HOH   HOH C . 
H 5 HOH   28  328 26  HOH   HOH C . 
H 5 HOH   29  329 91  HOH   HOH C . 
H 5 HOH   30  330 52  HOH   HOH C . 
H 5 HOH   31  331 54  HOH   HOH C . 
H 5 HOH   32  332 88  HOH   HOH C . 
H 5 HOH   33  333 141 HOH   HOH C . 
H 5 HOH   34  334 119 HOH   HOH C . 
H 5 HOH   35  335 160 HOH   HOH C . 
H 5 HOH   36  336 187 HOH   HOH C . 
H 5 HOH   37  337 64  HOH   HOH C . 
H 5 HOH   38  338 145 HOH   HOH C . 
H 5 HOH   39  339 44  HOH   HOH C . 
H 5 HOH   40  340 191 HOH   HOH C . 
H 5 HOH   41  341 72  HOH   HOH C . 
H 5 HOH   42  342 144 HOH   HOH C . 
H 5 HOH   43  343 65  HOH   HOH C . 
H 5 HOH   44  344 66  HOH   HOH C . 
H 5 HOH   45  345 156 HOH   HOH C . 
H 5 HOH   46  346 60  HOH   HOH C . 
H 5 HOH   47  347 135 HOH   HOH C . 
H 5 HOH   48  348 76  HOH   HOH C . 
H 5 HOH   49  349 24  HOH   HOH C . 
H 5 HOH   50  350 158 HOH   HOH C . 
H 5 HOH   51  351 56  HOH   HOH C . 
H 5 HOH   52  352 84  HOH   HOH C . 
H 5 HOH   53  353 85  HOH   HOH C . 
H 5 HOH   54  354 77  HOH   HOH C . 
H 5 HOH   55  355 50  HOH   HOH C . 
H 5 HOH   56  356 178 HOH   HOH C . 
H 5 HOH   57  357 163 HOH   HOH C . 
H 5 HOH   58  358 129 HOH   HOH C . 
H 5 HOH   59  359 4   HOH   HOH C . 
H 5 HOH   60  360 150 HOH   HOH C . 
H 5 HOH   61  361 182 HOH   HOH C . 
H 5 HOH   62  362 74  HOH   HOH C . 
H 5 HOH   63  363 40  HOH   HOH C . 
H 5 HOH   64  364 157 HOH   HOH C . 
H 5 HOH   65  365 51  HOH   HOH C . 
H 5 HOH   66  366 190 HOH   HOH C . 
H 5 HOH   67  367 94  HOH   HOH C . 
H 5 HOH   68  368 142 HOH   HOH C . 
H 5 HOH   69  369 89  HOH   HOH C . 
H 5 HOH   70  370 15  HOH   HOH C . 
H 5 HOH   71  371 126 HOH   HOH C . 
H 5 HOH   72  372 18  HOH   HOH C . 
H 5 HOH   73  373 110 HOH   HOH C . 
H 5 HOH   74  374 164 HOH   HOH C . 
H 5 HOH   75  375 1   HOH   HOH C . 
H 5 HOH   76  376 63  HOH   HOH C . 
H 5 HOH   77  377 36  HOH   HOH C . 
H 5 HOH   78  378 177 HOH   HOH C . 
H 5 HOH   79  379 79  HOH   HOH C . 
H 5 HOH   80  380 168 HOH   HOH C . 
H 5 HOH   81  381 11  HOH   HOH C . 
H 5 HOH   82  382 149 HOH   HOH C . 
H 5 HOH   83  383 138 HOH   HOH C . 
H 5 HOH   84  384 152 HOH   HOH C . 
H 5 HOH   85  385 105 HOH   HOH C . 
H 5 HOH   86  386 14  HOH   HOH C . 
H 5 HOH   87  387 90  HOH   HOH C . 
H 5 HOH   88  388 10  HOH   HOH C . 
H 5 HOH   89  389 39  HOH   HOH C . 
H 5 HOH   90  390 134 HOH   HOH C . 
H 5 HOH   91  391 33  HOH   HOH C . 
H 5 HOH   92  392 28  HOH   HOH C . 
H 5 HOH   93  393 209 HOH   HOH C . 
H 5 HOH   94  394 98  HOH   HOH C . 
H 5 HOH   95  395 140 HOH   HOH C . 
H 5 HOH   96  396 195 HOH   HOH C . 
H 5 HOH   97  397 123 HOH   HOH C . 
H 5 HOH   98  398 154 HOH   HOH C . 
H 5 HOH   99  399 99  HOH   HOH C . 
H 5 HOH   100 400 206 HOH   HOH C . 
H 5 HOH   101 401 210 HOH   HOH C . 
H 5 HOH   102 402 104 HOH   HOH C . 
H 5 HOH   103 403 192 HOH   HOH C . 
H 5 HOH   104 404 200 HOH   HOH C . 
H 5 HOH   105 405 148 HOH   HOH C . 
H 5 HOH   106 406 196 HOH   HOH C . 
H 5 HOH   107 407 172 HOH   HOH C . 
H 5 HOH   108 408 165 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           7I79 
_cell.length_a           86.861 
_cell.length_b           57.344 
_cell.length_c           64.772 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.78 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I79 
_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          7I79 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.53 
_exptl_crystal.density_percent_sol   51.36 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-02-20 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92204 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I79 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             39.27 
_reflns.d_resolution_high            1.29 
_reflns.number_obs                   75400 
_reflns.percent_possible_obs         94.4 
_reflns.pdbx_Rmerge_I_obs            0.089 
_reflns.pdbx_netI_over_sigmaI        8.0 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.097 
_reflns.pdbx_Rpim_I_all              0.038 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     428700 
_reflns.pdbx_chi_squared             0.48 
_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                  1.29 
_reflns_shell.d_res_low                   1.31 
_reflns_shell.number_measured_all         6218 
_reflns_shell.number_unique_obs           2294 
_reflns_shell.Rmerge_I_obs                1.917 
_reflns_shell.pdbx_chi_squared            0.10 
_reflns_shell.pdbx_redundancy             2.7 
_reflns_shell.percent_possible_obs        57.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             2.415 
_reflns_shell.pdbx_Rpim_I_all             1.429 
_reflns_shell.pdbx_CC_half                0.339 
_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                                 7I79 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     72081 
_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                             18.80 
_refine.ls_d_res_high                            1.290 
_refine.ls_percent_reflns_obs                    90.4 
_refine.ls_R_factor_obs                          0.2242 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2237 
_refine.ls_R_factor_R_free                       0.2334 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.990 
_refine.ls_number_reflns_R_free                  3599 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.934 
_refine.correlation_coeff_Fo_to_Fc_free          0.941 
_refine.B_iso_mean                               23.76 
_refine.aniso_B[1][1]                            -1.77600 
_refine.aniso_B[2][2]                            -1.27860 
_refine.aniso_B[3][3]                            3.05460 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -4.92060 
_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             0.059 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.057 
_refine.pdbx_overall_SU_R_Blow_DPI               0.060 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.058 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I79 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_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        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         27 
_refine_hist.number_atoms_solvent             214 
_refine_hist.number_atoms_total               2407 
_refine_hist.d_res_high                       1.290 
_refine_hist.d_res_low                        18.80 
# 
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                  0.012 ? 2.00  2261 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.07  ? 2.00  3082 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  757  '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  401  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2261 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.64  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.03 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  279  '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  1883 '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                       1.29 
_refine_ls_shell.d_res_low                        1.32 
_refine_ls_shell.number_reflns_R_work             1363 
_refine_ls_shell.R_factor_R_work                  0.4728 
_refine_ls_shell.percent_reflns_obs               28.55 
_refine_ls_shell.R_factor_R_free                  0.4061 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.48 
_refine_ls_shell.number_reflns_R_free             79 
_refine_ls_shell.number_reflns_all                1442 
_refine_ls_shell.R_factor_all                     0.4692 
# 
_struct.entry_id                  7I79 
_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-0038123-001 (A71EV2A-x5182)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I79 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 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 7I79 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I79 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 ? ? ? ? ? ? ? 2.346 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.389 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.247 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
# 
_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_555 109.0 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.1 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.2 ? 
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_555 103.2 ? 
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_555 103.5 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 117.9 ? 
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_555 109.9 ? 
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_555 106.7 ? 
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_555 117.4 ? 
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_555 105.7 ? 
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_555 101.3 ? 
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_555 115.2 ? 
# 
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 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N 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                   7I79 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 CYS C 56  ? ? -171.55 -177.98 
2 1 SER C 105 ? ? -160.20 112.11  
# 
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 14.9599 8.2530   14.3667 0.0027  -0.0312 -0.0220 0.0095 0.0008 0.0020 1.3379 0.9608 0.6190 0.8632  
-0.3052 -0.2225 -0.0170 0.0385 0.0795 0.0156 0.0567 0.0218 -0.0270 -0.0433 -0.0397 
'X-RAY DIFFRACTION' 2 ? refined 25.8401 -20.2387 17.7547 -0.0071 -0.0289 -0.0023 0.0053 0.0061 0.0130 0.6607 1.0736 0.4446 -0.0562 
-0.1562 -0.1815 0.0326  0.0088 0.1187 0.0244 0.0530 0.0373 0.0132  0.0261  -0.0857 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 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 
A1B5X N1   N  N N 1   
A1B5X N3   N  N N 2   
A1B5X C4   C  Y N 3   
A1B5X C5   C  Y N 4   
A1B5X C6   C  N N 5   
A1B5X C7   C  N N 6   
A1B5X C8   C  N N 7   
A1B5X C10  C  N N 8   
A1B5X O2   O  N N 9   
A1B5X C9   C  N S 10  
A1B5X C11  C  N N 11  
A1B5X N2   N  N N 12  
A1B5X S1   S  N N 13  
A1B5X O    O  N N 14  
A1B5X O1   O  N N 15  
A1B5X C1   C  Y N 16  
A1B5X S    S  N N 17  
A1B5X C    C  N N 18  
A1B5X N    N  Y N 19  
A1B5X C3   C  Y N 20  
A1B5X C2   C  Y N 21  
A1B5X H7   H  N N 22  
A1B5X H15  H  N N 23  
A1B5X H14  H  N N 24  
A1B5X H6   H  N N 25  
A1B5X H8   H  N N 26  
A1B5X H9   H  N N 27  
A1B5X H10  H  N N 28  
A1B5X H11  H  N N 29  
A1B5X H12  H  N N 30  
A1B5X H13  H  N N 31  
A1B5X H    H  N N 32  
A1B5X H16  H  N N 33  
A1B5X H17  H  N N 34  
A1B5X H2   H  N N 35  
A1B5X H1   H  N N 36  
A1B5X H3   H  N N 37  
A1B5X H5   H  N N 38  
A1B5X H4   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 
A1B5X C   S    sing N N 1   
A1B5X S   C1   sing N N 2   
A1B5X C1  C2   doub Y N 3   
A1B5X C2  C3   sing Y N 4   
A1B5X C3  N    doub Y N 5   
A1B5X N   C4   sing Y N 6   
A1B5X C4  C5   doub Y N 7   
A1B5X C1  C5   sing Y N 8   
A1B5X C5  N1   sing N N 9   
A1B5X N1  S1   sing N N 10  
A1B5X O   S1   doub N N 11  
A1B5X O1  S1   doub N N 12  
A1B5X S1  N2   sing N N 13  
A1B5X N2  C6   sing N N 14  
A1B5X C6  C7   sing N N 15  
A1B5X C7  C8   sing N N 16  
A1B5X C8  C9   sing N N 17  
A1B5X C9  C10  sing N N 18  
A1B5X N3  C10  sing N N 19  
A1B5X C10 O2   doub N N 20  
A1B5X C11 C9   sing N N 21  
A1B5X N2  C11  sing N N 22  
A1B5X N1  H7   sing N N 23  
A1B5X N3  H15  sing N N 24  
A1B5X N3  H14  sing N N 25  
A1B5X C4  H6   sing N N 26  
A1B5X C6  H8   sing N N 27  
A1B5X C6  H9   sing N N 28  
A1B5X C7  H10  sing N N 29  
A1B5X C7  H11  sing N N 30  
A1B5X C8  H12  sing N N 31  
A1B5X C8  H13  sing N N 32  
A1B5X C9  H    sing N N 33  
A1B5X C11 H16  sing N N 34  
A1B5X C11 H17  sing N N 35  
A1B5X C   H2   sing N N 36  
A1B5X C   H1   sing N N 37  
A1B5X C   H3   sing N N 38  
A1B5X C3  H5   sing N N 39  
A1B5X C2  H4   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_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I79 
_atom_sites.fract_transf_matrix[1][1]   0.011513 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000963 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017439 
_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]   0.015493 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.520 8.263   24.745 1.00 20.37 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.800 8.306   24.011 1.00 21.63 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.961 7.101   23.106 1.00 21.37 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.248 6.101   23.272 1.00 22.51 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.975 8.396   24.987 1.00 25.06 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.147 7.182   25.698 1.00 27.62 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.875 7.188   22.140 1.00 20.23 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.132 6.051   21.254 1.00 18.97 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.596 6.504   19.880 1.00 18.59 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.290 7.617   19.462 1.00 19.72 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.304 5.639   19.167 1.00 17.39 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.812 5.997   17.839 1.00 17.87 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.814 4.774   16.944 1.00 17.44 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.709 3.640   17.419 1.00 17.56 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.254 6.504   17.987 1.00 18.38 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.899 5.012   15.616 1.00 16.27 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.104 3.937   14.636 1.00 16.36 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.578 4.016   14.261 1.00 17.16 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.070 5.130   13.960 1.00 17.01 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.257 4.145   13.356 1.00 16.37 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.746 4.263   13.675 1.00 17.37 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.498 2.991   12.367 1.00 18.42 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.940 4.817   12.467 1.00 16.73 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.301 2.873   14.243 1.00 17.42 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.711 2.888   13.848 1.00 18.43 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.824 2.043   12.552 1.00 18.58 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.794 0.819   12.612 1.00 18.36 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.562 2.289   14.976 1.00 19.85 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.607 3.181   16.200 1.00 19.40 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.473 4.271   16.265 1.00 20.08 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.752 2.967   17.275 1.00 20.43 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.506 5.108   17.377 1.00 21.25 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.768 3.816   18.392 1.00 21.00 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.631 4.897   18.423 1.00 21.99 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.652 5.764   19.514 1.00 22.48 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.928 2.687   11.390 1.00 18.90 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.993 2.021   10.104 1.00 19.94 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.240 2.524   9.407  1.00 21.23 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.447 3.745   9.311  1.00 20.00 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.705 2.276   9.256  1.00 21.09 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.355 3.777   9.150  1.00 21.63 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.853 1.678   7.856  1.00 22.67 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.117 1.605   8.985  1.00 22.70 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.358 2.032   8.337  1.00 22.07 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.176 2.933   9.247  1.00 21.68 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.292 2.626   10.446 1.00 21.80 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.625 4.089   8.718  1.00 20.87 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.316 5.076   9.539  1.00 21.41 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.410 6.255   9.849  1.00 20.34 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.873 7.405   9.960  1.00 21.21 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.630 5.549   8.923  1.00 23.63 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.708 4.496   9.026  1.00 27.80 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.487 4.430   9.987  1.00 29.06 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.735 3.606   8.071  1.00 29.16 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.122 5.961   10.102 1.00 18.63 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.165 7.006   10.440 1.00 18.84 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.456 6.692   11.748 1.00 18.10 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.218 5.504   12.081 1.00 18.40 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.072 7.121   9.350  1.00 18.55 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.576 7.504   7.979  1.00 19.59 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.205 8.719   7.759  1.00 21.08 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.332 6.697   6.886  1.00 21.64 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.670 9.075   6.494  1.00 22.10 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.790 7.043   5.617  1.00 22.78 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.412 8.254   5.417  1.00 23.89 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.850 8.600   4.146  1.00 27.46 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.100 7.757   12.470 1.00 17.56 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.308 7.687   13.697 1.00 17.05 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.080 8.553   13.447 1.00 16.79 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.233 9.759   13.138 1.00 17.62 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.132 8.197   14.917 1.00 17.59 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.298 8.568   16.165 1.00 18.38 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.213 8.923   17.360 1.00 19.47 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.642 10.011  18.188 1.00 19.62 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.971 9.810   19.316 1.00 23.71 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.753 8.571   19.757 1.00 23.97 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.498 10.846  20.008 1.00 22.35 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.864 7.929   13.478 1.00 16.28 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.611 8.676   13.232 1.00 15.97 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.917 8.876   14.566 1.00 16.21 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.624 7.895   15.260 1.00 16.55 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.663 7.886   12.308 1.00 17.54 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.454 8.747   11.895 1.00 18.58 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.392 7.354   11.079 1.00 19.10 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.676 10.141  14.942 1.00 15.06 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.025 10.488  16.209 0.50 15.42 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.053 10.462  16.218 0.50 17.24 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.893 11.466  15.998 1.00 16.80 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.762 12.093  14.912 1.00 17.31 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.005 11.144  17.227 0.50 13.91 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.191 11.060  17.117 0.50 19.63 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.920 10.127  17.875 0.50 15.74 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.711 11.507  18.488 0.50 21.15 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.741 12.372  16.654 0.50 11.52 ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.317 10.067  17.290 0.50 20.87 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.027 11.655  17.052 1.00 16.33 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.027 12.723  16.951 1.00 16.62 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.812 14.035  16.953 1.00 16.78 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.717 14.220  17.799 1.00 17.08 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.156 12.722  18.214 1.00 16.47 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.314 11.472  18.316 1.00 17.39 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.723 10.457  18.924 1.00 18.16 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.121 11.495  17.719 1.00 18.33 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.472 14.972  16.069 1.00 15.76 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.208 16.258  16.044 1.00 15.86 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.155 16.959  17.399 1.00 17.90 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.153 17.502  17.869 1.00 19.29 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.579 17.164  14.973 1.00 17.05 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.382 18.478  14.741 1.00 18.60 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.656 19.343  13.747 1.00 19.09 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.399 20.544  13.306 1.00 20.66 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.401 21.709  13.951 1.00 23.77 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.830 21.817  15.140 1.00 23.65 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.998 22.777  13.412 1.00 25.44 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.002 16.861  18.086 1.00 16.62 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.856 17.554  19.367 1.00 17.42 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.706 16.960  20.494 1.00 19.43 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.866 17.624  21.524 1.00 20.88 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.353 17.691  19.768 1.00 16.90 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.701 16.455  20.289 1.00 17.62 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.050 15.590  19.439 1.00 18.80 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.534 16.022  21.565 1.00 18.94 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.554 14.618  20.206 1.00 18.35 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.804 14.849  21.501 1.00 19.54 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.222 15.740  20.332 1.00 18.60 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.096 15.061  21.296 1.00 18.48 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.577 15.003  20.883 1.00 20.33 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.391 14.391  21.581 1.00 21.25 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.564 13.659  21.605 1.00 18.29 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.146 13.663  22.172 1.00 19.74 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.718 12.230  22.427 1.00 19.85 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.076 14.506  23.508 1.00 21.74 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.929 15.626  19.731 1.00 18.76 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.319 15.620  19.291 1.00 19.09 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.276 16.261  20.287 1.00 21.00 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.963 17.303  20.901 1.00 21.69 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.449 16.281  17.907 1.00 18.67 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.459 15.629  20.433 1.00 19.81 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.524 16.112  21.332 1.00 20.63 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.436 17.134  20.619 1.00 21.10 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.351 17.306  19.389 1.00 19.58 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.378 14.946  21.833 1.00 23.20 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.136 14.394  20.734 1.00 24.21 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.549 13.852  22.486 1.00 23.79 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.355 17.804  21.368 1.00 21.63 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.318 18.698  20.742 1.00 22.20 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.218 17.900  19.790 1.00 22.35 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.498 18.389  18.706 1.00 22.14 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.200 19.403  21.809 1.00 24.56 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.377 20.129  21.195 1.00 33.90 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.198 21.273  20.434 1.00 38.41 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.687 19.775  21.140 1.00 37.41 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.407 21.649  20.044 1.00 39.08 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.337 20.760  20.413 1.00 40.13 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.593 16.649  20.157 1.00 21.64 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.418 15.845  19.243 1.00 22.34 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.679 15.554  17.953 1.00 20.76 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.301 15.545  16.900 1.00 20.86 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.914 14.570  19.904 1.00 24.22 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.909 13.826  19.048 1.00 33.15 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.076 14.244  18.889 1.00 36.65 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.462 12.743  18.418 1.00 34.99 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.347 15.334  18.024 1.00 19.26 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.546 15.115  16.806 1.00 17.40 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.620 16.345  15.882 1.00 17.99 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.833 16.189  14.692 1.00 19.39 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.068 14.824  17.108 1.00 18.75 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.845 13.466  17.730 1.00 20.06 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.506 12.490  17.287 1.00 18.75 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.994 13.365  18.631 1.00 19.49 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.391 17.565  16.438 1.00 17.95 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.437 18.773  15.623 1.00 18.29 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.861 19.020  15.072 1.00 19.02 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.010 19.646  14.024 1.00 20.19 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.968 19.994  16.487 1.00 18.63 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.458 20.093  16.607 1.00 19.37 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.678 19.729  17.678 1.00 20.64 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.545 20.510  15.580 1.00 19.65 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.353 19.971  17.407 1.00 19.87 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.237 20.459  16.122 1.00 19.94 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.710 21.029  14.298 1.00 21.33 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.103 20.792  15.365 1.00 21.12 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.596 21.323  13.551 1.00 21.88 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.322 21.302  14.106 1.00 22.21 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.901 18.641  15.844 1.00 19.48 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.281 18.861  15.399 1.00 20.06 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.743 17.852  14.341 1.00 20.94 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.793 18.038  13.747 1.00 22.04 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.217 18.836  16.608 1.00 21.53 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.947 16.792  14.107 1.00 19.67 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.231 15.743  13.095 1.00 19.54 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.987 15.563  12.219 1.00 19.70 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.630 14.448  11.870 1.00 19.40 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.634 14.420  13.808 1.00 20.85 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.965 14.592  14.497 1.00 25.60 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.015 14.531  13.863 1.00 27.26 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.987 14.903  15.810 1.00 25.55 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.338 16.663  11.861 1.00 19.44 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.054 16.626  11.166 1.00 18.93 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.137 16.175  9.743  1.00 19.66 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 30.002 16.681  8.979  1.00 21.55 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.452 18.044  11.206 1.00 17.58 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.052 18.195  10.603 1.00 19.50 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.022 17.398  11.425 1.00 19.12 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.582 19.651  10.648 1.00 22.40 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.193 15.301  9.350  1.00 18.56 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.040 14.889  7.961  1.00 18.94 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.797 15.601  7.379  1.00 19.44 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.871 16.176  6.282  1.00 21.99 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.918 13.354  7.856  1.00 19.95 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.572 12.934  6.435  1.00 21.93 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.194 12.664  8.357  1.00 21.10 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.632 15.544  8.086  1.00 18.84 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.373 16.087  7.559  1.00 18.79 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.382 16.274  8.699  1.00 20.43 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.442 15.504  9.657  1.00 19.63 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.790 15.069  6.544  1.00 19.80 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.393 15.307  6.051  1.00 21.16 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 22.000 16.162  5.065  1.00 23.76 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.191 14.695  6.559  1.00 21.62 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.629 16.097  4.900  1.00 25.27 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.108 15.198  5.809  1.00 23.44 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.929 13.768  7.570  1.00 21.60 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.786 14.774  6.015  1.00 24.70 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.623 13.335  7.754  1.00 22.06 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.567 13.850  6.998  1.00 23.18 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.565 17.317  8.651  1.00 21.10 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.532 17.532  9.639  1.00 20.97 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.307 18.133  8.982  1.00 21.33 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.431 18.896  8.005  1.00 21.60 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.022 18.379  10.816 1.00 20.66 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.660 19.721  10.441 1.00 21.68 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.700 20.881  10.215 1.00 24.36 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.038 21.821  9.446  1.00 27.15 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.591 20.877  10.798 1.00 24.63 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.129 17.869  9.538  1.00 19.84 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.903 18.414  9.008  1.00 20.05 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.938 18.593  10.166 1.00 20.40 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.435 17.600  10.720 1.00 20.46 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.327 17.476  7.934  1.00 21.63 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.107 18.019  7.247  1.00 27.25 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.344 18.747  7.895  1.00 30.62 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.904 17.698  6.057  1.00 28.26 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.718 19.842  10.598 1.00 20.96 ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.830 20.120  11.723 0.50 20.67 ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.831 20.092  11.735 0.50 21.53 ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.384 19.704  11.420 1.00 21.31 ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.663 19.256  12.337 1.00 22.21 ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.922 21.602  12.095 0.50 21.36 ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.925 21.552  12.166 0.50 24.69 ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.920 21.994  13.014 0.50 22.19 ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.572 22.369  11.065 0.50 29.67 ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.943 19.825  10.131 1.00 20.21 ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.558 19.417  9.786  1.00 20.49 ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.319 17.918  9.968  1.00 20.52 ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.184 17.516  10.129 1.00 22.20 ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.169 19.809  8.361  1.00 23.54 ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.795 18.991  7.381  1.00 29.28 ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.375 17.109  9.988  1.00 18.50 ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.237 15.662  10.198 1.00 18.23 ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.674 15.214  11.614 1.00 17.02 ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.605 14.013  11.916 1.00 16.79 ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.127 14.926  9.169  1.00 18.78 ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.574 15.071  7.753  1.00 18.97 ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.469 14.395  6.702  1.00 18.66 ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.388 12.940  6.841  1.00 18.51 ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.568 12.079  5.845  1.00 21.91 ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.808 12.522  4.606  1.00 23.80 ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.458 10.759  6.064  1.00 19.32 ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.258 16.144  12.437 1.00 16.61 ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.885 15.825  13.729 1.00 16.79 ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.030 14.838  13.580 1.00 17.40 ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.214 13.964  14.450 1.00 16.53 ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.849 15.319  14.773 1.00 18.54 ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.437 15.099  16.142 1.00 18.06 ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.224 15.933  16.590 1.00 19.44 ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.058 14.100  16.803 1.00 17.79 ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.840 14.953  12.481 1.00 16.22 ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.925 14.011  12.295 1.00 14.93 ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.273 14.706  12.143 1.00 16.36 ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.348 15.821  11.595 1.00 17.57 ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.712 13.148  11.018 1.00 15.48 ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.619 12.049  11.072 1.00 16.67 ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.576 11.287  9.729  1.00 17.33 ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.899 11.051  12.194 1.00 17.78 ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.311 14.046  12.665 1.00 16.06 ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.700 14.475  12.521 1.00 15.93 ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.566 13.260  12.371 1.00 16.89 ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.356 12.230  13.045 1.00 16.99 ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.141 15.344  13.724 1.00 15.36 ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.589 15.949  13.631 1.00 16.33 ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.724 17.299  14.333 1.00 17.04 ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.642 15.016  14.258 1.00 17.26 ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.534 13.327  11.412 1.00 16.31 ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.466 12.216  11.171 1.00 16.26 ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.887 12.723  11.347 1.00 15.92 ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.236 13.779  10.797 1.00 16.79 ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.277 11.658  9.750  1.00 16.08 ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.323 10.581  9.459  1.00 18.36 ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.842 11.104  9.577  1.00 16.71 ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.688 12.055  12.170 1.00 16.57 ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.101 12.415  12.375 1.00 16.07 ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.016 11.267  11.907 1.00 17.46 ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.538 10.129  11.670 1.00 17.76 ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.393 12.792  13.824 1.00 16.93 ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.087 11.730  14.712 1.00 18.86 ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.341 11.548  11.752 1.00 19.34 ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.258 10.485  11.318 1.00 20.38 ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.893 9.756   12.521 1.00 22.38 ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.057 10.354  13.596 1.00 23.32 ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.333 11.076  10.422 1.00 23.09 ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.084 12.010  11.184 1.00 25.48 ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.261 8.463   12.343 1.00 23.15 ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.820 7.667   13.429 1.00 24.93 ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.154 7.066   13.029 1.00 26.89 ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.406 6.861   11.830 1.00 26.55 ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.872 6.503   13.820 1.00 26.24 ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.738 5.591   12.728 1.00 27.43 ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.516 6.980   14.242 1.00 25.99 ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.992 6.726   14.021 1.00 28.35 ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.272 6.106   13.736 1.00 30.84 ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.063 4.607   13.514 1.00 31.25 ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.585 4.053   12.544 1.00 32.71 ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.276 6.406   14.872 1.00 35.16 ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.830 5.764   16.063 1.00 39.14 ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.423 7.890   15.120 1.00 36.15 ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.271 3.963   14.380 1.00 31.13 ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.986 2.529   14.239 1.00 31.81 ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.781 2.269   13.336 1.00 30.99 ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.862 3.100   13.262 1.00 30.13 ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.711 1.921   15.606 1.00 33.63 ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.767 1.089   12.679 1.00 30.03 ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.665 0.695   11.809 1.00 30.20 ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.547 0.104   12.646 1.00 28.08 ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.811 -0.674  13.586 1.00 28.03 ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.140 -0.332  10.767 1.00 34.44 ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.808 0.317   9.553  1.00 39.70 ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.146 -0.713  8.501  1.00 44.70 ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.028 -1.553  8.689  1.00 44.41 ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.441 -0.679  7.375  1.00 46.56 ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.317 0.465   12.301 1.00 25.20 ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.107 0.030   12.988 1.00 24.02 ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.509 -1.219  12.405 1.00 23.26 ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.846 -1.617  11.284 1.00 24.06 ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.597 -1.852  13.196 1.00 22.17 ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 27.019 -3.142  12.800 1.00 23.04 ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.597 -3.120  12.351 1.00 23.13 ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 25.104 -4.173  11.944 1.00 24.11 ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.186 -4.176  13.910 1.00 24.65 ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.897 -4.588  14.259 1.00 28.79 ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.911 -1.968  12.431 1.00 19.58 ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.525 -1.904  12.002 1.00 19.28 ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.417 -1.843  10.470 1.00 20.99 ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.265 -1.258  9.811  1.00 23.02 ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.866 -0.650  12.599 1.00 18.24 ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.755 -0.700  14.124 1.00 21.88 ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.440 -1.808  14.664 1.00 21.83 ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.900 0.365   14.775 1.00 20.50 ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.386 -2.438  9.919  1.00 21.66 ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.082 -2.356  8.489  1.00 23.13 ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.798 -1.601  8.300  1.00 21.84 ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.850 -1.804  9.077  1.00 22.21 ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.900 -3.760  7.938  1.00 28.88 ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.201 -4.386  7.944  1.00 33.20 ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.310 -3.788  6.520  1.00 31.47 ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.735 -0.726  7.273  1.00 21.00 ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.495 0.006   7.028  1.00 19.78 ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.522 -0.774  6.153  1.00 20.31 ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.907 -1.303  5.088  1.00 20.25 ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.777 1.408   6.416  1.00 19.94 ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.857 2.177   7.191  1.00 21.38 ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.493 2.252   6.258  1.00 20.01 ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.492 2.477   8.683  1.00 21.25 ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.238 -0.798  6.550  1.00 18.91 ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.192 -1.419  5.749  1.00 18.84 ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.951 -0.613  4.480  1.00 20.58 ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.921 0.626   4.504  1.00 20.27 ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.884 -1.453  6.538  1.00 18.53 ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.738 -1.323  3.342  1.00 22.43 ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.428 -0.632  2.087  1.00 22.92 ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.151 -1.350  1.591  1.00 24.66 ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.191 -2.341  0.810  1.00 25.62 ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.628 -0.753  1.077  1.00 22.75 ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.944 -0.142  1.579  1.00 22.91 ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.897 1.365   1.822  1.00 21.85 ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.202 1.830   2.327  1.00 21.26 ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.397 3.005   2.930  1.00 23.05 ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.379 3.840   3.118  1.00 23.16 ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.609 3.339   3.385  1.00 24.41 ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 13.007 -0.851  2.043  1.00 24.52 ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.707 -1.550  1.884  1.00 25.47 ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.514 -0.629  2.126  1.00 25.98 ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.704 0.532   2.477  1.00 27.58 ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.680 -2.693  2.887  1.00 24.89 ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.598 -2.122  4.611  1.00 23.59 ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.247  -1.190  2.064  1.00 27.19 ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 8.100  -0.365  2.402  1.00 28.75 ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.270  -1.083  3.506  1.00 27.73 ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 6.061  -0.979  3.524  1.00 28.24 ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.202  -0.075  1.177  1.00 35.54 ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.582  -1.306  0.560  1.00 46.17 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.995  -2.438  0.933  1.00 48.54 ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.662  -1.147  -0.290 1.00 51.77 ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.943  -1.729  4.450  1.00 25.71 ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.270  -2.360  5.599  1.00 22.78 ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.524  -1.284  6.394  1.00 23.66 ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.978  -0.139  6.547  1.00 25.47 ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.290  -3.071  6.493  1.00 20.21 ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.956  -4.640  5.852  1.00 24.78 ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.371  -1.673  6.921  1.00 21.63 ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.565  -0.836  7.838  1.00 21.89 ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.303  -1.616  9.146  1.00 20.40 ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.408  -1.247  9.900  1.00 21.72 ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.206  -0.433  7.249  1.00 24.32 ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.262  0.685   6.252  1.00 30.38 ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.853  1.168   5.894  1.00 36.08 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.343  0.935   4.791  1.00 39.72 ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.163  1.862   6.806  1.00 32.03 ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 5.047  -2.718  9.377  1.00 18.50 ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 5.072  -3.425  10.633 1.00 18.57 ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.515  -3.642  11.061 1.00 18.04 ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.416  -3.885  10.216 1.00 19.69 ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.268  -4.717  10.649 1.00 21.55 ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.872  -5.642  9.756  1.00 26.97 ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.838  -4.509  10.236 1.00 20.94 ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.740  -3.547  12.354 1.00 16.13 ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.079  -3.763  12.879 1.00 15.77 ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.105  -3.832  14.377 1.00 15.40 ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.079  -4.031  14.990 1.00 17.67 ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.270  -3.634  14.974 1.00 15.52 ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.468  -3.707  16.411 1.00 15.67 ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.339 -2.511  16.841 1.00 15.38 ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.331 -2.185  16.162 1.00 16.29 ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.172 -5.050  16.757 1.00 17.13 ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.560 -5.108  18.217 1.00 20.45 ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.266  -6.245  16.400 1.00 17.73 ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.924  -1.801  17.916 1.00 13.86 ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.772 -0.706  18.411 1.00 13.54 ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.229 -0.935  19.853 1.00 15.04 ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.513 -1.571  20.615 1.00 15.94 ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.079 0.698   18.282 1.00 14.37 ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.055  1.050   19.351 1.00 14.60 ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.793  0.475   19.343 1.00 16.39 ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.366  1.942   20.368 1.00 16.13 ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.851  0.802   20.308 1.00 17.26 ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.414  2.309   21.311 1.00 16.78 ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.180  1.704   21.291 1.00 16.49 ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.233  1.959   22.256 1.00 18.83 ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.350 -0.331  20.220 1.00 15.34 ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.840 -0.363  21.607 1.00 14.04 ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.332 0.846   22.393 1.00 15.12 ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.602 1.997   22.006 1.00 15.44 ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.390 -0.398  21.672 1.00 14.58 ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.858 -0.532  23.089 1.00 16.64 ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.501 -1.631  23.846 1.00 17.51 ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.572 0.490   23.708 1.00 17.05 ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.895 -1.740  25.173 1.00 18.43 ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.983 0.390   25.031 1.00 16.41 ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.646 -0.734  25.754 1.00 18.43 ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.041 -0.890  27.079 1.00 20.61 ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.695 0.559   23.537 1.00 14.56 ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.174 1.557   24.482 1.00 15.28 ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.021 1.532   25.780 1.00 16.84 ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.837 0.650   26.644 1.00 17.53 ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.719  1.191   24.759 1.00 15.83 ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 8.929  2.320   25.943 1.00 18.37 ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.918 2.525   25.949 1.00 17.35 ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.787 2.535   27.131 1.00 16.82 ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.019 2.703   28.455 1.00 18.19 ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.444 2.151   29.472 1.00 19.66 ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.867 3.613   27.036 1.00 18.82 ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.365 4.932   27.051 1.00 21.86 ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.876 3.442   28.431 1.00 16.95 ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.051 3.667   29.625 1.00 16.59 ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.313 2.410   30.098 1.00 16.47 ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.666  2.458   31.130 1.00 17.70 ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.092 4.836   29.429 1.00 17.87 ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.119  4.604   28.420 1.00 19.41 ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.390 1.310   29.319 1.00 16.41 ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.820  0.015   29.694 1.00 17.73 ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.866 -1.100  29.611 1.00 18.64 ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.536 -2.250  29.905 1.00 20.15 ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.653  -0.343  28.769 1.00 17.76 ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.483  0.637   28.926 1.00 18.18 ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.708  0.315   30.180 1.00 18.35 ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.540  1.190   30.307 1.00 20.42 ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.541  2.348   30.945 1.00 20.95 ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.663  2.819   31.485 1.00 22.01 ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.412  3.048   31.069 1.00 23.73 ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.107 -0.794  29.163 1.00 19.48 ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.155 -1.824  28.910 1.00 21.05 ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.594 -2.972  28.059 1.00 22.69 ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.809 -4.172  28.338 1.00 25.80 ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.744 -2.392  30.192 1.00 23.89 ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.701 -1.477  30.812 1.00 25.67 ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.566 -2.310  31.725 1.00 28.04 ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.302 -1.362  32.532 1.00 29.21 ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.944 -0.984  33.753 1.00 27.05 ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.874 -1.531  34.346 1.00 27.35 ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.656 -0.079  34.402 1.00 26.88 ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.824 -2.610  27.037 1.00 20.32 ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.143 -3.612  26.220 1.00 19.89 ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.061 -3.257  24.771 1.00 18.41 ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 11.001 -2.089  24.446 1.00 19.04 ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.698  -3.803  26.723 1.00 24.12 ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.604  -4.859  27.833 1.00 31.16 ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 8.172  -5.114  28.291 1.00 38.93 ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 8.087  -6.221  29.330 1.00 44.55 ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.868  -5.899  30.559 1.00 48.94 ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 11.059 -4.275  23.903 1.00 17.83 ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.822 -4.121  22.473 1.00 17.54 ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.379  -4.474  22.170 1.00 18.18 ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.883  -5.530  22.613 1.00 22.77 ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.762 -5.076  21.690 1.00 16.18 ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.235 -4.778  21.817 1.00 17.46 ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.957 -4.087  20.823 1.00 21.69 ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 14.079 -5.092  22.822 1.00 17.90 ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.210 -4.035  21.272 1.00 20.26 ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.332 -4.649  22.436 1.00 21.70 ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.667  -3.611  21.453 1.00 16.57 ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.246  -3.838  21.167 1.00 16.66 ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.996  -3.958  19.691 1.00 16.89 ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.447  -3.083  18.927 1.00 16.18 ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.421  -2.595  21.666 1.00 17.27 ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.339  -2.442  23.176 1.00 17.66 ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.574  -3.321  23.948 1.00 18.46 ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.037  -1.442  23.832 1.00 17.70 ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.453  -3.157  25.326 1.00 20.44 ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.896  -1.242  25.201 1.00 19.37 ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.109  -2.113  25.945 1.00 20.25 ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.046  -1.963  27.331 1.00 23.16 ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.171  -4.923  19.274 1.00 17.14 ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.735  -4.940  17.885 1.00 17.79 ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.708  -3.848  17.596 1.00 19.45 ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.771  -3.624  18.424 1.00 21.41 ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.093  -6.313  17.694 1.00 19.78 ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.733  -6.751  19.044 1.00 19.85 ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.543  -6.005  20.069 1.00 17.24 ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.852  -3.159  16.455 1.00 17.59 ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.905  -2.098  16.117 1.00 19.23 ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.575  -2.099  14.638 1.00 18.80 ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.408  -2.507  13.816 1.00 18.80 ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.460  -0.713  16.502 1.00 22.68 ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.390  -0.507  18.018 1.00 24.41 ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.887  -0.505  15.982 1.00 22.85 ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.400  -1.561  14.296 1.00 18.88 ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.994  -1.170  12.959 1.00 19.33 ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.211  0.363   12.884 1.00 18.20 ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.816  1.067   13.843 1.00 18.89 ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.503  -1.426  12.748 1.00 24.01 ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.266  -2.823  12.676 1.00 32.27 ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.822  0.874   11.789 1.00 17.44 ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.118  2.294   11.713 1.00 17.86 ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.730  2.854   10.375 1.00 18.98 ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.672  2.135   9.357  1.00 20.40 ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.610  2.567   12.076 1.00 17.83 ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.627  1.756   11.289 1.00 18.11 ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.072  0.531   11.754 1.00 17.93 ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.205  2.267   10.142 1.00 18.10 ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.989  -0.214  11.039 1.00 19.58 ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.160  1.531   9.440  1.00 19.53 ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.541  0.298   9.898  1.00 19.02 ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.411  4.146   10.373 1.00 19.02 ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 1.992  4.818   9.142  1.00 19.34 ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.166  5.098   8.183  1.00 19.45 ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.321  4.938   8.553  1.00 20.29 ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.232  6.111   9.473  1.00 21.46 ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.098  7.044   10.111 1.00 23.00 ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.870  5.428   6.938  1.00 19.48 ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.913  5.722   5.956  1.00 19.83 ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.521  7.087   6.266  1.00 21.49 ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.853  7.940   6.877  1.00 21.59 ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.279  5.720   4.550  1.00 21.25 ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.955  4.324   4.075  1.00 26.10 ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.482  4.313   2.617  1.00 32.72 ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.569  2.903   2.072  1.00 39.58 ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.328  2.864   0.611  1.00 43.86 ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.804  7.305   5.935  1.00 20.70 ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.450  8.599   6.260  1.00 21.60 ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.635  9.779   5.693  1.00 22.23 ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.198  9.770   4.533  1.00 24.27 ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.857  8.483   5.645  1.00 24.07 ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.042  7.010   5.310  1.00 24.87 ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.706  6.370   5.216  1.00 22.12 ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.365  10.753  6.559  1.00 21.09 ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.476  11.853  6.199  1.00 22.61 ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.871  13.158  6.897  1.00 21.55 ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.723  13.172  7.789  1.00 19.06 ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.055  11.491  6.617  1.00 28.60 ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.648  10.200  6.179  1.00 39.10 ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.209  14.258  6.510  1.00 23.82 ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.388  15.567  7.132  1.00 24.32 ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.322  15.673  8.257  1.00 24.93 ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.128  15.671  7.974  1.00 26.95 ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.180  16.640  6.048  1.00 25.41 ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.510  18.048  6.392  1.00 28.44 ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 5.969  18.205  6.683  1.00 28.79 ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.132  18.982  5.225  1.00 29.92 ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.756  15.686  9.528  1.00 23.49 ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.859  15.663  10.704 1.00 24.63 ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.096  16.858  11.612 1.00 25.48 ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.234  17.253  11.836 1.00 24.71 ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.142  14.354  11.503 1.00 25.86 ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.865  13.070  10.664 1.00 28.32 ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.402  14.308  12.866 1.00 26.60 ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 1.426  13.008  10.152 1.00 31.52 ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 2.022  17.448  12.149 1.00 26.13 ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.166  18.569  13.069 1.00 27.41 ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.576  18.056  14.443 1.00 28.09 ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 2.034  17.076  14.956 1.00 28.61 ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.853  19.345  13.163 1.00 28.39 ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.053  20.665  13.843 1.00 31.83 ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.669  21.713  13.186 1.00 33.79 ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.627  20.859  15.136 1.00 34.02 ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.854  22.938  13.804 1.00 36.77 ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.810  22.100  15.758 1.00 34.69 ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.421  23.124  15.087 1.00 36.57 ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.643  18.648  14.992 1.00 27.39 ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 4.165  18.260  16.291 1.00 27.31 ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 4.095  19.495  17.209 1.00 28.53 ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.578  20.554  16.832 1.00 28.70 ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.612  17.743  16.163 1.00 26.27 ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 6.176  17.389  17.549 1.00 25.59 ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.649  16.530  15.194 1.00 25.10 ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.513  19.323  18.414 1.00 30.29 ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.355  20.439  19.349 1.00 33.03 ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.680  20.969  19.841 1.00 33.92 ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.687  20.281  19.751 1.00 33.48 ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.504  20.002  20.563 1.00 37.87 ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 1.060  19.686  20.254 1.00 46.29 ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 0.347  20.813  19.552 1.00 56.87 ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 0.469  21.985  19.987 1.00 58.25 ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.319 20.514  18.536 1.00 60.62 ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.669  22.215  20.389 1.00 34.92 ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.873  22.859  20.937 1.00 34.78 ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.383  22.041  22.079 1.00 33.84 ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.587  21.543  22.868 1.00 34.89 ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.542  24.259  21.447 1.00 35.32 ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.695  21.846  22.141 1.00 31.63 ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.351  21.119  23.213 1.00 30.85 ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.524  22.000  23.682 1.00 30.43 ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.737  23.103  23.141 1.00 31.54 ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 8.898  19.796  22.692 1.00 31.52 ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 9.958  20.018  21.771 1.00 31.47 ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.320 21.488  24.636 1.00 30.29 ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.499 22.235  25.067 1.00 30.43 ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.594 22.225  23.972 1.00 27.97 ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.529 22.995  24.072 1.00 26.69 ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.040 21.709  26.409 1.00 34.96 ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 12.735 20.376  26.337 1.00 43.66 ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 13.473 19.952  27.591 1.00 55.00 ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 14.691 20.233  27.687 1.00 58.83 ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 12.842 19.320  28.468 1.00 57.35 ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.453 21.398  22.895 1.00 26.79 ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.483 21.339  21.833 1.00 25.47 ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.142 22.024  20.531 1.00 25.01 ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 14.059 22.423  19.813 1.00 24.96 ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.798 19.872  21.546 1.00 24.69 ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.426 19.198  22.737 1.00 25.61 ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.760 19.404  23.052 1.00 26.93 ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.684 18.358  23.557 1.00 29.39 ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 16.356 18.756  24.125 1.00 29.36 ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.260 17.729  24.655 1.00 30.90 ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 15.592 17.938  24.940 1.00 31.69 ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.169 17.291  26.007 1.00 35.42 ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.834 22.140  20.195 1.00 25.12 ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.375 22.793  18.969 1.00 25.12 ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 10.040 23.550  19.223 1.00 27.72 ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.185  23.059  19.957 1.00 28.84 ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 11.074 21.743  17.856 1.00 23.57 ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.245 20.890  17.387 1.00 21.10 ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 13.143 21.365  16.437 1.00 21.58 ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.359 19.569  17.781 1.00 20.04 ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.205 20.572  15.989 1.00 20.23 ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.403 18.772  17.345 1.00 19.82 ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.317 19.275  16.433 1.00 19.73 ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.360 18.470  16.001 1.00 18.03 ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.804  24.620  18.465 1.00 30.05 ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.468  25.258  18.500 1.00 31.97 ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.442  24.379  17.743 1.00 33.99 ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.845  23.436  17.026 1.00 33.23 ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.705  26.587  17.776 1.00 32.36 ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.803  26.321  16.864 1.00 32.18 ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.690 25.265  17.484 1.00 29.36 ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 6.115  24.632  17.884 1.00 35.46 ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.110  23.810  17.167 1.00 36.07 ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.353  23.985  15.655 1.00 34.91 ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.605  25.092  15.199 1.00 36.99 ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.686  24.242  17.551 1.00 37.51 ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.546  22.876  14.939 1.00 31.39 ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.903  22.945  13.530 1.00 28.79 ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.442  21.614  12.895 1.00 28.25 ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.954  20.732  13.589 1.00 29.80 ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.471  23.095  13.389 1.00 27.13 ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.266  21.753  13.597 1.00 27.22 ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.600  21.878  14.276 1.00 27.05 ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.500 20.747  13.964 1.00 25.76 ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.424 19.533  14.502 1.00 26.88 ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.475  19.248  15.401 1.00 27.66 ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.306 18.591  14.158 1.00 22.34 ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.633  21.500  11.587 1.00 27.99 ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.433  20.290  10.850 1.00 27.22 ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.785  19.593  10.743 1.00 24.47 ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.776  20.179  10.286 1.00 24.41 ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.904  20.599  9.459  1.00 28.17 ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.430  20.936  9.466  1.00 29.84 ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.469  19.939  9.384  1.00 30.55 ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.997  22.233  9.657  1.00 32.11 ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.110  20.233  9.437  1.00 32.84 ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.639  22.540  9.703  1.00 33.64 ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.700  21.530  9.629  1.00 34.71 ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.656 21.773  9.708  1.00 38.04 ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.809  18.304  11.125 1.00 22.26 ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 8.015  17.473  11.003 1.00 20.52 ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.776  16.559  9.803  1.00 20.22 ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.691  15.981  9.660  1.00 19.41 ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.268  16.657  12.294 1.00 21.20 ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.469  15.747  12.216 1.00 20.29 ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.982  15.264  13.568 1.00 20.17 ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 10.015 15.987  14.546 1.00 22.07 ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.464 14.013  13.599 1.00 20.07 ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.788  16.405  8.955  1.00 19.60 ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.656  15.591  7.761  1.00 19.02 ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.264  14.207  7.986  1.00 19.86 ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.032 13.993  8.930  1.00 20.79 ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.321  16.304  6.582  1.00 20.74 ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.724 16.413  6.824  1.00 24.71 ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.875  13.260  7.088  1.00 19.58 ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.363  11.895  7.060  1.00 18.77 ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.072  11.200  8.411  1.00 18.44 ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.868  10.371  8.850  1.00 18.27 ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.877 11.863  6.692  1.00 20.03 ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.160 12.426  5.316  1.00 22.68 ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.267 11.606  4.203  1.00 25.94 ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.351 13.707  4.927  1.00 24.31 ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.510 12.409  3.173  1.00 25.45 ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.594 13.682  3.559  1.00 25.22 ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.941  11.522  9.043  1.00 16.78 ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.577  10.981  10.367 1.00 17.66 ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.480  9.907   10.229 1.00 18.01 ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.556  10.064  9.447  1.00 19.22 ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.027  12.159  11.240 1.00 18.81 ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.735  11.788  12.748 1.00 21.26 ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 7.980  11.429  13.474 1.00 20.75 ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.065  12.977  13.477 1.00 23.17 ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.623  8.786   10.966 1.00 17.45 ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.662  7.660   10.943 1.00 17.71 ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.089  7.503   12.328 1.00 18.59 ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.851  7.579   13.288 1.00 19.51 ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.428  6.392   10.587 1.00 19.11 ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.103  6.532   9.234  1.00 19.96 ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.159  5.147   8.708  1.00 21.62 ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.331  5.186   9.908  1.00 19.22 ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.772  7.338   12.447 1.00 17.76 ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.166  7.212   13.771 1.00 18.93 ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.677  5.805   14.072 1.00 18.33 ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.222  5.091   13.155 1.00 19.16 ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 1.956  8.151   13.913 1.00 20.55 ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.233  9.635   13.800 1.00 24.09 ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.967  10.466  14.055 1.00 27.21 ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.312  10.089  14.771 1.00 24.67 ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.704  5.442   15.361 1.00 16.83 ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.192  4.136   15.783 1.00 17.72 ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.542  4.276   17.164 1.00 17.26 ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.830  5.228   17.877 1.00 18.35 ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.349  3.111   15.919 1.00 18.62 ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.716  3.299   17.537 1.00 17.76 ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.176  3.229   18.867 1.00 18.39 ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.213  2.460   19.722 1.00 19.93 ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.583  1.334   19.398 1.00 21.33 ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.193 2.522   18.871 1.00 18.90 ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.652 2.308   20.298 1.00 19.52 ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.215 3.336   18.068 1.00 18.74 ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.705  3.124   20.749 1.00 20.40 ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.681  2.512   21.640 1.00 21.22 ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.111  3.476   22.723 1.00 20.29 ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 2.924  4.682   22.598 1.00 21.34 ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.710  2.970   23.798 1.00 19.27 ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.200  3.825   24.853 1.00 20.35 ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.459  4.542   24.499 1.00 20.50 ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.400  3.953   23.938 1.00 20.34 ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.500  3.009   26.131 1.00 20.40 ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 4.840  3.897   27.294 1.00 21.26 ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 3.904  4.761   27.823 1.00 22.81 ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.029  4.116   27.915 1.00 20.88 ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.559  5.498   28.715 1.00 22.61 ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 5.831  5.123   28.814 1.00 22.27 ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.526  5.804   24.848 1.00 21.68 ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.722  6.582   24.753 1.00 21.17 ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 6.712  7.733   25.768 1.00 22.06 ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.624  8.182   26.190 1.00 24.45 ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.006  7.058   23.326 1.00 21.68 ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 6.021  7.978   22.876 1.00 22.13 ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 7.939  8.141   26.191 1.00 20.98 ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.319  9.286   27.029 1.00 22.25 ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.447  10.048  26.334 1.00 23.37 ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.100 9.510   25.439 1.00 21.92 ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 8.798  8.812   28.406 1.00 24.44 ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.702  7.996   29.082 1.00 24.57 ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 7.927  7.437   30.467 1.00 27.68 ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.751  7.985   31.238 1.00 29.28 ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.230  6.452   30.794 1.00 27.61 ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.648  11.339  26.633 1.00 25.24 ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.683 12.114  25.892 1.00 25.84 ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.061 11.435  25.773 1.00 24.70 ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.676 11.416  24.687 1.00 23.83 ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 10.731 13.444  26.664 1.00 27.44 ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.392  13.557  27.278 1.00 28.28 ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 8.921  12.171  27.612 1.00 25.80 ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.540 10.863  26.869 1.00 21.71 ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 13.818 10.156  26.929 1.00 20.67 ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 13.895 8.876   26.112 1.00 19.40 ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 14.970 8.294   26.006 1.00 20.37 ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.760 8.424   25.542 1.00 18.01 ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.736 7.258   24.650 1.00 18.13 ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.272 7.589   23.254 1.00 18.36 ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.590 6.668   22.489 1.00 17.13 ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.333 6.648   24.521 1.00 17.79 ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 10.959 5.917   25.789 1.00 17.38 ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.853 5.304   26.388 1.00 17.34 ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.779  5.982   26.188 1.00 19.24 ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.433 8.891   22.940 1.00 18.10 ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 13.992 9.266   21.610 1.00 17.95 ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.344 8.570   21.373 1.00 18.19 ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.171 8.466   22.286 1.00 17.47 ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.138 10.776  21.523 1.00 19.16 ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.577 11.644  21.256 1.00 19.30 ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.524 8.030   20.175 1.00 17.58 ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.757 7.341   19.848 1.00 17.56 ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.596 5.837   19.760 1.00 16.54 ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.454 5.154   19.196 1.00 16.58 ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.515 5.308   20.358 1.00 16.45 ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.300 3.871   20.271 1.00 15.67 ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.087 3.436   18.827 1.00 15.00 ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.405 4.135   18.067 1.00 15.75 ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.658 2.264   18.444 1.00 14.62 ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.464 1.824   17.040 1.00 14.05 ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.134 1.165   16.751 1.00 13.92 ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.660 0.350   17.528 1.00 14.91 ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.647 0.863   16.717 1.00 15.27 ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.919 1.721   16.463 1.00 17.59 ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.378 -0.014  15.492 1.00 15.67 ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.204 0.947   16.373 1.00 21.70 ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.560 1.506   15.579 1.00 13.68 ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.459 0.779   14.985 1.00 13.43 ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.097 -0.100  13.861 1.00 14.67 ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.869 0.443   13.056 1.00 15.07 ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.440 1.757   14.352 1.00 14.82 ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.377 1.113   13.450 1.00 15.48 ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.374  0.299   14.308 1.00 16.77 ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.547  2.204   12.679 1.00 16.21 ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.801 -1.381  13.849 1.00 15.23 ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.362 -2.329  12.850 1.00 15.24 ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.304 -3.246  12.290 1.00 16.74 ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.268 -3.540  12.920 1.00 16.21 ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.525 -3.100  13.478 1.00 16.03 ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 14.080 -4.054  14.572 1.00 18.28 ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.295 -4.792  15.103 1.00 19.27 ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.114 -3.938  15.962 1.00 21.77 ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.415 -3.748  15.805 1.00 21.97 ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 18.039 -4.224  14.729 1.00 22.36 ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 18.089 -2.996  16.666 1.00 20.66 ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.573 -3.743  11.078 1.00 17.22 ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.721 -4.734  10.416 1.00 19.72 ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.615 -5.917  9.999  1.00 22.27 ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.772 -5.966  10.382 1.00 22.42 ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 11.023 -4.100  9.229  1.00 20.59 ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.198 -3.695  7.874  1.00 19.97 ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 12.060 -6.891  9.239  1.00 25.10 ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.864 -8.027  8.804  1.00 27.55 ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 14.099 -7.635  7.944  1.00 28.25 ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 15.089 -8.359  7.914  1.00 30.91 ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.991 -9.069  8.066  1.00 31.52 ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.469 -8.560  6.733  1.00 38.65 ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.588 -9.553  6.015  1.00 47.96 ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 9.353  -9.543  6.150  1.00 50.61 ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 11.194 -10.417 5.220  1.00 48.94 ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 14.061 -6.444  7.336  1.00 24.43 ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 15.156 -5.973  6.449  1.00 23.21 ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.265 -5.174  7.125  1.00 23.37 ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.328 -4.898  6.517  1.00 25.66 ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.521 -5.148  5.324  1.00 20.77 ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.440 -5.906  4.617  1.00 22.26 ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 12.124 -5.533  4.680  1.00 25.06 ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.557 -6.948  3.749  1.00 25.36 ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.456 -6.399  3.930  1.00 28.86 ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 12.288 -7.263  3.338  1.00 27.70 ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.996 -4.705  8.350  1.00 21.19 ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.998 -3.932  9.048  1.00 19.24 ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.377 -2.747  9.769  1.00 17.75 ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.187 -2.756  10.092 1.00 18.22 ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.211 -1.719  10.037 1.00 16.91 ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.764 -0.511  10.758 1.00 16.47 ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.901 0.380   9.875  1.00 15.65 ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.305 0.744   8.775  1.00 16.35 ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.957 0.275   11.360 1.00 17.40 ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.510 1.579   12.027 1.00 18.06 ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.722 -0.593  12.353 1.00 18.44 ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.719 0.751   10.380 1.00 14.68 ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.741 1.568   9.650  1.00 15.32 ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.867 3.043   10.091 1.00 16.05 ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.732 3.958   9.284  1.00 16.97 ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.284 1.061   9.947  1.00 17.68 ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.207 1.984   9.347  1.00 18.09 ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.114 -0.352  9.439  1.00 18.77 ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.103 3.295   11.384 1.00 15.97 ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.186 4.661   11.889 1.00 16.38 ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.391 4.714   13.377 1.00 15.49 ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.725 3.688   13.967 1.00 16.14 ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.237 5.905   13.994 1.00 15.13 ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.458 6.013   15.439 1.00 14.67 ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.281 6.776   16.050 1.00 14.94 ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.680 7.629   15.401 1.00 14.67 ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.770 6.743   15.828 1.00 16.32 ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 15.932 8.059   15.034 1.00 16.41 ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 16.977 5.819   15.622 1.00 17.94 ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.164 8.873   15.601 1.00 17.73 ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 12.993 6.500   17.322 1.00 14.81 ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 11.908 7.265   18.013 1.00 14.28 ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.257 8.761   18.007 1.00 15.43 ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.414 9.114   18.313 1.00 15.73 ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.820 6.766   19.470 1.00 14.64 ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.806 7.629   20.277 1.00 16.09 ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.379 5.299   19.500 1.00 15.63 ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.275 9.630   17.669 1.00 15.70 ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.482 11.053  17.601 1.00 16.85 ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.374 11.816  18.323 1.00 18.14 ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.640 12.923  18.743 1.00 19.12 ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.596 11.464  16.147 1.00 18.39 ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.758 12.863  15.985 1.00 19.06 ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.131  11.292  18.392 1.00 17.36 ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 7.995  12.066  19.007 1.00 19.56 ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.111  11.089  19.818 1.00 21.08 ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.266  9.864   19.698 1.00 19.47 ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.094  12.745  17.901 1.00 20.09 ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.264  11.801  17.225 1.00 20.37 ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 7.852  13.605  16.905 1.00 20.83 ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.139  11.612  20.568 1.00 22.51 ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.188  10.722  21.214 1.00 23.25 ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.210  11.486  22.074 1.00 25.30 ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.258  12.706  22.186 1.00 26.46 ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.416  10.709  22.774 1.00 27.05 ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.488  11.257  23.758 1.00 29.47 ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.191  10.506  23.714 1.00 31.94 ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 0.760  10.121  22.628 1.00 33.33 ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.508  10.391  24.863 1.00 31.11 ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.811 9.793   24.992 1.00 30.35 ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -1.034 8.484   24.260 1.00 27.27 ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.104 8.263   23.678 1.00 25.84 ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.831 10.821  24.561 1.00 33.56 ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.864 12.033  25.449 1.00 38.94 ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -2.243 11.949  26.623 1.00 40.83 ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.504 13.185  24.888 1.00 39.63 ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.095 7.567   24.425 1.00 24.53 ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.244 6.266   23.805 1.00 24.31 ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.102  6.282   22.331 1.00 21.90 ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? -0.105 5.271   21.675 1.00 22.54 ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.788  7.308   21.852 1.00 20.12 ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.350  7.302   20.484 1.00 20.69 ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.881  7.379   20.534 1.00 21.22 ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.466  7.915   21.502 1.00 22.85 ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.837  8.529   19.724 1.00 21.73 ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.634 8.544   19.442 1.00 24.06 ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.073 9.928   19.008 1.00 26.17 ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -1.024 7.468   18.396 1.00 25.13 ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.550  6.889   19.477 1.00 17.26 ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.006  7.047   19.361 1.00 17.30 ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.266  7.391   17.870 1.00 17.03 ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.619  6.797   17.003 1.00 17.78 ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.732  5.745   19.828 1.00 18.17 ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.178  4.497   19.108 1.00 18.74 ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.265  5.865   19.681 1.00 18.60 ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.138  8.349   17.593 1.00 16.50 ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.487  8.723   16.222 1.00 16.56 ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 7.926  8.396   15.925 1.00 16.87 ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.802  8.537   16.786 1.00 17.60 ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.187  7.943   14.707 1.00 16.10 ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.565  7.550   14.350 1.00 15.22 ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.059 8.364   13.154 1.00 16.13 ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.334  8.519   12.189 1.00 17.38 ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.552  6.074   13.903 1.00 16.25 ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.929  5.120   14.920 1.00 16.92 ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.653  4.675   16.016 1.00 15.51 ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.609  4.732   14.797 1.00 18.58 ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.076  3.801   16.956 1.00 16.01 ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.043  3.848   15.717 1.00 17.76 ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.779  3.396   16.789 1.00 16.61 ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.312 8.804   13.211 1.00 15.95 ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 11.947 9.502   12.069 1.00 16.15 ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.450 8.419   11.124 1.00 15.67 ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.311 7.629   11.507 1.00 16.26 ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.102 10.355  12.596 1.00 16.85 ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.892 8.353   9.867  1.00 15.92 ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.298 7.343   8.919  1.00 16.76 ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.716 7.650   8.416  1.00 17.07 ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.086 8.838   8.223  1.00 18.99 ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.338 7.420   7.687  1.00 17.92 ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.545 6.362   6.625  1.00 26.84 ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.754 5.191   6.990  1.00 21.96 ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.533 6.716   5.418  1.00 34.63 ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.492 6.596   8.120  1.00 15.71 ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.827 6.773   7.495  1.00 15.08 ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.993 5.946   6.203  1.00 17.11 ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.067 5.964   5.623  1.00 16.56 ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.011 6.443   8.452  1.00 15.94 ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.052 7.402   9.654  1.00 16.79 ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.049 4.970   8.908  1.00 16.00 ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.937 5.237   5.762  1.00 17.18 ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 15.025 4.302   4.637  1.00 17.48 ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.313 5.007   3.306  1.00 18.93 ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.779 4.352   2.351  1.00 19.43 ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.767 3.438   4.539  1.00 18.52 ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.642 2.475   5.741  1.00 17.97 ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.327 1.696   5.577  1.00 19.39 ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.179 2.579   5.814  1.00 19.96 ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.912  2.165   5.889  1.00 20.08 ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.605  0.893   5.632  1.00 22.22 ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.938  3.037   6.183  1.00 20.19 ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.981 6.287   3.188  1.00 19.08 ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.261 7.030   1.952  1.00 20.54 ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.694 7.545   1.858  1.00 19.35 ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 17.068 8.072   0.798  1.00 20.33 ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.254 8.187   1.805  1.00 21.22 ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.448 9.227   2.897  1.00 26.03 ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.568 8.838   4.089  1.00 25.74 ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.543 10.423  2.566  1.00 26.35 ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.487 7.486   2.961  1.00 19.02 ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.846 8.051   3.009  1.00 17.72 ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.817 7.020   2.469  1.00 17.82 ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.507 6.325   3.221  1.00 18.38 ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.168 8.437   4.464  1.00 18.05 ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.165 9.448   5.082  1.00 19.06 ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.571 9.744   6.527  1.00 19.53 ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.205 10.783  4.316  1.00 21.02 ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.826 6.875   1.147  1.00 18.59 ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.598 5.790   0.518  1.00 19.43 ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.095 5.934   0.756  1.00 20.48 ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.808 4.914   0.781  1.00 21.59 ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.278 5.690   -0.997 1.00 20.87 ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.751 5.655   -1.317 1.00 23.10 ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.495 5.389   -2.826 1.00 25.41 ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.963 4.610   -0.485 1.00 24.76 ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.585 7.176   0.916  1.00 20.32 ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 24.007 7.430   1.106  1.00 19.41 ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.572 6.847   2.396  1.00 21.03 ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.803 6.723   2.527  1.00 21.63 ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.311 8.935   0.984  1.00 19.89 ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.479 9.798   1.879  1.00 19.94 ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.310 10.431  1.566  1.00 21.02 ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.765 10.116  3.245  1.00 19.56 ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.866 11.152  2.653  1.00 21.52 ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.744 10.972  3.694  1.00 20.44 ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.814 9.784   4.121  1.00 20.13 ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.736 11.487  4.990  1.00 21.32 ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.843 10.344  5.384  1.00 22.00 ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.795 11.151  5.815  1.00 21.15 ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.692 6.460   3.356  1.00 19.08 ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.211 5.843   4.586  1.00 21.21 ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.900 4.506   4.270  1.00 23.72 ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.706 4.052   5.090  1.00 23.85 ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 23.049 5.570   5.552  1.00 20.04 ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.452 6.802   6.211  1.00 19.94 ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.175 6.415   7.015  1.00 21.44 ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.504 7.466   7.186  1.00 19.75 ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.585 3.879   3.114  1.00 25.60 ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.140 2.566   2.738  1.00 29.35 ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.472 2.643   2.003  1.00 33.70 ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.992 1.590   1.617  1.00 34.26 ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.176 1.822   1.785  1.00 30.83 ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.832 1.432   2.339  1.00 35.71 ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.668 1.477   3.565  1.00 37.66 ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.924 1.117   1.539  1.00 40.12 ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.993 3.846   1.732  1.00 36.28 ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.219 3.982   0.943  1.00 39.90 ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.196 5.020   1.532  1.00 42.77 ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.872 5.686   2.520  1.00 42.67 ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.804 4.401   -0.485 1.00 43.88 ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.207 5.798   -0.508 1.00 49.64 ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.492 6.217   -1.776 1.00 56.62 ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 26.281 7.440   -1.953 1.00 57.03 ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 26.136 5.329   -2.586 1.00 59.42 ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.364 5.200   0.869  1.00 45.53 ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.398 6.180   1.190  1.00 48.39 ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 31.864 6.078   2.630  1.00 50.63 ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 33.075 6.105   2.865  1.00 51.93 ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.939 7.608   0.803  1.00 51.20 ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.671 8.763   1.480  1.00 58.80 ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.952 9.244   0.822  1.00 66.85 ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 33.382 10.376  1.139  1.00 68.57 ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.524 8.500   -0.008 1.00 69.75 ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.847 -21.320 7.626  1.00 25.22 ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.690 -21.163 8.525  1.00 25.03 ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.673 -22.240 9.612  1.00 24.09 ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.344 -23.262 9.479  1.00 24.89 ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.396 -21.204 7.719  1.00 29.12 ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.171 -22.502 7.192  1.00 33.15 ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.895 -22.008 10.688 1.00 22.88 ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.781 -23.005 11.752 1.00 22.07 ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.497 -22.372 13.103 1.00 20.85 ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.913 -21.246 13.362 1.00 20.59 ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.821 -23.126 13.989 1.00 19.94 ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.523 -22.602 15.330 1.00 19.88 ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.660 -23.725 16.370 1.00 18.28 ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.677 -24.912 16.008 1.00 19.15 ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.076 -22.069 15.348 1.00 21.66 ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.730 -23.335 17.663 1.00 17.53 ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.664 -24.298 18.781 1.00 16.96 ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.260 -24.104 19.390 1.00 17.72 ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.827 -22.963 19.611 1.00 18.00 ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.699 -23.976 19.860 1.00 17.34 ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.144 -23.906 19.282 1.00 18.54 ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.613 -25.013 20.990 1.00 19.06 ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.143 -23.260 20.281 1.00 19.75 ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.554 -25.209 19.699 1.00 17.75 ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.217 -25.127 20.298 1.00 18.55 ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.296 -25.819 21.675 1.00 19.06 ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.345 -27.027 21.734 1.00 21.53 ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.181 -25.818 19.386 1.00 19.62 ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.967 -25.068 18.085 1.00 20.61 ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.123 -23.962 18.025 1.00 21.47 ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.662 -25.420 16.933 1.00 21.27 ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.939 -23.258 16.844 1.00 23.36 ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.503 -24.708 15.750 1.00 23.62 ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.648 -23.627 15.711 1.00 24.97 ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.513 -22.891 14.555 1.00 26.34 ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.321 -25.067 22.777 1.00 19.35 ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.422 -25.632 24.132 1.00 19.71 ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.285 -25.013 24.971 1.00 20.13 ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 14.120 -23.804 24.977 1.00 20.11 ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.825 -25.353 24.730 1.00 21.41 ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.202 -23.857 24.627 1.00 21.40 ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.894 -25.867 26.172 1.00 22.60 ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.458 -25.843 25.647 1.00 21.32 ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.346 -25.275 26.413 1.00 21.66 ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.414 -24.452 25.555 1.00 21.54 ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.105 -24.852 24.424 1.00 22.82 ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 11.084 -23.233 26.014 1.00 20.66 ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.298 -22.334 25.188 1.00 21.32 ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.173 -21.245 24.612 1.00 21.38 ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.724 -20.100 24.461 1.00 21.74 ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 9.100  -21.729 25.958 1.00 23.53 ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.990  -22.763 26.161 1.00 30.90 ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 7.069  -22.895 25.340 1.00 34.03 ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 8.119  -23.566 27.190 1.00 31.87 ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.399 -21.611 24.206 1.00 19.59 ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.319 -20.643 23.609 1.00 19.39 ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.821 -21.117 22.236 1.00 18.66 ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 14.001 -22.327 22.007 1.00 18.72 ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.555 -20.459 24.502 1.00 20.61 ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.248 -19.941 25.900 1.00 22.72 ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.694 -18.685 26.091 1.00 24.88 ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.642 -20.655 27.027 1.00 24.78 ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.431 -18.201 27.377 1.00 26.27 ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.392 -20.177 28.312 1.00 26.50 ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.828 -18.933 28.478 1.00 28.98 ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.620 -18.448 29.756 1.00 33.03 ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 14.064 -20.149 21.345 1.00 17.47 ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.659 -20.384 20.023 1.00 18.20 ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.911 -19.525 19.970 1.00 17.70 ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.836 -18.306 20.200 1.00 18.27 ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.672 -19.987 18.891 1.00 19.23 ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.306 -19.755 17.484 1.00 21.64 ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.226 -19.524 16.412 1.00 21.95 ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.647 -18.559 15.387 1.00 23.79 ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.143 -18.876 14.189 1.00 24.91 ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.342 -20.152 13.854 1.00 24.41 ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.466 -17.918 13.324 1.00 25.40 ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.099 -20.155 19.754 1.00 16.84 ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.377 -19.414 19.722 1.00 16.61 ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.853 -19.378 18.287 1.00 17.26 ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 19.006 -20.433 17.655 1.00 17.15 ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.456 -20.113 20.573 1.00 18.64 ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.714 -19.257 20.678 1.00 20.51 ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.927 -20.523 21.954 1.00 19.11 ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.059 -18.160 17.732 1.00 16.98 ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.510 -17.979 16.345 0.50 16.53 ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.479 -18.003 16.346 0.50 18.34 ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.655 -17.003 16.272 1.00 17.65 ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.897 -16.225 17.226 1.00 17.61 ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.390 -17.429 15.416 0.50 16.35 ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.216 -17.493 15.568 0.50 21.76 ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.384 -18.497 15.045 0.50 17.90 ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.482 -17.217 14.105 0.50 22.44 ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.765 -16.139 15.972 0.50 14.48 ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 17.078 -18.487 15.685 0.50 24.57 ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.379 -16.963 15.094 1.00 16.62 ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.360 -15.906 14.906 1.00 16.58 ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.562 -14.567 14.862 1.00 17.35 ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.573 -14.460 14.142 1.00 17.48 ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 23.035 -16.065 13.534 1.00 16.52 ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.865 -17.342 13.454 1.00 17.90 ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.405 -18.413 13.016 1.00 19.16 ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.117 -17.256 13.898 1.00 19.13 ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.026 -13.536 15.562 1.00 17.61 ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.300 -12.247 15.588 1.00 16.28 ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.165 -11.683 14.151 1.00 17.85 ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.127 -11.120 13.793 1.00 19.43 ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.069 -11.244 16.443 1.00 16.05 ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.299 -9.901  16.662 1.00 18.15 ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.150 -8.958  17.467 1.00 20.54 ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.501 -7.696  17.901 1.00 20.09 ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.379 -6.596  17.159 1.00 20.49 ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.740 -6.601  15.881 1.00 23.42 ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.867 -5.479  17.690 1.00 20.36 ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.187 -11.906 13.288 1.00 17.94 ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.118 -11.354 11.915 1.00 17.63 ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.101 -12.086 11.021 1.00 18.93 ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.756 -11.554 9.957  1.00 20.48 ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.531 -11.282 11.248 1.00 18.39 ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.080 -12.600 10.797 1.00 18.64 ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.862 -13.374 11.637 1.00 20.59 ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.028 -13.184 9.572  1.00 19.67 ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.215 -14.453 10.922 1.00 21.07 ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.750 -14.362 9.658  1.00 20.47 ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.600 -13.273 11.449 1.00 19.31 ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.562 -14.005 10.714 1.00 20.14 ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.188 -13.957 11.380 1.00 20.82 ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.257 -14.671 10.943 1.00 22.48 ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 20.039 -15.449 10.516 1.00 20.40 ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.344 -15.579 9.709  1.00 21.64 ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.778 -17.057 9.610  1.00 22.50 ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.189 -14.934 8.315  1.00 22.48 ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 18.037 -13.162 12.478 1.00 20.32 ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.743 -13.112 13.177 1.00 21.46 ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.640 -12.556 12.300 1.00 23.33 ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.865 -11.595 11.522 1.00 24.68 ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.858 -12.293 14.457 1.00 21.76 ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.448 -13.161 12.418 1.00 23.60 ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.254 -12.749 11.665 1.00 23.45 ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.446 -11.668 12.419 1.00 24.43 ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.699 -11.384 13.589 1.00 25.22 ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.340 -13.991 11.428 1.00 24.65 ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.798 -14.421 12.670 1.00 25.87 ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.055 -15.158 10.755 1.00 23.93 ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.410 -11.081 11.756 1.00 25.32 ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.498 -10.151 12.446 1.00 26.92 ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.804  -10.868 13.595 1.00 26.00 ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.677  -10.272 14.662 1.00 26.58 ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.414  -9.628  11.487 1.00 28.28 ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.298  -8.887  12.187 1.00 31.63 ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.515  -7.661  12.791 1.00 34.12 ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.027  -9.280  12.447 1.00 34.47 ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.348  -7.290  13.300 1.00 34.71 ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.421  -8.242  13.141 1.00 35.49 ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.400  -12.154 13.425 1.00 25.90 ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.758  -12.864 14.530 1.00 25.77 ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.710  -13.009 15.714 1.00 23.57 ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.276  -12.943 16.860 1.00 22.90 ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.243  -14.241 14.097 1.00 28.61 ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.416  -14.918 15.180 1.00 34.67 ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.282  -14.520 15.471 1.00 36.11 ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 7.978  -15.931 15.837 1.00 36.27 ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 11.033 -13.215 15.444 1.00 22.40 ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.999 -13.321 16.541 1.00 22.33 ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 12.039 -12.001 17.339 1.00 22.69 ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 12.015 -12.026 18.568 1.00 23.05 ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.401 -13.641 16.016 1.00 21.52 ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.559 -15.052 15.522 1.00 22.09 ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.984 -15.967 16.156 1.00 21.71 ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.264 -15.250 14.512 1.00 22.40 ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.153 -10.854 16.634 1.00 22.41 ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.203 -9.563  17.327 1.00 22.39 ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.867 -9.246  18.051 1.00 22.16 ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.870 -8.575  19.083 1.00 22.38 ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.538 -8.456  16.316 1.00 22.38 ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 14.018 -8.378  16.012 1.00 21.74 ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.652 -8.872  14.904 1.00 22.57 ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 15.056 -7.850  16.868 1.00 21.38 ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 16.017 -8.635  14.993 1.00 23.08 ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.283 -7.995  16.179 1.00 22.83 ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 15.053 -7.139  18.078 1.00 23.24 ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.481 -7.515  16.679 1.00 22.72 ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.263 -6.701  18.595 1.00 24.86 ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.460 -6.863  17.867 1.00 24.01 ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.733  -9.685  17.478 1.00 21.48 ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.403  -9.457  18.094 1.00 24.00 ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.174  -10.329 19.334 1.00 25.67 ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.204  -10.124 20.072 1.00 26.32 ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.305  -9.727  17.081 1.00 23.88 ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 9.030  -11.348 19.549 1.00 25.36 ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.913  -12.254 20.707 1.00 24.99 ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.287 -12.324 21.397 1.00 23.71 ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.727 -13.389 21.816 1.00 22.21 ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.449  -13.639 20.214 1.00 26.39 ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 7.022  -13.598 19.727 1.00 27.62 ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 6.062  -13.598 20.537 1.00 31.17 ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.853  -13.536 18.419 1.00 27.63 ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 11.006 -11.196 21.468 1.00 23.90 ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.374 -11.175 21.994 1.00 22.65 ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.496 -11.495 23.476 1.00 23.70 ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.707 -10.985 24.309 1.00 24.66 ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.961 -9.789  21.728 1.00 22.65 ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.410 -9.623  22.099 1.00 22.89 ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.308 -10.534 21.217 1.00 22.43 ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.857 -8.170  21.872 1.00 24.84 ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.492 -12.349 23.808 1.00 22.69 ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.845 -12.618 25.188 1.00 22.85 ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.165 -11.897 25.510 1.00 24.01 ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.248 -11.183 26.530 1.00 24.47 ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 14.000 -14.127 25.422 1.00 24.14 ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.543 -14.417 26.812 1.00 25.16 ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.673 -14.839 25.205 1.00 24.34 ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.212 -12.046 24.628 1.00 22.14 ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.517 -11.458 24.901 1.00 22.21 ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.328 -11.434 23.578 1.00 21.80 ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.106 -12.318 22.741 1.00 21.11 ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.235 -12.363 25.943 1.00 22.95 ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.721 -12.131 26.138 1.00 23.61 ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.304 -11.190 26.939 1.00 25.56 ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.807 -12.826 25.485 1.00 22.36 ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.683 -11.287 26.867 1.00 25.82 ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 22.013 -12.281 25.985 1.00 23.78 ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.875 -13.852 24.523 1.00 22.59 ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.266 -12.741 25.580 1.00 23.69 ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.122 -14.323 24.157 1.00 23.85 ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.290 -13.735 24.649 1.00 23.78 ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.163 -10.422 23.379 1.00 20.84 ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 20.031 -10.352 22.209 1.00 20.29 ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.322 -9.690  22.583 1.00 20.17 ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.369 -8.831  23.494 1.00 20.67 ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.350 -9.630  21.039 1.00 21.55 ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.763 -8.265  21.365 1.00 22.24 ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.742 -7.107  21.301 1.00 25.86 ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.522 -6.095  22.007 1.00 27.16 ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.738 -7.213  20.549 1.00 24.37 ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.405 -10.049 21.866 1.00 19.29 ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.684 -9.412  22.093 1.00 19.64 ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.434 -9.368  20.766 1.00 20.65 ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.841 -10.424 20.258 1.00 21.19 ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.433 -10.203 23.153 1.00 21.74 ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.740 -9.597  23.566 1.00 28.41 ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.407 -8.979  22.710 1.00 32.92 ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 26.128 -9.771  24.735 1.00 28.42 ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.579 -8.176  20.169 1.00 20.36 ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.265 -8.029  18.892 0.50 21.17 ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.258 -8.059  18.889 0.50 21.42 ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.738 -8.446  18.989 1.00 21.51 ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.276 -9.013  18.011 1.00 21.55 ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.137 -6.593  18.380 0.50 22.71 ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.101 -6.649  18.335 0.50 23.77 ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.028 -6.312  17.307 0.50 23.76 ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.614 -5.726  19.276 0.50 26.37 ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.403 -8.191  20.159 1.00 21.16 ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.816 -8.577  20.272 1.00 21.90 ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 29.025 -10.077 20.203 1.00 20.53 ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.110 -10.525 19.832 1.00 21.48 ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.438 -8.044  21.557 1.00 25.65 ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 28.979 -8.709  22.718 1.00 31.70 ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 27.987 -10.874 20.490 1.00 19.26 ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 28.080 -12.334 20.413 1.00 18.90 ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.437 -12.914 19.141 1.00 19.34 ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.436 -14.149 18.958 1.00 18.81 ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.339 -12.945 21.634 1.00 20.38 ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 28.042 -12.620 22.938 1.00 21.82 ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.285 -13.173 24.168 1.00 19.76 ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.325 -14.648 24.215 1.00 18.67 ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.292 -15.368 25.337 1.00 20.34 ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.209 -14.770 26.518 1.00 21.05 ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.400 -16.698 25.286 1.00 18.63 ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.713 -12.071 18.360 1.00 18.58 ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.906 -12.513 17.214 1.00 17.95 ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.807 -13.475 17.673 1.00 18.62 ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.535 -14.441 16.953 1.00 17.34 ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.749 -13.158 16.100 1.00 17.45 ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.972 -13.493 14.860 1.00 20.38 ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.108 -12.703 14.479 1.00 21.89 ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.287 -14.512 14.219 1.00 18.48 ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.179 -13.234 18.860 1.00 18.04 ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.124 -14.142 19.326 1.00 17.91 ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.829 -13.397 19.597 1.00 18.78 ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.853 -12.245 20.071 1.00 19.63 ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.507 -14.881 20.623 1.00 17.10 ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.576 -15.969 20.518 1.00 18.75 ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.822 -16.596 21.919 1.00 18.99 ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.142 -17.085 19.555 1.00 20.07 ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.708 -14.089 19.335 1.00 17.58 ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.371 -13.607 19.661 1.00 17.96 ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.552 -14.811 20.111 1.00 18.21 ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.607 -15.886 19.492 1.00 19.04 ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.744 -12.869 18.461 1.00 17.58 ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.335 -12.244 18.753 1.00 18.43 ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.107 -10.951 17.990 1.00 21.62 ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.218 -13.207 18.408 1.00 18.52 ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.776 -14.634 21.203 1.00 18.36 ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.896 -15.663 21.722 1.00 18.77 ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.457 -15.119 21.713 1.00 18.68 ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.215 -14.014 22.204 1.00 19.43 ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.309 -16.073 23.148 1.00 19.07 ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.320 -17.087 23.727 1.00 20.08 ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.731 -16.654 23.143 1.00 19.28 ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.527 -15.867 21.122 1.00 18.92 ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 13.118 -15.492 21.112 1.00 19.86 ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.299 -16.583 21.826 1.00 20.87 ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.809 -17.692 22.092 1.00 20.47 ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.620 -15.291 19.688 1.00 22.24 ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.790 -16.449 18.895 1.00 21.73 ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 11.026 -16.243 22.199 1.00 21.06 ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.180 -17.232 22.874 1.00 22.24 ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.354  -18.039 21.869 1.00 24.56 ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 9.046  -17.567 20.788 1.00 25.71 ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.279  -16.520 23.887 1.00 25.74 ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.413  -15.629 23.214 1.00 30.64 ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.976  -19.278 22.225 1.00 24.53 ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.231  -20.150 21.320 1.00 25.34 ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.950  -20.636 21.995 1.00 28.98 ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.900  -20.696 23.210 1.00 29.46 ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 9.079  -21.383 20.928 1.00 25.68 ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.366  -22.137 22.101 1.00 26.80 ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.390 -21.017 20.241 1.00 25.53 ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.960  -21.050 21.195 1.00 31.13 ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.728  -21.592 21.749 1.00 33.75 ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.939  -23.055 22.112 1.00 34.36 ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.563  -23.487 23.203 1.00 35.93 ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.565  -21.365 20.779 1.00 38.14 ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.796  -22.137 19.605 1.00 42.21 ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.412  -19.911 20.393 1.00 37.87 ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.557  -23.830 21.207 1.00 32.83 ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.828  -25.236 21.464 1.00 32.02 ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.169  -25.434 22.163 1.00 29.57 ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.087  -24.614 22.009 1.00 28.82 ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.807  -26.020 20.160 1.00 33.39 ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.297  -26.521 22.908 1.00 29.03 ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.525  -26.847 23.612 1.00 29.89 ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.530  -27.488 22.638 1.00 29.17 ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 9.143  -28.256 21.757 1.00 30.44 ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.235  -27.781 24.804 1.00 34.35 ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.783  -27.011 26.047 1.00 42.07 ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.629  -27.947 27.219 1.00 51.59 ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.720  -28.778 27.262 1.00 54.78 ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.525  -27.840 28.193 1.00 54.07 ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.795 -27.135 22.794 1.00 26.63 ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.897 -27.665 21.988 1.00 25.14 ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.561 -28.857 22.646 1.00 24.41 ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.363 -29.088 23.848 1.00 27.02 ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.333 -29.619 21.885 1.00 21.86 ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.921 -30.852 22.414 1.00 22.74 ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.398 -30.880 22.500 1.00 23.62 ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.916 -31.922 22.898 1.00 25.86 ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.409 -32.039 21.607 1.00 24.02 ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.619 -31.974 21.386 1.00 32.50 ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.111 -29.789 22.179 1.00 20.95 ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.565 -29.807 22.267 1.00 19.74 ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.986 -29.617 23.718 1.00 20.56 ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.276 -28.949 24.506 1.00 22.73 ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.162 -28.634 21.430 1.00 20.75 ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.975 -28.805 19.931 1.00 25.77 ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 18.026 -29.951 19.456 1.00 24.19 ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.848 -27.776 19.219 1.00 22.68 ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.111 -30.218 24.091 1.00 19.41 ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.675 -30.003 25.415 1.00 19.72 ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.955 -29.189 25.248 1.00 20.32 ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.784 -29.517 24.385 1.00 20.47 ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 20.066 -31.367 25.996 1.00 22.22 ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.880 -32.140 26.198 1.00 24.94 ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.839 -31.240 27.334 1.00 23.56 ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.137 -28.173 26.092 1.00 18.79 ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.366 -27.370 26.043 1.00 18.12 ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.448 -28.053 26.866 1.00 17.69 ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.226 -28.490 28.012 1.00 19.29 ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.133 -25.962 26.610 1.00 19.38 ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.944 -25.270 25.968 1.00 21.21 ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.408 -25.117 26.513 1.00 19.74 ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 21.066 -25.167 24.369 1.00 24.13 ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.667 -28.123 26.295 1.00 16.68 ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.782 -28.674 27.034 1.00 15.94 ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.151 -27.782 28.203 1.00 16.99 ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.171 -26.549 28.042 1.00 17.24 ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.990 -28.786 26.109 1.00 17.00 ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.532 -28.378 29.343 1.00 16.94 ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.996 -27.587 30.500 1.00 17.43 ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.322 -28.255 30.871 1.00 17.42 ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.382 -29.308 31.546 1.00 19.36 ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.976 -27.645 31.664 1.00 18.66 ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.613 -27.080 31.263 1.00 17.39 ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.640 -25.598 30.908 1.00 19.21 ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.284 -25.159 30.543 1.00 19.92 ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 23.028 -24.053 29.851 1.00 20.90 ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 24.019 -23.254 29.469 1.00 20.09 ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.780 -23.742 29.524 1.00 20.84 ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.409 -27.683 30.329 1.00 17.33 ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.721 -28.342 30.411 1.00 17.70 ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.835 -27.407 29.910 1.00 17.59 ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.545 -26.305 29.434 1.00 17.90 ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.669 -29.563 29.485 1.00 18.83 ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.517 -29.136 27.704 1.00 17.35 ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 33.108 -27.907 29.890 1.00 19.46 ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.210 -27.156 29.292 1.00 20.15 ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.888 -28.018 28.185 1.00 21.21 ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 36.089 -27.929 27.993 1.00 21.85 ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.220 -26.758 30.369 1.00 22.61 ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.891 -27.915 31.063 1.00 28.40 ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.543 -29.074 30.766 1.00 27.41 ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.820 -27.666 31.872 1.00 35.52 ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 34.097 -28.806 27.444 1.00 19.88 ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.637 -29.624 26.314 1.00 18.08 ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.294 -28.743 25.308 1.00 18.18 ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.828 -27.625 25.060 1.00 18.80 ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.540 -30.420 25.622 1.00 17.26 ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.970 -31.856 26.559 1.00 19.36 ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.366 -29.278 24.695 1.00 17.64 ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 37.012 -28.613 23.558 1.00 18.65 ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.062 -29.557 22.363 1.00 18.08 ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.839 -29.316 21.422 1.00 18.13 ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.434 -28.160 23.893 1.00 19.82 ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.497 -26.909 24.800 1.00 20.73 ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.891 -26.376 24.951 1.00 26.40 ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.488 -26.468 26.037 1.00 29.44 ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.433 -25.829 23.873 1.00 22.69 ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.288 -30.665 22.384 1.00 17.85 ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.127 -31.535 21.213 1.00 18.92 ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.663 -31.777 20.991 1.00 18.45 ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.876 -31.857 21.934 1.00 19.45 ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.922 -32.822 21.265 1.00 21.71 ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.385 -33.598 22.311 1.00 24.62 ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.397 -32.566 21.508 1.00 22.17 ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.284 -31.872 19.711 1.00 15.88 ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.898 -32.086 19.357 1.00 16.01 ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.722 -32.307 17.865 1.00 16.21 ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.697 -32.611 17.177 1.00 17.16 ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.507 -32.223 17.385 1.00 16.11 ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.146 -32.413 15.970 1.00 15.70 ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.241 -31.265 15.547 1.00 15.05 ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.296 -30.901 16.282 1.00 16.15 ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.433 -33.774 15.820 1.00 16.24 ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.908 -33.966 14.392 1.00 17.13 ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.379 -34.940 16.212 1.00 16.77 ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.512 -30.657 14.353 1.00 15.33 ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.634 -29.591 13.867 1.00 13.89 ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.055 -29.930 12.493 1.00 15.32 ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.710 -30.639 11.740 1.00 16.62 ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.314 -28.176 13.816 1.00 14.58 ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.196 -27.880 12.604 1.00 14.99 ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.470 -28.416 12.501 1.00 16.62 ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.749 -27.029 11.583 1.00 17.07 ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.306 -28.101 11.420 1.00 18.92 ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.588 -26.697 10.510 1.00 18.27 ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.846 -27.266 10.422 1.00 19.76 ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.681 -26.945 9.352  1.00 21.81 ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.898 -29.373 12.199 1.00 15.77 ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.265 -29.564 10.885 1.00 15.97 ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.646 -28.416 9.953  1.00 15.62 ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.385 -27.238 10.253 1.00 16.25 ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.741 -29.618 10.960 1.00 16.16 ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.146 -29.915 9.597  1.00 18.03 ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.499 -31.062 8.892  1.00 18.76 ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.277 -29.032 8.996  1.00 17.85 ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.011 -31.309 7.612  1.00 19.19 ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.748 -29.291 7.734  1.00 19.83 ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.115 -30.438 7.048  1.00 20.31 ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.618 -30.714 5.779  1.00 23.39 ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.191 -28.788 8.775  1.00 15.62 ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.582 -27.827 7.728  1.00 16.15 ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.602 -28.028 6.518  1.00 17.60 ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.780 -28.959 5.717  1.00 18.82 ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.016 -28.121 7.321  1.00 16.80 ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.599 -27.040 5.979  1.00 19.86 ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.622 -27.106 6.357  1.00 18.03 ? 66  SER   C N   1 
ATOM   1558 C  CA  . SER   B 1 60  ? 25.642 -27.274 5.293  1.00 18.77 ? 66  SER   C CA  1 
ATOM   1559 C  C   . SER   B 1 60  ? 26.273 -27.193 3.909  1.00 19.03 ? 66  SER   C C   1 
ATOM   1560 O  O   . SER   B 1 60  ? 25.780 -27.875 3.018  1.00 21.05 ? 66  SER   C O   1 
ATOM   1561 C  CB  . SER   B 1 60  ? 24.530 -26.248 5.409  1.00 21.51 ? 66  SER   C CB  1 
ATOM   1562 O  OG  . SER   B 1 60  ? 23.558 -26.566 4.427  1.00 27.12 ? 66  SER   C OG  1 
ATOM   1563 N  N   . SER   B 1 61  ? 27.306 -26.378 3.734  1.00 18.43 ? 67  SER   C N   1 
ATOM   1564 C  CA  . SER   B 1 61  ? 27.941 -26.229 2.407  1.00 19.00 ? 67  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 61  ? 28.743 -27.447 1.964  1.00 20.15 ? 67  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 61  ? 29.197 -27.489 0.813  1.00 21.35 ? 67  SER   C O   1 
ATOM   1567 C  CB  . SER   B 1 61  ? 28.809 -24.976 2.371  1.00 19.77 ? 67  SER   C CB  1 
ATOM   1568 O  OG  . SER   B 1 61  ? 29.920 -25.027 3.246  1.00 21.73 ? 67  SER   C OG  1 
ATOM   1569 N  N   . ARG   B 1 62  ? 28.910 -28.439 2.840  1.00 19.98 ? 68  ARG   C N   1 
ATOM   1570 C  CA  . ARG   B 1 62  ? 29.545 -29.699 2.491  1.00 19.76 ? 68  ARG   C CA  1 
ATOM   1571 C  C   . ARG   B 1 62  ? 28.602 -30.881 2.767  1.00 21.16 ? 68  ARG   C C   1 
ATOM   1572 O  O   . ARG   B 1 62  ? 28.970 -32.027 2.500  1.00 22.13 ? 68  ARG   C O   1 
ATOM   1573 C  CB  . ARG   B 1 62  ? 30.818 -29.904 3.311  1.00 19.83 ? 68  ARG   C CB  1 
ATOM   1574 C  CG  . ARG   B 1 62  ? 31.875 -28.833 3.041  1.00 23.97 ? 68  ARG   C CG  1 
ATOM   1575 C  CD  . ARG   B 1 62  ? 32.598 -29.137 1.752  1.00 24.64 ? 68  ARG   C CD  1 
ATOM   1576 N  NE  . ARG   B 1 62  ? 33.626 -28.117 1.484  1.00 26.96 ? 68  ARG   C NE  1 
ATOM   1577 C  CZ  . ARG   B 1 62  ? 33.414 -26.998 0.796  1.00 32.11 ? 68  ARG   C CZ  1 
ATOM   1578 N  NH1 . ARG   B 1 62  ? 32.213 -26.739 0.287  1.00 36.03 ? 68  ARG   C NH1 1 
ATOM   1579 N  NH2 . ARG   B 1 62  ? 34.411 -26.140 0.581  1.00 30.93 ? 68  ARG   C NH2 1 
ATOM   1580 N  N   . ARG   B 1 63  ? 27.377 -30.630 3.295  1.00 20.62 ? 69  ARG   C N   1 
ATOM   1581 C  CA  . ARG   B 1 63  ? 26.421 -31.671 3.713  1.00 21.20 ? 69  ARG   C CA  1 
ATOM   1582 C  C   . ARG   B 1 63  ? 27.109 -32.700 4.586  1.00 22.09 ? 69  ARG   C C   1 
ATOM   1583 O  O   . ARG   B 1 63  ? 26.923 -33.917 4.407  1.00 24.16 ? 69  ARG   C O   1 
ATOM   1584 C  CB  . ARG   B 1 63  ? 25.730 -32.330 2.514  1.00 23.30 ? 69  ARG   C CB  1 
ATOM   1585 C  CG  . ARG   B 1 63  ? 24.827 -31.436 1.725  1.00 26.84 ? 69  ARG   C CG  1 
ATOM   1586 C  CD  . ARG   B 1 63  ? 23.523 -31.089 2.381  1.00 33.45 ? 69  ARG   C CD  1 
ATOM   1587 N  NE  . ARG   B 1 63  ? 22.543 -30.644 1.389  1.00 36.46 ? 69  ARG   C NE  1 
ATOM   1588 C  CZ  . ARG   B 1 63  ? 22.413 -29.394 0.968  1.00 36.68 ? 69  ARG   C CZ  1 
ATOM   1589 N  NH1 . ARG   B 1 63  ? 23.242 -28.448 1.400  1.00 34.10 ? 69  ARG   C NH1 1 
ATOM   1590 N  NH2 . ARG   B 1 63  ? 21.483 -29.085 0.076  1.00 36.39 ? 69  ARG   C NH2 1 
ATOM   1591 N  N   . LYS   B 1 64  ? 27.932 -32.204 5.518  1.00 20.16 ? 70  LYS   C N   1 
ATOM   1592 C  CA  . LYS   B 1 64  ? 28.724 -33.115 6.336  1.00 21.03 ? 70  LYS   C CA  1 
ATOM   1593 C  C   . LYS   B 1 64  ? 28.894 -32.649 7.743  1.00 19.00 ? 70  LYS   C C   1 
ATOM   1594 O  O   . LYS   B 1 64  ? 28.926 -31.460 7.998  1.00 18.05 ? 70  LYS   C O   1 
ATOM   1595 C  CB  . LYS   B 1 64  ? 30.146 -33.239 5.730  1.00 25.74 ? 70  LYS   C CB  1 
ATOM   1596 C  CG  . LYS   B 1 64  ? 30.243 -34.362 4.695  1.00 35.24 ? 70  LYS   C CG  1 
ATOM   1597 C  CD  . LYS   B 1 64  ? 31.662 -34.546 4.173  1.00 44.11 ? 70  LYS   C CD  1 
ATOM   1598 C  CE  . LYS   B 1 64  ? 31.764 -35.718 3.227  1.00 49.73 ? 70  LYS   C CE  1 
ATOM   1599 N  NZ  . LYS   B 1 64  ? 30.865 -35.579 2.051  1.00 53.82 ? 70  LYS   C NZ  1 
ATOM   1600 N  N   . HIS   B 1 65  ? 28.991 -33.618 8.682  1.00 18.63 ? 71  HIS   C N   1 
ATOM   1601 C  CA  . HIS   B 1 65  ? 29.309 -33.333 10.077 1.00 19.53 ? 71  HIS   C CA  1 
ATOM   1602 C  C   . HIS   B 1 65  ? 30.777 -33.607 10.246 1.00 19.51 ? 71  HIS   C C   1 
ATOM   1603 O  O   . HIS   B 1 65  ? 31.270 -34.688 9.857  1.00 23.28 ? 71  HIS   C O   1 
ATOM   1604 C  CB  . HIS   B 1 65  ? 28.478 -34.232 11.028 1.00 18.43 ? 71  HIS   C CB  1 
ATOM   1605 C  CG  . HIS   B 1 65  ? 27.001 -33.992 10.966 1.00 17.74 ? 71  HIS   C CG  1 
ATOM   1606 N  ND1 . HIS   B 1 65  ? 26.330 -33.215 11.925 1.00 20.03 ? 71  HIS   C ND1 1 
ATOM   1607 C  CD2 . HIS   B 1 65  ? 26.106 -34.420 10.057 1.00 19.07 ? 71  HIS   C CD2 1 
ATOM   1608 C  CE1 . HIS   B 1 65  ? 25.050 -33.248 11.583 1.00 19.21 ? 71  HIS   C CE1 1 
ATOM   1609 N  NE2 . HIS   B 1 65  ? 24.861 -33.971 10.485 1.00 21.48 ? 71  HIS   C NE2 1 
ATOM   1610 N  N   . TYR   B 1 66  ? 31.523 -32.658 10.833 1.00 17.28 ? 72  TYR   C N   1 
ATOM   1611 C  CA  . TYR   B 1 66  ? 32.950 -32.855 10.997 1.00 17.00 ? 72  TYR   C CA  1 
ATOM   1612 C  C   . TYR   B 1 66  ? 33.323 -32.915 12.463 1.00 16.52 ? 72  TYR   C C   1 
ATOM   1613 O  O   . TYR   B 1 66  ? 32.932 -32.007 13.222 1.00 17.61 ? 72  TYR   C O   1 
ATOM   1614 C  CB  . TYR   B 1 66  ? 33.707 -31.631 10.399 1.00 18.62 ? 72  TYR   C CB  1 
ATOM   1615 C  CG  . TYR   B 1 66  ? 33.665 -31.539 8.879  1.00 20.76 ? 72  TYR   C CG  1 
ATOM   1616 C  CD1 . TYR   B 1 66  ? 34.476 -32.340 8.100  1.00 23.33 ? 72  TYR   C CD1 1 
ATOM   1617 C  CD2 . TYR   B 1 66  ? 32.897 -30.571 8.236  1.00 21.91 ? 72  TYR   C CD2 1 
ATOM   1618 C  CE1 . TYR   B 1 66  ? 34.486 -32.219 6.711  1.00 23.76 ? 72  TYR   C CE1 1 
ATOM   1619 C  CE2 . TYR   B 1 66  ? 32.907 -30.433 6.851  1.00 23.45 ? 72  TYR   C CE2 1 
ATOM   1620 C  CZ  . TYR   B 1 66  ? 33.701 -31.271 6.095  1.00 24.31 ? 72  TYR   C CZ  1 
ATOM   1621 O  OH  . TYR   B 1 66  ? 33.675 -31.136 4.713  1.00 26.06 ? 72  TYR   C OH  1 
ATOM   1622 N  N   . PRO   B 1 67  ? 34.129 -33.889 12.866 1.00 16.58 ? 73  PRO   C N   1 
ATOM   1623 C  CA  . PRO   B 1 67  ? 34.708 -33.841 14.227 1.00 16.43 ? 73  PRO   C CA  1 
ATOM   1624 C  C   . PRO   B 1 67  ? 35.780 -32.775 14.316 1.00 18.04 ? 73  PRO   C C   1 
ATOM   1625 O  O   . PRO   B 1 67  ? 36.628 -32.654 13.389 1.00 19.80 ? 73  PRO   C O   1 
ATOM   1626 C  CB  . PRO   B 1 67  ? 35.298 -35.228 14.442 1.00 19.67 ? 73  PRO   C CB  1 
ATOM   1627 C  CG  . PRO   B 1 67  ? 35.494 -35.765 13.078 1.00 21.68 ? 73  PRO   C CG  1 
ATOM   1628 C  CD  . PRO   B 1 67  ? 34.637 -35.046 12.084 1.00 18.58 ? 73  PRO   C CD  1 
ATOM   1629 N  N   . VAL   B 1 68  ? 35.730 -31.941 15.391 1.00 16.20 ? 74  VAL   C N   1 
ATOM   1630 C  CA  . VAL   B 1 68  ? 36.692 -30.850 15.494 1.00 16.34 ? 74  VAL   C CA  1 
ATOM   1631 C  C   . VAL   B 1 68  ? 37.138 -30.677 16.925 1.00 16.47 ? 74  VAL   C C   1 
ATOM   1632 O  O   . VAL   B 1 68  ? 36.411 -30.999 17.853 1.00 17.71 ? 74  VAL   C O   1 
ATOM   1633 C  CB  . VAL   B 1 68  ? 36.075 -29.496 14.998 1.00 19.11 ? 74  VAL   C CB  1 
ATOM   1634 C  CG1 . VAL   B 1 68  ? 35.990 -29.419 13.473 1.00 21.14 ? 74  VAL   C CG1 1 
ATOM   1635 C  CG2 . VAL   B 1 68  ? 34.711 -29.206 15.668 1.00 19.19 ? 74  VAL   C CG2 1 
ATOM   1636 N  N   . SER   B 1 69  ? 38.332 -30.119 17.091 1.00 17.09 ? 75  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 69  ? 38.867 -29.541 18.321 1.00 17.11 ? 75  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 69  ? 38.583 -28.019 18.220 1.00 16.52 ? 75  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 69  ? 38.697 -27.409 17.136 1.00 17.09 ? 75  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 69  ? 40.382 -29.723 18.386 1.00 19.02 ? 75  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 69  ? 40.692 -31.086 18.671 1.00 24.16 ? 75  SER   C OG  1 
ATOM   1642 N  N   . PHE   B 1 70  ? 38.116 -27.405 19.326 1.00 15.75 ? 76  PHE   C N   1 
ATOM   1643 C  CA  . PHE   B 1 70  ? 37.757 -25.971 19.257 1.00 15.85 ? 76  PHE   C CA  1 
ATOM   1644 C  C   . PHE   B 1 70  ? 38.300 -25.240 20.475 1.00 16.73 ? 76  PHE   C C   1 
ATOM   1645 O  O   . PHE   B 1 70  ? 38.475 -25.841 21.546 1.00 17.55 ? 76  PHE   C O   1 
ATOM   1646 C  CB  . PHE   B 1 70  ? 36.240 -25.721 19.022 1.00 17.05 ? 76  PHE   C CB  1 
ATOM   1647 C  CG  . PHE   B 1 70  ? 35.383 -26.453 20.040 1.00 15.65 ? 76  PHE   C CG  1 
ATOM   1648 C  CD1 . PHE   B 1 70  ? 34.927 -27.733 19.793 1.00 16.32 ? 76  PHE   C CD1 1 
ATOM   1649 C  CD2 . PHE   B 1 70  ? 34.931 -25.798 21.176 1.00 16.77 ? 76  PHE   C CD2 1 
ATOM   1650 C  CE1 . PHE   B 1 70  ? 34.137 -28.396 20.721 1.00 17.19 ? 76  PHE   C CE1 1 
ATOM   1651 C  CE2 . PHE   B 1 70  ? 34.095 -26.439 22.082 1.00 17.40 ? 76  PHE   C CE2 1 
ATOM   1652 C  CZ  . PHE   B 1 70  ? 33.701 -27.717 21.858 1.00 17.69 ? 76  PHE   C CZ  1 
ATOM   1653 N  N   . SER   B 1 71  ? 38.536 -23.959 20.326 1.00 15.91 ? 77  SER   C N   1 
ATOM   1654 C  CA  . SER   B 1 71  ? 39.160 -23.172 21.411 1.00 16.71 ? 77  SER   C CA  1 
ATOM   1655 C  C   . SER   B 1 71  ? 38.168 -22.761 22.503 1.00 19.04 ? 77  SER   C C   1 
ATOM   1656 O  O   . SER   B 1 71  ? 36.954 -23.046 22.411 1.00 19.22 ? 77  SER   C O   1 
ATOM   1657 C  CB  . SER   B 1 71  ? 39.903 -21.980 20.820 1.00 18.21 ? 77  SER   C CB  1 
ATOM   1658 O  OG  . SER   B 1 71  ? 38.967 -21.088 20.234 1.00 19.65 ? 77  SER   C OG  1 
ATOM   1659 N  N   . LYS   B 1 72  ? 38.681 -22.188 23.593 1.00 19.43 ? 78  LYS   C N   1 
ATOM   1660 C  CA  . LYS   B 1 72  ? 37.781 -21.778 24.715 1.00 18.96 ? 78  LYS   C CA  1 
ATOM   1661 C  C   . LYS   B 1 72  ? 37.124 -20.443 24.340 1.00 19.64 ? 78  LYS   C C   1 
ATOM   1662 O  O   . LYS   B 1 72  ? 37.710 -19.648 23.583 1.00 20.64 ? 78  LYS   C O   1 
ATOM   1663 C  CB  . LYS   B 1 72  ? 38.636 -21.597 25.978 1.00 21.79 ? 78  LYS   C CB  1 
ATOM   1664 C  CG  . LYS   B 1 72  ? 39.154 -22.919 26.495 1.00 26.80 ? 78  LYS   C CG  1 
ATOM   1665 C  CD  . LYS   B 1 72  ? 39.737 -22.786 27.902 1.00 37.64 ? 78  LYS   C CD  1 
ATOM   1666 C  CE  . LYS   B 1 72  ? 39.707 -24.125 28.604 1.00 44.41 ? 78  LYS   C CE  1 
ATOM   1667 N  NZ  . LYS   B 1 72  ? 40.087 -23.998 30.032 1.00 49.02 ? 78  LYS   C NZ  1 
ATOM   1668 N  N   . PRO   B 1 73  ? 35.895 -20.196 24.799 1.00 19.04 ? 79  PRO   C N   1 
ATOM   1669 C  CA  . PRO   B 1 73  ? 35.185 -18.943 24.406 1.00 19.94 ? 79  PRO   C CA  1 
ATOM   1670 C  C   . PRO   B 1 73  ? 35.974 -17.696 24.772 1.00 20.18 ? 79  PRO   C C   1 
ATOM   1671 O  O   . PRO   B 1 73  ? 36.495 -17.562 25.896 1.00 21.51 ? 79  PRO   C O   1 
ATOM   1672 C  CB  . PRO   B 1 73  ? 33.849 -18.997 25.151 1.00 21.55 ? 79  PRO   C CB  1 
ATOM   1673 C  CG  . PRO   B 1 73  ? 33.738 -20.389 25.646 1.00 21.59 ? 79  PRO   C CG  1 
ATOM   1674 C  CD  . PRO   B 1 73  ? 35.101 -21.041 25.713 1.00 19.30 ? 79  PRO   C CD  1 
ATOM   1675 N  N   . SER   B 1 74  ? 36.154 -16.812 23.776 1.00 19.16 ? 80  SER   C N   1 
ATOM   1676 C  CA  . SER   B 1 74  ? 37.051 -15.676 23.954 1.00 20.11 ? 80  SER   C CA  1 
ATOM   1677 C  C   . SER   B 1 74  ? 36.659 -14.478 23.087 1.00 19.94 ? 80  SER   C C   1 
ATOM   1678 O  O   . SER   B 1 74  ? 35.756 -14.588 22.251 1.00 19.40 ? 80  SER   C O   1 
ATOM   1679 C  CB  . SER   B 1 74  ? 38.467 -16.085 23.533 1.00 25.13 ? 80  SER   C CB  1 
ATOM   1680 O  OG  . SER   B 1 74  ? 38.930 -17.267 24.164 1.00 32.08 ? 80  SER   C OG  1 
ATOM   1681 N  N   . LEU   B 1 75  ? 37.354 -13.322 23.276 1.00 21.04 ? 81  LEU   C N   1 
ATOM   1682 C  CA  . LEU   B 1 75  ? 37.137 -12.119 22.455 1.00 23.30 ? 81  LEU   C CA  1 
ATOM   1683 C  C   . LEU   B 1 75  ? 38.105 -12.219 21.265 1.00 24.37 ? 81  LEU   C C   1 
ATOM   1684 O  O   . LEU   B 1 75  ? 39.329 -12.167 21.465 1.00 25.88 ? 81  LEU   C O   1 
ATOM   1685 C  CB  . LEU   B 1 75  ? 37.471 -10.869 23.297 1.00 25.57 ? 81  LEU   C CB  1 
ATOM   1686 C  CG  . LEU   B 1 75  ? 37.112 -9.490  22.720 1.00 28.48 ? 81  LEU   C CG  1 
ATOM   1687 C  CD1 . LEU   B 1 75  ? 35.631 -9.363  22.508 1.00 28.25 ? 81  LEU   C CD1 1 
ATOM   1688 C  CD2 . LEU   B 1 75  ? 37.590 -8.395  23.687 1.00 30.78 ? 81  LEU   C CD2 1 
ATOM   1689 N  N   . ILE   B 1 76  ? 37.580 -12.397 20.043 1.00 23.83 ? 82  ILE   C N   1 
ATOM   1690 C  CA  . ILE   B 1 76  ? 38.392 -12.659 18.852 1.00 24.31 ? 82  ILE   C CA  1 
ATOM   1691 C  C   . ILE   B 1 76  ? 38.132 -11.598 17.804 1.00 24.66 ? 82  ILE   C C   1 
ATOM   1692 O  O   . ILE   B 1 76  ? 36.977 -11.264 17.560 1.00 23.53 ? 82  ILE   C O   1 
ATOM   1693 C  CB  . ILE   B 1 76  ? 38.009 -14.081 18.279 1.00 26.86 ? 82  ILE   C CB  1 
ATOM   1694 C  CG1 . ILE   B 1 76  ? 38.306 -15.233 19.250 1.00 28.98 ? 82  ILE   C CG1 1 
ATOM   1695 C  CG2 . ILE   B 1 76  ? 38.678 -14.356 16.915 1.00 27.64 ? 82  ILE   C CG2 1 
ATOM   1696 C  CD1 . ILE   B 1 76  ? 39.762 -15.309 19.631 1.00 31.24 ? 82  ILE   C CD1 1 
ATOM   1697 N  N   . PHE   B 1 77  ? 39.207 -11.114 17.139 1.00 24.01 ? 83  PHE   C N   1 
ATOM   1698 C  CA  . PHE   B 1 77  ? 39.021 -10.173 16.037 1.00 24.89 ? 83  PHE   C CA  1 
ATOM   1699 C  C   . PHE   B 1 77  ? 38.607 -10.995 14.801 1.00 25.49 ? 83  PHE   C C   1 
ATOM   1700 O  O   . PHE   B 1 77  ? 39.252 -12.002 14.458 1.00 27.72 ? 83  PHE   C O   1 
ATOM   1701 C  CB  . PHE   B 1 77  ? 40.321 -9.409  15.747 1.00 25.16 ? 83  PHE   C CB  1 
ATOM   1702 C  CG  . PHE   B 1 77  ? 40.074 -8.266  14.787 1.00 26.78 ? 83  PHE   C CG  1 
ATOM   1703 C  CD1 . PHE   B 1 77  ? 39.426 -7.116  15.212 1.00 27.19 ? 83  PHE   C CD1 1 
ATOM   1704 C  CD2 . PHE   B 1 77  ? 40.425 -8.371  13.440 1.00 28.31 ? 83  PHE   C CD2 1 
ATOM   1705 C  CE1 . PHE   B 1 77  ? 39.163 -6.076  14.321 1.00 28.59 ? 83  PHE   C CE1 1 
ATOM   1706 C  CE2 . PHE   B 1 77  ? 40.158 -7.333  12.555 1.00 29.07 ? 83  PHE   C CE2 1 
ATOM   1707 C  CZ  . PHE   B 1 77  ? 39.545 -6.197  13.000 1.00 29.17 ? 83  PHE   C CZ  1 
ATOM   1708 N  N   . VAL   B 1 78  ? 37.521 -10.593 14.170 1.00 22.42 ? 84  VAL   C N   1 
ATOM   1709 C  CA  . VAL   B 1 78  ? 36.963 -11.299 13.028 1.00 22.36 ? 84  VAL   C CA  1 
ATOM   1710 C  C   . VAL   B 1 78  ? 37.054 -10.358 11.822 1.00 22.40 ? 84  VAL   C C   1 
ATOM   1711 O  O   . VAL   B 1 78  ? 36.572 -9.228  11.915 1.00 22.58 ? 84  VAL   C O   1 
ATOM   1712 C  CB  . VAL   B 1 78  ? 35.474 -11.648 13.344 1.00 23.23 ? 84  VAL   C CB  1 
ATOM   1713 C  CG1 . VAL   B 1 78  ? 34.858 -12.405 12.180 1.00 24.30 ? 84  VAL   C CG1 1 
ATOM   1714 C  CG2 . VAL   B 1 78  ? 35.346 -12.478 14.605 1.00 23.18 ? 84  VAL   C CG2 1 
ATOM   1715 N  N   . GLU   B 1 79  ? 37.575 -10.837 10.681 1.00 21.81 ? 85  GLU   C N   1 
ATOM   1716 C  CA  . GLU   B 1 79  ? 37.592 -9.996  9.471  1.00 22.69 ? 85  GLU   C CA  1 
ATOM   1717 C  C   . GLU   B 1 79  ? 36.175 -9.746  8.943  1.00 22.92 ? 85  GLU   C C   1 
ATOM   1718 O  O   . GLU   B 1 79  ? 35.214 -10.423 9.327  1.00 22.85 ? 85  GLU   C O   1 
ATOM   1719 C  CB  . GLU   B 1 79  ? 38.449 -10.636 8.362  1.00 24.60 ? 85  GLU   C CB  1 
ATOM   1720 C  CG  . GLU   B 1 79  ? 39.931 -10.702 8.708  1.00 31.06 ? 85  GLU   C CG  1 
ATOM   1721 C  CD  . GLU   B 1 79  ? 40.556 -9.360  9.048  1.00 39.78 ? 85  GLU   C CD  1 
ATOM   1722 O  OE1 . GLU   B 1 79  ? 40.271 -8.358  8.349  1.00 42.38 ? 85  GLU   C OE1 1 
ATOM   1723 O  OE2 . GLU   B 1 79  ? 41.328 -9.308  10.030 1.00 39.65 ? 85  GLU   C OE2 1 
ATOM   1724 N  N   . ALA   B 1 80  ? 36.004 -8.732  8.099  1.00 23.47 ? 86  ALA   C N   1 
ATOM   1725 C  CA  . ALA   B 1 80  ? 34.711 -8.379  7.539  1.00 24.01 ? 86  ALA   C CA  1 
ATOM   1726 C  C   . ALA   B 1 80  ? 34.096 -9.557  6.805  1.00 25.59 ? 86  ALA   C C   1 
ATOM   1727 O  O   . ALA   B 1 80  ? 34.799 -10.348 6.170  1.00 27.12 ? 86  ALA   C O   1 
ATOM   1728 C  CB  . ALA   B 1 80  ? 34.892 -7.187  6.579  1.00 24.64 ? 86  ALA   C CB  1 
ATOM   1729 N  N   . SER   B 1 81  ? 32.779 -9.714  6.978  1.00 25.52 ? 87  SER   C N   1 
ATOM   1730 C  CA  . SER   B 1 81  ? 32.033 -10.769 6.319  1.00 25.77 ? 87  SER   C CA  1 
ATOM   1731 C  C   . SER   B 1 81  ? 30.897 -10.129 5.535  1.00 26.41 ? 87  SER   C C   1 
ATOM   1732 O  O   . SER   B 1 81  ? 30.790 -8.904  5.525  1.00 25.73 ? 87  SER   C O   1 
ATOM   1733 C  CB  . SER   B 1 81  ? 31.511 -11.749 7.368  1.00 25.82 ? 87  SER   C CB  1 
ATOM   1734 O  OG  . SER   B 1 81  ? 30.501 -11.089 8.119  1.00 26.32 ? 87  SER   C OG  1 
ATOM   1735 N  N   . GLU   B 1 82  ? 30.047 -10.927 4.866  1.00 28.34 ? 88  GLU   C N   1 
ATOM   1736 C  CA  . GLU   B 1 82  ? 28.939 -10.305 4.135  1.00 30.27 ? 88  GLU   C CA  1 
ATOM   1737 C  C   . GLU   B 1 82  ? 27.906 -9.649  5.079  1.00 30.41 ? 88  GLU   C C   1 
ATOM   1738 O  O   . GLU   B 1 82  ? 27.129 -8.797  4.646  1.00 31.51 ? 88  GLU   C O   1 
ATOM   1739 C  CB  . GLU   B 1 82  ? 28.290 -11.294 3.151  1.00 34.97 ? 88  GLU   C CB  1 
ATOM   1740 C  CG  . GLU   B 1 82  ? 27.551 -12.455 3.781  1.00 41.29 ? 88  GLU   C CG  1 
ATOM   1741 C  CD  . GLU   B 1 82  ? 26.792 -13.255 2.739  1.00 47.41 ? 88  GLU   C CD  1 
ATOM   1742 O  OE1 . GLU   B 1 82  ? 27.337 -13.430 1.624  1.00 49.68 ? 88  GLU   C OE1 1 
ATOM   1743 O  OE2 . GLU   B 1 82  ? 25.650 -13.686 3.027  1.00 47.47 ? 88  GLU   C OE2 1 
ATOM   1744 N  N   . TYR   B 1 83  ? 27.943 -9.983  6.383  1.00 27.78 ? 89  TYR   C N   1 
ATOM   1745 C  CA  . TYR   B 1 83  ? 26.925 -9.504  7.304  1.00 26.61 ? 89  TYR   C CA  1 
ATOM   1746 C  C   . TYR   B 1 83  ? 27.444 -8.614  8.458  1.00 26.21 ? 89  TYR   C C   1 
ATOM   1747 O  O   . TYR   B 1 83  ? 26.604 -8.043  9.169  1.00 27.48 ? 89  TYR   C O   1 
ATOM   1748 C  CB  . TYR   B 1 83  ? 26.084 -10.710 7.841  1.00 25.09 ? 89  TYR   C CB  1 
ATOM   1749 C  CG  . TYR   B 1 83  ? 26.915 -11.915 8.261  1.00 24.80 ? 89  TYR   C CG  1 
ATOM   1750 C  CD1 . TYR   B 1 83  ? 27.275 -12.906 7.340  1.00 25.14 ? 89  TYR   C CD1 1 
ATOM   1751 C  CD2 . TYR   B 1 83  ? 27.406 -12.030 9.555  1.00 24.15 ? 89  TYR   C CD2 1 
ATOM   1752 C  CE1 . TYR   B 1 83  ? 28.059 -13.995 7.719  1.00 23.81 ? 89  TYR   C CE1 1 
ATOM   1753 C  CE2 . TYR   B 1 83  ? 28.185 -13.110 9.943  1.00 25.19 ? 89  TYR   C CE2 1 
ATOM   1754 C  CZ  . TYR   B 1 83  ? 28.522 -14.092 9.023  1.00 24.36 ? 89  TYR   C CZ  1 
ATOM   1755 O  OH  . TYR   B 1 83  ? 29.327 -15.150 9.428  1.00 24.20 ? 89  TYR   C OH  1 
ATOM   1756 N  N   . TYR   B 1 84  ? 28.783 -8.506  8.684  1.00 24.21 ? 90  TYR   C N   1 
ATOM   1757 C  CA  . TYR   B 1 84  ? 29.326 -7.614  9.713  1.00 23.46 ? 90  TYR   C CA  1 
ATOM   1758 C  C   . TYR   B 1 84  ? 30.657 -7.003  9.178  1.00 23.71 ? 90  TYR   C C   1 
ATOM   1759 O  O   . TYR   B 1 84  ? 31.391 -7.664  8.423  1.00 22.79 ? 90  TYR   C O   1 
ATOM   1760 C  CB  . TYR   B 1 84  ? 29.690 -8.395  11.017 1.00 22.28 ? 90  TYR   C CB  1 
ATOM   1761 C  CG  . TYR   B 1 84  ? 28.514 -8.825  11.880 1.00 20.54 ? 90  TYR   C CG  1 
ATOM   1762 C  CD1 . TYR   B 1 84  ? 27.645 -7.890  12.427 1.00 20.53 ? 90  TYR   C CD1 1 
ATOM   1763 C  CD2 . TYR   B 1 84  ? 28.330 -10.150 12.215 1.00 19.58 ? 90  TYR   C CD2 1 
ATOM   1764 C  CE1 . TYR   B 1 84  ? 26.606 -8.274  13.272 1.00 20.09 ? 90  TYR   C CE1 1 
ATOM   1765 C  CE2 . TYR   B 1 84  ? 27.258 -10.559 13.003 1.00 19.44 ? 90  TYR   C CE2 1 
ATOM   1766 C  CZ  . TYR   B 1 84  ? 26.398 -9.620  13.543 1.00 20.44 ? 90  TYR   C CZ  1 
ATOM   1767 O  OH  . TYR   B 1 84  ? 25.320 -10.047 14.318 1.00 20.22 ? 90  TYR   C OH  1 
ATOM   1768 N  N   . PRO   B 1 85  ? 31.042 -5.827  9.681  1.00 24.94 ? 91  PRO   C N   1 
ATOM   1769 C  CA  . PRO   B 1 85  ? 32.380 -5.306  9.356  1.00 25.06 ? 91  PRO   C CA  1 
ATOM   1770 C  C   . PRO   B 1 85  ? 33.448 -6.064  10.177 1.00 24.37 ? 91  PRO   C C   1 
ATOM   1771 O  O   . PRO   B 1 85  ? 33.118 -6.921  11.031 1.00 24.06 ? 91  PRO   C O   1 
ATOM   1772 C  CB  . PRO   B 1 85  ? 32.265 -3.846  9.808  1.00 26.58 ? 91  PRO   C CB  1 
ATOM   1773 C  CG  . PRO   B 1 85  ? 31.415 -3.953  11.067 1.00 26.93 ? 91  PRO   C CG  1 
ATOM   1774 C  CD  . PRO   B 1 85  ? 30.345 -4.973  10.679 1.00 25.25 ? 91  PRO   C CD  1 
ATOM   1775 N  N   . ALA   B 1 86  ? 34.725 -5.742  9.967  1.00 23.83 ? 92  ALA   C N   1 
ATOM   1776 C  CA  . ALA   B 1 86  ? 35.799 -6.301  10.794 1.00 24.70 ? 92  ALA   C CA  1 
ATOM   1777 C  C   . ALA   B 1 86  ? 35.616 -5.754  12.231 1.00 24.94 ? 92  ALA   C C   1 
ATOM   1778 O  O   . ALA   B 1 86  ? 35.357 -4.564  12.408 1.00 26.24 ? 92  ALA   C O   1 
ATOM   1779 C  CB  . ALA   B 1 86  ? 37.168 -5.901  10.251 1.00 25.31 ? 92  ALA   C CB  1 
ATOM   1780 N  N   . ARG   B 1 87  ? 35.599 -6.658  13.208 1.00 23.65 ? 93  ARG   C N   1 
ATOM   1781 C  CA  . ARG   B 1 87  ? 35.344 -6.271  14.579 1.00 24.37 ? 93  ARG   C CA  1 
ATOM   1782 C  C   . ARG   B 1 87  ? 35.720 -7.361  15.557 1.00 23.94 ? 93  ARG   C C   1 
ATOM   1783 O  O   . ARG   B 1 87  ? 35.977 -8.506  15.166 1.00 22.46 ? 93  ARG   C O   1 
ATOM   1784 C  CB  . ARG   B 1 87  ? 33.829 -5.949  14.745 1.00 24.43 ? 93  ARG   C CB  1 
ATOM   1785 C  CG  . ARG   B 1 87  ? 32.959 -7.209  14.625 1.00 24.02 ? 93  ARG   C CG  1 
ATOM   1786 C  CD  . ARG   B 1 87  ? 31.473 -6.968  14.792 1.00 23.54 ? 93  ARG   C CD  1 
ATOM   1787 N  NE  . ARG   B 1 87  ? 30.796 -8.251  15.009 1.00 24.82 ? 93  ARG   C NE  1 
ATOM   1788 C  CZ  . ARG   B 1 87  ? 29.706 -8.435  15.745 1.00 26.98 ? 93  ARG   C CZ  1 
ATOM   1789 N  NH1 . ARG   B 1 87  ? 29.112 -7.403  16.337 1.00 24.01 ? 93  ARG   C NH1 1 
ATOM   1790 N  NH2 . ARG   B 1 87  ? 29.212 -9.657  15.912 1.00 27.51 ? 93  ARG   C NH2 1 
ATOM   1791 N  N   . TYR   B 1 88  ? 35.606 -7.044  16.874 1.00 25.33 ? 94  TYR   C N   1 
ATOM   1792 C  CA  . TYR   B 1 88  ? 35.796 -8.082  17.896 1.00 26.26 ? 94  TYR   C CA  1 
ATOM   1793 C  C   . TYR   B 1 88  ? 34.461 -8.704  18.198 1.00 24.09 ? 94  TYR   C C   1 
ATOM   1794 O  O   . TYR   B 1 88  ? 33.462 -7.998  18.376 1.00 25.56 ? 94  TYR   C O   1 
ATOM   1795 C  CB  . TYR   B 1 88  ? 36.348 -7.497  19.227 1.00 29.38 ? 94  TYR   C CB  1 
ATOM   1796 C  CG  . TYR   B 1 88  ? 37.794 -7.134  19.098 1.00 34.72 ? 94  TYR   C CG  1 
ATOM   1797 C  CD1 . TYR   B 1 88  ? 38.788 -8.071  19.334 1.00 37.61 ? 94  TYR   C CD1 1 
ATOM   1798 C  CD2 . TYR   B 1 88  ? 38.169 -5.877  18.634 1.00 37.83 ? 94  TYR   C CD2 1 
ATOM   1799 C  CE1 . TYR   B 1 88  ? 40.126 -7.744  19.172 1.00 39.67 ? 94  TYR   C CE1 1 
ATOM   1800 C  CE2 . TYR   B 1 88  ? 39.493 -5.540  18.468 1.00 39.96 ? 94  TYR   C CE2 1 
ATOM   1801 C  CZ  . TYR   B 1 88  ? 40.469 -6.474  18.727 1.00 41.87 ? 94  TYR   C CZ  1 
ATOM   1802 O  OH  . TYR   B 1 88  ? 41.750 -6.045  18.508 1.00 45.38 ? 94  TYR   C OH  1 
ATOM   1803 N  N   . GLN   B 1 89  ? 34.434 -10.021 18.237 1.00 22.18 ? 95  GLN   C N   1 
ATOM   1804 C  CA  . GLN   B 1 89  ? 33.211 -10.736 18.632 1.00 21.16 ? 95  GLN   C CA  1 
ATOM   1805 C  C   . GLN   B 1 89  ? 33.560 -11.460 19.926 1.00 20.21 ? 95  GLN   C C   1 
ATOM   1806 O  O   . GLN   B 1 89  ? 34.643 -12.034 20.039 1.00 20.60 ? 95  GLN   C O   1 
ATOM   1807 C  CB  . GLN   B 1 89  ? 32.791 -11.724 17.522 1.00 22.20 ? 95  GLN   C CB  1 
ATOM   1808 C  CG  . GLN   B 1 89  ? 31.526 -12.493 17.826 1.00 21.32 ? 95  GLN   C CG  1 
ATOM   1809 C  CD  . GLN   B 1 89  ? 30.855 -13.070 16.596 1.00 22.25 ? 95  GLN   C CD  1 
ATOM   1810 O  OE1 . GLN   B 1 89  ? 30.799 -12.439 15.500 1.00 21.37 ? 95  GLN   C OE1 1 
ATOM   1811 N  NE2 . GLN   B 1 89  ? 30.319 -14.249 16.779 1.00 20.35 ? 95  GLN   C NE2 1 
ATOM   1812 N  N   . SER   B 1 90  ? 32.639 -11.449 20.892 1.00 19.29 ? 96  SER   C N   1 
ATOM   1813 C  CA  . SER   B 1 90  ? 32.891 -12.088 22.173 1.00 19.35 ? 96  SER   C CA  1 
ATOM   1814 C  C   . SER   B 1 90  ? 32.253 -13.499 22.233 1.00 18.59 ? 96  SER   C C   1 
ATOM   1815 O  O   . SER   B 1 90  ? 31.395 -13.844 21.409 1.00 18.77 ? 96  SER   C O   1 
ATOM   1816 C  CB  . SER   B 1 90  ? 32.386 -11.214 23.332 1.00 21.62 ? 96  SER   C CB  1 
ATOM   1817 O  OG  . SER   B 1 90  ? 30.976 -11.139 23.270 1.00 22.34 ? 96  SER   C OG  1 
ATOM   1818 N  N   . HIS   B 1 91  ? 32.712 -14.293 23.227 1.00 17.87 ? 97  HIS   C N   1 
ATOM   1819 C  CA  . HIS   B 1 91  ? 32.237 -15.646 23.493 1.00 17.58 ? 97  HIS   C CA  1 
ATOM   1820 C  C   . HIS   B 1 91  ? 32.331 -16.523 22.228 1.00 17.91 ? 97  HIS   C C   1 
ATOM   1821 O  O   . HIS   B 1 91  ? 31.460 -17.345 21.988 1.00 17.74 ? 97  HIS   C O   1 
ATOM   1822 C  CB  . HIS   B 1 91  ? 30.805 -15.633 24.070 1.00 19.02 ? 97  HIS   C CB  1 
ATOM   1823 C  CG  . HIS   B 1 91  ? 30.700 -14.880 25.375 1.00 22.52 ? 97  HIS   C CG  1 
ATOM   1824 N  ND1 . HIS   B 1 91  ? 30.742 -15.541 26.607 1.00 24.80 ? 97  HIS   C ND1 1 
ATOM   1825 C  CD2 . HIS   B 1 91  ? 30.562 -13.534 25.600 1.00 24.05 ? 97  HIS   C CD2 1 
ATOM   1826 C  CE1 . HIS   B 1 91  ? 30.604 -14.593 27.537 1.00 25.22 ? 97  HIS   C CE1 1 
ATOM   1827 N  NE2 . HIS   B 1 91  ? 30.479 -13.364 26.980 1.00 25.11 ? 97  HIS   C NE2 1 
ATOM   1828 N  N   . LEU   B 1 92  ? 33.387 -16.331 21.441 1.00 17.20 ? 98  LEU   C N   1 
ATOM   1829 C  CA  . LEU   B 1 92  ? 33.600 -17.048 20.179 1.00 17.22 ? 98  LEU   C CA  1 
ATOM   1830 C  C   . LEU   B 1 92  ? 34.680 -18.126 20.351 1.00 16.76 ? 98  LEU   C C   1 
ATOM   1831 O  O   . LEU   B 1 92  ? 35.679 -17.924 21.043 1.00 17.70 ? 98  LEU   C O   1 
ATOM   1832 C  CB  . LEU   B 1 92  ? 34.052 -16.023 19.064 1.00 18.80 ? 98  LEU   C CB  1 
ATOM   1833 C  CG  . LEU   B 1 92  ? 34.115 -16.566 17.636 1.00 19.53 ? 98  LEU   C CG  1 
ATOM   1834 C  CD1 . LEU   B 1 92  ? 32.729 -16.935 17.105 1.00 19.94 ? 98  LEU   C CD1 1 
ATOM   1835 C  CD2 . LEU   B 1 92  ? 34.761 -15.532 16.684 1.00 20.39 ? 98  LEU   C CD2 1 
ATOM   1836 N  N   . MET   B 1 93  ? 34.445 -19.297 19.746 1.00 16.16 ? 99  MET   C N   1 
ATOM   1837 C  CA  . MET   B 1 93  ? 35.405 -20.418 19.791 1.00 15.30 ? 99  MET   C CA  1 
ATOM   1838 C  C   . MET   B 1 93  ? 35.792 -20.735 18.344 1.00 15.43 ? 99  MET   C C   1 
ATOM   1839 O  O   . MET   B 1 93  ? 34.905 -20.767 17.511 1.00 17.31 ? 99  MET   C O   1 
ATOM   1840 C  CB  . MET   B 1 93  ? 34.684 -21.662 20.382 1.00 17.49 ? 99  MET   C CB  1 
ATOM   1841 C  CG  . MET   B 1 93  ? 34.187 -21.356 21.759 1.00 18.07 ? 99  MET   C CG  1 
ATOM   1842 S  SD  . MET   B 1 93  ? 33.182 -22.684 22.438 1.00 19.91 ? 99  MET   C SD  1 
ATOM   1843 C  CE  . MET   B 1 93  ? 31.891 -22.692 21.466 1.00 19.26 ? 99  MET   C CE  1 
ATOM   1844 N  N   . LEU   B 1 94  ? 37.049 -21.016 18.065 1.00 14.96 ? 100 LEU   C N   1 
ATOM   1845 C  CA  . LEU   B 1 94  ? 37.456 -21.313 16.693 1.00 16.58 ? 100 LEU   C CA  1 
ATOM   1846 C  C   . LEU   B 1 94  ? 37.901 -22.753 16.549 1.00 16.31 ? 100 LEU   C C   1 
ATOM   1847 O  O   . LEU   B 1 94  ? 38.458 -23.349 17.453 1.00 17.29 ? 100 LEU   C O   1 
ATOM   1848 C  CB  . LEU   B 1 94  ? 38.699 -20.448 16.323 1.00 18.08 ? 100 LEU   C CB  1 
ATOM   1849 C  CG  . LEU   B 1 94  ? 38.534 -18.958 16.282 1.00 20.85 ? 100 LEU   C CG  1 
ATOM   1850 C  CD1 . LEU   B 1 94  ? 39.867 -18.296 15.886 1.00 24.45 ? 100 LEU   C CD1 1 
ATOM   1851 C  CD2 . LEU   B 1 94  ? 37.333 -18.543 15.386 1.00 22.56 ? 100 LEU   C CD2 1 
ATOM   1852 N  N   . ALA   B 1 95  ? 37.725 -23.284 15.332 1.00 16.87 ? 101 ALA   C N   1 
ATOM   1853 C  CA  . ALA   B 1 95  ? 38.277 -24.589 14.941 1.00 16.92 ? 101 ALA   C CA  1 
ATOM   1854 C  C   . ALA   B 1 95  ? 38.867 -24.482 13.541 1.00 17.45 ? 101 ALA   C C   1 
ATOM   1855 O  O   . ALA   B 1 95  ? 38.530 -23.548 12.826 1.00 17.46 ? 101 ALA   C O   1 
ATOM   1856 C  CB  . ALA   B 1 95  ? 37.178 -25.656 14.930 1.00 17.68 ? 101 ALA   C CB  1 
ATOM   1857 N  N   . VAL   B 1 96  ? 39.728 -25.424 13.134 1.00 17.41 ? 102 VAL   C N   1 
ATOM   1858 C  CA  . VAL   B 1 96  ? 40.194 -25.458 11.753 1.00 19.19 ? 102 VAL   C CA  1 
ATOM   1859 C  C   . VAL   B 1 96  ? 39.120 -26.182 10.961 1.00 19.39 ? 102 VAL   C C   1 
ATOM   1860 O  O   . VAL   B 1 96  ? 38.803 -27.363 11.245 1.00 20.67 ? 102 VAL   C O   1 
ATOM   1861 C  CB  . VAL   B 1 96  ? 41.548 -26.184 11.675 1.00 19.92 ? 102 VAL   C CB  1 
ATOM   1862 C  CG1 . VAL   B 1 96  ? 41.978 -26.328 10.210 1.00 21.13 ? 102 VAL   C CG1 1 
ATOM   1863 C  CG2 . VAL   B 1 96  ? 42.598 -25.459 12.513 1.00 20.05 ? 102 VAL   C CG2 1 
ATOM   1864 N  N   . GLY   B 1 97  ? 38.527 -25.480 9.998  1.00 21.02 ? 103 GLY   C N   1 
ATOM   1865 C  CA  . GLY   B 1 97  ? 37.469 -26.095 9.216  1.00 21.05 ? 103 GLY   C CA  1 
ATOM   1866 C  C   . GLY   B 1 97  ? 36.788 -25.136 8.298  1.00 22.00 ? 103 GLY   C C   1 
ATOM   1867 O  O   . GLY   B 1 97  ? 37.051 -23.930 8.307  1.00 24.19 ? 103 GLY   C O   1 
ATOM   1868 N  N   . HIS   B 1 98  ? 35.926 -25.689 7.475  1.00 21.70 ? 104 HIS   C N   1 
ATOM   1869 C  CA  . HIS   B 1 98  ? 35.223 -24.932 6.457  1.00 21.69 ? 104 HIS   C CA  1 
ATOM   1870 C  C   . HIS   B 1 98  ? 33.968 -24.253 6.983  1.00 22.23 ? 104 HIS   C C   1 
ATOM   1871 O  O   . HIS   B 1 98  ? 33.180 -24.895 7.702  1.00 22.00 ? 104 HIS   C O   1 
ATOM   1872 C  CB  . HIS   B 1 98  ? 34.801 -25.873 5.333  1.00 22.29 ? 104 HIS   C CB  1 
ATOM   1873 C  CG  . HIS   B 1 98  ? 34.295 -25.103 4.164  1.00 25.98 ? 104 HIS   C CG  1 
ATOM   1874 N  ND1 . HIS   B 1 98  ? 35.088 -24.140 3.524  1.00 28.44 ? 104 HIS   C ND1 1 
ATOM   1875 C  CD2 . HIS   B 1 98  ? 33.063 -25.097 3.614  1.00 28.46 ? 104 HIS   C CD2 1 
ATOM   1876 C  CE1 . HIS   B 1 98  ? 34.311 -23.593 2.605  1.00 30.56 ? 104 HIS   C CE1 1 
ATOM   1877 N  NE2 . HIS   B 1 98  ? 33.089 -24.163 2.598  1.00 30.78 ? 104 HIS   C NE2 1 
ATOM   1878 N  N   . SER   B 1 99  ? 33.703 -22.988 6.544  1.00 22.00 ? 105 SER   C N   1 
ATOM   1879 C  CA  . SER   B 1 99  ? 32.485 -22.242 6.946  1.00 22.25 ? 105 SER   C CA  1 
ATOM   1880 C  C   . SER   B 1 99  ? 32.208 -21.090 5.940  1.00 23.19 ? 105 SER   C C   1 
ATOM   1881 O  O   . SER   B 1 99  ? 33.012 -20.162 5.848  1.00 25.24 ? 105 SER   C O   1 
ATOM   1882 C  CB  . SER   B 1 99  ? 32.738 -21.593 8.304  1.00 22.96 ? 105 SER   C CB  1 
ATOM   1883 O  OG  . SER   B 1 99  ? 31.610 -20.843 8.752  1.00 26.94 ? 105 SER   C OG  1 
ATOM   1884 N  N   . GLU   B 1 100 ? 31.114 -21.195 5.164  1.00 21.53 ? 106 GLU   C N   1 
ATOM   1885 C  CA  . GLU   B 1 100 ? 30.637 -20.162 4.224  1.00 20.36 ? 106 GLU   C CA  1 
ATOM   1886 C  C   . GLU   B 1 100 ? 29.537 -19.396 4.999  1.00 20.26 ? 106 GLU   C C   1 
ATOM   1887 O  O   . GLU   B 1 100 ? 28.976 -19.917 5.977  1.00 20.44 ? 106 GLU   C O   1 
ATOM   1888 C  CB  . GLU   B 1 100 ? 29.934 -20.823 2.999  1.00 22.99 ? 106 GLU   C CB  1 
ATOM   1889 C  CG  . GLU   B 1 100 ? 30.748 -21.794 2.196  1.00 29.68 ? 106 GLU   C CG  1 
ATOM   1890 C  CD  . GLU   B 1 100 ? 31.623 -21.184 1.143  1.00 35.86 ? 106 GLU   C CD  1 
ATOM   1891 O  OE1 . GLU   B 1 100 ? 32.270 -21.949 0.397  1.00 38.69 ? 106 GLU   C OE1 1 
ATOM   1892 O  OE2 . GLU   B 1 100 ? 31.665 -19.938 1.077  1.00 35.76 ? 106 GLU   C OE2 1 
ATOM   1893 N  N   . PRO   B 1 101 ? 29.138 -18.207 4.541  1.00 20.36 ? 107 PRO   C N   1 
ATOM   1894 C  CA  . PRO   B 1 101 ? 28.057 -17.468 5.239  1.00 20.30 ? 107 PRO   C CA  1 
ATOM   1895 C  C   . PRO   B 1 101 ? 26.793 -18.288 5.471  1.00 21.19 ? 107 PRO   C C   1 
ATOM   1896 O  O   . PRO   B 1 101 ? 26.200 -18.193 6.549  1.00 22.27 ? 107 PRO   C O   1 
ATOM   1897 C  CB  . PRO   B 1 101 ? 27.785 -16.262 4.300  1.00 23.03 ? 107 PRO   C CB  1 
ATOM   1898 C  CG  . PRO   B 1 101 ? 29.026 -16.123 3.483  1.00 24.90 ? 107 PRO   C CG  1 
ATOM   1899 C  CD  . PRO   B 1 101 ? 29.739 -17.431 3.416  1.00 21.86 ? 107 PRO   C CD  1 
ATOM   1900 N  N   . GLY   B 1 102 ? 26.355 -19.086 4.489  1.00 19.65 ? 108 GLY   C N   1 
ATOM   1901 C  CA  . GLY   B 1 102 ? 25.143 -19.892 4.655  1.00 19.16 ? 108 GLY   C CA  1 
ATOM   1902 C  C   . GLY   B 1 102 ? 25.232 -21.003 5.681  1.00 18.53 ? 108 GLY   C C   1 
ATOM   1903 O  O   . GLY   B 1 102 ? 24.232 -21.688 5.971  1.00 20.10 ? 108 GLY   C O   1 
ATOM   1904 N  N   . ASP   B 1 103 ? 26.465 -21.287 6.146  1.00 18.49 ? 109 ASP   C N   1 
ATOM   1905 C  CA  . ASP   B 1 103 ? 26.652 -22.308 7.173  1.00 18.05 ? 109 ASP   C CA  1 
ATOM   1906 C  C   . ASP   B 1 103 ? 26.286 -21.819 8.563  1.00 16.96 ? 109 ASP   C C   1 
ATOM   1907 O  O   . ASP   B 1 103 ? 26.161 -22.633 9.495  1.00 17.06 ? 109 ASP   C O   1 
ATOM   1908 C  CB  . ASP   B 1 103 ? 28.098 -22.831 7.218  1.00 18.70 ? 109 ASP   C CB  1 
ATOM   1909 C  CG  . ASP   B 1 103 ? 28.423 -23.633 6.000  1.00 20.60 ? 109 ASP   C CG  1 
ATOM   1910 O  OD1 . ASP   B 1 103 ? 27.579 -24.367 5.556  1.00 21.83 ? 109 ASP   C OD1 1 
ATOM   1911 O  OD2 . ASP   B 1 103 ? 29.531 -23.498 5.484  1.00 21.99 ? 109 ASP   C OD2 1 
ATOM   1912 N  N   . CYS   B 1 104 ? 26.091 -20.498 8.755  1.00 16.50 ? 110 CYS   C N   1 
ATOM   1913 C  CA  . CYS   B 1 104 ? 25.724 -19.945 10.082 1.00 16.97 ? 110 CYS   C CA  1 
ATOM   1914 C  C   . CYS   B 1 104 ? 24.472 -20.624 10.605 1.00 17.63 ? 110 CYS   C C   1 
ATOM   1915 O  O   . CYS   B 1 104 ? 23.535 -20.836 9.827  1.00 18.75 ? 110 CYS   C O   1 
ATOM   1916 C  CB  . CYS   B 1 104 ? 25.523 -18.435 9.990  1.00 18.19 ? 110 CYS   C CB  1 
ATOM   1917 S  SG  . CYS   B 1 104 ? 27.063 -17.499 9.906  1.00 19.77 ? 110 CYS   C SG  1 
ATOM   1918 N  N   . GLY   B 1 105 ? 24.490 -21.000 11.865 1.00 15.48 ? 111 GLY   C N   1 
ATOM   1919 C  CA  . GLY   B 1 105 ? 23.318 -21.675 12.433 1.00 16.49 ? 111 GLY   C CA  1 
ATOM   1920 C  C   . GLY   B 1 105 ? 23.539 -23.165 12.640 1.00 17.00 ? 111 GLY   C C   1 
ATOM   1921 O  O   . GLY   B 1 105 ? 22.768 -23.807 13.347 1.00 17.94 ? 111 GLY   C O   1 
ATOM   1922 N  N   . GLY   B 1 106 ? 24.547 -23.741 11.947 1.00 17.31 ? 112 GLY   C N   1 
ATOM   1923 C  CA  . GLY   B 1 106 ? 24.865 -25.168 12.130 1.00 16.65 ? 112 GLY   C CA  1 
ATOM   1924 C  C   . GLY   B 1 106 ? 25.248 -25.469 13.564 1.00 15.90 ? 112 GLY   C C   1 
ATOM   1925 O  O   . GLY   B 1 106 ? 25.970 -24.676 14.189 1.00 16.05 ? 112 GLY   C O   1 
ATOM   1926 N  N   . ILE   B 1 107 ? 24.782 -26.588 14.115 1.00 15.17 ? 113 ILE   C N   1 
ATOM   1927 C  CA  . ILE   B 1 107 ? 25.099 -26.896 15.514 1.00 15.52 ? 113 ILE   C CA  1 
ATOM   1928 C  C   . ILE   B 1 107 ? 26.448 -27.528 15.713 1.00 15.23 ? 113 ILE   C C   1 
ATOM   1929 O  O   . ILE   B 1 107 ? 26.851 -28.431 14.967 1.00 15.73 ? 113 ILE   C O   1 
ATOM   1930 C  CB  . ILE   B 1 107 ? 23.929 -27.800 16.081 1.00 18.57 ? 113 ILE   C CB  1 
ATOM   1931 C  CG1 . ILE   B 1 107 ? 22.716 -26.838 16.500 1.00 22.97 ? 113 ILE   C CG1 1 
ATOM   1932 C  CG2 . ILE   B 1 107 ? 24.394 -28.664 17.291 1.00 18.61 ? 113 ILE   C CG2 1 
ATOM   1933 C  CD1 . ILE   B 1 107 ? 21.360 -27.548 16.863 1.00 27.38 ? 113 ILE   C CD1 1 
ATOM   1934 N  N   . LEU   B 1 108 ? 27.130 -27.110 16.808 1.00 14.26 ? 114 LEU   C N   1 
ATOM   1935 C  CA  . LEU   B 1 108 ? 28.298 -27.789 17.331 1.00 13.34 ? 114 LEU   C CA  1 
ATOM   1936 C  C   . LEU   B 1 108 ? 27.809 -28.547 18.599 1.00 14.99 ? 114 LEU   C C   1 
ATOM   1937 O  O   . LEU   B 1 108 ? 27.195 -27.946 19.455 1.00 14.21 ? 114 LEU   C O   1 
ATOM   1938 C  CB  . LEU   B 1 108 ? 29.380 -26.761 17.710 1.00 14.62 ? 114 LEU   C CB  1 
ATOM   1939 C  CG  . LEU   B 1 108 ? 30.548 -27.277 18.518 1.00 15.75 ? 114 LEU   C CG  1 
ATOM   1940 C  CD1 . LEU   B 1 108 ? 31.443 -28.221 17.657 1.00 15.86 ? 114 LEU   C CD1 1 
ATOM   1941 C  CD2 . LEU   B 1 108 ? 31.403 -26.113 19.044 1.00 16.63 ? 114 LEU   C CD2 1 
ATOM   1942 N  N   . ARG   B 1 109 ? 28.091 -29.823 18.660 1.00 15.11 ? 115 ARG   C N   1 
ATOM   1943 C  CA  . ARG   B 1 109 ? 27.673 -30.654 19.806 1.00 17.10 ? 115 ARG   C CA  1 
ATOM   1944 C  C   . ARG   B 1 109 ? 28.799 -31.501 20.356 1.00 17.45 ? 115 ARG   C C   1 
ATOM   1945 O  O   . ARG   B 1 109 ? 29.719 -31.974 19.640 1.00 16.38 ? 115 ARG   C O   1 
ATOM   1946 C  CB  . ARG   B 1 109 ? 26.482 -31.520 19.398 1.00 20.19 ? 115 ARG   C CB  1 
ATOM   1947 C  CG  . ARG   B 1 109 ? 26.820 -32.565 18.393 1.00 25.96 ? 115 ARG   C CG  1 
ATOM   1948 C  CD  . ARG   B 1 109 ? 25.589 -33.377 17.966 1.00 33.81 ? 115 ARG   C CD  1 
ATOM   1949 N  NE  . ARG   B 1 109 ? 24.649 -32.636 17.115 1.00 40.44 ? 115 ARG   C NE  1 
ATOM   1950 C  CZ  . ARG   B 1 109 ? 23.392 -32.336 17.471 1.00 46.86 ? 115 ARG   C CZ  1 
ATOM   1951 N  NH1 . ARG   B 1 109 ? 22.935 -32.670 18.679 1.00 46.15 ? 115 ARG   C NH1 1 
ATOM   1952 N  NH2 . ARG   B 1 109 ? 22.604 -31.656 16.643 1.00 47.74 ? 115 ARG   C NH2 1 
ATOM   1953 N  N   . CYS   B 1 110 ? 28.684 -31.775 21.666 1.00 16.67 ? 116 CYS   C N   1 
ATOM   1954 C  CA  . CYS   B 1 110 ? 29.624 -32.657 22.366 1.00 16.66 ? 116 CYS   C CA  1 
ATOM   1955 C  C   . CYS   B 1 110 ? 28.818 -33.758 23.075 1.00 18.41 ? 116 CYS   C C   1 
ATOM   1956 O  O   . CYS   B 1 110 ? 27.614 -33.829 22.862 1.00 18.82 ? 116 CYS   C O   1 
ATOM   1957 C  CB  . CYS   B 1 110 ? 30.475 -31.869 23.352 1.00 16.80 ? 116 CYS   C CB  1 
ATOM   1958 S  SG  . CYS   B 1 110 ? 29.487 -31.169 24.746 1.00 16.80 ? 116 CYS   C SG  1 
ATOM   1959 N  N   . GLN   B 1 111 ? 29.459 -34.587 23.926 1.00 18.64 ? 117 GLN   C N   1 
ATOM   1960 C  CA  . GLN   B 1 111 ? 28.718 -35.649 24.624 1.00 20.74 ? 117 GLN   C CA  1 
ATOM   1961 C  C   . GLN   B 1 111 ? 27.625 -35.096 25.562 1.00 20.76 ? 117 GLN   C C   1 
ATOM   1962 O  O   . GLN   B 1 111 ? 26.668 -35.810 25.909 1.00 22.60 ? 117 GLN   C O   1 
ATOM   1963 C  CB  . GLN   B 1 111 ? 29.689 -36.572 25.403 1.00 22.94 ? 117 GLN   C CB  1 
ATOM   1964 C  CG  . GLN   B 1 111 ? 30.357 -35.884 26.570 1.00 26.40 ? 117 GLN   C CG  1 
ATOM   1965 C  CD  . GLN   B 1 111 ? 31.303 -36.795 27.333 1.00 35.75 ? 117 GLN   C CD  1 
ATOM   1966 O  OE1 . GLN   B 1 111 ? 32.510 -36.850 27.055 1.00 40.00 ? 117 GLN   C OE1 1 
ATOM   1967 N  NE2 . GLN   B 1 111 ? 30.786 -37.496 28.336 1.00 35.36 ? 117 GLN   C NE2 1 
ATOM   1968 N  N   . HIS   B 1 112 ? 27.733 -33.809 25.955 1.00 19.44 ? 118 HIS   C N   1 
ATOM   1969 C  CA  . HIS   B 1 112 ? 26.762 -33.211 26.884 1.00 18.38 ? 118 HIS   C CA  1 
ATOM   1970 C  C   . HIS   B 1 112 ? 25.598 -32.519 26.210 1.00 20.54 ? 118 HIS   C C   1 
ATOM   1971 O  O   . HIS   B 1 112 ? 24.624 -32.144 26.897 1.00 21.46 ? 118 HIS   C O   1 
ATOM   1972 C  CB  . HIS   B 1 112 ? 27.503 -32.248 27.798 1.00 18.52 ? 118 HIS   C CB  1 
ATOM   1973 C  CG  . HIS   B 1 112 ? 28.689 -32.881 28.483 1.00 19.61 ? 118 HIS   C CG  1 
ATOM   1974 N  ND1 . HIS   B 1 112 ? 30.014 -32.598 28.132 1.00 18.07 ? 118 HIS   C ND1 1 
ATOM   1975 C  CD2 . HIS   B 1 112 ? 28.707 -33.741 29.523 1.00 20.61 ? 118 HIS   C CD2 1 
ATOM   1976 C  CE1 . HIS   B 1 112 ? 30.774 -33.301 28.954 1.00 21.17 ? 118 HIS   C CE1 1 
ATOM   1977 N  NE2 . HIS   B 1 112 ? 30.036 -33.991 29.815 1.00 22.24 ? 118 HIS   C NE2 1 
ATOM   1978 N  N   . GLY   B 1 113 ? 25.698 -32.244 24.911 1.00 19.14 ? 119 GLY   C N   1 
ATOM   1979 C  CA  . GLY   B 1 113 ? 24.604 -31.563 24.225 1.00 17.91 ? 119 GLY   C CA  1 
ATOM   1980 C  C   . GLY   B 1 113 ? 25.105 -30.492 23.279 1.00 16.71 ? 119 GLY   C C   1 
ATOM   1981 O  O   . GLY   B 1 113 ? 26.220 -30.594 22.775 1.00 17.05 ? 119 GLY   C O   1 
ATOM   1982 N  N   . VAL   B 1 114 ? 24.247 -29.490 23.003 1.00 15.65 ? 120 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 114 ? 24.579 -28.410 22.082 1.00 16.86 ? 120 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 114 ? 25.517 -27.419 22.740 1.00 16.19 ? 120 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 114 ? 25.237 -26.863 23.817 1.00 17.19 ? 120 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 114 ? 23.308 -27.702 21.581 1.00 18.28 ? 120 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 114 ? 23.665 -26.452 20.737 1.00 19.44 ? 120 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 114 ? 22.400 -28.663 20.800 1.00 19.95 ? 120 VAL   C CG2 1 
ATOM   1989 N  N   . VAL   B 1 115 ? 26.685 -27.181 22.100 1.00 14.70 ? 121 VAL   C N   1 
ATOM   1990 C  CA  . VAL   B 1 115 ? 27.717 -26.250 22.617 1.00 15.44 ? 121 VAL   C CA  1 
ATOM   1991 C  C   . VAL   B 1 115 ? 27.500 -24.840 22.068 1.00 17.00 ? 121 VAL   C C   1 
ATOM   1992 O  O   . VAL   B 1 115 ? 27.728 -23.848 22.769 1.00 16.82 ? 121 VAL   C O   1 
ATOM   1993 C  CB  . VAL   B 1 115 ? 29.119 -26.787 22.183 1.00 14.98 ? 121 VAL   C CB  1 
ATOM   1994 C  CG1 . VAL   B 1 115 ? 30.225 -25.820 22.581 1.00 15.53 ? 121 VAL   C CG1 1 
ATOM   1995 C  CG2 . VAL   B 1 115 ? 29.359 -28.160 22.806 1.00 16.29 ? 121 VAL   C CG2 1 
ATOM   1996 N  N   . GLY   B 1 116 ? 27.129 -24.746 20.793 1.00 16.16 ? 122 GLY   C N   1 
ATOM   1997 C  CA  . GLY   B 1 116 ? 26.921 -23.447 20.168 1.00 16.43 ? 122 GLY   C CA  1 
ATOM   1998 C  C   . GLY   B 1 116 ? 26.548 -23.591 18.709 1.00 16.03 ? 122 GLY   C C   1 
ATOM   1999 O  O   . GLY   B 1 116 ? 26.211 -24.690 18.288 1.00 16.11 ? 122 GLY   C O   1 
ATOM   2000 N  N   . ILE   B 1 117 ? 26.561 -22.468 17.967 1.00 14.29 ? 123 ILE   C N   1 
ATOM   2001 C  CA  . ILE   B 1 117 ? 26.183 -22.514 16.565 1.00 14.13 ? 123 ILE   C CA  1 
ATOM   2002 C  C   . ILE   B 1 117 ? 27.238 -21.786 15.741 1.00 14.44 ? 123 ILE   C C   1 
ATOM   2003 O  O   . ILE   B 1 117 ? 27.861 -20.836 16.212 1.00 15.98 ? 123 ILE   C O   1 
ATOM   2004 C  CB  . ILE   B 1 117 ? 24.811 -21.834 16.274 1.00 16.60 ? 123 ILE   C CB  1 
ATOM   2005 C  CG1 . ILE   B 1 117 ? 24.694 -20.465 16.966 1.00 17.58 ? 123 ILE   C CG1 1 
ATOM   2006 C  CG2 . ILE   B 1 117 ? 23.651 -22.752 16.712 1.00 17.92 ? 123 ILE   C CG2 1 
ATOM   2007 C  CD1 . ILE   B 1 117 ? 23.372 -19.671 16.502 1.00 18.86 ? 123 ILE   C CD1 1 
ATOM   2008 N  N   . VAL   B 1 118 ? 27.393 -22.210 14.473 1.00 14.78 ? 124 VAL   C N   1 
ATOM   2009 C  CA  . VAL   B 1 118 ? 28.343 -21.492 13.565 1.00 14.19 ? 124 VAL   C CA  1 
ATOM   2010 C  C   . VAL   B 1 118 ? 27.975 -20.019 13.447 1.00 16.36 ? 124 VAL   C C   1 
ATOM   2011 O  O   . VAL   B 1 118 ? 26.791 -19.687 13.275 1.00 16.64 ? 124 VAL   C O   1 
ATOM   2012 C  CB  . VAL   B 1 118 ? 28.302 -22.167 12.176 1.00 14.79 ? 124 VAL   C CB  1 
ATOM   2013 C  CG1 . VAL   B 1 118 ? 29.153 -21.389 11.162 1.00 16.61 ? 124 VAL   C CG1 1 
ATOM   2014 C  CG2 . VAL   B 1 118 ? 28.781 -23.611 12.268 1.00 16.01 ? 124 VAL   C CG2 1 
ATOM   2015 N  N   . SER   B 1 119 ? 29.002 -19.128 13.559 1.00 15.53 ? 125 SER   C N   1 
ATOM   2016 C  CA  . SER   B 1 119 ? 28.771 -17.704 13.461 1.00 17.16 ? 125 SER   C CA  1 
ATOM   2017 C  C   . SER   B 1 119 ? 29.769 -17.008 12.535 1.00 18.17 ? 125 SER   C C   1 
ATOM   2018 O  O   . SER   B 1 119 ? 29.446 -15.940 11.998 1.00 18.94 ? 125 SER   C O   1 
ATOM   2019 C  CB  . SER   B 1 119 ? 28.849 -17.114 14.858 1.00 17.60 ? 125 SER   C CB  1 
ATOM   2020 O  OG  . SER   B 1 119 ? 28.683 -15.689 14.800 1.00 19.84 ? 125 SER   C OG  1 
ATOM   2021 N  N   . THR   B 1 120 ? 30.988 -17.554 12.368 1.00 17.25 ? 126 THR   C N   1 
ATOM   2022 C  CA  . THR   B 1 120 ? 32.031 -16.875 11.558 1.00 17.81 ? 126 THR   C CA  1 
ATOM   2023 C  C   . THR   B 1 120 ? 32.765 -17.895 10.684 1.00 17.71 ? 126 THR   C C   1 
ATOM   2024 O  O   . THR   B 1 120 ? 32.676 -19.128 10.908 1.00 17.93 ? 126 THR   C O   1 
ATOM   2025 C  CB  . THR   B 1 120 ? 33.107 -16.149 12.463 1.00 19.37 ? 126 THR   C CB  1 
ATOM   2026 O  OG1 . THR   B 1 120 ? 34.011 -17.083 13.097 1.00 20.70 ? 126 THR   C OG1 1 
ATOM   2027 C  CG2 . THR   B 1 120 ? 32.523 -15.225 13.447 1.00 20.21 ? 126 THR   C CG2 1 
ATOM   2028 N  N   . GLY   B 1 121 ? 33.479 -17.395 9.673  1.00 19.23 ? 127 GLY   C N   1 
ATOM   2029 C  CA  . GLY   B 1 121 ? 34.285 -18.274 8.824  1.00 21.22 ? 127 GLY   C CA  1 
ATOM   2030 C  C   . GLY   B 1 121 ? 35.314 -17.451 8.072  1.00 24.77 ? 127 GLY   C C   1 
ATOM   2031 O  O   . GLY   B 1 121 ? 35.090 -16.276 7.797  1.00 25.46 ? 127 GLY   C O   1 
ATOM   2032 N  N   . GLY   B 1 122 ? 36.379 -18.085 7.684  1.00 28.53 ? 128 GLY   C N   1 
ATOM   2033 C  CA  . GLY   B 1 122 ? 37.440 -17.378 6.975  1.00 30.82 ? 128 GLY   C CA  1 
ATOM   2034 C  C   . GLY   B 1 122 ? 38.796 -17.865 7.354  1.00 30.86 ? 128 GLY   C C   1 
ATOM   2035 O  O   . GLY   B 1 122 ? 39.006 -18.334 8.473  1.00 30.41 ? 128 GLY   C O   1 
ATOM   2036 N  N   . ASN   B 1 123 ? 39.729 -17.749 6.382  1.00 30.23 ? 129 ASN   C N   1 
ATOM   2037 C  CA  . ASN   B 1 123 ? 41.104 -18.201 6.542  1.00 31.28 ? 129 ASN   C CA  1 
ATOM   2038 C  C   . ASN   B 1 123 ? 41.233 -19.650 6.979  1.00 29.06 ? 129 ASN   C C   1 
ATOM   2039 O  O   . ASN   B 1 123 ? 42.195 -19.970 7.690  1.00 31.05 ? 129 ASN   C O   1 
ATOM   2040 C  CB  . ASN   B 1 123 ? 41.861 -17.261 7.497  1.00 35.36 ? 129 ASN   C CB  1 
ATOM   2041 C  CG  . ASN   B 1 123 ? 42.148 -15.954 6.836  1.00 42.69 ? 129 ASN   C CG  1 
ATOM   2042 O  OD1 . ASN   B 1 123 ? 42.973 -15.884 5.916  1.00 43.88 ? 129 ASN   C OD1 1 
ATOM   2043 N  ND2 . ASN   B 1 123 ? 41.468 -14.896 7.267  1.00 45.47 ? 129 ASN   C ND2 1 
ATOM   2044 N  N   . GLY   B 1 124 ? 40.316 -20.530 6.557  1.00 25.70 ? 130 GLY   C N   1 
ATOM   2045 C  CA  . GLY   B 1 124 ? 40.402 -21.938 6.955  1.00 23.89 ? 130 GLY   C CA  1 
ATOM   2046 C  C   . GLY   B 1 124 ? 39.934 -22.191 8.383  1.00 22.41 ? 130 GLY   C C   1 
ATOM   2047 O  O   . GLY   B 1 124 ? 40.191 -23.258 8.936  1.00 22.51 ? 130 GLY   C O   1 
ATOM   2048 N  N   . LEU   B 1 125 ? 39.236 -21.199 8.990  1.00 20.74 ? 131 LEU   C N   1 
ATOM   2049 C  CA  . LEU   B 1 125 ? 38.734 -21.331 10.349 1.00 19.65 ? 131 LEU   C CA  1 
ATOM   2050 C  C   . LEU   B 1 125 ? 37.235 -21.230 10.357 1.00 19.60 ? 131 LEU   C C   1 
ATOM   2051 O  O   . LEU   B 1 125 ? 36.618 -20.623 9.465  1.00 22.23 ? 131 LEU   C O   1 
ATOM   2052 C  CB  . LEU   B 1 125 ? 39.293 -20.225 11.276 1.00 21.86 ? 131 LEU   C CB  1 
ATOM   2053 C  CG  . LEU   B 1 125 ? 40.801 -20.138 11.429 1.00 26.09 ? 131 LEU   C CG  1 
ATOM   2054 C  CD1 . LEU   B 1 125 ? 41.172 -18.804 12.057 1.00 29.46 ? 131 LEU   C CD1 1 
ATOM   2055 C  CD2 . LEU   B 1 125 ? 41.369 -21.300 12.211 1.00 28.35 ? 131 LEU   C CD2 1 
ATOM   2056 N  N   . VAL   B 1 126 ? 36.626 -21.915 11.309 1.00 16.54 ? 132 VAL   C N   1 
ATOM   2057 C  CA  . VAL   B 1 126 ? 35.183 -21.798 11.533 1.00 16.00 ? 132 VAL   C CA  1 
ATOM   2058 C  C   . VAL   B 1 126 ? 34.999 -21.320 12.997 1.00 15.88 ? 132 VAL   C C   1 
ATOM   2059 O  O   . VAL   B 1 126 ? 35.702 -21.794 13.908 1.00 16.60 ? 132 VAL   C O   1 
ATOM   2060 C  CB  . VAL   B 1 126 ? 34.436 -23.137 11.316 1.00 16.87 ? 132 VAL   C CB  1 
ATOM   2061 C  CG1 . VAL   B 1 126 ? 35.106 -24.284 12.049 1.00 19.44 ? 132 VAL   C CG1 1 
ATOM   2062 C  CG2 . VAL   B 1 126 ? 32.933 -23.048 11.662 1.00 17.43 ? 132 VAL   C CG2 1 
ATOM   2063 N  N   . GLY   B 1 127 ? 34.114 -20.371 13.196 1.00 15.20 ? 133 GLY   C N   1 
ATOM   2064 C  CA  . GLY   B 1 127 ? 33.910 -19.867 14.543 1.00 15.25 ? 133 GLY   C CA  1 
ATOM   2065 C  C   . GLY   B 1 127 ? 32.513 -20.169 15.034 1.00 16.18 ? 133 GLY   C C   1 
ATOM   2066 O  O   . GLY   B 1 127 ? 31.554 -20.069 14.266 1.00 16.28 ? 133 GLY   C O   1 
ATOM   2067 N  N   . PHE   B 1 128 ? 32.402 -20.513 16.292 1.00 14.64 ? 134 PHE   C N   1 
ATOM   2068 C  CA  . PHE   B 1 128 ? 31.093 -20.855 16.881 1.00 14.90 ? 134 PHE   C CA  1 
ATOM   2069 C  C   . PHE   B 1 128 ? 30.762 -19.906 18.018 1.00 15.87 ? 134 PHE   C C   1 
ATOM   2070 O  O   . PHE   B 1 128 ? 31.606 -19.674 18.884 1.00 17.01 ? 134 PHE   C O   1 
ATOM   2071 C  CB  . PHE   B 1 128 ? 31.175 -22.291 17.480 1.00 14.66 ? 134 PHE   C CB  1 
ATOM   2072 C  CG  . PHE   B 1 128 ? 31.696 -23.331 16.500 1.00 14.93 ? 134 PHE   C CG  1 
ATOM   2073 C  CD1 . PHE   B 1 128 ? 30.851 -23.919 15.587 1.00 14.49 ? 134 PHE   C CD1 1 
ATOM   2074 C  CD2 . PHE   B 1 128 ? 33.036 -23.709 16.506 1.00 16.29 ? 134 PHE   C CD2 1 
ATOM   2075 C  CE1 . PHE   B 1 128 ? 31.334 -24.901 14.704 1.00 15.40 ? 134 PHE   C CE1 1 
ATOM   2076 C  CE2 . PHE   B 1 128 ? 33.511 -24.697 15.637 1.00 16.75 ? 134 PHE   C CE2 1 
ATOM   2077 C  CZ  . PHE   B 1 128 ? 32.657 -25.282 14.748 1.00 15.99 ? 134 PHE   C CZ  1 
ATOM   2078 N  N   . ALA   B 1 129 ? 29.507 -19.467 18.074 1.00 15.64 ? 135 ALA   C N   1 
ATOM   2079 C  CA  . ALA   B 1 129 ? 29.028 -18.654 19.198 1.00 15.35 ? 135 ALA   C CA  1 
ATOM   2080 C  C   . ALA   B 1 129 ? 28.648 -19.618 20.336 1.00 16.20 ? 135 ALA   C C   1 
ATOM   2081 O  O   . ALA   B 1 129 ? 27.751 -20.458 20.179 1.00 16.52 ? 135 ALA   C O   1 
ATOM   2082 C  CB  . ALA   B 1 129 ? 27.803 -17.849 18.752 1.00 16.91 ? 135 ALA   C CB  1 
ATOM   2083 N  N   . ASP   B 1 130 ? 29.344 -19.507 21.475 1.00 16.52 ? 136 ASP   C N   1 
ATOM   2084 C  CA  . ASP   B 1 130 ? 29.093 -20.424 22.587 1.00 16.14 ? 136 ASP   C CA  1 
ATOM   2085 C  C   . ASP   B 1 130 ? 27.750 -20.069 23.226 1.00 16.87 ? 136 ASP   C C   1 
ATOM   2086 O  O   . ASP   B 1 130 ? 27.388 -18.885 23.343 1.00 18.05 ? 136 ASP   C O   1 
ATOM   2087 C  CB  . ASP   B 1 130 ? 30.178 -20.175 23.668 1.00 16.50 ? 136 ASP   C CB  1 
ATOM   2088 C  CG  . ASP   B 1 130 ? 30.170 -21.127 24.847 1.00 21.77 ? 136 ASP   C CG  1 
ATOM   2089 O  OD1 . ASP   B 1 130 ? 29.947 -22.333 24.642 1.00 21.71 ? 136 ASP   C OD1 1 
ATOM   2090 O  OD2 . ASP   B 1 130 ? 30.326 -20.649 25.985 1.00 26.22 ? 136 ASP   C OD2 1 
ATOM   2091 N  N   . VAL   B 1 131 ? 27.056 -21.083 23.763 1.00 14.87 ? 137 VAL   C N   1 
ATOM   2092 C  CA  . VAL   B 1 131 ? 25.825 -20.838 24.551 1.00 16.27 ? 137 VAL   C CA  1 
ATOM   2093 C  C   . VAL   B 1 131 ? 25.877 -21.522 25.918 1.00 17.70 ? 137 VAL   C C   1 
ATOM   2094 O  O   . VAL   B 1 131 ? 24.902 -21.446 26.667 1.00 18.62 ? 137 VAL   C O   1 
ATOM   2095 C  CB  . VAL   B 1 131 ? 24.517 -21.283 23.811 1.00 16.69 ? 137 VAL   C CB  1 
ATOM   2096 C  CG1 . VAL   B 1 131 ? 24.328 -20.459 22.519 1.00 16.91 ? 137 VAL   C CG1 1 
ATOM   2097 C  CG2 . VAL   B 1 131 ? 24.508 -22.789 23.484 1.00 17.16 ? 137 VAL   C CG2 1 
ATOM   2098 N  N   . ARG   B 1 132 ? 27.001 -22.168 26.252 1.00 17.33 ? 138 ARG   C N   1 
ATOM   2099 C  CA  . ARG   B 1 132 ? 27.080 -22.962 27.497 1.00 16.36 ? 138 ARG   C CA  1 
ATOM   2100 C  C   . ARG   B 1 132 ? 27.016 -22.131 28.778 1.00 17.90 ? 138 ARG   C C   1 
ATOM   2101 O  O   . ARG   B 1 132 ? 26.763 -22.691 29.858 1.00 19.36 ? 138 ARG   C O   1 
ATOM   2102 C  CB  . ARG   B 1 132 ? 28.334 -23.826 27.486 1.00 15.75 ? 138 ARG   C CB  1 
ATOM   2103 C  CG  . ARG   B 1 132 ? 28.313 -24.873 26.376 1.00 15.15 ? 138 ARG   C CG  1 
ATOM   2104 C  CD  . ARG   B 1 132 ? 29.627 -25.658 26.413 1.00 15.83 ? 138 ARG   C CD  1 
ATOM   2105 N  NE  . ARG   B 1 132 ? 30.717 -24.783 25.959 1.00 17.07 ? 138 ARG   C NE  1 
ATOM   2106 C  CZ  . ARG   B 1 132 ? 31.963 -25.189 25.764 1.00 18.92 ? 138 ARG   C CZ  1 
ATOM   2107 N  NH1 . ARG   B 1 132 ? 32.342 -26.401 26.147 1.00 16.79 ? 138 ARG   C NH1 1 
ATOM   2108 N  NH2 . ARG   B 1 132 ? 32.872 -24.354 25.279 1.00 19.30 ? 138 ARG   C NH2 1 
ATOM   2109 N  N   . ASP   B 1 133 ? 27.320 -20.856 28.680 1.00 17.61 ? 139 ASP   C N   1 
ATOM   2110 C  CA  . ASP   B 1 133 ? 27.269 -19.966 29.843 1.00 18.36 ? 139 ASP   C CA  1 
ATOM   2111 C  C   . ASP   B 1 133 ? 25.867 -19.445 30.116 1.00 19.99 ? 139 ASP   C C   1 
ATOM   2112 O  O   . ASP   B 1 133 ? 25.666 -18.809 31.170 1.00 20.07 ? 139 ASP   C O   1 
ATOM   2113 C  CB  . ASP   B 1 133 ? 28.268 -18.781 29.671 1.00 19.97 ? 139 ASP   C CB  1 
ATOM   2114 C  CG  . ASP   B 1 133 ? 27.888 -17.869 28.539 1.00 22.45 ? 139 ASP   C CG  1 
ATOM   2115 O  OD1 . ASP   B 1 133 ? 27.536 -18.383 27.466 1.00 21.88 ? 139 ASP   C OD1 1 
ATOM   2116 O  OD2 . ASP   B 1 133 ? 27.837 -16.622 28.760 1.00 25.55 ? 139 ASP   C OD2 1 
ATOM   2117 N  N   . LEU   B 1 134 ? 24.925 -19.625 29.174 1.00 19.24 ? 140 LEU   C N   1 
ATOM   2118 C  CA  . LEU   B 1 134 ? 23.576 -19.054 29.280 1.00 18.29 ? 140 LEU   C CA  1 
ATOM   2119 C  C   . LEU   B 1 134 ? 22.702 -20.022 30.076 1.00 18.90 ? 140 LEU   C C   1 
ATOM   2120 O  O   . LEU   B 1 134 ? 21.874 -20.745 29.514 1.00 20.03 ? 140 LEU   C O   1 
ATOM   2121 C  CB  . LEU   B 1 134 ? 23.008 -18.808 27.869 1.00 18.18 ? 140 LEU   C CB  1 
ATOM   2122 C  CG  . LEU   B 1 134 ? 23.889 -17.893 26.989 1.00 19.97 ? 140 LEU   C CG  1 
ATOM   2123 C  CD1 . LEU   B 1 134 ? 23.272 -17.763 25.571 1.00 20.48 ? 140 LEU   C CD1 1 
ATOM   2124 C  CD2 . LEU   B 1 134 ? 24.004 -16.481 27.597 1.00 21.05 ? 140 LEU   C CD2 1 
ATOM   2125 N  N   . LEU   B 1 135 ? 22.931 -20.065 31.411 1.00 19.02 ? 141 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 135 ? 22.287 -21.099 32.227 1.00 19.86 ? 141 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 135 ? 20.769 -20.976 32.280 1.00 20.25 ? 141 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 135 ? 20.077 -21.991 32.484 1.00 20.89 ? 141 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 135 ? 22.893 -21.172 33.655 1.00 20.19 ? 141 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 135 ? 24.432 -21.114 33.708 1.00 21.37 ? 141 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 135 ? 24.965 -21.122 35.178 1.00 22.08 ? 141 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 135 ? 25.074 -22.253 32.911 1.00 20.80 ? 141 LEU   C CD2 1 
ATOM   2133 N  N   . TRP   B 1 136 ? 20.266 -19.748 32.083 1.00 20.77 ? 142 TRP   C N   1 
ATOM   2134 C  CA  . TRP   B 1 136 ? 18.820 -19.478 32.122 1.00 22.01 ? 142 TRP   C CA  1 
ATOM   2135 C  C   . TRP   B 1 136 ? 18.052 -20.171 30.983 1.00 22.29 ? 142 TRP   C C   1 
ATOM   2136 O  O   . TRP   B 1 136 ? 16.829 -20.301 31.075 1.00 23.18 ? 142 TRP   C O   1 
ATOM   2137 C  CB  . TRP   B 1 136 ? 18.553 -17.962 32.133 1.00 22.36 ? 142 TRP   C CB  1 
ATOM   2138 C  CG  . TRP   B 1 136 ? 19.231 -17.213 31.017 1.00 20.92 ? 142 TRP   C CG  1 
ATOM   2139 C  CD1 . TRP   B 1 136 ? 20.432 -16.561 31.081 1.00 22.13 ? 142 TRP   C CD1 1 
ATOM   2140 C  CD2 . TRP   B 1 136 ? 18.735 -17.013 29.677 1.00 21.07 ? 142 TRP   C CD2 1 
ATOM   2141 N  NE1 . TRP   B 1 136 ? 20.696 -15.933 29.871 1.00 22.93 ? 142 TRP   C NE1 1 
ATOM   2142 C  CE2 . TRP   B 1 136 ? 19.672 -16.207 28.994 1.00 22.31 ? 142 TRP   C CE2 1 
ATOM   2143 C  CE3 . TRP   B 1 136 ? 17.563 -17.392 29.012 1.00 21.91 ? 142 TRP   C CE3 1 
ATOM   2144 C  CZ2 . TRP   B 1 136 ? 19.497 -15.823 27.657 1.00 22.22 ? 142 TRP   C CZ2 1 
ATOM   2145 C  CZ3 . TRP   B 1 136 ? 17.361 -16.962 27.710 1.00 22.72 ? 142 TRP   C CZ3 1 
ATOM   2146 C  CH2 . TRP   B 1 136 ? 18.334 -16.210 27.039 1.00 22.45 ? 142 TRP   C CH2 1 
ATOM   2147 N  N   . LEU   B 1 137 ? 18.751 -20.657 29.943 1.00 20.92 ? 143 LEU   C N   1 
ATOM   2148 C  CA  . LEU   B 1 137 ? 18.042 -21.381 28.872 1.00 21.40 ? 143 LEU   C CA  1 
ATOM   2149 C  C   . LEU   B 1 137 ? 17.433 -22.688 29.432 1.00 23.85 ? 143 LEU   C C   1 
ATOM   2150 O  O   . LEU   B 1 137 ? 16.517 -23.227 28.818 1.00 25.48 ? 143 LEU   C O   1 
ATOM   2151 C  CB  . LEU   B 1 137 ? 19.017 -21.750 27.747 1.00 20.75 ? 143 LEU   C CB  1 
ATOM   2152 C  CG  . LEU   B 1 137 ? 19.481 -20.601 26.866 1.00 21.77 ? 143 LEU   C CG  1 
ATOM   2153 C  CD1 . LEU   B 1 137 ? 20.614 -21.073 25.924 1.00 20.97 ? 143 LEU   C CD1 1 
ATOM   2154 C  CD2 . LEU   B 1 137 ? 18.329 -20.055 26.020 1.00 21.11 ? 143 LEU   C CD2 1 
ATOM   2155 N  N   . ASP   B 1 138 ? 17.942 -23.195 30.576 1.00 23.27 ? 144 ASP   C N   1 
ATOM   2156 C  CA  . ASP   B 1 138 ? 17.467 -24.457 31.147 1.00 24.58 ? 144 ASP   C CA  1 
ATOM   2157 C  C   . ASP   B 1 138 ? 16.248 -24.302 32.063 1.00 28.19 ? 144 ASP   C C   1 
ATOM   2158 O  O   . ASP   B 1 138 ? 15.809 -25.320 32.624 1.00 28.74 ? 144 ASP   C O   1 
ATOM   2159 C  CB  . ASP   B 1 138 ? 18.568 -25.126 31.996 1.00 24.11 ? 144 ASP   C CB  1 
ATOM   2160 C  CG  . ASP   B 1 138 ? 19.801 -25.594 31.235 1.00 26.27 ? 144 ASP   C CG  1 
ATOM   2161 O  OD1 . ASP   B 1 138 ? 19.748 -25.663 29.994 1.00 27.20 ? 144 ASP   C OD1 1 
ATOM   2162 O  OD2 . ASP   B 1 138 ? 20.826 -25.900 31.896 1.00 27.09 ? 144 ASP   C OD2 1 
ATOM   2163 N  N   . GLU   B 1 139 ? 15.767 -23.087 32.286 1.00 30.17 ? 145 GLU   C N   1 
ATOM   2164 C  CA  . GLU   B 1 139 ? 14.667 -22.847 33.233 1.00 34.64 ? 145 GLU   C CA  1 
ATOM   2165 C  C   . GLU   B 1 139 ? 13.620 -21.839 32.707 1.00 39.36 ? 145 GLU   C C   1 
ATOM   2166 O  O   . GLU   B 1 139 ? 13.803 -21.253 31.641 1.00 39.88 ? 145 GLU   C O   1 
ATOM   2167 C  CB  . GLU   B 1 139 ? 15.303 -22.307 34.535 1.00 37.41 ? 145 GLU   C CB  1 
ATOM   2168 C  CG  . GLU   B 1 139 ? 15.902 -20.924 34.346 1.00 42.72 ? 145 GLU   C CG  1 
ATOM   2169 C  CD  . GLU   B 1 139 ? 16.808 -20.407 35.444 1.00 48.79 ? 145 GLU   C CD  1 
ATOM   2170 O  OE1 . GLU   B 1 139 ? 17.054 -19.178 35.476 1.00 47.90 ? 145 GLU   C OE1 1 
ATOM   2171 O  OE2 . GLU   B 1 139 ? 17.268 -21.227 36.270 1.00 52.11 ? 145 GLU   C OE2 1 
ATOM   2172 N  N   . GLU   B 1 140 ? 12.559 -21.574 33.514 1.00 41.86 ? 146 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 140 ? 11.511 -20.579 33.253 1.00 44.49 ? 146 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 140 ? 10.854 -20.757 31.891 1.00 46.46 ? 146 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 140 ? 9.633  -20.636 31.767 1.00 47.65 ? 146 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 140 ? 12.053 -19.150 33.466 1.00 47.28 ? 146 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 140 ? 11.283 -18.006 32.816 1.00 54.77 ? 146 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 140 ? 10.119 -17.426 33.597 1.00 62.39 ? 146 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 140 ? 9.693  -16.297 33.263 1.00 63.46 ? 146 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 140 ? 9.631  -18.094 34.538 1.00 65.70 ? 146 GLU   C OE2 1 
HETATM 2181 N  N1  . A1B5X C 2 .   ? 7.806  14.566  23.526 1.00 29.10 ? 201 A1B5X A N1  1 
HETATM 2182 N  N3  . A1B5X C 2 .   ? 10.811 15.524  17.213 1.00 22.84 ? 201 A1B5X A N3  1 
HETATM 2183 C  C4  . A1B5X C 2 .   ? 6.053  13.448  24.809 1.00 29.33 ? 201 A1B5X A C4  1 
HETATM 2184 C  C5  . A1B5X C 2 .   ? 7.149  13.383  23.952 1.00 29.05 ? 201 A1B5X A C5  1 
HETATM 2185 C  C6  . A1B5X C 2 .   ? 9.938  16.104  22.413 1.00 27.24 ? 201 A1B5X A C6  1 
HETATM 2186 C  C7  . A1B5X C 2 .   ? 11.347 16.036  21.832 1.00 27.85 ? 201 A1B5X A C7  1 
HETATM 2187 C  C8  . A1B5X C 2 .   ? 11.371 16.645  20.423 1.00 27.17 ? 201 A1B5X A C8  1 
HETATM 2188 C  C10 . A1B5X C 2 .   ? 10.355 16.403  18.092 1.00 25.32 ? 201 A1B5X A C10 1 
HETATM 2189 O  O2  . A1B5X C 2 .   ? 9.880  17.495  17.764 1.00 25.90 ? 201 A1B5X A O2  1 
HETATM 2190 C  C9  . A1B5X C 2 .   ? 10.329 15.939  19.536 1.00 26.39 ? 201 A1B5X A C9  1 
HETATM 2191 C  C11 . A1B5X C 2 .   ? 8.945  16.124  20.158 1.00 26.59 ? 201 A1B5X A C11 1 
HETATM 2192 N  N2  . A1B5X C 2 .   ? 8.955  15.491  21.491 1.00 27.82 ? 201 A1B5X A N2  1 
HETATM 2193 S  S1  . A1B5X C 2 .   ? 7.468  15.286  22.101 1.00 28.26 ? 201 A1B5X A S1  1 
HETATM 2194 O  O   . A1B5X C 2 .   ? 6.897  16.580  22.339 1.00 28.34 ? 201 A1B5X A O   1 
HETATM 2195 O  O1  . A1B5X C 2 .   ? 6.747  14.406  21.239 1.00 28.72 ? 201 A1B5X A O1  1 
HETATM 2196 C  C1  . A1B5X C 2 .   ? 7.609  12.113  23.587 1.00 27.75 ? 201 A1B5X A C1  1 
HETATM 2197 S  S   . A1B5X C 2 .   ? 8.987  11.976  22.491 1.00 26.77 ? 201 A1B5X A S   1 
HETATM 2198 C  C   . A1B5X C 2 .   ? 9.344  10.217  22.489 1.00 27.12 ? 201 A1B5X A C   1 
HETATM 2199 N  N   . A1B5X C 2 .   ? 5.426  12.375  25.296 1.00 29.80 ? 201 A1B5X A N   1 
HETATM 2200 C  C3  . A1B5X C 2 .   ? 5.896  11.179  24.945 1.00 28.98 ? 201 A1B5X A C3  1 
HETATM 2201 C  C2  . A1B5X C 2 .   ? 6.970  10.988  24.096 1.00 27.95 ? 201 A1B5X A C2  1 
HETATM 2202 ZN ZN  . ZN    D 3 .   ? 11.279 -4.082  5.860  1.00 23.36 2 202 ZN    A ZN  1 
HETATM 2203 ZN ZN  . ZN    E 3 .   ? 30.706 -31.245 26.713 1.00 18.02 2 201 ZN    C ZN  1 
HETATM 2204 S  S   . DMS   F 4 .   ? 21.031 -32.893 10.433 1.00 59.66 ? 202 DMS   C S   1 
HETATM 2205 O  O   . DMS   F 4 .   ? 21.401 -32.149 9.177  1.00 59.42 ? 202 DMS   C O   1 
HETATM 2206 C  C1  . DMS   F 4 .   ? 21.897 -32.067 11.802 1.00 59.52 ? 202 DMS   C C1  1 
HETATM 2207 C  C2  . DMS   F 4 .   ? 19.386 -32.261 10.878 1.00 59.70 ? 202 DMS   C C2  1 
HETATM 2208 O  O   . HOH   G 5 .   ? 11.244 8.747   4.199  1.00 28.18 ? 301 HOH   A O   1 
HETATM 2209 O  O   . HOH   G 5 .   ? 35.342 -3.819  7.850  1.00 30.15 ? 302 HOH   A O   1 
HETATM 2210 O  O   . HOH   G 5 .   ? 37.446 15.192  14.223 1.00 49.53 ? 303 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 5 .   ? 2.872  -3.403  20.817 1.00 36.47 ? 304 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 5 .   ? 30.495 10.573  15.646 1.00 34.24 ? 305 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? 23.374 21.691  7.201  1.00 29.81 ? 306 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? 11.688 18.018  4.990  1.00 37.68 ? 307 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 10.785 5.376   3.288  1.00 34.23 ? 308 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 8.467  25.402  23.434 1.00 37.89 ? 309 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 3.951  9.348   27.874 1.00 39.32 ? 310 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? 4.732  -3.606  28.941 1.00 30.74 ? 311 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? 17.347 1.132   28.211 1.00 26.41 ? 312 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 10.273 10.173  31.303 1.00 28.42 ? 313 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? 27.818 8.256   1.681  1.00 39.17 ? 314 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 29.834 11.817  18.410 1.00 40.12 ? 315 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 28.221 3.157   5.182  1.00 36.80 ? 316 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 16.603 4.011   23.646 1.00 24.07 ? 317 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 19.302 10.112  19.628 1.00 18.18 ? 318 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 35.278 11.241  12.537 1.00 58.85 ? 319 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 7.583  20.758  17.165 1.00 27.77 ? 320 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 8.789  19.506  19.377 1.00 25.71 ? 321 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 13.666 4.075   23.411 1.00 16.91 ? 322 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 31.593 20.094  11.848 1.00 26.68 ? 323 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? -0.180 1.254   15.694 1.00 16.24 ? 324 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 15.018 11.316  0.031  1.00 36.58 ? 325 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 24.766 5.276   21.449 1.00 33.81 ? 326 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 18.408 21.941  9.511  1.00 25.13 ? 327 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 21.023 -4.129  14.208 1.00 23.55 ? 328 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 29.042 3.480   12.753 1.00 22.27 ? 329 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 11.344 12.631  10.950 1.00 21.39 ? 330 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 30.637 3.034   14.942 1.00 26.78 ? 331 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 22.768 0.983   17.494 1.00 22.68 ? 332 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 9.551  4.034   33.438 1.00 18.52 ? 333 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 13.985 13.788  23.957 1.00 22.18 ? 334 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 20.961 -2.540  16.926 1.00 20.34 ? 335 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 11.929 11.178  29.599 1.00 26.80 ? 336 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 13.292 11.398  9.116  1.00 17.08 ? 337 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 23.039 -0.575  5.474  1.00 27.00 ? 338 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 29.090 15.930  4.541  1.00 35.88 ? 339 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 17.595 20.076  17.003 1.00 21.54 ? 340 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 4.077  14.280  19.825 1.00 53.11 ? 341 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 32.359 2.021   6.150  1.00 38.98 ? 342 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 30.409 4.660   5.934  1.00 29.36 ? 343 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 22.526 19.529  19.845 1.00 35.34 ? 344 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 27.007 -1.204  9.005  1.00 31.45 ? 345 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 6.125  2.388   5.505  1.00 29.62 ? 346 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 15.352 21.912  8.233  1.00 38.43 ? 347 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 4.037  0.111   23.909 1.00 23.97 ? 348 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 6.599  -6.861  23.756 1.00 32.49 ? 349 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 7.913  16.545  25.619 1.00 36.68 ? 350 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 29.440 11.892  21.355 1.00 35.24 ? 351 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 14.354 -2.436  17.854 1.00 22.33 ? 352 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 17.575 10.830  26.073 1.00 27.29 ? 353 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 27.341 -1.358  16.033 1.00 35.33 ? 354 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 16.406 9.512   -1.623 1.00 25.94 ? 355 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 18.124 17.809  4.202  1.00 44.38 ? 356 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 5.302  5.381   32.675 1.00 29.32 ? 357 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 1.534  11.406  27.381 1.00 46.61 ? 358 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 19.420 3.027   19.401 1.00 28.12 ? 359 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 25.100 17.755  4.607  1.00 38.74 ? 360 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 19.767 13.049  1.982  1.00 44.85 ? 361 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 32.118 8.770   7.705  1.00 30.93 ? 362 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 16.994 6.315   26.855 1.00 31.56 ? 363 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 17.562 1.016   20.280 1.00 24.54 ? 364 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 15.114 15.039  3.140  1.00 35.72 ? 365 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 36.311 -0.339  12.416 1.00 43.34 ? 366 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 14.644 24.375  17.705 1.00 36.37 ? 367 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 2.622  16.601  19.041 1.00 43.39 ? 368 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 16.711 21.323  19.189 1.00 29.24 ? 369 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 3.941  -4.081  6.028  1.00 33.13 ? 370 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 8.135  6.674   33.809 1.00 26.38 ? 371 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 6.255  23.971  10.096 1.00 38.87 ? 372 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 27.869 17.558  24.280 1.00 30.41 ? 373 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 5.459  27.086  19.451 1.00 38.05 ? 374 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 15.409 -5.025  0.329  1.00 42.69 ? 375 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 7.369  13.661  4.528  1.00 27.38 ? 376 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 3.003  7.394   24.464 1.00 34.57 ? 377 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 0.065  5.390   5.832  1.00 32.28 ? 378 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 23.287 19.181  6.357  1.00 26.27 ? 379 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 0.460  -1.221  16.628 1.00 25.94 ? 380 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 34.204 7.727   16.802 1.00 40.28 ? 381 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 17.005 -5.690  12.243 1.00 38.37 ? 382 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 16.892 -4.138  2.905  1.00 31.65 ? 383 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 33.875 5.153   16.863 1.00 38.40 ? 384 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 19.308 -0.449  32.858 1.00 42.08 ? 385 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 20.986 10.069  21.900 1.00 21.91 ? 386 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 32.086 7.099   5.647  1.00 45.86 ? 387 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 20.796 -4.603  11.513 1.00 32.43 ? 388 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 17.291 -2.260  19.605 1.00 25.23 ? 389 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 23.342 8.387   21.771 1.00 36.15 ? 390 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 22.736 3.451   20.970 1.00 29.70 ? 391 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 0.732  7.649   27.499 1.00 39.61 ? 392 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 3.066  12.639  17.861 1.00 45.43 ? 393 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? -1.465 -2.852  15.569 1.00 42.17 ? 394 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 5.871  18.533  25.374 1.00 45.89 ? 395 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 15.811 13.149  25.915 1.00 32.89 ? 396 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 2.668  -0.493  26.391 1.00 38.10 ? 397 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 18.603 2.240   22.723 1.00 42.84 ? 398 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 29.881 0.852   16.663 1.00 42.96 ? 399 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 0.076  0.058   23.027 1.00 31.29 ? 400 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 23.967 1.003   19.838 1.00 46.22 ? 401 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 21.508 -0.941  18.962 1.00 34.63 ? 402 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 31.192 4.675   17.127 1.00 32.00 ? 403 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 37.661 -4.637  6.498  1.00 35.32 ? 404 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 2.604  -1.687  22.751 1.00 36.21 ? 405 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 3.895  -6.750  23.508 1.00 46.43 ? 406 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 29.571 -26.051 -1.110 1.00 33.78 ? 301 HOH   C O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 14.896 -18.610 31.946 1.00 46.13 ? 302 HOH   C O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 30.853 -18.316 26.858 1.00 24.12 ? 303 HOH   C O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 18.797 -8.895  13.764 1.00 33.32 ? 304 HOH   C O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 38.280 -7.383  6.966  1.00 27.83 ? 305 HOH   C O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 19.143 -32.275 19.973 1.00 43.70 ? 306 HOH   C O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 23.992 -8.196  9.451  1.00 32.21 ? 307 HOH   C O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 20.805 -18.789 12.813 1.00 19.53 ? 308 HOH   C O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 17.886 -27.543 16.581 1.00 22.97 ? 309 HOH   C O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 37.262 -32.196 10.854 1.00 33.48 ? 310 HOH   C O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 19.809 -4.200  20.172 1.00 27.06 ? 311 HOH   C O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 38.754 -18.667 21.348 1.00 28.51 ? 312 HOH   C O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 14.659 -23.923 12.387 1.00 38.43 ? 313 HOH   C O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 21.868 -26.192 34.335 1.00 34.48 ? 314 HOH   C O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 37.214 -18.813 28.149 1.00 33.74 ? 315 HOH   C O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 31.078 -21.603 28.369 1.00 22.36 ? 316 HOH   C O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 30.903 -33.212 0.792  1.00 42.73 ? 317 HOH   C O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 10.412 -16.909 15.254 1.00 43.07 ? 318 HOH   C O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 21.851 -28.606 4.866  1.00 34.39 ? 319 HOH   C O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 40.499 -27.372 15.126 1.00 17.22 ? 320 HOH   C O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 23.056 -5.960  21.142 1.00 24.06 ? 321 HOH   C O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 10.090 -8.841  23.967 1.00 31.66 ? 322 HOH   C O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 10.950 -6.558  13.296 1.00 32.33 ? 323 HOH   C O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 17.379 -24.044 8.548  1.00 44.99 ? 324 HOH   C O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 10.286 -17.493 18.344 1.00 40.00 ? 325 HOH   C O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 26.044 -25.337 8.792  1.00 19.03 ? 326 HOH   C O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 32.671 -23.815 29.134 1.00 23.47 ? 327 HOH   C O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 29.958 -15.265 19.536 1.00 22.10 ? 328 HOH   C O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 9.406  -7.979  21.359 1.00 31.22 ? 329 HOH   C O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 11.992 -24.225 21.803 1.00 21.28 ? 330 HOH   C O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 19.236 -27.729 28.215 1.00 23.52 ? 331 HOH   C O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 25.847 -37.889 24.243 1.00 37.35 ? 332 HOH   C O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 31.149 -35.816 31.605 1.00 42.10 ? 333 HOH   C O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 26.584 -15.254 30.848 1.00 37.58 ? 334 HOH   C O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 20.788 -25.729 13.817 1.00 28.18 ? 335 HOH   C O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 23.657 -33.660 29.057 1.00 31.14 ? 336 HOH   C O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 24.886 -15.773 7.229  1.00 24.71 ? 337 HOH   C O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 29.749 -31.463 32.740 1.00 30.63 ? 338 HOH   C O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 22.944 -8.535  14.021 1.00 20.99 ? 339 HOH   C O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 14.826 -18.319 10.543 1.00 45.80 ? 340 HOH   C O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 40.340 -25.321 6.999  1.00 43.06 ? 341 HOH   C O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 27.148 -35.811 20.886 1.00 31.38 ? 342 HOH   C O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 35.203 -13.185 8.677  1.00 25.62 ? 343 HOH   C O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 31.230 -12.203 10.644 1.00 23.70 ? 344 HOH   C O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 14.688 -28.897 25.712 1.00 41.24 ? 345 HOH   C O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 23.193 -25.379 8.974  1.00 26.50 ? 346 HOH   C O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 32.032 -10.493 13.739 1.00 25.57 ? 347 HOH   C O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 33.005 -9.846  11.053 1.00 22.22 ? 348 HOH   C O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 28.195 -16.447 22.073 1.00 19.87 ? 349 HOH   C O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 22.927 -33.472 5.403  1.00 48.23 ? 350 HOH   C O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 26.434 -31.270 14.858 1.00 24.15 ? 351 HOH   C O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 43.296 -25.861 23.654 1.00 28.22 ? 352 HOH   C O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 36.381 -21.224 6.658  1.00 31.59 ? 353 HOH   C O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 29.702 -13.142 12.917 1.00 23.57 ? 354 HOH   C O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 26.813 -12.062 27.468 1.00 30.45 ? 355 HOH   C O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 31.156 -24.063 -1.248 1.00 32.47 ? 356 HOH   C O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 21.690 -18.957 5.945  1.00 35.87 ? 357 HOH   C O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 31.393 -13.432 4.262  1.00 40.29 ? 358 HOH   C O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 22.913 -28.240 12.620 1.00 25.59 ? 359 HOH   C O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 38.995 -13.128 25.677 1.00 32.40 ? 360 HOH   C O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 22.210 -23.811 6.155  1.00 42.58 ? 361 HOH   C O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 35.704 -24.769 24.700 1.00 24.46 ? 362 HOH   C O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 10.084 -24.860 19.884 1.00 28.52 ? 363 HOH   C O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 8.737  -13.346 10.834 1.00 31.60 ? 364 HOH   C O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 33.131 -30.482 31.658 1.00 24.76 ? 365 HOH   C O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 38.969 -16.407 3.887  1.00 50.92 ? 366 HOH   C O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 4.300  -10.359 19.707 1.00 41.06 ? 367 HOH   C O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 22.726 -13.808 29.844 1.00 43.67 ? 368 HOH   C O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 36.743 -16.349 12.299 1.00 41.91 ? 369 HOH   C O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 26.115 -31.072 30.874 1.00 22.26 ? 370 HOH   C O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 30.288 -18.233 8.364  1.00 32.67 ? 371 HOH   C O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 17.229 -25.315 12.811 1.00 29.82 ? 372 HOH   C O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 11.668 -22.573 28.832 1.00 30.89 ? 373 HOH   C O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 35.199 -4.225  17.657 1.00 34.90 ? 374 HOH   C O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 28.803 -36.451 7.865  1.00 26.42 ? 375 HOH   C O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 36.992 -29.349 10.015 1.00 29.93 ? 376 HOH   C O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 34.438 -13.507 25.502 1.00 26.10 ? 377 HOH   C O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 26.694 -6.075  22.168 1.00 44.71 ? 378 HOH   C O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 6.558  -22.887 18.565 1.00 39.08 ? 379 HOH   C O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 33.589 -20.536 -1.908 1.00 46.74 ? 380 HOH   C O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 41.932 -12.310 17.631 1.00 35.45 ? 381 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 6.563  -20.130 18.381 1.00 40.04 ? 382 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 38.284 -13.781 10.627 1.00 39.56 ? 383 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 35.159 -13.766 6.059  1.00 44.24 ? 384 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 20.521 -32.240 22.279 1.00 33.98 ? 385 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 32.833 -14.422 9.321  1.00 23.13 ? 386 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 15.203 -30.204 18.275 1.00 41.66 ? 387 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 40.043 -30.019 14.530 1.00 23.53 ? 388 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 35.735 -28.766 7.816  1.00 25.67 ? 389 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 16.427 -20.470 11.570 1.00 32.80 ? 390 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 18.820 -19.074 10.823 1.00 28.45 ? 391 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 18.629 -8.246  25.585 1.00 26.97 ? 392 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 23.686 -17.606 33.348 1.00 28.57 ? 393 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 33.166 -34.217 23.980 1.00 46.24 ? 394 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 26.992 -6.486  24.745 1.00 61.10 ? 395 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 34.204 -15.572 27.221 1.00 47.01 ? 396 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 34.251 -31.908 29.529 1.00 33.66 ? 397 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 5.507  -17.141 22.259 1.00 58.15 ? 398 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 37.720 -30.928 28.734 1.00 53.01 ? 399 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 23.878 -15.830 31.568 1.00 42.11 ? 400 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 21.341 -17.508 34.559 1.00 33.38 ? 401 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 31.720 -15.805 6.865  1.00 36.70 ? 402 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 10.440 -27.187 18.494 1.00 43.50 ? 403 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 28.476 -12.793 30.362 1.00 53.00 ? 404 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 32.671 -19.449 29.095 1.00 33.39 ? 405 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 9.145  -23.336 17.844 1.00 39.90 ? 406 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 35.283 -23.203 28.927 1.00 36.43 ? 407 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 3.192  -8.887  21.965 1.00 44.56 ? 408 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   ? 0.2915 0.2527 0.2296 -0.0085 -0.0037 -0.0093 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3051 0.2675 0.2493 -0.0069 -0.0073 -0.0073 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2987 0.2628 0.2506 -0.0027 -0.0098 -0.0028 7   SER   A C   
4    O O   . SER   A 1   ? 0.3131 0.2778 0.2645 -0.0020 -0.0102 -0.0005 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3489 0.3147 0.2887 -0.0127 -0.0117 -0.0061 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3804 0.3505 0.3187 -0.0148 -0.0166 -0.0005 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2818 0.2463 0.2407 -0.0004 -0.0109 -0.0022 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2628 0.2285 0.2295 0.0029  -0.0120 0.0007  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2563 0.2212 0.2287 0.0053  -0.0100 -0.0012 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2720 0.2348 0.2424 0.0053  -0.0075 -0.0038 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2382 0.2045 0.2183 0.0069  -0.0106 0.0003  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2428 0.2089 0.2274 0.0079  -0.0081 -0.0018 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2354 0.2014 0.2259 0.0093  -0.0062 -0.0018 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2359 0.2018 0.2296 0.0101  -0.0073 0.0004  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2468 0.2156 0.2361 0.0068  -0.0100 -0.0017 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2201 0.1860 0.2119 0.0090  -0.0030 -0.0043 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2195 0.1851 0.2168 0.0090  0.0002  -0.0060 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2261 0.1938 0.2320 0.0090  0.0013  -0.0072 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2244 0.1935 0.2285 0.0078  0.0012  -0.0081 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2217 0.1868 0.2133 0.0068  0.0034  -0.0082 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2370 0.2014 0.2216 0.0068  0.0021  -0.0065 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2465 0.2110 0.2425 0.0052  0.0077  -0.0114 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2301 0.1960 0.2097 0.0041  0.0036  -0.0067 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2258 0.1938 0.2424 0.0104  0.0027  -0.0072 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2339 0.2049 0.2615 0.0106  0.0045  -0.0084 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2347 0.2039 0.2674 0.0095  0.0116  -0.0134 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2300 0.1969 0.2706 0.0110  0.0138  -0.0137 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2471 0.2207 0.2863 0.0131  0.0005  -0.0035 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2427 0.2189 0.2755 0.0122  -0.0060 0.0005  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2500 0.2298 0.2830 0.0106  -0.0075 0.0002  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2585 0.2334 0.2842 0.0120  -0.0099 0.0039  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2665 0.2482 0.2926 0.0085  -0.0127 0.0027  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2676 0.2447 0.2858 0.0097  -0.0147 0.0063  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2791 0.2593 0.2972 0.0078  -0.0159 0.0053  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2876 0.2693 0.2973 0.0044  -0.0198 0.0065  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2401 0.2101 0.2678 0.0062  0.0154  -0.0176 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2532 0.2221 0.2825 0.0030  0.0227  -0.0234 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2663 0.2386 0.3018 0.0013  0.0264  -0.0265 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2518 0.2266 0.2813 -0.0002 0.0239  -0.0251 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2731 0.2407 0.2874 -0.0015 0.0237  -0.0250 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2827 0.2524 0.2868 -0.0031 0.0197  -0.0221 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2936 0.2607 0.3070 -0.0070 0.0316  -0.0317 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2803 0.2527 0.3294 0.0017  0.0327  -0.0305 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2685 0.2449 0.3253 0.0000  0.0371  -0.0338 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2602 0.2412 0.3222 0.0029  0.0307  -0.0284 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2591 0.2408 0.3282 0.0072  0.0251  -0.0230 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2508 0.2349 0.3071 -0.0006 0.0308  -0.0295 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2556 0.2437 0.3143 0.0008  0.0248  -0.0250 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2484 0.2340 0.2906 -0.0007 0.0193  -0.0221 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2597 0.2473 0.2990 -0.0025 0.0169  -0.0208 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2790 0.2724 0.3464 -0.0015 0.0288  -0.0277 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3234 0.3204 0.4124 0.0017  0.0328  -0.0288 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3334 0.3352 0.4355 0.0051  0.0281  -0.0239 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3395 0.3346 0.4338 0.0004  0.0416  -0.0350 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2312 0.2126 0.2642 0.0001  0.0173  -0.0207 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2389 0.2178 0.2590 -0.0006 0.0129  -0.0179 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2309 0.2077 0.2492 0.0028  0.0080  -0.0143 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2333 0.2093 0.2566 0.0050  0.0083  -0.0139 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2397 0.2164 0.2488 -0.0039 0.0155  -0.0193 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2528 0.2316 0.2598 -0.0091 0.0202  -0.0224 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2716 0.2520 0.2771 -0.0113 0.0193  -0.0213 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2794 0.2585 0.2841 -0.0130 0.0257  -0.0264 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2847 0.2675 0.2874 -0.0170 0.0236  -0.0237 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2943 0.2760 0.2953 -0.0193 0.0303  -0.0295 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3082 0.2919 0.3077 -0.0212 0.0290  -0.0276 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3539 0.3406 0.3488 -0.0283 0.0336  -0.0302 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2267 0.2023 0.2381 0.0026  0.0040  -0.0120 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2224 0.1960 0.2294 0.0044  0.0000  -0.0094 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2236 0.1937 0.2205 0.0036  0.0003  -0.0092 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2355 0.2046 0.2295 0.0019  0.0005  -0.0094 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2277 0.2037 0.2370 0.0040  -0.0042 -0.0074 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2412 0.2148 0.2423 0.0037  -0.0075 -0.0059 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2534 0.2306 0.2559 0.0015  -0.0119 -0.0041 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2598 0.2337 0.2521 -0.0011 -0.0126 -0.0055 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3140 0.2870 0.2999 -0.0022 -0.0145 -0.0046 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3157 0.2910 0.3041 -0.0008 -0.0168 -0.0013 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3008 0.2704 0.2781 -0.0052 -0.0137 -0.0072 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2191 0.1873 0.2121 0.0048  0.0005  -0.0085 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2182 0.1842 0.2043 0.0044  0.0007  -0.0075 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2229 0.1869 0.2060 0.0060  -0.0014 -0.0064 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2271 0.1914 0.2103 0.0071  -0.0025 -0.0058 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2387 0.2053 0.2226 0.0036  0.0025  -0.0073 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2535 0.2196 0.2328 0.0030  0.0021  -0.0048 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2570 0.2256 0.2431 0.0009  0.0056  -0.0098 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2101 0.1717 0.1906 0.0057  -0.0014 -0.0064 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.2165 0.1759 0.1936 0.0061  -0.0019 -0.0068 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.2395 0.1989 0.2166 0.0061  -0.0019 -0.0068 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.2352 0.1916 0.2114 0.0070  0.0003  -0.0063 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.2411 0.1972 0.2195 0.0069  0.0011  -0.0046 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1980 0.1567 0.1738 0.0039  -0.0032 -0.0085 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2700 0.2293 0.2466 0.0039  -0.0034 -0.0084 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.2191 0.1819 0.1969 0.0031  -0.0064 -0.0074 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2918 0.2488 0.2630 0.0023  -0.0033 -0.0100 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1677 0.1248 0.1452 0.0024  -0.0021 -0.0096 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2829 0.2466 0.2636 0.0034  -0.0061 -0.0073 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.2308 0.1851 0.2046 0.0075  0.0014  -0.0073 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.2347 0.1858 0.2109 0.0088  0.0044  -0.0070 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.2376 0.1848 0.2152 0.0073  0.0057  -0.0087 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.2429 0.1890 0.2170 0.0047  0.0052  -0.0119 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.2342 0.1837 0.2080 0.0089  0.0067  -0.0094 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.2451 0.1981 0.2174 0.0099  0.0057  -0.0077 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.2556 0.2106 0.2237 0.0085  0.0034  -0.0080 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.2551 0.2095 0.2317 0.0121  0.0070  -0.0051 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.2237 0.1687 0.2065 0.0084  0.0070  -0.0062 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.2259 0.1660 0.2105 0.0068  0.0086  -0.0077 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2542 0.1890 0.2370 0.0054  0.0121  -0.0130 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2736 0.2060 0.2535 0.0020  0.0123  -0.0165 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.2391 0.1775 0.2312 0.0085  0.0096  -0.0027 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.2596 0.1925 0.2544 0.0066  0.0110  -0.0031 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2636 0.1948 0.2670 0.0083  0.0115  0.0034  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2841 0.2102 0.2908 0.0063  0.0124  0.0046  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.3246 0.2422 0.3362 0.0064  0.0166  0.0017  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.3243 0.2377 0.3366 0.0077  0.0209  -0.0038 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.3461 0.2589 0.3615 0.0044  0.0173  0.0039  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.2381 0.1716 0.2217 0.0070  0.0150  -0.0144 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2509 0.1790 0.2320 0.0046  0.0198  -0.0207 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2791 0.2095 0.2496 -0.0004 0.0177  -0.0248 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.3004 0.2266 0.2664 -0.0046 0.0213  -0.0306 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2431 0.1695 0.2295 0.0075  0.0248  -0.0214 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2520 0.1839 0.2335 0.0078  0.0235  -0.0211 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2641 0.2015 0.2489 0.0111  0.0203  -0.0154 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2714 0.2036 0.2448 0.0044  0.0253  -0.0259 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2591 0.1997 0.2385 0.0102  0.0201  -0.0167 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2774 0.2152 0.2499 0.0062  0.0230  -0.0226 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2675 0.2046 0.2345 -0.0004 0.0123  -0.0217 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2674 0.2082 0.2266 -0.0049 0.0087  -0.0230 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2894 0.2335 0.2495 -0.0067 0.0043  -0.0214 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.3008 0.2495 0.2570 -0.0101 0.0003  -0.0208 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2642 0.2100 0.2208 -0.0037 0.0060  -0.0202 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2836 0.2274 0.2390 -0.0028 0.0104  -0.0222 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2843 0.2330 0.2370 -0.0021 0.0074  -0.0189 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.3126 0.2525 0.2610 -0.0084 0.0149  -0.0287 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2681 0.2105 0.2341 -0.0048 0.0049  -0.0200 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2706 0.2163 0.2383 -0.0067 0.0017  -0.0189 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2964 0.2419 0.2596 -0.0127 0.0009  -0.0224 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.3084 0.2477 0.2682 -0.0156 0.0049  -0.0269 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2640 0.2077 0.2375 -0.0047 0.0031  -0.0170 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2786 0.2311 0.2428 -0.0148 -0.0039 -0.0204 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2895 0.2443 0.2499 -0.0215 -0.0062 -0.0224 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2948 0.2478 0.2591 -0.0233 -0.0051 -0.0236 24  THR   A C   
141  O O   . THR   A 18  ? 0.2742 0.2255 0.2444 -0.0193 -0.0033 -0.0219 24  THR   A O   
142  C CB  . THR   A 18  ? 0.3182 0.2827 0.2805 -0.0230 -0.0125 -0.0180 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.3261 0.2951 0.2986 -0.0191 -0.0142 -0.0145 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.3263 0.2926 0.2852 -0.0215 -0.0141 -0.0157 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.3023 0.2566 0.2629 -0.0302 -0.0064 -0.0262 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.3085 0.2620 0.2730 -0.0326 -0.0058 -0.0270 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.3045 0.2663 0.2784 -0.0294 -0.0092 -0.0222 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.3009 0.2607 0.2795 -0.0279 -0.0070 -0.0218 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.3398 0.2949 0.2983 -0.0417 -0.0074 -0.0305 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.4560 0.4127 0.4195 -0.0447 -0.0079 -0.0306 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.5156 0.4631 0.4808 -0.0441 -0.0028 -0.0331 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4952 0.4622 0.4641 -0.0474 -0.0130 -0.0274 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.5213 0.4731 0.4906 -0.0476 -0.0046 -0.0323 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.5295 0.4935 0.5018 -0.0494 -0.0106 -0.0290 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2914 0.2620 0.2687 -0.0283 -0.0140 -0.0184 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2943 0.2720 0.2826 -0.0250 -0.0157 -0.0146 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.2746 0.2483 0.2657 -0.0191 -0.0116 -0.0143 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2730 0.2491 0.2707 -0.0181 -0.0102 -0.0137 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.3131 0.3002 0.3070 -0.0245 -0.0210 -0.0100 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.4190 0.4135 0.4269 -0.0215 -0.0217 -0.0070 26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.4594 0.4594 0.4737 -0.0245 -0.0229 -0.0066 26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.4405 0.4349 0.4540 -0.0158 -0.0201 -0.0054 26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.2592 0.2274 0.2451 -0.0159 -0.0097 -0.0147 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.2361 0.2012 0.2237 -0.0115 -0.0065 -0.0139 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.2453 0.2056 0.2328 -0.0129 -0.0034 -0.0148 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.2613 0.2233 0.2523 -0.0120 -0.0019 -0.0135 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.2564 0.2170 0.2389 -0.0086 -0.0052 -0.0139 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2714 0.2362 0.2545 -0.0068 -0.0078 -0.0120 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.2508 0.2210 0.2407 -0.0054 -0.0092 -0.0100 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2669 0.2294 0.2443 -0.0070 -0.0080 -0.0126 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.2483 0.2022 0.2316 -0.0155 -0.0018 -0.0172 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.2541 0.2026 0.2384 -0.0168 0.0010  -0.0172 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.2604 0.2135 0.2486 -0.0203 0.0001  -0.0170 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.2753 0.2265 0.2654 -0.0211 0.0020  -0.0156 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2626 0.2022 0.2431 -0.0192 0.0037  -0.0206 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2741 0.2078 0.2540 -0.0153 0.0065  -0.0202 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2920 0.2244 0.2678 -0.0146 0.0072  -0.0227 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2777 0.2073 0.2618 -0.0118 0.0086  -0.0164 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2830 0.2104 0.2615 -0.0106 0.0104  -0.0214 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2825 0.2085 0.2667 -0.0087 0.0109  -0.0170 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2978 0.2268 0.2859 -0.0118 0.0088  -0.0122 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2966 0.2195 0.2864 -0.0048 0.0126  -0.0126 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.3044 0.2306 0.2964 -0.0086 0.0099  -0.0075 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.3091 0.2320 0.3030 -0.0051 0.0118  -0.0075 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.2636 0.2233 0.2533 -0.0231 -0.0029 -0.0181 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.2672 0.2326 0.2623 -0.0265 -0.0036 -0.0180 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2735 0.2460 0.2760 -0.0238 -0.0032 -0.0159 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2841 0.2613 0.2920 -0.0263 -0.0024 -0.0160 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2838 0.2549 0.2793 -0.0310 -0.0075 -0.0190 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.2572 0.2303 0.2598 -0.0193 -0.0029 -0.0147 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.2517 0.2302 0.2607 -0.0171 -0.0010 -0.0140 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.2570 0.2308 0.2608 -0.0148 0.0015  -0.0132 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.2519 0.2278 0.2575 -0.0123 0.0024  -0.0131 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.2636 0.2487 0.2799 -0.0145 -0.0036 -0.0130 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.3190 0.3111 0.3425 -0.0175 -0.0067 -0.0123 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.3352 0.3331 0.3676 -0.0187 -0.0051 -0.0127 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.3196 0.3120 0.3391 -0.0197 -0.0112 -0.0115 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.2577 0.2251 0.2559 -0.0161 0.0026  -0.0123 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.2540 0.2177 0.2478 -0.0143 0.0038  -0.0101 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.2619 0.2292 0.2557 -0.0161 0.0061  -0.0093 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.2847 0.2541 0.2798 -0.0200 0.0078  -0.0094 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.2403 0.1965 0.2312 -0.0153 0.0041  -0.0083 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.2664 0.2193 0.2550 -0.0133 0.0046  -0.0044 31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.2623 0.2146 0.2497 -0.0092 0.0037  -0.0051 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.3055 0.2506 0.2949 -0.0139 0.0054  -0.0020 31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.2485 0.2165 0.2400 -0.0143 0.0065  -0.0084 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.2531 0.2243 0.2420 -0.0174 0.0090  -0.0079 32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.2624 0.2304 0.2458 -0.0184 0.0077  -0.0027 32  VAL   A C   
209  O O   . VAL   A 26  ? 0.2953 0.2645 0.2758 -0.0230 0.0084  0.0001  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.2643 0.2389 0.2549 -0.0159 0.0107  -0.0108 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.2902 0.2674 0.2758 -0.0205 0.0138  -0.0110 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.2747 0.2529 0.2742 -0.0147 0.0120  -0.0145 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.2561 0.2209 0.2388 -0.0143 0.0057  -0.0008 33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.2568 0.2200 0.2373 -0.0146 0.0042  0.0049  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.2782 0.2370 0.2611 -0.0094 0.0030  0.0056  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.2680 0.2268 0.2512 -0.0066 0.0030  0.0017  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.2693 0.2378 0.2454 -0.0174 0.0046  0.0058  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.2867 0.2561 0.2611 -0.0178 0.0022  0.0123  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.3196 0.2905 0.2927 -0.0218 0.0004  0.0193  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.2923 0.2620 0.2673 -0.0142 0.0009  0.0133  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.3378 0.3107 0.3117 -0.0208 -0.0023 0.0250  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.3145 0.2867 0.2895 -0.0162 -0.0018 0.0210  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.2920 0.2607 0.2680 -0.0100 0.0014  0.0090  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.3293 0.3036 0.3057 -0.0139 -0.0035 0.0240  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2974 0.2673 0.2734 -0.0081 0.0000  0.0116  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.3104 0.2833 0.2871 -0.0099 -0.0023 0.0187  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.2871 0.2421 0.2725 -0.0084 0.0022  0.0104  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.2857 0.2368 0.2745 -0.0038 0.0023  0.0107  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.2887 0.2399 0.2818 -0.0032 0.0012  0.0182  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2915 0.2431 0.2860 -0.0062 0.0001  0.0238  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.2831 0.2275 0.2742 -0.0025 0.0041  0.0066  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2966 0.2364 0.2906 -0.0050 0.0050  0.0084  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.3300 0.2643 0.3311 -0.0033 0.0059  0.0141  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.3652 0.2973 0.3691 -0.0058 0.0056  0.0185  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.3327 0.2650 0.3381 0.0006  0.0070  0.0146  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.2689 0.2199 0.2650 0.0006  0.0012  0.0192  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.2688 0.2211 0.2719 0.0018  -0.0001 0.0272  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.2724 0.2207 0.2821 0.0071  0.0023  0.0253  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.2733 0.2244 0.2799 0.0086  0.0025  0.0222  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.2874 0.2484 0.2861 -0.0014 -0.0033 0.0317  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.3548 0.3195 0.3611 -0.0012 -0.0061 0.0417  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.3953 0.3560 0.4121 0.0036  -0.0047 0.0440  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.3665 0.3385 0.3685 -0.0065 -0.0095 0.0474  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.2788 0.2201 0.2975 0.0095  0.0051  0.0264  36  SER   A N   
245  C CA  A SER   A 30  ? 0.2742 0.2111 0.2999 0.0139  0.0091  0.0234  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2851 0.2221 0.3107 0.0139  0.0091  0.0233  36  SER   A CA  
247  C C   . SER   A 30  ? 0.2780 0.2210 0.3107 0.0166  0.0077  0.0296  36  SER   A C   
248  O O   . SER   A 30  ? 0.2890 0.2321 0.3230 0.0193  0.0103  0.0256  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2829 0.2102 0.3184 0.0154  0.0134  0.0231  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.3253 0.2526 0.3603 0.0154  0.0135  0.0226  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2917 0.2147 0.3366 0.0195  0.0185  0.0208  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3848 0.3127 0.4297 0.0156  0.0113  0.0327  36  SER   A OG  
253  N N   . SER   A 31  ? 0.2606 0.2099 0.2975 0.0150  0.0032  0.0396  37  SER   A N   
254  C CA  . SER   A 31  ? 0.2592 0.2161 0.3033 0.0167  0.0009  0.0465  37  SER   A CA  
255  C C   . SER   A 31  ? 0.2610 0.2242 0.2945 0.0153  -0.0005 0.0423  37  SER   A C   
256  O O   . SER   A 31  ? 0.2788 0.2468 0.3178 0.0173  -0.0007 0.0449  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2938 0.2576 0.3430 0.0137  -0.0047 0.0590  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.3690 0.3393 0.4042 0.0072  -0.0088 0.0596  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.2399 0.2028 0.2600 0.0121  -0.0009 0.0358  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.2380 0.2054 0.2493 0.0108  -0.0016 0.0315  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.2260 0.1880 0.2328 0.0131  0.0019  0.0223  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.2243 0.1891 0.2247 0.0123  0.0015  0.0190  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.2472 0.2185 0.2479 0.0051  -0.0042 0.0309  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.2468 0.2256 0.2483 0.0007  -0.0082 0.0399  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.2454 0.2278 0.2357 -0.0062 -0.0093 0.0380  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.2451 0.2300 0.2282 -0.0078 -0.0083 0.0323  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.2893 0.2792 0.2639 -0.0144 -0.0089 0.0313  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.3130 0.3073 0.2838 -0.0209 -0.0108 0.0361  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.2579 0.2486 0.2276 -0.0153 -0.0072 0.0257  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.2225 0.1771 0.2316 0.0147  0.0052  0.0183  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.2282 0.1785 0.2313 0.0149  0.0077  0.0101  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.2383 0.1908 0.2320 0.0120  0.0053  0.0070  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.2288 0.1817 0.2175 0.0119  0.0054  0.0029  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.2499 0.2007 0.2538 0.0171  0.0101  0.0076  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.2474 0.1943 0.2444 0.0160  0.0124  0.0002  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2670 0.2086 0.2632 0.0147  0.0143  -0.0034 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.2448 0.1943 0.2371 0.0157  0.0122  -0.0018 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.2233 0.1775 0.2155 0.0094  0.0033  0.0092  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.2082 0.1648 0.1942 0.0070  0.0021  0.0060  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.2272 0.1814 0.2128 0.0049  0.0024  0.0041  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.2423 0.1942 0.2310 0.0041  0.0027  0.0071  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.2141 0.1765 0.1975 0.0043  0.0004  0.0088  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.2284 0.1945 0.2105 0.0048  -0.0002 0.0096  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.2363 0.2077 0.2144 0.0003  -0.0012 0.0112  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.2438 0.2084 0.2234 0.0065  0.0006  0.0047  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.2242 0.1791 0.2070 0.0041  0.0021  -0.0001 41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.2226 0.1771 0.2055 0.0018  0.0021  -0.0020 41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.2335 0.1924 0.2159 0.0009  0.0015  -0.0042 41  LEU   A C   
289  O O   . LEU   A 35  ? 0.2345 0.1947 0.2165 0.0025  0.0008  -0.0054 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.2169 0.1668 0.2000 0.0017  0.0028  -0.0050 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.2290 0.1788 0.2127 -0.0014 0.0026  -0.0068 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.2400 0.1835 0.2240 -0.0027 0.0042  -0.0088 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.2393 0.1936 0.2229 -0.0023 0.0008  -0.0093 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.2249 0.1863 0.2084 -0.0019 0.0023  -0.0045 42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.2221 0.1875 0.2080 -0.0026 0.0030  -0.0071 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.2162 0.1829 0.2059 -0.0043 0.0031  -0.0088 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.2278 0.1933 0.2167 -0.0068 0.0038  -0.0080 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.2195 0.1878 0.2037 -0.0055 0.0053  -0.0070 42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.2457 0.2174 0.2346 -0.0063 0.0078  -0.0108 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.2287 0.1970 0.2092 -0.0047 0.0047  -0.0050 42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.2221 0.1912 0.2164 -0.0031 0.0020  -0.0103 43  SER   A N   
302  C CA  . SER   A 37  ? 0.2130 0.1852 0.2126 -0.0049 0.0015  -0.0114 43  SER   A CA  
303  C C   . SER   A 37  ? 0.2259 0.2034 0.2342 -0.0046 0.0034  -0.0128 43  SER   A C   
304  O O   . SER   A 37  ? 0.2290 0.2068 0.2389 -0.0027 0.0048  -0.0133 43  SER   A O   
305  C CB  . SER   A 37  ? 0.2241 0.1958 0.2233 -0.0050 -0.0020 -0.0112 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.2476 0.2209 0.2481 -0.0027 -0.0042 -0.0101 43  SER   A OG  
307  N N   . SER   A 38  ? 0.2460 0.2278 0.2612 -0.0064 0.0040  -0.0138 44  SER   A N   
308  C CA  . SER   A 38  ? 0.2536 0.2407 0.2802 -0.0057 0.0068  -0.0154 44  SER   A CA  
309  C C   . SER   A 38  ? 0.2741 0.2654 0.3108 -0.0030 0.0030  -0.0130 44  SER   A C   
310  O O   . SER   A 38  ? 0.2867 0.2786 0.3210 -0.0038 -0.0019 -0.0106 44  SER   A O   
311  C CB  . SER   A 38  ? 0.2853 0.2760 0.3160 -0.0093 0.0102  -0.0175 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.3144 0.3070 0.3467 -0.0108 0.0066  -0.0159 44  SER   A OG  
313  N N   . THR   A 39  ? 0.2791 0.2732 0.3273 -0.0004 0.0053  -0.0133 45  THR   A N   
314  C CA  . THR   A 39  ? 0.2963 0.2948 0.3561 0.0023  0.0011  -0.0092 45  THR   A CA  
315  C C   . THR   A 39  ? 0.3126 0.3179 0.3913 0.0033  0.0042  -0.0096 45  THR   A C   
316  O O   . THR   A 39  ? 0.3071 0.3121 0.3895 0.0025  0.0114  -0.0144 45  THR   A O   
317  C CB  . THR   A 39  ? 0.3143 0.3091 0.3736 0.0055  0.0005  -0.0076 45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.3282 0.3210 0.3929 0.0066  0.0074  -0.0115 45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.3185 0.3075 0.3613 0.0049  -0.0019 -0.0072 45  THR   A CG2 
320  N N   . THR   A 40  ? 0.3247 0.3365 0.4161 0.0046  -0.0010 -0.0043 46  THR   A N   
321  C CA  . THR   A 40  ? 0.3464 0.3657 0.4596 0.0063  0.0017  -0.0035 46  THR   A CA  
322  C C   . THR   A 40  ? 0.3481 0.3652 0.4742 0.0110  0.0058  -0.0034 46  THR   A C   
323  O O   . THR   A 40  ? 0.3622 0.3800 0.5009 0.0120  0.0139  -0.0080 46  THR   A O   
324  C CB  . THR   A 40  ? 0.3947 0.4235 0.5177 0.0053  -0.0063 0.0035  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.4450 0.4741 0.5680 0.0069  -0.0132 0.0101  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.4117 0.4412 0.5207 -0.0001 -0.0097 0.0025  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.3487 0.3626 0.4713 0.0131  0.0011  0.0011  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.3546 0.3650 0.4890 0.0173  0.0047  0.0015  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.3521 0.3532 0.4724 0.0165  0.0111  -0.0054 47  ALA   A C   
330  O O   . ALA   A 41  ? 0.3492 0.3464 0.4491 0.0136  0.0094  -0.0073 47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.3762 0.3879 0.5135 0.0192  -0.0037 0.0105  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.3371 0.3346 0.4691 0.0187  0.0185  -0.0089 48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.3461 0.3356 0.4657 0.0169  0.0247  -0.0154 48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.3234 0.3080 0.4356 0.0187  0.0198  -0.0110 48  GLN   A C   
335  O O   . GLN   A 42  ? 0.3180 0.3039 0.4432 0.0223  0.0156  -0.0043 48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.3956 0.3827 0.5303 0.0174  0.0357  -0.0222 48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.4616 0.4516 0.5952 0.0132  0.0433  -0.0298 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.5217 0.5086 0.6679 0.0123  0.0557  -0.0382 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.5093 0.4979 0.6800 0.0165  0.0595  -0.0375 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.5521 0.5345 0.6823 0.0063  0.0624  -0.0463 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.2952 0.2749 0.3875 0.0158  0.0200  -0.0140 49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.2849 0.2601 0.3676 0.0166  0.0160  -0.0108 49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.2762 0.2452 0.3622 0.0167  0.0223  -0.0146 49  GLY   A C   
344  O O   . GLY   A 43  ? 0.2852 0.2525 0.3765 0.0150  0.0308  -0.0216 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.2649 0.2304 0.3470 0.0180  0.0185  -0.0105 50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.2767 0.2357 0.3630 0.0181  0.0240  -0.0134 50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.2852 0.2402 0.3535 0.0144  0.0252  -0.0168 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.2987 0.2481 0.3693 0.0133  0.0302  -0.0201 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.2930 0.2506 0.3932 0.0222  0.0202  -0.0058 50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.3344 0.2969 0.4626 0.0268  0.0201  -0.0011 50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.2448 0.2024 0.2965 0.0123  0.0207  -0.0159 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.2469 0.2022 0.2834 0.0088  0.0213  -0.0180 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.2707 0.2255 0.3016 0.0036  0.0283  -0.0255 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2946 0.2522 0.3277 0.0021  0.0310  -0.0284 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.2370 0.1955 0.2606 0.0087  0.0148  -0.0142 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.2825 0.2415 0.3073 0.0118  0.0083  -0.0076 51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.2813 0.2373 0.3108 0.0130  0.0080  -0.0052 51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.2655 0.2276 0.2856 0.0122  0.0039  -0.0050 51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2826 0.2346 0.3058 -0.0002 0.0310  -0.0285 52  THR   A N   
360  C CA  . THR   A 46  ? 0.3039 0.2565 0.3183 -0.0072 0.0367  -0.0349 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2917 0.2475 0.2905 -0.0105 0.0320  -0.0321 52  THR   A C   
362  O O   . THR   A 46  ? 0.2977 0.2526 0.2934 -0.0085 0.0278  -0.0280 52  THR   A O   
363  C CB  . THR   A 46  ? 0.3772 0.3242 0.3958 -0.0104 0.0441  -0.0410 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.4270 0.3714 0.4630 -0.0074 0.0498  -0.0442 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.4140 0.3620 0.4196 -0.0199 0.0494  -0.0477 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.2828 0.2427 0.2725 -0.0157 0.0327  -0.0336 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.2701 0.2339 0.2475 -0.0188 0.0280  -0.0295 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.2794 0.2435 0.2487 -0.0261 0.0309  -0.0327 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2796 0.2431 0.2467 -0.0328 0.0375  -0.0394 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.2723 0.2410 0.2443 -0.0210 0.0259  -0.0273 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.2881 0.2564 0.2679 -0.0151 0.0238  -0.0253 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.2748 0.2478 0.2377 -0.0230 0.0203  -0.0213 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2858 0.2527 0.2687 -0.0082 0.0179  -0.0199 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.2629 0.2286 0.2270 -0.0260 0.0264  -0.0283 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.2642 0.2318 0.2198 -0.0338 0.0279  -0.0302 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.2873 0.2619 0.2327 -0.0419 0.0271  -0.0293 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.2823 0.2613 0.2265 -0.0399 0.0222  -0.0235 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.2603 0.2296 0.2142 -0.0312 0.0225  -0.0244 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.3130 0.2887 0.2505 -0.0521 0.0319  -0.0350 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.3203 0.3040 0.2464 -0.0618 0.0305  -0.0333 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.3441 0.3315 0.2614 -0.0703 0.0296  -0.0333 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.3590 0.3445 0.2702 -0.0795 0.0362  -0.0415 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.3195 0.3020 0.2429 -0.0684 0.0382  -0.0414 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.3193 0.2986 0.2528 -0.0603 0.0394  -0.0418 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.3043 0.2885 0.2375 -0.0563 0.0318  -0.0326 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2947 0.2756 0.2374 -0.0495 0.0335  -0.0340 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.3159 0.2979 0.2621 -0.0434 0.0279  -0.0274 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.3172 0.3029 0.2599 -0.0423 0.0210  -0.0193 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.3310 0.3105 0.2857 -0.0383 0.0296  -0.0291 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.3405 0.3333 0.2577 -0.0676 0.0220  -0.0245 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.3530 0.3497 0.2649 -0.0735 0.0201  -0.0233 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.3561 0.3619 0.2689 -0.0715 0.0112  -0.0119 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.3740 0.3818 0.2922 -0.0649 0.0070  -0.0055 56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.3464 0.3341 0.2654 -0.0676 0.0237  -0.0278 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.3268 0.3114 0.2580 -0.0525 0.0186  -0.0209 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.3707 0.3818 0.2805 -0.0763 0.0085  -0.0093 57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3861 0.4060 0.3005 -0.0731 0.0007  0.0016  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3720 0.3891 0.2924 -0.0675 0.0005  0.0017  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3752 0.4008 0.2970 -0.0695 -0.0041 0.0081  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.4703 0.5034 0.3766 -0.0852 -0.0044 0.0079  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.6075 0.6429 0.5040 -0.0969 -0.0020 0.0028  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.6411 0.6663 0.5368 -0.0962 0.0049  -0.0072 57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.6764 0.7241 0.5667 -0.1071 -0.0073 0.0091  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.3485 0.3547 0.2735 -0.0605 0.0052  -0.0044 58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.3107 0.3137 0.2412 -0.0550 0.0050  -0.0038 58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.3174 0.3262 0.2556 -0.0475 -0.0004 0.0049  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.3387 0.3481 0.2810 -0.0422 -0.0023 0.0084  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2806 0.2714 0.2158 -0.0484 0.0100  -0.0100 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.3428 0.3247 0.2739 -0.0557 0.0182  -0.0208 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2895 0.3020 0.2303 -0.0473 -0.0021 0.0078  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.2883 0.3053 0.2380 -0.0400 -0.0054 0.0146  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.2705 0.2815 0.2230 -0.0352 -0.0030 0.0121  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.2838 0.2991 0.2425 -0.0314 -0.0045 0.0163  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.3137 0.3441 0.2661 -0.0447 -0.0103 0.0225  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.3876 0.4258 0.3408 -0.0473 -0.0144 0.0288  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.4527 0.5051 0.4130 -0.0501 -0.0200 0.0388  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.4975 0.5594 0.4523 -0.0602 -0.0235 0.0423  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.3962 0.4512 0.3696 -0.0418 -0.0208 0.0438  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.2509 0.2523 0.1996 -0.0360 0.0010  0.0055  60  THR   A N   
420  C CA  . THR   A 54  ? 0.2532 0.2477 0.2045 -0.0315 0.0030  0.0038  60  THR   A CA  
421  C C   . THR   A 54  ? 0.2496 0.2339 0.2019 -0.0271 0.0056  -0.0004 60  THR   A C   
422  O O   . THR   A 54  ? 0.2724 0.2532 0.2224 -0.0301 0.0080  -0.0047 60  THR   A O   
423  C CB  . THR   A 54  ? 0.2921 0.2860 0.2407 -0.0370 0.0044  0.0021  60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.3643 0.3527 0.3078 -0.0433 0.0080  -0.0040 60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.2805 0.2859 0.2291 -0.0417 0.0013  0.0068  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.2255 0.2059 0.1815 -0.0208 0.0054  0.0009  61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.2230 0.1951 0.1813 -0.0168 0.0069  -0.0015 61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.2185 0.1877 0.1791 -0.0120 0.0058  0.0009  61  GLY   A C   
429  O O   . GLY   A 55  ? 0.2465 0.2184 0.2063 -0.0126 0.0052  0.0032  61  GLY   A O   
430  N N   . VAL   A 56  ? 0.2205 0.1852 0.1838 -0.0080 0.0055  0.0007  62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.2230 0.1853 0.1872 -0.0048 0.0040  0.0033  62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.2188 0.1818 0.1839 -0.0010 0.0025  0.0038  62  VAL   A C   
433  O O   . VAL   A 56  ? 0.2300 0.1917 0.1974 -0.0002 0.0029  0.0019  62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.2426 0.1979 0.2106 -0.0050 0.0049  0.0034  62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.2849 0.2386 0.2535 -0.0026 0.0022  0.0074  62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.2512 0.2046 0.2181 -0.0093 0.0070  0.0025  62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1995 0.1647 0.1624 0.0005  0.0014  0.0056  63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1955 0.1606 0.1585 0.0030  0.0003  0.0054  63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.2158 0.1791 0.1767 0.0031  -0.0015 0.0074  63  TYR   A C   
440  O O   . TYR   A 57  ? 0.2279 0.1914 0.1861 0.0013  -0.0015 0.0092  63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.2046 0.1739 0.1674 0.0042  0.0013  0.0049  63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.2074 0.1789 0.1682 0.0040  0.0026  0.0055  63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.2291 0.2038 0.1899 0.0024  0.0037  0.0066  63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.2278 0.1985 0.1865 0.0047  0.0033  0.0043  63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.2396 0.2168 0.1995 0.0020  0.0059  0.0066  63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.2360 0.2087 0.1930 0.0039  0.0060  0.0035  63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.2308 0.2068 0.1888 0.0028  0.0073  0.0047  63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.2600 0.2384 0.2168 0.0016  0.0108  0.0037  63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.2196 0.1821 0.1812 0.0042  -0.0031 0.0073  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.2043 0.1666 0.1626 0.0029  -0.0055 0.0097  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.2192 0.1837 0.1716 0.0018  -0.0040 0.0076  64  TYR   A C   
452  O O   . TYR   A 58  ? 0.2228 0.1875 0.1762 0.0032  -0.0028 0.0049  64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.2099 0.1712 0.1727 0.0038  -0.0085 0.0112  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.2368 0.1994 0.1960 0.0011  -0.0121 0.0151  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.2485 0.2106 0.2064 -0.0011 -0.0140 0.0196  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.2426 0.2071 0.1982 -0.0004 -0.0137 0.0143  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.2610 0.2253 0.2141 -0.0049 -0.0180 0.0241  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.2354 0.2023 0.1859 -0.0046 -0.0175 0.0180  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.2614 0.2285 0.2105 -0.0069 -0.0199 0.0234  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2898 0.2603 0.2330 -0.0123 -0.0244 0.0284  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.2138 0.1793 0.1603 -0.0013 -0.0039 0.0088  65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.2243 0.1915 0.1647 -0.0036 -0.0011 0.0060  65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.2463 0.2139 0.1796 -0.0081 -0.0042 0.0078  65  CYS   A C   
464  O O   . CYS   A 59  ? 0.2563 0.2249 0.1850 -0.0118 -0.0062 0.0115  65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.2313 0.2004 0.1698 -0.0049 0.0022  0.0056  65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.2649 0.2358 0.1973 -0.0081 0.0077  0.0008  65  CYS   A SG  
467  N N   . SER   A 60  ? 0.2532 0.2206 0.1853 -0.0087 -0.0048 0.0055  66  SER   A N   
468  C CA  . SER   A 60  ? 0.2483 0.2174 0.1733 -0.0142 -0.0085 0.0077  66  SER   A CA  
469  C C   . SER   A 60  ? 0.2688 0.2397 0.1825 -0.0208 -0.0059 0.0059  66  SER   A C   
470  O O   . SER   A 60  ? 0.2890 0.2625 0.1957 -0.0266 -0.0101 0.0103  66  SER   A O   
471  C CB  . SER   A 60  ? 0.2735 0.2424 0.1990 -0.0144 -0.0093 0.0050  66  SER   A CB  
472  O OG  . SER   A 60  ? 0.3135 0.2805 0.2365 -0.0147 -0.0035 -0.0018 66  SER   A OG  
473  N N   . SER   A 61  ? 0.2538 0.2238 0.1663 -0.0202 0.0011  -0.0001 67  SER   A N   
474  C CA  . SER   A 61  ? 0.2520 0.2236 0.1546 -0.0266 0.0057  -0.0035 67  SER   A CA  
475  C C   . SER   A 61  ? 0.2509 0.2248 0.1500 -0.0292 0.0043  0.0012  67  SER   A C   
476  O O   . SER   A 61  ? 0.2689 0.2447 0.1588 -0.0355 0.0078  -0.0010 67  SER   A O   
477  C CB  . SER   A 61  ? 0.2677 0.2377 0.1736 -0.0245 0.0144  -0.0113 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.2837 0.2538 0.2000 -0.0181 0.0166  -0.0105 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.2479 0.2211 0.1544 -0.0249 0.0000  0.0071  68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.2649 0.2393 0.1694 -0.0273 -0.0019 0.0124  68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.2755 0.2489 0.1837 -0.0269 -0.0097 0.0207  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.2947 0.2681 0.2026 -0.0288 -0.0119 0.0262  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.2630 0.2369 0.1749 -0.0226 0.0018  0.0110  68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.2678 0.2437 0.1791 -0.0228 0.0096  0.0043  68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.2724 0.2510 0.1740 -0.0299 0.0125  0.0039  68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2972 0.2780 0.2009 -0.0296 0.0211  -0.0028 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.3052 0.2857 0.2050 -0.0323 0.0268  -0.0095 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.3218 0.3005 0.2139 -0.0360 0.0242  -0.0104 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.3382 0.3206 0.2427 -0.0317 0.0355  -0.0154 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.2846 0.2572 0.1983 -0.0241 -0.0134 0.0218  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.3021 0.2738 0.2240 -0.0222 -0.0198 0.0294  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.3213 0.2894 0.2516 -0.0181 -0.0188 0.0314  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.3598 0.3266 0.2938 -0.0191 -0.0225 0.0385  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.3389 0.3139 0.2550 -0.0290 -0.0261 0.0374  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.3619 0.3407 0.2726 -0.0330 -0.0289 0.0369  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.3906 0.3734 0.3012 -0.0382 -0.0374 0.0479  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.4068 0.3947 0.3082 -0.0448 -0.0400 0.0470  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.3835 0.3754 0.2687 -0.0548 -0.0399 0.0461  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.3902 0.3820 0.2670 -0.0590 -0.0375 0.0469  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.3829 0.3790 0.2593 -0.0615 -0.0418 0.0442  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.2908 0.2573 0.2242 -0.0141 -0.0137 0.0255  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.2842 0.2479 0.2235 -0.0118 -0.0121 0.0262  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.2638 0.2261 0.2098 -0.0070 -0.0091 0.0214  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.2715 0.2355 0.2163 -0.0055 -0.0069 0.0169  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.3394 0.3050 0.2720 -0.0151 -0.0088 0.0252  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.4301 0.3956 0.3581 -0.0202 -0.0119 0.0319  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.5299 0.4975 0.4519 -0.0238 -0.0081 0.0308  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.6027 0.5700 0.5199 -0.0295 -0.0114 0.0382  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.6602 0.6304 0.5689 -0.0347 -0.0154 0.0420  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.2552 0.2140 0.2081 -0.0054 -0.0087 0.0223  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.2503 0.2084 0.2077 -0.0028 -0.0057 0.0178  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.2588 0.2183 0.2136 -0.0047 -0.0029 0.0165  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.3177 0.2755 0.2718 -0.0072 -0.0031 0.0194  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.2317 0.1849 0.1981 -0.0011 -0.0060 0.0186  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.2463 0.1990 0.2182 0.0011  -0.0086 0.0201  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2985 0.2515 0.2742 0.0035  -0.0071 0.0161  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.2510 0.2038 0.2254 0.0007  -0.0128 0.0257  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.2785 0.2317 0.2596 0.0048  -0.0101 0.0190  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.2967 0.2500 0.2778 0.0032  -0.0138 0.0251  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.2373 0.2006 0.1917 -0.0038 -0.0005 0.0130  72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.2377 0.2044 0.1910 -0.0058 0.0017  0.0125  72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.2391 0.2068 0.1959 -0.0060 0.0027  0.0104  72  TYR   A C   
523  O O   . TYR   A 66  ? 0.2291 0.1981 0.1877 -0.0041 0.0027  0.0086  72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.2440 0.2164 0.1956 -0.0052 0.0037  0.0111  72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.2508 0.2235 0.1967 -0.0071 0.0041  0.0120  72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.2619 0.2353 0.2041 -0.0107 0.0047  0.0141  72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.2523 0.2246 0.1955 -0.0064 0.0041  0.0104  72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.2889 0.2634 0.2244 -0.0139 0.0054  0.0147  72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.2754 0.2487 0.2117 -0.0098 0.0051  0.0104  72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2877 0.2622 0.2197 -0.0137 0.0057  0.0126  72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.3270 0.3028 0.2503 -0.0186 0.0067  0.0126  72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.2423 0.2102 0.1989 -0.0092 0.0038  0.0106  73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.2491 0.2199 0.2071 -0.0113 0.0047  0.0086  73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.2668 0.2463 0.2258 -0.0109 0.0047  0.0094  73  PRO   A C   
535  O O   . PRO   A 67  ? 0.2902 0.2738 0.2494 -0.0108 0.0054  0.0110  73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.2753 0.2439 0.2323 -0.0159 0.0058  0.0085  73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.2772 0.2445 0.2326 -0.0159 0.0055  0.0115  73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.2447 0.2109 0.1993 -0.0122 0.0040  0.0129  73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.2416 0.2244 0.2023 -0.0109 0.0040  0.0088  74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.2583 0.2497 0.2228 -0.0103 0.0035  0.0111  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.2509 0.2476 0.2156 -0.0144 0.0021  0.0120  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.2534 0.2461 0.2147 -0.0168 0.0021  0.0094  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.3011 0.2921 0.2685 -0.0052 0.0035  0.0113  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.3241 0.3129 0.2907 -0.0028 0.0053  0.0107  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.3057 0.2913 0.2713 -0.0041 0.0027  0.0092  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.2473 0.2535 0.2167 -0.0155 0.0008  0.0158  75  SER   A N   
547  C CA  . SER   A 69  ? 0.2499 0.2640 0.2206 -0.0193 -0.0018 0.0188  75  SER   A CA  
548  C C   . SER   A 69  ? 0.2324 0.2492 0.2099 -0.0143 -0.0029 0.0220  75  SER   A C   
549  O O   . SER   A 69  ? 0.2387 0.2562 0.2228 -0.0091 -0.0013 0.0232  75  SER   A O   
550  C CB  . SER   A 69  ? 0.3044 0.3289 0.2791 -0.0232 -0.0032 0.0230  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.4119 0.4339 0.3802 -0.0290 -0.0022 0.0200  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.2230 0.2409 0.1989 -0.0162 -0.0050 0.0232  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.2258 0.2447 0.2082 -0.0116 -0.0059 0.0263  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.2361 0.2640 0.2209 -0.0159 -0.0099 0.0325  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.2553 0.2869 0.2329 -0.0236 -0.0117 0.0324  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.2301 0.2390 0.2084 -0.0082 -0.0040 0.0215  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.2380 0.2424 0.2076 -0.0127 -0.0037 0.0173  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.2395 0.2373 0.2043 -0.0137 -0.0014 0.0122  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.2381 0.2443 0.2055 -0.0158 -0.0052 0.0183  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.2637 0.2571 0.2232 -0.0175 0.0001  0.0078  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.2599 0.2619 0.2201 -0.0202 -0.0035 0.0133  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.2567 0.2521 0.2139 -0.0207 -0.0005 0.0078  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.2318 0.2638 0.2271 -0.0117 -0.0112 0.0382  77  SER   A N   
564  C CA  . SER   A 71  ? 0.2312 0.2729 0.2309 -0.0155 -0.0160 0.0465  77  SER   A CA  
565  C C   . SER   A 71  ? 0.2364 0.2747 0.2278 -0.0191 -0.0174 0.0455  77  SER   A C   
566  O O   . SER   A 71  ? 0.2525 0.2809 0.2375 -0.0170 -0.0142 0.0385  77  SER   A O   
567  C CB  . SER   A 71  ? 0.2507 0.2973 0.2675 -0.0093 -0.0166 0.0538  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.2722 0.3095 0.2920 -0.0027 -0.0134 0.0508  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.2339 0.2813 0.2249 -0.0255 -0.0222 0.0525  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.2418 0.2873 0.2244 -0.0302 -0.0233 0.0520  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.2616 0.3022 0.2525 -0.0230 -0.0229 0.0547  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.2577 0.3000 0.2626 -0.0164 -0.0231 0.0598  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.2566 0.3149 0.2358 -0.0405 -0.0292 0.0601  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.3210 0.3824 0.2881 -0.0499 -0.0287 0.0552  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.4029 0.4771 0.3633 -0.0625 -0.0344 0.0623  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.4952 0.5687 0.4401 -0.0732 -0.0317 0.0538  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.5490 0.6340 0.4834 -0.0876 -0.0364 0.0587  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.2563 0.2902 0.2398 -0.0240 -0.0213 0.0504  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.2671 0.2956 0.2580 -0.0178 -0.0205 0.0522  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.2682 0.3049 0.2714 -0.0175 -0.0253 0.0646  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.2916 0.3382 0.2924 -0.0252 -0.0305 0.0722  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.3039 0.3271 0.2835 -0.0219 -0.0190 0.0469  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.3180 0.3412 0.2856 -0.0283 -0.0170 0.0397  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.2801 0.3113 0.2490 -0.0314 -0.0194 0.0433  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.2505 0.2833 0.2677 -0.0089 -0.0234 0.0668  80  SER   A N   
586  C CA  . SER   A 74  ? 0.2618 0.3017 0.2955 -0.0068 -0.0270 0.0788  80  SER   A CA  
587  C C   . SER   A 74  ? 0.2474 0.2783 0.2932 0.0013  -0.0234 0.0789  80  SER   A C   
588  O O   . SER   A 74  ? 0.2211 0.2412 0.2620 0.0052  -0.0182 0.0691  80  SER   A O   
589  C CB  . SER   A 74  ? 0.3314 0.3794 0.3759 -0.0049 -0.0276 0.0826  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.4658 0.5212 0.4988 -0.0126 -0.0303 0.0814  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.2688 0.3046 0.3317 0.0036  -0.0263 0.0903  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.2730 0.3003 0.3507 0.0113  -0.0222 0.0912  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.2755 0.3027 0.3690 0.0186  -0.0171 0.0894  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2931 0.3308 0.4001 0.0190  -0.0201 0.0983  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.2809 0.3139 0.3706 0.0095  -0.0280 0.1056  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.3175 0.3412 0.4219 0.0158  -0.0245 0.1079  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.3307 0.3421 0.4209 0.0152  -0.0207 0.0976  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.3293 0.3607 0.4469 0.0133  -0.0316 0.1249  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.2618 0.2780 0.3527 0.0234  -0.0096 0.0777  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.2730 0.2881 0.3749 0.0290  -0.0033 0.0734  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2835 0.2875 0.3973 0.0353  0.0044  0.0688  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2800 0.2740 0.3848 0.0349  0.0065  0.0628  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2953 0.3080 0.3794 0.0268  -0.0008 0.0622  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.3270 0.3495 0.3995 0.0201  -0.0071 0.0651  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.3030 0.3131 0.3946 0.0314  0.0067  0.0557  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.3583 0.3941 0.4450 0.0195  -0.0107 0.0754  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2842 0.2897 0.4188 0.0408  0.0093  0.0713  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.3003 0.2944 0.4469 0.0462  0.0184  0.0654  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.3163 0.3024 0.4488 0.0457  0.0258  0.0504  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.3233 0.3143 0.4494 0.0444  0.0266  0.0467  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.3014 0.3002 0.4773 0.0522  0.0222  0.0728  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.3440 0.3302 0.5350 0.0573  0.0315  0.0682  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.3685 0.3488 0.5666 0.0582  0.0295  0.0743  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3717 0.3517 0.5691 0.0605  0.0428  0.0574  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.4058 0.3733 0.6182 0.0625  0.0388  0.0695  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3798 0.3473 0.5911 0.0644  0.0526  0.0519  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.4032 0.3642 0.6222 0.0655  0.0506  0.0580  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.3141 0.2880 0.4388 0.0454  0.0301  0.0423  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.3204 0.2869 0.4305 0.0436  0.0362  0.0288  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.3352 0.2912 0.4577 0.0468  0.0468  0.0221  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.3370 0.2862 0.4674 0.0482  0.0477  0.0244  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.3160 0.2785 0.4037 0.0388  0.0316  0.0244  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.3144 0.2701 0.3877 0.0363  0.0371  0.0120  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.3015 0.2736 0.3785 0.0354  0.0226  0.0303  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.3579 0.3121 0.4810 0.0470  0.0552  0.0133  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.3921 0.3362 0.5267 0.0490  0.0670  0.0051  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.4120 0.3444 0.5324 0.0451  0.0694  -0.0036 85  GLU   A C   
628  O O   . GLU   A 79  ? 0.4132 0.3461 0.5130 0.0406  0.0628  -0.0051 85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.4529 0.3986 0.5874 0.0482  0.0757  -0.0036 85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.5497 0.5064 0.7029 0.0524  0.0760  0.0038  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.6733 0.6306 0.8569 0.0592  0.0782  0.0128  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.6902 0.6366 0.8863 0.0615  0.0876  0.0076  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.7131 0.6818 0.9083 0.0617  0.0703  0.0257  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.4241 0.3457 0.5568 0.0466  0.0796  -0.0097 86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.4304 0.3403 0.5509 0.0421  0.0832  -0.0189 86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.4265 0.3362 0.5230 0.0351  0.0846  -0.0298 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.4389 0.3521 0.5345 0.0342  0.0898  -0.0346 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.4347 0.3331 0.5741 0.0444  0.0958  -0.0250 86  ALA   A CB  
639  N N   . SER   A 81  ? 0.4058 0.3127 0.4832 0.0299  0.0794  -0.0326 87  SER   A N   
640  C CA  . SER   A 81  ? 0.4035 0.3105 0.4581 0.0225  0.0793  -0.0414 87  SER   A CA  
641  C C   . SER   A 81  ? 0.4044 0.3013 0.4506 0.0172  0.0824  -0.0491 87  SER   A C   
642  O O   . SER   A 81  ? 0.4167 0.3064 0.4754 0.0198  0.0849  -0.0475 87  SER   A O   
643  C CB  . SER   A 81  ? 0.4138 0.3299 0.4539 0.0212  0.0674  -0.0351 87  SER   A CB  
644  O OG  . SER   A 81  ? 0.4145 0.3294 0.4520 0.0213  0.0603  -0.0300 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.4095 0.3066 0.4347 0.0093  0.0814  -0.0563 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.4170 0.3064 0.4328 0.0031  0.0830  -0.0630 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.3859 0.2768 0.4000 0.0046  0.0730  -0.0552 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.3731 0.2575 0.3836 0.0006  0.0741  -0.0590 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.4812 0.3719 0.4753 -0.0069 0.0840  -0.0718 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.5932 0.4937 0.5722 -0.0092 0.0723  -0.0661 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.7430 0.6454 0.7014 -0.0197 0.0713  -0.0725 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.7947 0.6957 0.7447 -0.0248 0.0673  -0.0737 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.7742 0.6803 0.7247 -0.0235 0.0739  -0.0756 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3672 0.2664 0.3844 0.0097  0.0640  -0.0446 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.3505 0.2517 0.3656 0.0103  0.0554  -0.0379 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.3396 0.2395 0.3713 0.0163  0.0541  -0.0292 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.3397 0.2379 0.3706 0.0154  0.0500  -0.0260 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.3408 0.2521 0.3451 0.0098  0.0463  -0.0331 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3575 0.2706 0.3452 0.0032  0.0454  -0.0393 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3779 0.2895 0.3559 -0.0023 0.0427  -0.0424 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.4058 0.3229 0.3879 0.0019  0.0469  -0.0415 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.4124 0.3272 0.3758 -0.0089 0.0405  -0.0463 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.4292 0.3488 0.3960 -0.0050 0.0453  -0.0458 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.4426 0.3613 0.4003 -0.0104 0.0418  -0.0478 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4933 0.4159 0.4366 -0.0177 0.0389  -0.0502 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.3352 0.2370 0.3822 0.0219  0.0569  -0.0246 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.3292 0.2313 0.3937 0.0272  0.0549  -0.0145 90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.3564 0.2550 0.4418 0.0323  0.0635  -0.0141 90  TYR   A C   
669  O O   . TYR   A 84  ? 0.3693 0.2710 0.4555 0.0330  0.0678  -0.0181 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.3063 0.2201 0.3694 0.0292  0.0454  -0.0041 90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2790 0.1973 0.3253 0.0253  0.0373  -0.0032 90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2856 0.2026 0.3315 0.0240  0.0331  0.0014  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2679 0.1925 0.3010 0.0232  0.0340  -0.0057 90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2716 0.1931 0.3040 0.0205  0.0269  0.0017  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2679 0.1964 0.2888 0.0202  0.0276  -0.0048 90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.2672 0.1944 0.2882 0.0190  0.0243  -0.0013 90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.2477 0.1790 0.2583 0.0161  0.0190  -0.0011 90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.3812 0.2755 0.4851 0.0363  0.0647  -0.0073 91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.3977 0.2908 0.5262 0.0423  0.0716  -0.0040 91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.4164 0.3232 0.5518 0.0461  0.0647  0.0070  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.4084 0.3239 0.5302 0.0438  0.0547  0.0125  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3998 0.2846 0.5452 0.0449  0.0728  0.0023  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.4011 0.2890 0.5325 0.0414  0.0627  0.0081  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.3731 0.2642 0.4782 0.0355  0.0596  -0.0008 91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.4270 0.3365 0.5837 0.0514  0.0701  0.0101  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.4277 0.3514 0.5914 0.0541  0.0632  0.0209  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.4096 0.3389 0.5779 0.0546  0.0524  0.0357  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.4338 0.3564 0.6151 0.0564  0.0534  0.0407  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.4367 0.3622 0.6264 0.0600  0.0713  0.0225  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.3666 0.3064 0.5196 0.0512  0.0424  0.0409  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.3320 0.2775 0.4844 0.0493  0.0324  0.0532  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.3237 0.2834 0.4662 0.0465  0.0241  0.0587  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.3441 0.3075 0.4806 0.0464  0.0263  0.0527  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.3197 0.2576 0.4534 0.0445  0.0304  0.0479  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.3285 0.2700 0.4359 0.0394  0.0266  0.0404  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.3344 0.2667 0.4265 0.0361  0.0294  0.0297  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.3233 0.2605 0.3951 0.0313  0.0233  0.0275  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.3398 0.2816 0.3999 0.0299  0.0225  0.0224  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.3480 0.2906 0.4123 0.0321  0.0271  0.0187  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2863 0.2315 0.3310 0.0260  0.0175  0.0209  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.3188 0.2859 0.4587 0.0433  0.0150  0.0697  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.3092 0.2883 0.4366 0.0386  0.0072  0.0739  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2839 0.2595 0.3864 0.0331  0.0049  0.0661  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2863 0.2568 0.3842 0.0309  0.0035  0.0669  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.3143 0.3038 0.4521 0.0366  -0.0012 0.0901  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.3247 0.3220 0.4872 0.0414  -0.0009 0.0995  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.3298 0.3392 0.4918 0.0400  -0.0040 0.1020  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.3468 0.3388 0.5345 0.0477  0.0036  0.1049  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.3479 0.3657 0.5343 0.0445  -0.0034 0.1106  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.3550 0.3546 0.5686 0.0527  0.0046  0.1136  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.3644 0.3773 0.5772 0.0512  0.0011  0.1162  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.3947 0.4166 0.6340 0.0561  0.0021  0.1247  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.2597 0.2388 0.3474 0.0307  0.0045  0.0593  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.2452 0.2224 0.3119 0.0258  0.0023  0.0525  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.2403 0.2284 0.2995 0.0204  -0.0048 0.0591  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.2258 0.2224 0.2893 0.0202  -0.0067 0.0632  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.2588 0.2317 0.3151 0.0265  0.0069  0.0408  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.2539 0.2253 0.2919 0.0222  0.0048  0.0348  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.2571 0.2227 0.2865 0.0228  0.0090  0.0244  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2821 0.2411 0.3155 0.0250  0.0141  0.0197  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.2592 0.2271 0.2762 0.0199  0.0067  0.0210  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.2363 0.2245 0.2838 0.0152  -0.0081 0.0594  96  SER   A N   
723  C CA  . SER   A 90  ? 0.2286 0.2265 0.2674 0.0085  -0.0139 0.0644  96  SER   A CA  
724  C C   . SER   A 90  ? 0.2450 0.2422 0.2674 0.0052  -0.0127 0.0548  96  SER   A C   
725  O O   . SER   A 90  ? 0.2610 0.2505 0.2784 0.0078  -0.0087 0.0457  96  SER   A O   
726  C CB  . SER   A 90  ? 0.2507 0.2499 0.2875 0.0037  -0.0176 0.0711  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.3069 0.2977 0.3343 0.0031  -0.0147 0.0630  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.2411 0.2470 0.2560 -0.0010 -0.0165 0.0575  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.2355 0.2413 0.2366 -0.0050 -0.0153 0.0496  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.2325 0.2339 0.2342 0.0000  -0.0116 0.0425  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.2348 0.2315 0.2279 -0.0004 -0.0092 0.0345  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.2564 0.2569 0.2477 -0.0080 -0.0138 0.0440  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.2893 0.2948 0.2777 -0.0146 -0.0172 0.0506  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.3322 0.3439 0.3094 -0.0235 -0.0188 0.0504  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.3081 0.3128 0.3029 -0.0140 -0.0190 0.0575  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.3251 0.3406 0.3013 -0.0286 -0.0218 0.0574  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.3201 0.3313 0.3070 -0.0230 -0.0223 0.0622  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.2071 0.2107 0.2196 0.0044  -0.0110 0.0458  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.2193 0.2193 0.2324 0.0085  -0.0071 0.0396  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.2215 0.2292 0.2335 0.0058  -0.0087 0.0413  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.2318 0.2485 0.2500 0.0035  -0.0122 0.0492  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.2303 0.2271 0.2574 0.0149  -0.0036 0.0409  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.2629 0.2552 0.2897 0.0184  0.0016  0.0336  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.2629 0.2473 0.2782 0.0179  0.0035  0.0253  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2830 0.2727 0.3248 0.0237  0.0063  0.0344  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.2181 0.2227 0.2223 0.0055  -0.0064 0.0344  99  MET   A N   
747  C CA  . MET   A 93  ? 0.2202 0.2306 0.2222 0.0026  -0.0073 0.0349  99  MET   A CA  
748  C C   . MET   A 93  ? 0.2308 0.2387 0.2367 0.0070  -0.0035 0.0315  99  MET   A C   
749  O O   . MET   A 93  ? 0.2463 0.2464 0.2487 0.0097  -0.0004 0.0257  99  MET   A O   
750  C CB  . MET   A 93  ? 0.2431 0.2508 0.2322 -0.0023 -0.0074 0.0294  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.2549 0.2647 0.2386 -0.0077 -0.0098 0.0311  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.2817 0.2872 0.2525 -0.0136 -0.0079 0.0233  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2546 0.2500 0.2257 -0.0074 -0.0046 0.0172  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.2154 0.2306 0.2288 0.0071  -0.0037 0.0353  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.2296 0.2430 0.2467 0.0106  0.0008  0.0318  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.2237 0.2392 0.2337 0.0071  0.0007  0.0295  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.2329 0.2548 0.2403 0.0022  -0.0027 0.0327  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.2424 0.2622 0.2764 0.0143  0.0024  0.0373  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2845 0.3014 0.3295 0.0186  0.0037  0.0399  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.3153 0.3381 0.3803 0.0229  0.0065  0.0450  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2977 0.3030 0.3367 0.0211  0.0082  0.0319  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.2074 0.2179 0.2141 0.0088  0.0047  0.0242  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.2202 0.2320 0.2209 0.0056  0.0050  0.0225  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.2135 0.2248 0.2176 0.0079  0.0099  0.0199  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.2275 0.2348 0.2348 0.0113  0.0134  0.0174  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.2385 0.2425 0.2266 0.0032  0.0041  0.0180  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.2193 0.2342 0.2215 0.0051  0.0105  0.0199  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.2273 0.2415 0.2298 0.0057  0.0154  0.0169  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.2543 0.2597 0.2432 0.0038  0.0154  0.0125  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.2752 0.2784 0.2568 0.0007  0.0124  0.0129  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.2295 0.2522 0.2366 0.0031  0.0159  0.0195  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.2384 0.2599 0.2433 0.0025  0.0214  0.0157  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.2187 0.2517 0.2418 0.0051  0.0153  0.0253  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.2626 0.2632 0.2492 0.0053  0.0188  0.0087  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.2792 0.2730 0.2539 0.0030  0.0181  0.0059  103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.2695 0.2595 0.2419 0.0036  0.0221  0.0016  103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2801 0.2705 0.2604 0.0066  0.0254  0.0002  103 GLY   A O   
778  N N   . HIS   A 98  ? 0.2615 0.2476 0.2232 0.0002  0.0219  -0.0003 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2778 0.2607 0.2348 -0.0012 0.0254  -0.0048 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.2815 0.2598 0.2377 0.0006  0.0230  -0.0057 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.2810 0.2573 0.2347 0.0009  0.0175  -0.0030 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2831 0.2646 0.2274 -0.0071 0.0247  -0.0052 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2969 0.2763 0.2346 -0.0106 0.0290  -0.0105 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.3147 0.2957 0.2563 -0.0111 0.0373  -0.0157 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2962 0.2722 0.2249 -0.0138 0.0265  -0.0116 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.3160 0.2936 0.2497 -0.0150 0.0401  -0.0208 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.3153 0.2904 0.2405 -0.0171 0.0333  -0.0181 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2962 0.2725 0.2551 0.0014  0.0276  -0.0100 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2919 0.2635 0.2488 0.0019  0.0262  -0.0118 105 SER   A CA  
790  C C   . SER   A 99  ? 0.3049 0.2735 0.2599 -0.0004 0.0329  -0.0184 105 SER   A C   
791  O O   . SER   A 99  ? 0.3329 0.3029 0.2931 -0.0003 0.0399  -0.0216 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2954 0.2668 0.2615 0.0068  0.0234  -0.0088 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.2964 0.2698 0.2747 0.0103  0.0279  -0.0088 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2951 0.2597 0.2424 -0.0032 0.0311  -0.0207 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.3138 0.2742 0.2573 -0.0067 0.0365  -0.0275 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.3283 0.2849 0.2746 -0.0045 0.0335  -0.0273 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.3090 0.2668 0.2571 -0.0018 0.0268  -0.0220 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.3466 0.3077 0.2743 -0.0152 0.0357  -0.0298 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.3482 0.3132 0.2723 -0.0181 0.0386  -0.0297 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3923 0.3592 0.3004 -0.0274 0.0379  -0.0307 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.4164 0.3814 0.3146 -0.0337 0.0382  -0.0344 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3912 0.3617 0.2961 -0.0293 0.0372  -0.0276 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.3530 0.3047 0.3012 -0.0055 0.0392  -0.0332 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.3607 0.3086 0.3125 -0.0034 0.0365  -0.0326 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.3484 0.2979 0.2921 -0.0057 0.0280  -0.0289 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.3355 0.2851 0.2847 -0.0019 0.0235  -0.0249 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.3832 0.3250 0.3344 -0.0068 0.0447  -0.0409 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.3924 0.3346 0.3474 -0.0070 0.0530  -0.0450 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.3611 0.3099 0.3092 -0.0087 0.0492  -0.0411 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.3140 0.2654 0.2455 -0.0122 0.0258  -0.0298 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.3018 0.2560 0.2276 -0.0147 0.0176  -0.0255 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.2830 0.2407 0.2133 -0.0104 0.0115  -0.0182 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.2950 0.2546 0.2244 -0.0112 0.0054  -0.0143 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.2632 0.2218 0.1992 -0.0063 0.0135  -0.0166 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.2625 0.2235 0.2030 -0.0027 0.0089  -0.0109 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.2630 0.2231 0.2116 0.0018  0.0072  -0.0094 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.2460 0.2075 0.1974 0.0036  0.0036  -0.0058 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.2565 0.2197 0.1996 -0.0012 0.0114  -0.0098 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.2537 0.2186 0.1880 -0.0062 0.0116  -0.0096 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.2550 0.2206 0.1832 -0.0097 0.0069  -0.0070 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.2768 0.2430 0.2111 -0.0069 0.0164  -0.0117 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.2594 0.2167 0.2115 0.0029  0.0101  -0.0123 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.2556 0.2123 0.2142 0.0062  0.0084  -0.0104 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.2586 0.2165 0.2158 0.0052  0.0033  -0.0084 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.2511 0.2093 0.2033 0.0019  0.0012  -0.0090 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.2710 0.2238 0.2330 0.0066  0.0120  -0.0135 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.2702 0.2219 0.2413 0.0100  0.0180  -0.0140 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.2489 0.2082 0.2108 0.0076  0.0015  -0.0058 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.2479 0.2083 0.2111 0.0072  -0.0020 -0.0043 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.2341 0.1961 0.1983 0.0075  -0.0037 -0.0017 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.2331 0.1956 0.2014 0.0081  -0.0053 -0.0006 111 GLY   A O   
832  N N   . GLY   A 106 ? 0.2338 0.1962 0.1948 0.0070  -0.0029 -0.0010 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.2234 0.1864 0.1856 0.0070  -0.0043 0.0015  112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.2135 0.1765 0.1800 0.0084  -0.0031 0.0013  112 GLY   A C   
835  O O   . GLY   A 106 ? 0.2225 0.1866 0.1894 0.0089  -0.0012 0.0005  112 GLY   A O   
836  N N   . ILE   A 107 ? 0.2077 0.1699 0.1780 0.0084  -0.0038 0.0022  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1997 0.1617 0.1725 0.0081  -0.0017 0.0008  113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1985 0.1613 0.1689 0.0067  -0.0005 0.0012  113 ILE   A C   
839  O O   . ILE   A 107 ? 0.2117 0.1736 0.1811 0.0062  -0.0010 0.0027  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.2136 0.1737 0.1929 0.0084  -0.0015 0.0004  113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.2416 0.2026 0.2242 0.0092  -0.0019 -0.0007 113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.2184 0.1773 0.1996 0.0067  0.0018  -0.0021 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.2908 0.2510 0.2825 0.0101  -0.0018 -0.0005 113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1950 0.1601 0.1647 0.0053  0.0009  0.0003  114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1918 0.1587 0.1598 0.0027  0.0019  0.0005  114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.2077 0.1727 0.1769 0.0000  0.0041  -0.0025 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.2124 0.1778 0.1823 -0.0007 0.0049  -0.0041 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.2080 0.1801 0.1750 0.0019  0.0016  0.0022  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.2157 0.1916 0.1809 -0.0022 0.0019  0.0030  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.2321 0.2083 0.1968 -0.0024 0.0021  0.0040  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.2223 0.2048 0.1888 -0.0032 0.0004  0.0065  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.2156 0.1780 0.1852 -0.0020 0.0056  -0.0035 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.2161 0.1754 0.1876 -0.0051 0.0092  -0.0076 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.2361 0.1958 0.2040 -0.0101 0.0111  -0.0090 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.2296 0.1905 0.1956 -0.0102 0.0095  -0.0064 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.2252 0.1790 0.2047 -0.0021 0.0103  -0.0081 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.2541 0.2048 0.2355 -0.0009 0.0090  -0.0051 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.2649 0.2108 0.2564 0.0020  0.0093  -0.0040 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.2950 0.2434 0.2885 0.0055  0.0054  -0.0006 115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.2951 0.2433 0.2963 0.0075  0.0057  -0.0011 115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.2987 0.2446 0.3063 0.0066  0.0107  -0.0057 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.2772 0.2284 0.2794 0.0096  0.0016  0.0023  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.2430 0.2016 0.2096 -0.0151 0.0150  -0.0138 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2762 0.2344 0.2387 -0.0215 0.0176  -0.0166 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.3094 0.2596 0.2771 -0.0234 0.0238  -0.0228 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.3099 0.2560 0.2858 -0.0187 0.0251  -0.0234 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.2873 0.2531 0.2418 -0.0280 0.0167  -0.0166 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.2801 0.2462 0.2326 -0.0323 0.0205  -0.0218 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.3472 0.2953 0.3112 -0.0306 0.0280  -0.0274 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.3791 0.3186 0.3493 -0.0327 0.0355  -0.0344 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3872 0.3263 0.3600 -0.0336 0.0400  -0.0397 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.4198 0.3517 0.4030 -0.0319 0.0459  -0.0441 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.4321 0.3693 0.3962 -0.0418 0.0400  -0.0397 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.5240 0.4690 0.4755 -0.0515 0.0404  -0.0428 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.6448 0.5886 0.5889 -0.0620 0.0444  -0.0480 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.6784 0.6280 0.6164 -0.0651 0.0398  -0.0438 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.6593 0.5959 0.6042 -0.0681 0.0534  -0.0577 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.3388 0.2857 0.3038 -0.0357 0.0370  -0.0382 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.3228 0.2706 0.2885 -0.0378 0.0412  -0.0430 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.3218 0.2698 0.2962 -0.0294 0.0386  -0.0396 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.3498 0.2977 0.3274 -0.0303 0.0427  -0.0436 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2936 0.2501 0.2456 -0.0462 0.0392  -0.0426 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.3151 0.2729 0.2577 -0.0559 0.0410  -0.0457 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.3506 0.3158 0.2860 -0.0583 0.0345  -0.0394 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3569 0.3103 0.2964 -0.0646 0.0492  -0.0548 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.4011 0.3666 0.3290 -0.0683 0.0380  -0.0441 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3885 0.3464 0.3177 -0.0728 0.0471  -0.0540 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2930 0.2422 0.2701 -0.0223 0.0319  -0.0322 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2656 0.2155 0.2497 -0.0156 0.0291  -0.0289 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.2468 0.2018 0.2257 -0.0123 0.0218  -0.0222 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.2539 0.2109 0.2274 -0.0131 0.0188  -0.0191 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.2346 0.1917 0.2161 -0.0087 0.0196  -0.0202 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.2291 0.1898 0.2070 -0.0056 0.0139  -0.0148 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.2197 0.1856 0.1894 -0.0096 0.0125  -0.0134 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.2288 0.1968 0.1957 -0.0137 0.0145  -0.0156 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.2390 0.1997 0.2224 -0.0013 0.0122  -0.0136 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.2479 0.2112 0.2273 0.0010  0.0077  -0.0095 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.2502 0.2074 0.2428 0.0025  0.0119  -0.0127 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.2075 0.1760 0.1742 -0.0085 0.0091  -0.0092 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.2152 0.1897 0.1770 -0.0117 0.0069  -0.0059 121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.2233 0.1992 0.1872 -0.0077 0.0040  -0.0020 121 VAL   A C   
902  O O   . VAL   A 115 ? 0.2343 0.2139 0.1967 -0.0099 0.0028  0.0006  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.2449 0.2220 0.2048 -0.0129 0.0054  -0.0034 121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.2481 0.2328 0.2063 -0.0152 0.0023  0.0019  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.2603 0.2354 0.2176 -0.0179 0.0086  -0.0075 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.2223 0.1951 0.1896 -0.0024 0.0031  -0.0015 122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.2267 0.1997 0.1960 0.0009  0.0014  0.0010  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.2160 0.1856 0.1868 0.0048  0.0010  0.0005  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.2249 0.1924 0.1960 0.0052  0.0012  -0.0009 122 GLY   A O   
910  N N   . ILE   A 117 ? 0.2111 0.1803 0.1833 0.0071  0.0005  0.0017  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.2064 0.1728 0.1780 0.0092  0.0004  0.0006  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.2093 0.1765 0.1819 0.0105  0.0015  0.0017  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.2041 0.1731 0.1802 0.0111  0.0020  0.0038  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.2279 0.1920 0.2001 0.0096  -0.0001 -0.0011 123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.2284 0.1924 0.2026 0.0096  0.0005  -0.0004 123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.2480 0.2118 0.2217 0.0089  -0.0009 -0.0021 123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.2459 0.2073 0.2203 0.0096  0.0003  -0.0024 123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.2088 0.1748 0.1790 0.0108  0.0022  0.0005  124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.2015 0.1678 0.1733 0.0119  0.0048  0.0003  124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.2158 0.1795 0.1909 0.0131  0.0066  -0.0009 124 VAL   A C   
921  O O   . VAL   A 118 ? 0.2214 0.1822 0.1940 0.0122  0.0059  -0.0030 124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.2082 0.1733 0.1747 0.0105  0.0056  -0.0017 124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.2261 0.1911 0.1943 0.0109  0.0100  -0.0037 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.2208 0.1879 0.1852 0.0093  0.0041  0.0001  124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.2165 0.1813 0.1987 0.0150  0.0089  0.0009  125 SER   A N   
926  C CA  . SER   A 119 ? 0.2304 0.1918 0.2179 0.0164  0.0112  0.0003  125 SER   A CA  
927  C C   . SER   A 119 ? 0.2448 0.2052 0.2391 0.0183  0.0163  -0.0010 125 SER   A C   
928  O O   . SER   A 119 ? 0.2579 0.2132 0.2552 0.0188  0.0198  -0.0038 125 SER   A O   
929  C CB  . SER   A 119 ? 0.2476 0.2112 0.2400 0.0169  0.0086  0.0052  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.2551 0.2150 0.2542 0.0183  0.0106  0.0059  125 SER   A OG  
931  N N   . THR   A 120 ? 0.2322 0.1972 0.2303 0.0192  0.0173  0.0010  126 THR   A N   
932  C CA  . THR   A 120 ? 0.2569 0.2217 0.2647 0.0215  0.0233  -0.0001 126 THR   A CA  
933  C C   . THR   A 120 ? 0.2760 0.2445 0.2803 0.0202  0.0250  -0.0018 126 THR   A C   
934  O O   . THR   A 120 ? 0.2574 0.2288 0.2536 0.0180  0.0209  -0.0005 126 THR   A O   
935  C CB  . THR   A 120 ? 0.2570 0.2262 0.2800 0.0249  0.0227  0.0070  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.2574 0.2348 0.2817 0.0244  0.0189  0.0124  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.2660 0.2328 0.2926 0.0256  0.0199  0.0107  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2916 0.2602 0.3033 0.0214  0.0315  -0.0044 127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.3003 0.2735 0.3098 0.0200  0.0333  -0.0052 127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.3232 0.2959 0.3421 0.0211  0.0421  -0.0093 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.3365 0.3045 0.3642 0.0233  0.0472  -0.0119 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.3450 0.3217 0.3609 0.0190  0.0445  -0.0109 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.3735 0.3501 0.3963 0.0189  0.0541  -0.0163 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.3997 0.3849 0.4291 0.0193  0.0548  -0.0130 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.4127 0.4043 0.4495 0.0218  0.0491  -0.0053 128 GLY   A O   
946  N N   . ASN   A 123 ? 0.3895 0.3756 0.4171 0.0165  0.0624  -0.0188 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.3744 0.3689 0.4097 0.0165  0.0650  -0.0168 129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.3348 0.3360 0.3653 0.0154  0.0562  -0.0095 129 ASN   A C   
949  O O   . ASN   A 123 ? 0.3097 0.3194 0.3529 0.0175  0.0556  -0.0043 129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.4056 0.4039 0.4656 0.0224  0.0708  -0.0147 129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.4737 0.4653 0.5407 0.0230  0.0823  -0.0235 129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.4997 0.4904 0.5612 0.0187  0.0908  -0.0315 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.4799 0.4665 0.5593 0.0277  0.0834  -0.0223 129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.3074 0.3050 0.3198 0.0114  0.0503  -0.0097 130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.3047 0.3068 0.3120 0.0096  0.0432  -0.0041 130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.2720 0.2757 0.2843 0.0125  0.0360  0.0021  130 GLY   A C   
957  O O   . GLY   A 124 ? 0.2798 0.2875 0.2892 0.0107  0.0308  0.0063  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.2493 0.2490 0.2661 0.0157  0.0355  0.0022  131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.2558 0.2563 0.2739 0.0170  0.0285  0.0076  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.2692 0.2614 0.2757 0.0160  0.0259  0.0047  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2935 0.2797 0.2951 0.0155  0.0296  -0.0008 131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.2621 0.2658 0.2976 0.0214  0.0296  0.0119  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.2832 0.2969 0.3340 0.0229  0.0310  0.0169  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.3027 0.3183 0.3733 0.0280  0.0334  0.0209  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.2951 0.3169 0.3430 0.0196  0.0236  0.0233  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.2203 0.2127 0.2227 0.0152  0.0197  0.0081  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.2256 0.2114 0.2202 0.0148  0.0172  0.0060  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.2199 0.2080 0.2193 0.0157  0.0131  0.0107  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.2266 0.2208 0.2281 0.0142  0.0102  0.0150  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.2418 0.2247 0.2238 0.0115  0.0146  0.0042  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.2480 0.2353 0.2289 0.0093  0.0115  0.0075  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.2510 0.2285 0.2273 0.0112  0.0119  0.0027  132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.2142 0.1980 0.2148 0.0172  0.0130  0.0102  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.2132 0.1991 0.2169 0.0171  0.0091  0.0147  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.2217 0.2030 0.2161 0.0152  0.0067  0.0122  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.2346 0.2102 0.2241 0.0155  0.0082  0.0077  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.2118 0.1961 0.2039 0.0126  0.0032  0.0150  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.2043 0.1848 0.1892 0.0108  0.0018  0.0122  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.2148 0.1964 0.2017 0.0097  0.0000  0.0153  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.2277 0.2151 0.2178 0.0078  -0.0020 0.0204  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.2188 0.2011 0.1977 0.0073  0.0004  0.0114  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.2281 0.2099 0.2050 0.0074  0.0016  0.0098  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.2131 0.1900 0.1862 0.0083  0.0024  0.0065  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.2465 0.2337 0.2258 0.0063  0.0015  0.0124  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.2204 0.1971 0.1910 0.0076  0.0031  0.0059  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.2369 0.2239 0.2140 0.0059  0.0027  0.0111  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.2258 0.2071 0.1982 0.0065  0.0036  0.0079  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.2149 0.1917 0.1994 0.0099  0.0004  0.0126  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.2170 0.1946 0.2020 0.0080  -0.0011 0.0150  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.2124 0.1923 0.1908 0.0035  -0.0022 0.0136  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.2221 0.1988 0.1969 0.0033  -0.0010 0.0089  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.2277 0.1994 0.2130 0.0097  0.0002  0.0120  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.2139 0.1998 0.1913 -0.0009 -0.0042 0.0179  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.2262 0.2142 0.1965 -0.0066 -0.0039 0.0155  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.2320 0.2170 0.1997 -0.0083 -0.0026 0.0124  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.2555 0.2400 0.2260 -0.0074 -0.0035 0.0153  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.2386 0.2348 0.2074 -0.0125 -0.0068 0.0215  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.3535 0.3526 0.3135 -0.0204 -0.0059 0.0184  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2939 0.2895 0.2510 -0.0206 -0.0031 0.0124  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.4518 0.4563 0.4077 -0.0270 -0.0078 0.0219  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.2166 0.2000 0.1802 -0.0111 0.0000  0.0068  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.2097 0.1916 0.1716 -0.0136 0.0021  0.0035  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.2365 0.2215 0.1920 -0.0215 0.0046  0.0004  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.2302 0.2144 0.1845 -0.0243 0.0075  -0.0032 137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.2211 0.1976 0.1870 -0.0091 0.0042  -0.0014 137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.2315 0.2050 0.2016 -0.0034 0.0022  0.0007  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.2223 0.1964 0.1892 -0.0084 0.0064  -0.0055 137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.2376 0.2262 0.1889 -0.0257 0.0040  0.0014  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.2432 0.2340 0.1872 -0.0344 0.0073  -0.0031 138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.2619 0.2580 0.1993 -0.0424 0.0069  -0.0010 138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.2701 0.2671 0.2009 -0.0503 0.0113  -0.0067 138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.2564 0.2502 0.1970 -0.0379 0.0063  -0.0022 138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.2497 0.2376 0.1955 -0.0317 0.0080  -0.0056 138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.2677 0.2592 0.2098 -0.0360 0.0068  -0.0043 138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.2721 0.2699 0.2166 -0.0340 0.0012  0.0041  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.2721 0.2748 0.2162 -0.0360 -0.0010 0.0072  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.3011 0.3028 0.2403 -0.0414 0.0016  0.0025  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.2697 0.2781 0.2192 -0.0330 -0.0055 0.0151  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.2620 0.2618 0.2012 -0.0412 0.0020  0.0071  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.2808 0.2859 0.2139 -0.0491 0.0008  0.0108  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.2666 0.2677 0.2008 -0.0482 0.0041  0.0070  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.2797 0.2849 0.2079 -0.0557 0.0041  0.0090  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.2863 0.2971 0.2228 -0.0485 -0.0062 0.0226  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.3454 0.3507 0.2928 -0.0381 -0.0076 0.0256  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.3420 0.3413 0.2945 -0.0305 -0.0055 0.0208  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.3480 0.3546 0.2984 -0.0382 -0.0104 0.0324  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.2621 0.2563 0.2041 -0.0396 0.0064  0.0025  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.2457 0.2368 0.1908 -0.0381 0.0089  -0.0004 140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.2480 0.2382 0.1909 -0.0425 0.0158  -0.0095 140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.2543 0.2399 0.2041 -0.0373 0.0191  -0.0151 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.2487 0.2341 0.2029 -0.0280 0.0076  -0.0003 140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.2603 0.2456 0.2181 -0.0234 0.0025  0.0073  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.2659 0.2454 0.2306 -0.0153 0.0025  0.0055  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.2847 0.2724 0.2418 -0.0266 0.0000  0.0139  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.2593 0.2542 0.1929 -0.0528 0.0182  -0.0109 141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.2710 0.2649 0.2023 -0.0585 0.0264  -0.0209 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.2827 0.2735 0.2221 -0.0551 0.0311  -0.0261 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.2958 0.2837 0.2406 -0.0548 0.0381  -0.0345 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.2917 0.2920 0.2092 -0.0723 0.0283  -0.0217 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.3208 0.3264 0.2304 -0.0770 0.0222  -0.0147 141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.3527 0.3656 0.2472 -0.0927 0.0244  -0.0163 141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.3415 0.3436 0.2555 -0.0717 0.0222  -0.0171 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.2796 0.2712 0.2212 -0.0526 0.0277  -0.0211 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.2661 0.2561 0.2154 -0.0501 0.0315  -0.0251 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.2837 0.2691 0.2461 -0.0404 0.0323  -0.0281 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.2886 0.2737 0.2595 -0.0387 0.0364  -0.0325 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.2721 0.2637 0.2201 -0.0505 0.0273  -0.0186 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.2726 0.2620 0.2230 -0.0439 0.0197  -0.0104 142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.2873 0.2789 0.2323 -0.0459 0.0144  -0.0024 142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.2662 0.2511 0.2258 -0.0346 0.0173  -0.0097 142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.2928 0.2807 0.2443 -0.0378 0.0098  0.0025  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.2780 0.2616 0.2371 -0.0314 0.0116  -0.0024 142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.2712 0.2537 0.2399 -0.0293 0.0195  -0.0143 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.2884 0.2676 0.2540 -0.0239 0.0090  -0.0010 142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.2942 0.2734 0.2684 -0.0225 0.0156  -0.0118 142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.2850 0.2621 0.2568 -0.0201 0.0109  -0.0059 142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.2593 0.2419 0.2238 -0.0344 0.0282  -0.0253 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.2836 0.2625 0.2597 -0.0263 0.0283  -0.0272 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.3135 0.2912 0.2966 -0.0275 0.0359  -0.0349 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.3116 0.2876 0.3071 -0.0216 0.0368  -0.0361 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.2699 0.2465 0.2452 -0.0214 0.0234  -0.0231 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.2693 0.2458 0.2423 -0.0180 0.0170  -0.0164 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.2893 0.2642 0.2610 -0.0145 0.0136  -0.0134 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.2649 0.2399 0.2454 -0.0130 0.0154  -0.0158 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.3394 0.3180 0.3153 -0.0354 0.0414  -0.0399 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.3854 0.3615 0.3682 -0.0373 0.0503  -0.0485 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.4379 0.4161 0.4265 -0.0409 0.0579  -0.0547 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.4433 0.4192 0.4394 -0.0427 0.0668  -0.0627 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.4080 0.3840 0.3792 -0.0460 0.0540  -0.0526 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.4721 0.4463 0.4386 -0.0439 0.0486  -0.0483 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.4950 0.4669 0.4689 -0.0351 0.0433  -0.0434 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.5311 0.5071 0.4860 -0.0520 0.0495  -0.0496 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.4703 0.4525 0.4556 -0.0426 0.0555  -0.0516 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.5138 0.4989 0.5033 -0.0472 0.0631  -0.0576 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.5466 0.5341 0.5442 -0.0422 0.0592  -0.0533 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.5455 0.5321 0.5437 -0.0360 0.0508  -0.0460 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.5688 0.5576 0.5407 -0.0596 0.0658  -0.0593 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.6444 0.6362 0.6054 -0.0608 0.0564  -0.0495 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.7373 0.7336 0.6804 -0.0728 0.0559  -0.0476 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.7436 0.7428 0.6805 -0.0745 0.0495  -0.0395 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.7751 0.7721 0.7106 -0.0810 0.0617  -0.0539 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.5787 0.5697 0.5815 -0.0462 0.0660  -0.0582 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.6115 0.6058 0.6211 -0.0438 0.0637  -0.0553 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.6351 0.6284 0.6600 -0.0334 0.0584  -0.0513 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.6458 0.6425 0.6849 -0.0310 0.0609  -0.0528 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.6516 0.6477 0.6461 -0.0486 0.0575  -0.0488 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.7457 0.7430 0.7456 -0.0447 0.0523  -0.0437 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.8445 0.8466 0.8490 -0.0495 0.0578  -0.0471 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.8659 0.8689 0.8706 -0.0489 0.0533  -0.0425 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.8791 0.8837 0.8872 -0.0543 0.0672  -0.0549 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.3321 0.3096 0.3165 -0.0003 -0.0147 0.0413  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.3252 0.3053 0.3204 -0.0009 -0.0156 0.0432  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.3138 0.2927 0.3089 -0.0012 -0.0156 0.0391  7   SER   C C   
1094 O O   . SER   B 1   ? 0.3279 0.3038 0.3142 -0.0012 -0.0166 0.0354  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.3759 0.3573 0.3731 -0.0024 -0.0213 0.0482  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.4308 0.4095 0.4192 -0.0041 -0.0267 0.0464  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.2946 0.2755 0.2994 -0.0012 -0.0141 0.0400  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.2849 0.2643 0.2894 -0.0014 -0.0137 0.0370  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.2662 0.2469 0.2792 -0.0004 -0.0090 0.0368  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.2614 0.2430 0.2780 0.0007  -0.0052 0.0366  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.2541 0.2340 0.2695 -0.0008 -0.0089 0.0365  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.2513 0.2314 0.2727 0.0004  -0.0039 0.0361  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.2336 0.2108 0.2502 0.0006  -0.0031 0.0333  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.2469 0.2223 0.2585 -0.0004 -0.0067 0.0327  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.2689 0.2518 0.3022 -0.0002 -0.0033 0.0412  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.2241 0.2001 0.2419 0.0020  0.0017  0.0316  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.2193 0.1923 0.2329 0.0026  0.0031  0.0301  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.2256 0.1993 0.2484 0.0023  0.0064  0.0338  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.2264 0.2015 0.2561 0.0031  0.0100  0.0352  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.2270 0.1977 0.2342 0.0044  0.0061  0.0258  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.2439 0.2152 0.2452 0.0048  0.0036  0.0223  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.2518 0.2190 0.2534 0.0052  0.0072  0.0248  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.2608 0.2311 0.2586 0.0062  0.0060  0.0182  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.2261 0.1985 0.2497 0.0014  0.0057  0.0355  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.2326 0.2060 0.2661 0.0012  0.0095  0.0395  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.2426 0.2115 0.2700 0.0025  0.0137  0.0380  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.2760 0.2426 0.2992 0.0016  0.0115  0.0380  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.2425 0.2187 0.2843 -0.0015 0.0048  0.0436  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.2517 0.2322 0.2992 -0.0026 0.0006  0.0458  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.2573 0.2417 0.3168 -0.0020 0.0031  0.0496  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.2626 0.2428 0.3028 -0.0037 -0.0054 0.0441  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.2784 0.2666 0.3427 -0.0026 -0.0009 0.0523  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.2901 0.2736 0.3336 -0.0044 -0.0091 0.0464  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.3019 0.2894 0.3573 -0.0039 -0.0071 0.0507  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.3173 0.3079 0.3757 -0.0043 -0.0108 0.0535  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.2474 0.2143 0.2733 0.0045  0.0198  0.0368  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.2563 0.2182 0.2742 0.0061  0.0241  0.0356  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.2593 0.2207 0.2848 0.0071  0.0317  0.0384  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.2570 0.2196 0.2875 0.0080  0.0348  0.0381  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2832 0.2420 0.2881 0.0078  0.0237  0.0302  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2819 0.2421 0.2891 0.0085  0.0255  0.0278  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.3033 0.2567 0.2987 0.0096  0.0279  0.0292  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2743 0.2338 0.3018 0.0070  0.0353  0.0415  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2761 0.2352 0.3118 0.0082  0.0434  0.0446  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.2669 0.2320 0.3195 0.0073  0.0434  0.0483  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2789 0.2488 0.3395 0.0049  0.0371  0.0508  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.2545 0.2192 0.3115 0.0093  0.0498  0.0482  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.2555 0.2259 0.3286 0.0090  0.0496  0.0518  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.2573 0.2280 0.3271 0.0095  0.0469  0.0485  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.2582 0.2304 0.3374 0.0108  0.0504  0.0500  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2797 0.2500 0.3645 0.0110  0.0593  0.0554  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.3690 0.3415 0.4636 0.0098  0.0612  0.0607  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.4008 0.3801 0.5121 0.0080  0.0580  0.0659  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3865 0.3535 0.4708 0.0104  0.0654  0.0596  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.2390 0.2085 0.2967 0.0086  0.0407  0.0444  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.2373 0.2074 0.2921 0.0088  0.0381  0.0413  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.2269 0.2008 0.2811 0.0066  0.0294  0.0419  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.2295 0.2034 0.2785 0.0052  0.0250  0.0418  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.2597 0.2241 0.2994 0.0100  0.0396  0.0348  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.2893 0.2483 0.3255 0.0121  0.0480  0.0330  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.3143 0.2724 0.3586 0.0135  0.0539  0.0336  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.3216 0.2753 0.3446 0.0130  0.0498  0.0301  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.3357 0.2875 0.3751 0.0156  0.0621  0.0312  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.3473 0.2950 0.3647 0.0151  0.0575  0.0281  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.3766 0.3231 0.4016 0.0163  0.0637  0.0282  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.4326 0.3720 0.4502 0.0185  0.0718  0.0255  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.2096 0.1861 0.2682 0.0065  0.0275  0.0425  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.2188 0.1980 0.2748 0.0049  0.0202  0.0427  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.2152 0.1925 0.2646 0.0057  0.0208  0.0384  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.2210 0.1976 0.2755 0.0069  0.0251  0.0384  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.2258 0.2102 0.2945 0.0040  0.0172  0.0487  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.2567 0.2432 0.3223 0.0029  0.0111  0.0492  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.2551 0.2467 0.3321 0.0020  0.0070  0.0556  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.2779 0.2708 0.3551 0.0024  0.0051  0.0572  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.2943 0.2877 0.3643 0.0010  -0.0011 0.0575  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.2911 0.2837 0.3529 -0.0008 -0.0060 0.0556  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.3001 0.2944 0.3707 0.0017  -0.0018 0.0597  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.2084 0.1845 0.2469 0.0051  0.0170  0.0346  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.2077 0.1826 0.2409 0.0056  0.0174  0.0304  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.2150 0.1927 0.2481 0.0045  0.0127  0.0319  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.2151 0.1934 0.2433 0.0036  0.0082  0.0322  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.2381 0.2100 0.2600 0.0060  0.0168  0.0252  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.2630 0.2342 0.2819 0.0063  0.0173  0.0209  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.2461 0.2147 0.2651 0.0071  0.0206  0.0243  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.2094 0.1881 0.2475 0.0047  0.0142  0.0330  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.2033 0.1840 0.2406 0.0040  0.0107  0.0350  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.2262 0.2070 0.2636 0.0040  0.0106  0.0351  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.2181 0.1980 0.2545 0.0043  0.0130  0.0323  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.2176 0.1953 0.2563 0.0048  0.0172  0.0294  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1971 0.1807 0.2434 0.0038  0.0095  0.0414  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.2654 0.2489 0.3125 0.0038  0.0097  0.0416  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.2157 0.2012 0.2631 0.0027  0.0050  0.0446  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.2738 0.2591 0.3196 0.0032  0.0061  0.0447  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.1702 0.1533 0.2269 0.0051  0.0148  0.0433  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2995 0.2845 0.3494 0.0031  0.0072  0.0442  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.2056 0.1868 0.2390 0.0037  0.0106  0.0332  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.2048 0.1855 0.2399 0.0038  0.0133  0.0317  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.2113 0.1916 0.2566 0.0043  0.0168  0.0355  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.2109 0.1928 0.2605 0.0045  0.0153  0.0410  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.2050 0.1869 0.2357 0.0034  0.0110  0.0335  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.2256 0.2076 0.2470 0.0032  0.0082  0.0300  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.2434 0.2253 0.2594 0.0030  0.0046  0.0311  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.2417 0.2236 0.2616 0.0034  0.0098  0.0256  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.2139 0.1920 0.2633 0.0044  0.0212  0.0327  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1941 0.1707 0.2535 0.0052  0.0252  0.0359  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.2122 0.1907 0.2754 0.0053  0.0241  0.0421  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.2294 0.2085 0.3002 0.0062  0.0248  0.0476  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1917 0.1647 0.2535 0.0048  0.0297  0.0309  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.2158 0.1858 0.2881 0.0058  0.0349  0.0334  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.2471 0.2126 0.3207 0.0050  0.0388  0.0276  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.2400 0.2008 0.3225 0.0060  0.0446  0.0284  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.2424 0.2021 0.3338 0.0064  0.0472  0.0327  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.2782 0.2413 0.3702 0.0059  0.0446  0.0375  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.2399 0.1945 0.3393 0.0074  0.0529  0.0325  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.2150 0.1944 0.2722 0.0044  0.0222  0.0418  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.2102 0.1906 0.2689 0.0047  0.0216  0.0479  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.2269 0.2097 0.2828 0.0050  0.0163  0.0533  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.2457 0.2292 0.3033 0.0055  0.0153  0.0593  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.2216 0.2018 0.2752 0.0039  0.0223  0.0462  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.2280 0.2096 0.2707 0.0035  0.0185  0.0442  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.2540 0.2358 0.2925 0.0030  0.0180  0.0378  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.2433 0.2256 0.2783 0.0036  0.0153  0.0476  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.2629 0.2455 0.2923 0.0031  0.0149  0.0376  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.2563 0.2389 0.2827 0.0033  0.0133  0.0431  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.2326 0.2166 0.2844 0.0046  0.0128  0.0514  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.2428 0.2292 0.2932 0.0043  0.0073  0.0559  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.2475 0.2356 0.3079 0.0049  0.0074  0.0585  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.2676 0.2581 0.3285 0.0042  0.0024  0.0617  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.2500 0.2362 0.2888 0.0032  0.0032  0.0522  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.2694 0.2542 0.2987 0.0030  0.0034  0.0503  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.2842 0.2681 0.3026 0.0023  -0.0001 0.0464  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.2804 0.2654 0.3082 0.0033  0.0020  0.0563  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.2390 0.2255 0.3074 0.0059  0.0132  0.0567  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.2497 0.2375 0.3280 0.0068  0.0146  0.0591  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.2691 0.2601 0.3574 0.0076  0.0124  0.0672  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.2854 0.2761 0.3761 0.0084  0.0130  0.0708  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.2531 0.2373 0.3364 0.0079  0.0219  0.0554  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.2692 0.2636 0.3638 0.0074  0.0097  0.0703  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.2620 0.2608 0.3681 0.0082  0.0065  0.0784  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.2692 0.2680 0.3908 0.0107  0.0132  0.0812  24  THR   C C   
1231 O O   . THR   B 18  ? 0.2803 0.2753 0.4026 0.0116  0.0201  0.0764  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.2755 0.2785 0.3827 0.0064  -0.0001 0.0803  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.2891 0.2920 0.4020 0.0066  0.0040  0.0780  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.2718 0.2738 0.3635 0.0040  -0.0064 0.0770  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.2750 0.2778 0.4092 0.0121  0.0111  0.0892  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.2896 0.2928 0.4404 0.0148  0.0177  0.0925  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.2759 0.2801 0.4317 0.0147  0.0209  0.0900  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.2828 0.2833 0.4439 0.0167  0.0293  0.0875  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.3004 0.3092 0.4649 0.0162  0.0134  0.1022  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.3359 0.3464 0.5197 0.0193  0.0196  0.1063  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.3672 0.3724 0.5567 0.0220  0.0287  0.1052  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.3652 0.3815 0.5632 0.0198  0.0187  0.1106  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.3681 0.3759 0.5750 0.0246  0.0330  0.1095  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.3735 0.3884 0.5867 0.0234  0.0275  0.1130  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.2743 0.2823 0.4273 0.0124  0.0147  0.0901  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.2710 0.2795 0.4287 0.0122  0.0184  0.0882  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.2494 0.2510 0.3951 0.0124  0.0250  0.0797  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.2402 0.2397 0.3905 0.0138  0.0321  0.0781  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.3058 0.3189 0.4624 0.0093  0.0104  0.0896  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.3795 0.3937 0.5439 0.0092  0.0147  0.0892  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.3908 0.4089 0.5725 0.0108  0.0181  0.0943  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.4051 0.4157 0.5573 0.0076  0.0154  0.0833  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.2411 0.2391 0.3710 0.0110  0.0226  0.0745  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.2459 0.2379 0.3646 0.0110  0.0277  0.0667  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.2502 0.2376 0.3744 0.0135  0.0364  0.0651  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.2568 0.2401 0.3788 0.0144  0.0425  0.0609  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.2413 0.2312 0.3451 0.0094  0.0236  0.0621  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.2508 0.2428 0.3459 0.0071  0.0166  0.0614  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.2454 0.2381 0.3413 0.0065  0.0166  0.0609  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.2570 0.2495 0.3445 0.0059  0.0116  0.0613  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.2447 0.2319 0.3749 0.0146  0.0370  0.0682  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.2443 0.2263 0.3802 0.0168  0.0453  0.0666  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.2365 0.2190 0.3864 0.0194  0.0516  0.0700  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.2410 0.2175 0.3918 0.0211  0.0598  0.0662  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.2427 0.2245 0.3831 0.0174  0.0444  0.0703  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.2399 0.2185 0.3676 0.0155  0.0425  0.0653  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.2520 0.2336 0.3721 0.0137  0.0358  0.0667  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.2396 0.2117 0.3608 0.0150  0.0474  0.0577  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.2627 0.2405 0.3736 0.0124  0.0368  0.0610  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.2611 0.2333 0.3731 0.0130  0.0434  0.0555  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.2647 0.2305 0.3876 0.0161  0.0550  0.0528  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.2632 0.2307 0.3694 0.0118  0.0461  0.0490  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.2898 0.2500 0.4048 0.0147  0.0570  0.0456  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.2810 0.2426 0.3889 0.0125  0.0523  0.0440  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.2218 0.2113 0.3830 0.0196  0.0478  0.0771  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.2478 0.2391 0.4249 0.0222  0.0538  0.0813  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.2713 0.2604 0.4434 0.0219  0.0583  0.0769  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.2759 0.2649 0.4591 0.0242  0.0654  0.0791  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.2384 0.2388 0.4299 0.0221  0.0473  0.0904  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.2735 0.2609 0.4292 0.0193  0.0544  0.0714  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.2720 0.2568 0.4209 0.0189  0.0581  0.0675  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.2645 0.2420 0.3944 0.0181  0.0592  0.0587  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.2497 0.2262 0.3681 0.0166  0.0568  0.0553  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.2873 0.2782 0.4371 0.0164  0.0508  0.0707  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.2937 0.2921 0.4637 0.0171  0.0500  0.0790  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.3349 0.3337 0.5155 0.0188  0.0570  0.0813  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.2899 0.2942 0.4656 0.0159  0.0416  0.0839  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.2694 0.2420 0.3966 0.0190  0.0622  0.0554  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.2611 0.2277 0.3719 0.0178  0.0619  0.0473  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.2798 0.2401 0.3805 0.0185  0.0677  0.0415  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.2915 0.2480 0.3974 0.0209  0.0760  0.0417  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.2615 0.2244 0.3749 0.0184  0.0644  0.0457  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.2707 0.2286 0.3703 0.0167  0.0632  0.0379  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.2660 0.2286 0.3576 0.0142  0.0543  0.0377  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.2952 0.2489 0.3999 0.0172  0.0665  0.0367  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.2726 0.2314 0.3580 0.0167  0.0635  0.0363  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.2812 0.2333 0.3538 0.0173  0.0678  0.0303  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.3011 0.2478 0.3636 0.0164  0.0671  0.0230  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.3109 0.2502 0.3685 0.0176  0.0732  0.0182  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.3000 0.2541 0.3633 0.0162  0.0634  0.0301  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.3205 0.2674 0.3682 0.0168  0.0666  0.0238  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.2973 0.2561 0.3714 0.0166  0.0644  0.0368  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.2772 0.2274 0.3367 0.0143  0.0598  0.0220  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.2819 0.2282 0.3335 0.0130  0.0585  0.0154  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.2739 0.2256 0.3286 0.0112  0.0520  0.0172  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.2628 0.2203 0.3190 0.0107  0.0473  0.0216  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.2976 0.2409 0.3335 0.0125  0.0564  0.0098  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.3094 0.2510 0.3368 0.0107  0.0523  0.0033  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.3378 0.2729 0.3606 0.0103  0.0550  -0.0030 33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.2931 0.2396 0.3168 0.0091  0.0450  0.0026  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.3425 0.2789 0.3597 0.0082  0.0491  -0.0075 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.3140 0.2575 0.3320 0.0077  0.0434  -0.0039 33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.2935 0.2463 0.3183 0.0086  0.0397  0.0067  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.3127 0.2601 0.3274 0.0061  0.0371  -0.0060 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.3103 0.2659 0.3302 0.0073  0.0340  0.0043  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.3113 0.2647 0.3274 0.0061  0.0330  -0.0017 33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.2621 0.2115 0.3182 0.0102  0.0524  0.0142  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.2530 0.2068 0.3112 0.0085  0.0474  0.0155  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.2539 0.2043 0.3082 0.0068  0.0471  0.0091  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.2626 0.2066 0.3163 0.0069  0.0515  0.0045  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.2638 0.2204 0.3346 0.0092  0.0484  0.0225  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.2712 0.2228 0.3512 0.0106  0.0553  0.0230  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.3177 0.2652 0.3994 0.0093  0.0570  0.0193  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.3353 0.2762 0.4205 0.0100  0.0629  0.0165  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.2985 0.2489 0.3783 0.0074  0.0527  0.0191  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.2421 0.1966 0.2942 0.0052  0.0420  0.0085  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.2476 0.2001 0.2985 0.0032  0.0413  0.0030  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.2573 0.2148 0.3127 0.0020  0.0384  0.0062  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.2641 0.2263 0.3148 0.0019  0.0339  0.0074  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.2783 0.2298 0.3178 0.0026  0.0380  -0.0032 35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.3637 0.3135 0.4023 0.0003  0.0364  -0.0095 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.4175 0.3696 0.4637 -0.0011 0.0361  -0.0085 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.3678 0.3141 0.3978 0.0000  0.0352  -0.0154 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.2510 0.2071 0.3154 0.0014  0.0413  0.0079  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.2586 0.2187 0.3271 0.0004  0.0397  0.0115  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.2618 0.2219 0.3301 0.0004  0.0396  0.0115  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.2634 0.2259 0.3279 -0.0015 0.0363  0.0067  36  SER   C C   
1338 O O   . SER   B 30  ? 0.2626 0.2299 0.3262 -0.0017 0.0337  0.0095  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.2757 0.2326 0.3547 0.0001  0.0443  0.0143  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.2890 0.2462 0.3679 0.0002  0.0442  0.0146  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.2869 0.2465 0.3694 -0.0012 0.0437  0.0167  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.3230 0.2746 0.4042 -0.0013 0.0471  0.0083  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.2608 0.2202 0.3229 -0.0030 0.0360  -0.0006 37  SER   C N   
1344 C CA  . SER   B 31  ? 0.2697 0.2325 0.3299 -0.0048 0.0321  -0.0048 37  SER   C CA  
1345 C C   . SER   B 31  ? 0.2536 0.2211 0.3054 -0.0036 0.0274  -0.0043 37  SER   C C   
1346 O O   . SER   B 31  ? 0.2640 0.2359 0.3161 -0.0044 0.0246  -0.0053 37  SER   C O   
1347 C CB  . SER   B 31  ? 0.3191 0.2777 0.3778 -0.0067 0.0316  -0.0127 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.4001 0.3560 0.4484 -0.0055 0.0300  -0.0161 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.2398 0.2066 0.2853 -0.0016 0.0270  -0.0024 38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.2367 0.2070 0.2744 -0.0004 0.0228  -0.0016 38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.2411 0.2144 0.2793 0.0007  0.0224  0.0049  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.2357 0.2113 0.2678 0.0016  0.0192  0.0058  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.2592 0.2263 0.2889 0.0008  0.0225  -0.0037 38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.2799 0.2437 0.3053 -0.0001 0.0217  -0.0106 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.2584 0.2180 0.2743 0.0014  0.0222  -0.0123 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.2462 0.2085 0.2547 0.0028  0.0185  -0.0108 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.2715 0.2313 0.2700 0.0038  0.0169  -0.0133 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.2842 0.2384 0.2773 0.0036  0.0187  -0.0177 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.2508 0.2130 0.2438 0.0051  0.0136  -0.0115 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.2294 0.2020 0.2744 0.0008  0.0255  0.0096  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.2208 0.1956 0.2659 0.0018  0.0245  0.0160  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.2308 0.2052 0.2713 0.0030  0.0230  0.0172  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.2151 0.1919 0.2518 0.0033  0.0198  0.0201  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.2143 0.1926 0.2561 0.0015  0.0219  0.0174  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.2514 0.2311 0.2920 0.0022  0.0206  0.0236  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.2689 0.2477 0.3151 0.0025  0.0224  0.0279  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.2288 0.2103 0.2629 0.0025  0.0177  0.0241  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.2246 0.1957 0.2653 0.0035  0.0254  0.0150  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.2241 0.1950 0.2616 0.0046  0.0247  0.0166  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.2333 0.2022 0.2782 0.0055  0.0290  0.0197  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.2437 0.2092 0.2931 0.0056  0.0333  0.0179  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.2174 0.1860 0.2463 0.0049  0.0240  0.0115  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.2400 0.2109 0.2615 0.0046  0.0193  0.0090  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.2468 0.2150 0.2599 0.0052  0.0187  0.0047  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.2564 0.2301 0.2761 0.0048  0.0161  0.0132  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.2169 0.1877 0.2635 0.0062  0.0280  0.0243  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.2192 0.1891 0.2739 0.0075  0.0320  0.0278  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.2230 0.1938 0.2750 0.0078  0.0309  0.0292  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.2338 0.2075 0.2821 0.0070  0.0259  0.0307  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.2101 0.1828 0.2750 0.0077  0.0318  0.0342  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.2173 0.1896 0.2935 0.0094  0.0363  0.0385  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.2542 0.2266 0.3405 0.0102  0.0383  0.0428  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.2157 0.1923 0.2955 0.0094  0.0332  0.0436  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.2253 0.1930 0.2792 0.0091  0.0361  0.0286  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.2306 0.1988 0.2837 0.0095  0.0365  0.0305  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.2247 0.1941 0.2910 0.0108  0.0409  0.0359  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.2336 0.1998 0.3048 0.0122  0.0468  0.0351  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.2397 0.2028 0.2819 0.0102  0.0393  0.0251  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.2526 0.2156 0.2947 0.0108  0.0409  0.0278  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.2463 0.2091 0.2771 0.0091  0.0342  0.0204  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.2240 0.1980 0.2969 0.0102  0.0379  0.0412  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.2302 0.2068 0.3175 0.0114  0.0416  0.0469  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.2427 0.2196 0.3306 0.0113  0.0432  0.0484  43  SER   C C   
1394 O O   . SER   B 37  ? 0.2417 0.2173 0.3189 0.0101  0.0401  0.0457  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.2550 0.2376 0.3524 0.0106  0.0361  0.0531  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.2491 0.2349 0.3415 0.0083  0.0284  0.0540  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.2403 0.2186 0.3414 0.0128  0.0488  0.0528  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.2542 0.2330 0.3578 0.0127  0.0513  0.0549  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.2776 0.2636 0.3920 0.0105  0.0446  0.0608  44  SER   C C   
1400 O O   . SER   B 38  ? 0.2875 0.2784 0.4111 0.0100  0.0400  0.0648  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.2966 0.2727 0.4086 0.0155  0.0617  0.0562  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.3513 0.3321 0.4808 0.0166  0.0627  0.0618  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.2776 0.2640 0.3905 0.0091  0.0437  0.0617  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.2827 0.2752 0.4050 0.0064  0.0367  0.0665  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.3238 0.3183 0.4590 0.0065  0.0419  0.0710  45  THR   C C   
1406 O O   . THR   B 39  ? 0.3329 0.3226 0.4638 0.0083  0.0501  0.0692  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2922 0.2829 0.4006 0.0038  0.0294  0.0631  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.3115 0.2967 0.4101 0.0044  0.0340  0.0600  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2950 0.2839 0.3910 0.0037  0.0246  0.0588  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.3437 0.3452 0.4940 0.0043  0.0367  0.0767  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.3710 0.3755 0.5360 0.0038  0.0411  0.0815  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.3828 0.3840 0.5387 0.0013  0.0391  0.0795  46  THR   C C   
1413 O O   . THR   B 40  ? 0.4036 0.4017 0.5599 0.0022  0.0469  0.0800  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.4163 0.4300 0.6029 0.0024  0.0360  0.0886  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.4680 0.4845 0.6511 -0.0014 0.0240  0.0886  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.4091 0.4254 0.6043 0.0053  0.0378  0.0909  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.3663 0.3675 0.5134 -0.0017 0.0292  0.0774  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.3603 0.3578 0.4986 -0.0040 0.0269  0.0754  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.3390 0.3286 0.4558 -0.0022 0.0294  0.0690  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.3333 0.3210 0.4405 -0.0004 0.0290  0.0653  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.3763 0.3768 0.5156 -0.0081 0.0154  0.0760  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.3362 0.3210 0.4457 -0.0027 0.0316  0.0679  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.3560 0.3337 0.4459 -0.0010 0.0332  0.0624  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.3509 0.3275 0.4300 -0.0029 0.0238  0.0588  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.3645 0.3433 0.4490 -0.0061 0.0173  0.0606  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.4154 0.3880 0.5016 -0.0005 0.0394  0.0635  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.5135 0.4838 0.6011 0.0028  0.0505  0.0646  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.6383 0.6027 0.7192 0.0035  0.0567  0.0656  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6747 0.6404 0.7663 0.0015  0.0580  0.0702  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.6781 0.6355 0.7410 0.0063  0.0605  0.0615  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.3247 0.2979 0.3893 -0.0010 0.0234  0.0538  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.3100 0.2817 0.3636 -0.0020 0.0162  0.0500  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.3067 0.2724 0.3482 -0.0016 0.0163  0.0476  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.3418 0.3041 0.3806 0.0000  0.0224  0.0483  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2775 0.2417 0.3115 -0.0027 0.0100  0.0451  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2938 0.2523 0.3179 -0.0023 0.0096  0.0433  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.3104 0.2661 0.3208 -0.0001 0.0079  0.0386  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.3429 0.2940 0.3456 0.0006  0.0073  0.0375  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.3089 0.2665 0.3371 -0.0056 0.0044  0.0449  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.4082 0.3708 0.4558 -0.0088 0.0052  0.0508  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.2765 0.2349 0.2846 0.0011  0.0074  0.0360  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.2655 0.2220 0.2624 0.0031  0.0057  0.0316  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2793 0.2328 0.2691 0.0058  0.0103  0.0302  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.3057 0.2592 0.2989 0.0064  0.0155  0.0318  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.2765 0.2371 0.2746 0.0032  0.0039  0.0296  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.3382 0.3010 0.3398 0.0010  -0.0012 0.0305  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.3201 0.2804 0.3186 -0.0002 -0.0046 0.0302  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2962 0.2628 0.3027 0.0005  -0.0018 0.0313  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.2690 0.2197 0.2488 0.0075  0.0085  0.0274  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.2768 0.2246 0.2480 0.0101  0.0114  0.0257  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.2849 0.2351 0.2521 0.0112  0.0090  0.0213  52  THR   C C   
1452 O O   . THR   B 46  ? 0.2865 0.2383 0.2529 0.0110  0.0048  0.0196  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.3127 0.2558 0.2759 0.0115  0.0104  0.0263  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.3464 0.2869 0.3141 0.0102  0.0130  0.0305  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.3344 0.2744 0.2865 0.0144  0.0119  0.0244  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.2665 0.2164 0.2311 0.0123  0.0120  0.0194  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.2582 0.2102 0.2198 0.0130  0.0097  0.0150  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.2570 0.2067 0.2084 0.0151  0.0071  0.0129  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2812 0.2266 0.2251 0.0165  0.0091  0.0137  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.2738 0.2258 0.2369 0.0129  0.0136  0.0133  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.2927 0.2467 0.2666 0.0114  0.0168  0.0162  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.2781 0.2323 0.2397 0.0130  0.0109  0.0087  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.3254 0.2842 0.3072 0.0097  0.0130  0.0174  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.2433 0.1960 0.1945 0.0154  0.0027  0.0103  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.2369 0.1885 0.1802 0.0176  -0.0004 0.0084  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.2525 0.2030 0.1900 0.0183  0.0003  0.0054  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.2537 0.2061 0.1953 0.0169  0.0016  0.0031  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.2477 0.2036 0.1945 0.0179  -0.0045 0.0064  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.2564 0.2034 0.1838 0.0204  -0.0010 0.0052  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.2658 0.2111 0.1853 0.0210  -0.0015 0.0018  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.2669 0.2137 0.1813 0.0231  -0.0077 0.0005  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2953 0.2386 0.2016 0.0253  -0.0089 0.0029  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.2866 0.2252 0.1970 0.0219  0.0036  0.0035  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.2684 0.2063 0.1862 0.0203  0.0100  0.0055  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2885 0.2287 0.2128 0.0185  0.0114  0.0021  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2950 0.2347 0.2272 0.0174  0.0175  0.0049  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.3033 0.2457 0.2451 0.0159  0.0193  0.0040  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.2912 0.2366 0.2354 0.0149  0.0159  0.0001  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2999 0.2423 0.2498 0.0152  0.0244  0.0073  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.2618 0.2141 0.1825 0.0223  -0.0116 -0.0028 56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.2655 0.2212 0.1856 0.0242  -0.0177 -0.0035 56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.2593 0.2214 0.1879 0.0228  -0.0209 -0.0075 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.2607 0.2241 0.1952 0.0203  -0.0182 -0.0094 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.2783 0.2345 0.2027 0.0254  -0.0176 0.0001  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.2537 0.2145 0.1913 0.0230  -0.0155 -0.0001 56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.2807 0.2472 0.2117 0.0244  -0.0264 -0.0081 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.2835 0.2570 0.2251 0.0231  -0.0290 -0.0112 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.2927 0.2706 0.2427 0.0247  -0.0298 -0.0091 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2964 0.2802 0.2536 0.0252  -0.0333 -0.0106 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.3151 0.2906 0.2534 0.0233  -0.0351 -0.0145 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.3903 0.3661 0.3229 0.0268  -0.0403 -0.0125 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.3791 0.3525 0.3098 0.0292  -0.0387 -0.0085 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.4801 0.4586 0.4110 0.0271  -0.0465 -0.0150 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.2770 0.2518 0.2265 0.0253  -0.0262 -0.0059 58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.2512 0.2286 0.2073 0.0268  -0.0260 -0.0044 58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.2470 0.2302 0.2136 0.0250  -0.0250 -0.0064 58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.2538 0.2374 0.2229 0.0222  -0.0226 -0.0077 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.2434 0.2157 0.1968 0.0267  -0.0223 -0.0014 58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.2758 0.2410 0.2189 0.0293  -0.0230 0.0020  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.2366 0.2239 0.2097 0.0270  -0.0263 -0.0062 59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.2443 0.2368 0.2276 0.0258  -0.0241 -0.0073 59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.2371 0.2282 0.2216 0.0275  -0.0212 -0.0054 59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.2337 0.2289 0.2261 0.0277  -0.0193 -0.0059 59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.2536 0.2534 0.2459 0.0262  -0.0276 -0.0094 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2643 0.2659 0.2573 0.0234  -0.0301 -0.0124 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.3299 0.3393 0.3340 0.0230  -0.0337 -0.0147 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.3681 0.3796 0.3709 0.0238  -0.0396 -0.0161 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2777 0.2916 0.2929 0.0218  -0.0303 -0.0148 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.2389 0.2237 0.2156 0.0289  -0.0207 -0.0034 60  THR   C N   
1510 C CA  . THR   B 54  ? 0.2539 0.2354 0.2297 0.0299  -0.0179 -0.0021 60  THR   C CA  
1511 C C   . THR   B 54  ? 0.2523 0.2274 0.2211 0.0279  -0.0162 -0.0006 60  THR   C C   
1512 O O   . THR   B 54  ? 0.2677 0.2398 0.2314 0.0273  -0.0172 0.0003  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2894 0.2700 0.2655 0.0339  -0.0191 -0.0014 60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.3301 0.3061 0.2991 0.0351  -0.0215 0.0003  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2896 0.2778 0.2749 0.0360  -0.0212 -0.0025 60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.2205 0.1937 0.1892 0.0268  -0.0134 -0.0003 61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.2256 0.1935 0.1893 0.0246  -0.0125 0.0012  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.2293 0.1949 0.1918 0.0237  -0.0104 0.0011  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.2403 0.2070 0.2045 0.0256  -0.0092 0.0000  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.2299 0.1924 0.1896 0.0211  -0.0102 0.0024  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.2268 0.1863 0.1834 0.0197  -0.0092 0.0024  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.2172 0.1788 0.1758 0.0166  -0.0088 0.0039  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.2306 0.1924 0.1907 0.0150  -0.0096 0.0054  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.2380 0.1902 0.1889 0.0196  -0.0105 0.0028  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.2521 0.2005 0.1984 0.0176  -0.0105 0.0026  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.2461 0.1956 0.1955 0.0232  -0.0105 0.0017  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.2203 0.1833 0.1789 0.0159  -0.0072 0.0038  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.2010 0.1656 0.1614 0.0132  -0.0071 0.0059  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.2224 0.1831 0.1767 0.0118  -0.0079 0.0067  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.2417 0.1993 0.1906 0.0132  -0.0071 0.0051  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.2057 0.1760 0.1725 0.0131  -0.0046 0.0059  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.2108 0.1820 0.1766 0.0139  -0.0020 0.0056  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.2311 0.2030 0.1973 0.0164  -0.0002 0.0036  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.2373 0.2087 0.2024 0.0122  -0.0009 0.0079  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.2600 0.2328 0.2259 0.0172  0.0033  0.0035  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.2528 0.2247 0.2165 0.0130  0.0024  0.0080  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.2715 0.2439 0.2354 0.0155  0.0048  0.0057  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.2976 0.2704 0.2605 0.0165  0.0090  0.0061  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.2276 0.1886 0.1830 0.0093  -0.0094 0.0093  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.2333 0.1909 0.1825 0.0076  -0.0113 0.0104  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.2278 0.1882 0.1773 0.0075  -0.0092 0.0118  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.2321 0.1969 0.1885 0.0068  -0.0081 0.0140  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.2353 0.1922 0.1865 0.0047  -0.0149 0.0130  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.2625 0.2159 0.2067 0.0028  -0.0181 0.0138  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.2771 0.2242 0.2116 0.0031  -0.0192 0.0110  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.2586 0.2144 0.2051 0.0009  -0.0200 0.0174  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.2866 0.2296 0.2127 0.0013  -0.0224 0.0112  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.2873 0.2399 0.2263 -0.0009 -0.0238 0.0182  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.2992 0.2451 0.2273 -0.0009 -0.0252 0.0149  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.3428 0.2845 0.2614 -0.0028 -0.0293 0.0151  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.2318 0.1888 0.1729 0.0082  -0.0083 0.0108  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.2388 0.1971 0.1779 0.0083  -0.0057 0.0126  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.2617 0.2157 0.1915 0.0062  -0.0095 0.0144  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.2826 0.2307 0.2017 0.0065  -0.0102 0.0122  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.2482 0.2057 0.1842 0.0110  -0.0012 0.0100  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.2879 0.2461 0.2204 0.0114  0.0033  0.0125  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.2648 0.2216 0.1987 0.0043  -0.0118 0.0184  66  SER   C N   
1558 C CA  . SER   B 60  ? 0.2779 0.2314 0.2040 0.0022  -0.0165 0.0205  66  SER   C CA  
1559 C C   . SER   B 60  ? 0.2866 0.2362 0.2004 0.0031  -0.0147 0.0205  66  SER   C C   
1560 O O   . SER   B 60  ? 0.3177 0.2618 0.2204 0.0018  -0.0188 0.0198  66  SER   C O   
1561 C CB  . SER   B 60  ? 0.3082 0.2662 0.2427 0.0005  -0.0191 0.0254  66  SER   C CB  
1562 O OG  . SER   B 60  ? 0.3826 0.3378 0.3101 -0.0017 -0.0250 0.0273  66  SER   C OG  
1563 N N   . SER   B 61  ? 0.2776 0.2295 0.1933 0.0051  -0.0088 0.0212  67  SER   C N   
1564 C CA  . SER   B 61  ? 0.2901 0.2381 0.1939 0.0062  -0.0058 0.0217  67  SER   C CA  
1565 C C   . SER   B 61  ? 0.3105 0.2520 0.2031 0.0079  -0.0037 0.0169  67  SER   C C   
1566 O O   . SER   B 61  ? 0.3314 0.2682 0.2118 0.0089  -0.0010 0.0169  67  SER   C O   
1567 C CB  . SER   B 61  ? 0.2960 0.2485 0.2067 0.0077  0.0005  0.0242  67  SER   C CB  
1568 O OG  . SER   B 61  ? 0.3168 0.2726 0.2364 0.0095  0.0053  0.0213  67  SER   C OG  
1569 N N   . ARG   B 62  ? 0.3074 0.2482 0.2036 0.0084  -0.0044 0.0131  68  ARG   C N   
1570 C CA  . ARG   B 62  ? 0.3101 0.2441 0.1966 0.0100  -0.0028 0.0086  68  ARG   C CA  
1571 C C   . ARG   B 62  ? 0.3307 0.2598 0.2136 0.0080  -0.0090 0.0062  68  ARG   C C   
1572 O O   . ARG   B 62  ? 0.3480 0.2701 0.2226 0.0090  -0.0084 0.0022  68  ARG   C O   
1573 C CB  . ARG   B 62  ? 0.3071 0.2442 0.2022 0.0131  0.0028  0.0062  68  ARG   C CB  
1574 C CG  . ARG   B 62  ? 0.3562 0.2982 0.2564 0.0150  0.0094  0.0081  68  ARG   C CG  
1575 C CD  . ARG   B 62  ? 0.3710 0.3070 0.2583 0.0170  0.0144  0.0070  68  ARG   C CD  
1576 N NE  . ARG   B 62  ? 0.3968 0.3376 0.2901 0.0186  0.0214  0.0093  68  ARG   C NE  
1577 C CZ  . ARG   B 62  ? 0.4621 0.4042 0.3537 0.0176  0.0229  0.0135  68  ARG   C CZ  
1578 N NH1 . ARG   B 62  ? 0.5152 0.4547 0.3992 0.0151  0.0173  0.0161  68  ARG   C NH1 
1579 N NH2 . ARG   B 62  ? 0.4436 0.3897 0.3417 0.0191  0.0299  0.0155  68  ARG   C NH2 
1580 N N   . ARG   B 63  ? 0.3206 0.2528 0.2102 0.0051  -0.0148 0.0087  69  ARG   C N   
1581 C CA  . ARG   B 63  ? 0.3291 0.2578 0.2187 0.0027  -0.0204 0.0071  69  ARG   C CA  
1582 C C   . ARG   B 63  ? 0.3402 0.2667 0.2326 0.0048  -0.0179 0.0034  69  ARG   C C   
1583 O O   . ARG   B 63  ? 0.3710 0.2902 0.2566 0.0042  -0.0200 0.0002  69  ARG   C O   
1584 C CB  . ARG   B 63  ? 0.3629 0.2839 0.2386 0.0003  -0.0256 0.0058  69  ARG   C CB  
1585 C CG  . ARG   B 63  ? 0.4077 0.3309 0.2810 -0.0021 -0.0301 0.0101  69  ARG   C CG  
1586 C CD  . ARG   B 63  ? 0.4854 0.4143 0.3710 -0.0050 -0.0357 0.0137  69  ARG   C CD  
1587 N NE  . ARG   B 63  ? 0.5253 0.4541 0.4059 -0.0077 -0.0420 0.0171  69  ARG   C NE  
1588 C CZ  . ARG   B 63  ? 0.5259 0.4594 0.4086 -0.0072 -0.0415 0.0219  69  ARG   C CZ  
1589 N NH1 . ARG   B 63  ? 0.4893 0.4276 0.3787 -0.0044 -0.0346 0.0236  69  ARG   C NH1 
1590 N NH2 . ARG   B 63  ? 0.5238 0.4571 0.4018 -0.0095 -0.0481 0.0253  69  ARG   C NH2 
1591 N N   . LYS   B 64  ? 0.3105 0.2430 0.2127 0.0073  -0.0134 0.0039  70  LYS   C N   
1592 C CA  . LYS   B 64  ? 0.3211 0.2521 0.2261 0.0099  -0.0110 0.0009  70  LYS   C CA  
1593 C C   . LYS   B 64  ? 0.2887 0.2267 0.2063 0.0107  -0.0101 0.0023  70  LYS   C C   
1594 O O   . LYS   B 64  ? 0.2723 0.2167 0.1967 0.0104  -0.0089 0.0047  70  LYS   C O   
1595 C CB  . LYS   B 64  ? 0.3828 0.3121 0.2831 0.0134  -0.0051 -0.0014 70  LYS   C CB  
1596 C CG  . LYS   B 64  ? 0.5111 0.4302 0.3975 0.0139  -0.0049 -0.0048 70  LYS   C CG  
1597 C CD  . LYS   B 64  ? 0.6252 0.5425 0.5082 0.0179  0.0021  -0.0071 70  LYS   C CD  
1598 C CE  . LYS   B 64  ? 0.7050 0.6110 0.5736 0.0187  0.0029  -0.0111 70  LYS   C CE  
1599 N NZ  . LYS   B 64  ? 0.7632 0.6636 0.6182 0.0155  -0.0007 -0.0110 70  LYS   C NZ  
1600 N N   . HIS   B 65  ? 0.2839 0.2199 0.2040 0.0118  -0.0107 0.0008  71  HIS   C N   
1601 C CA  . HIS   B 65  ? 0.2902 0.2318 0.2201 0.0132  -0.0098 0.0016  71  HIS   C CA  
1602 C C   . HIS   B 65  ? 0.2891 0.2317 0.2203 0.0170  -0.0060 -0.0005 71  HIS   C C   
1603 O O   . HIS   B 65  ? 0.3407 0.2775 0.2664 0.0190  -0.0049 -0.0028 71  HIS   C O   
1604 C CB  . HIS   B 65  ? 0.2767 0.2153 0.2081 0.0122  -0.0128 0.0019  71  HIS   C CB  
1605 C CG  . HIS   B 65  ? 0.2676 0.2061 0.2003 0.0084  -0.0164 0.0043  71  HIS   C CG  
1606 N ND1 . HIS   B 65  ? 0.2922 0.2359 0.2330 0.0073  -0.0167 0.0071  71  HIS   C ND1 
1607 C CD2 . HIS   B 65  ? 0.2877 0.2216 0.2151 0.0055  -0.0198 0.0044  71  HIS   C CD2 
1608 C CE1 . HIS   B 65  ? 0.2819 0.2245 0.2235 0.0040  -0.0200 0.0090  71  HIS   C CE1 
1609 N NE2 . HIS   B 65  ? 0.3151 0.2521 0.2490 0.0027  -0.0224 0.0076  71  HIS   C NE2 
1610 N N   . TYR   B 66  ? 0.2558 0.2056 0.1950 0.0183  -0.0039 0.0002  72  TYR   C N   
1611 C CA  . TYR   B 66  ? 0.2502 0.2025 0.1930 0.0218  -0.0006 -0.0014 72  TYR   C CA  
1612 C C   . TYR   B 66  ? 0.2403 0.1967 0.1906 0.0233  -0.0021 -0.0013 72  TYR   C C   
1613 O O   . TYR   B 66  ? 0.2509 0.2119 0.2062 0.0216  -0.0034 0.0000  72  TYR   C O   
1614 C CB  . TYR   B 66  ? 0.2675 0.2254 0.2147 0.0220  0.0030  -0.0007 72  TYR   C CB  
1615 C CG  . TYR   B 66  ? 0.2988 0.2525 0.2375 0.0215  0.0056  -0.0007 72  TYR   C CG  
1616 C CD1 . TYR   B 66  ? 0.3346 0.2840 0.2678 0.0242  0.0091  -0.0027 72  TYR   C CD1 
1617 C CD2 . TYR   B 66  ? 0.3139 0.2684 0.2504 0.0187  0.0049  0.0017  72  TYR   C CD2 
1618 C CE1 . TYR   B 66  ? 0.3447 0.2897 0.2684 0.0239  0.0120  -0.0028 72  TYR   C CE1 
1619 C CE2 . TYR   B 66  ? 0.3376 0.2882 0.2651 0.0185  0.0071  0.0021  72  TYR   C CE2 
1620 C CZ  . TYR   B 66  ? 0.3526 0.2982 0.2729 0.0210  0.0107  -0.0003 72  TYR   C CZ  
1621 O OH  . TYR   B 66  ? 0.3801 0.3209 0.2893 0.0208  0.0131  0.0000  72  TYR   C OH  
1622 N N   . PRO   B 67  ? 0.2414 0.1963 0.1924 0.0265  -0.0016 -0.0026 73  PRO   C N   
1623 C CA  . PRO   B 67  ? 0.2355 0.1953 0.1935 0.0283  -0.0032 -0.0023 73  PRO   C CA  
1624 C C   . PRO   B 67  ? 0.2502 0.2182 0.2170 0.0290  -0.0015 -0.0025 73  PRO   C C   
1625 O O   . PRO   B 67  ? 0.2714 0.2408 0.2401 0.0304  0.0022  -0.0032 73  PRO   C O   
1626 C CB  . PRO   B 67  ? 0.2784 0.2340 0.2348 0.0319  -0.0032 -0.0031 73  PRO   C CB  
1627 C CG  . PRO   B 67  ? 0.3076 0.2578 0.2584 0.0327  0.0001  -0.0046 73  PRO   C CG  
1628 C CD  . PRO   B 67  ? 0.2706 0.2192 0.2160 0.0290  0.0005  -0.0044 73  PRO   C CD  
1629 N N   . VAL   B 68  ? 0.2233 0.1966 0.1956 0.0278  -0.0038 -0.0021 74  VAL   C N   
1630 C CA  . VAL   B 68  ? 0.2195 0.2004 0.2009 0.0277  -0.0026 -0.0026 74  VAL   C CA  
1631 C C   . VAL   B 68  ? 0.2180 0.2032 0.2044 0.0285  -0.0062 -0.0031 74  VAL   C C   
1632 O O   . VAL   B 68  ? 0.2363 0.2187 0.2181 0.0281  -0.0091 -0.0026 74  VAL   C O   
1633 C CB  . VAL   B 68  ? 0.2537 0.2362 0.2363 0.0242  -0.0011 -0.0018 74  VAL   C CB  
1634 C CG1 . VAL   B 68  ? 0.2815 0.2614 0.2602 0.0238  0.0027  -0.0011 74  VAL   C CG1 
1635 C CG2 . VAL   B 68  ? 0.2569 0.2369 0.2355 0.0217  -0.0037 -0.0008 74  VAL   C CG2 
1636 N N   . SER   B 69  ? 0.2204 0.2126 0.2164 0.0293  -0.0060 -0.0040 75  SER   C N   
1637 C CA  . SER   B 69  ? 0.2169 0.2145 0.2189 0.0290  -0.0099 -0.0050 75  SER   C CA  
1638 C C   . SER   B 69  ? 0.2071 0.2075 0.2131 0.0252  -0.0087 -0.0057 75  SER   C C   
1639 O O   . SER   B 69  ? 0.2129 0.2143 0.2221 0.0240  -0.0046 -0.0052 75  SER   C O   
1640 C CB  . SER   B 69  ? 0.2352 0.2395 0.2478 0.0317  -0.0103 -0.0057 75  SER   C CB  
1641 O OG  . SER   B 69  ? 0.3020 0.3039 0.3119 0.0356  -0.0119 -0.0049 75  SER   C OG  
1642 N N   . PHE   B 70  ? 0.1978 0.1982 0.2023 0.0234  -0.0118 -0.0066 76  PHE   C N   
1643 C CA  . PHE   B 70  ? 0.1975 0.1993 0.2056 0.0199  -0.0103 -0.0073 76  PHE   C CA  
1644 C C   . PHE   B 70  ? 0.2059 0.2114 0.2185 0.0188  -0.0140 -0.0098 76  PHE   C C   
1645 O O   . PHE   B 70  ? 0.2176 0.2228 0.2264 0.0203  -0.0183 -0.0106 76  PHE   C O   
1646 C CB  . PHE   B 70  ? 0.2170 0.2131 0.2176 0.0180  -0.0085 -0.0058 76  PHE   C CB  
1647 C CG  . PHE   B 70  ? 0.2038 0.1952 0.1957 0.0188  -0.0111 -0.0054 76  PHE   C CG  
1648 C CD1 . PHE   B 70  ? 0.2158 0.2030 0.2012 0.0206  -0.0113 -0.0038 76  PHE   C CD1 
1649 C CD2 . PHE   B 70  ? 0.2188 0.2093 0.2089 0.0174  -0.0127 -0.0067 76  PHE   C CD2 
1650 C CE1 . PHE   B 70  ? 0.2306 0.2134 0.2089 0.0211  -0.0131 -0.0030 76  PHE   C CE1 
1651 C CE2 . PHE   B 70  ? 0.2311 0.2170 0.2129 0.0181  -0.0140 -0.0059 76  PHE   C CE2 
1652 C CZ  . PHE   B 70  ? 0.2378 0.2201 0.2142 0.0199  -0.0142 -0.0038 76  PHE   C CZ  
1653 N N   . SER   B 71  ? 0.1921 0.2004 0.2120 0.0160  -0.0126 -0.0111 77  SER   C N   
1654 C CA  . SER   B 71  ? 0.1995 0.2112 0.2244 0.0144  -0.0165 -0.0143 77  SER   C CA  
1655 C C   . SER   B 71  ? 0.2336 0.2401 0.2497 0.0129  -0.0182 -0.0158 77  SER   C C   
1656 O O   . SER   B 71  ? 0.2406 0.2415 0.2482 0.0132  -0.0161 -0.0139 77  SER   C O   
1657 C CB  . SER   B 71  ? 0.2126 0.2291 0.2500 0.0118  -0.0141 -0.0152 77  SER   C CB  
1658 O OG  . SER   B 71  ? 0.2326 0.2453 0.2686 0.0095  -0.0096 -0.0141 77  SER   C OG  
1659 N N   . LYS   B 72  ? 0.2375 0.2456 0.2551 0.0116  -0.0224 -0.0192 78  LYS   C N   
1660 C CA  . LYS   B 72  ? 0.2369 0.2391 0.2446 0.0105  -0.0236 -0.0211 78  LYS   C CA  
1661 C C   . LYS   B 72  ? 0.2452 0.2449 0.2562 0.0074  -0.0190 -0.0218 78  LYS   C C   
1662 O O   . LYS   B 72  ? 0.2529 0.2564 0.2748 0.0055  -0.0171 -0.0221 78  LYS   C O   
1663 C CB  . LYS   B 72  ? 0.2722 0.2765 0.2792 0.0100  -0.0300 -0.0249 78  LYS   C CB  
1664 C CG  . LYS   B 72  ? 0.3367 0.3426 0.3391 0.0136  -0.0348 -0.0235 78  LYS   C CG  
1665 C CD  . LYS   B 72  ? 0.4754 0.4817 0.4730 0.0133  -0.0419 -0.0269 78  LYS   C CD  
1666 C CE  . LYS   B 72  ? 0.5650 0.5696 0.5527 0.0172  -0.0456 -0.0245 78  LYS   C CE  
1667 N NZ  . LYS   B 72  ? 0.6265 0.6300 0.6061 0.0171  -0.0526 -0.0274 78  LYS   C NZ  
1668 N N   . PRO   B 73  ? 0.2424 0.2358 0.2452 0.0070  -0.0168 -0.0216 79  PRO   C N   
1669 C CA  . PRO   B 73  ? 0.2535 0.2440 0.2600 0.0045  -0.0120 -0.0217 79  PRO   C CA  
1670 C C   . PRO   B 73  ? 0.2535 0.2455 0.2676 0.0016  -0.0131 -0.0260 79  PRO   C C   
1671 O O   . PRO   B 73  ? 0.2716 0.2632 0.2824 0.0009  -0.0176 -0.0302 79  PRO   C O   
1672 C CB  . PRO   B 73  ? 0.2796 0.2633 0.2759 0.0051  -0.0100 -0.0213 79  PRO   C CB  
1673 C CG  . PRO   B 73  ? 0.2834 0.2663 0.2706 0.0079  -0.0128 -0.0198 79  PRO   C CG  
1674 C CD  . PRO   B 73  ? 0.2516 0.2399 0.2417 0.0090  -0.0179 -0.0209 79  PRO   C CD  
1675 N N   . SER   B 74  ? 0.2364 0.2305 0.2611 -0.0003 -0.0094 -0.0249 80  SER   C N   
1676 C CA  . SER   B 74  ? 0.2444 0.2406 0.2789 -0.0034 -0.0103 -0.0286 80  SER   C CA  
1677 C C   . SER   B 74  ? 0.2403 0.2346 0.2829 -0.0055 -0.0045 -0.0270 80  SER   C C   
1678 O O   . SER   B 74  ? 0.2346 0.2271 0.2754 -0.0043 -0.0002 -0.0226 80  SER   C O   
1679 C CB  . SER   B 74  ? 0.3022 0.3064 0.3462 -0.0033 -0.0133 -0.0287 80  SER   C CB  
1680 O OG  . SER   B 74  ? 0.3912 0.3980 0.4296 -0.0008 -0.0187 -0.0292 80  SER   C OG  
1681 N N   . LEU   B 75  ? 0.2508 0.2458 0.3028 -0.0088 -0.0045 -0.0305 81  LEU   C N   
1682 C CA  . LEU   B 75  ? 0.2770 0.2702 0.3382 -0.0109 0.0011  -0.0287 81  LEU   C CA  
1683 C C   . LEU   B 75  ? 0.2844 0.2845 0.3568 -0.0111 0.0027  -0.0255 81  LEU   C C   
1684 O O   . LEU   B 75  ? 0.2990 0.3044 0.3800 -0.0126 -0.0004 -0.0281 81  LEU   C O   
1685 C CB  . LEU   B 75  ? 0.3053 0.2949 0.3713 -0.0145 0.0002  -0.0345 81  LEU   C CB  
1686 C CG  . LEU   B 75  ? 0.3406 0.3261 0.4153 -0.0168 0.0062  -0.0334 81  LEU   C CG  
1687 C CD1 . LEU   B 75  ? 0.3421 0.3216 0.4099 -0.0147 0.0111  -0.0299 81  LEU   C CD1 
1688 C CD2 . LEU   B 75  ? 0.3698 0.3513 0.4485 -0.0207 0.0043  -0.0403 81  LEU   C CD2 
1689 N N   . ILE   B 76  ? 0.2777 0.2778 0.3500 -0.0094 0.0075  -0.0198 82  ILE   C N   
1690 C CA  . ILE   B 76  ? 0.2794 0.2851 0.3591 -0.0089 0.0099  -0.0162 82  ILE   C CA  
1691 C C   . ILE   B 76  ? 0.2823 0.2859 0.3688 -0.0102 0.0162  -0.0123 82  ILE   C C   
1692 O O   . ILE   B 76  ? 0.2714 0.2700 0.3527 -0.0096 0.0188  -0.0097 82  ILE   C O   
1693 C CB  . ILE   B 76  ? 0.3147 0.3213 0.3846 -0.0051 0.0094  -0.0127 82  ILE   C CB  
1694 C CG1 . ILE   B 76  ? 0.3431 0.3515 0.4065 -0.0033 0.0036  -0.0157 82  ILE   C CG1 
1695 C CG2 . ILE   B 76  ? 0.3215 0.3321 0.3965 -0.0041 0.0133  -0.0087 82  ILE   C CG2 
1696 C CD1 . ILE   B 76  ? 0.3663 0.3813 0.4393 -0.0042 0.0002  -0.0187 82  ILE   C CD1 
1697 N N   . PHE   B 77  ? 0.2686 0.2765 0.3671 -0.0118 0.0188  -0.0113 83  PHE   C N   
1698 C CA  . PHE   B 77  ? 0.2784 0.2844 0.3828 -0.0127 0.0253  -0.0067 83  PHE   C CA  
1699 C C   . PHE   B 77  ? 0.2886 0.2949 0.3850 -0.0094 0.0281  -0.0008 83  PHE   C C   
1700 O O   . PHE   B 77  ? 0.3160 0.3266 0.4106 -0.0076 0.0273  -0.0005 83  PHE   C O   
1701 C CB  . PHE   B 77  ? 0.2752 0.2855 0.3955 -0.0155 0.0277  -0.0072 83  PHE   C CB  
1702 C CG  . PHE   B 77  ? 0.2947 0.3016 0.4212 -0.0168 0.0346  -0.0025 83  PHE   C CG  
1703 C CD1 . PHE   B 77  ? 0.3011 0.3019 0.4302 -0.0190 0.0359  -0.0036 83  PHE   C CD1 
1704 C CD2 . PHE   B 77  ? 0.3127 0.3217 0.4412 -0.0155 0.0401  0.0033  83  PHE   C CD2 
1705 C CE1 . PHE   B 77  ? 0.3181 0.3153 0.4529 -0.0198 0.0423  0.0014  83  PHE   C CE1 
1706 C CE2 . PHE   B 77  ? 0.3221 0.3274 0.4551 -0.0164 0.0464  0.0084  83  PHE   C CE2 
1707 C CZ  . PHE   B 77  ? 0.3240 0.3237 0.4607 -0.0185 0.0473  0.0076  83  PHE   C CZ  
1708 N N   . VAL   B 78  ? 0.2531 0.2546 0.3444 -0.0087 0.0311  0.0035  84  VAL   C N   
1709 C CA  . VAL   B 78  ? 0.2556 0.2563 0.3376 -0.0060 0.0329  0.0087  84  VAL   C CA  
1710 C C   . VAL   B 78  ? 0.2548 0.2542 0.3419 -0.0066 0.0391  0.0143  84  VAL   C C   
1711 O O   . VAL   B 78  ? 0.2567 0.2525 0.3488 -0.0082 0.0412  0.0156  84  VAL   C O   
1712 C CB  . VAL   B 78  ? 0.2717 0.2679 0.3431 -0.0047 0.0303  0.0097  84  VAL   C CB  
1713 C CG1 . VAL   B 78  ? 0.2887 0.2840 0.3504 -0.0023 0.0310  0.0147  84  VAL   C CG1 
1714 C CG2 . VAL   B 78  ? 0.2725 0.2692 0.3388 -0.0041 0.0250  0.0046  84  VAL   C CG2 
1715 N N   . GLU   B 79  ? 0.2476 0.2488 0.3321 -0.0051 0.0422  0.0179  85  GLU   C N   
1716 C CA  . GLU   B 79  ? 0.2588 0.2579 0.3456 -0.0053 0.0484  0.0239  85  GLU   C CA  
1717 C C   . GLU   B 79  ? 0.2663 0.2603 0.3442 -0.0041 0.0482  0.0288  85  GLU   C C   
1718 O O   . GLU   B 79  ? 0.2689 0.2614 0.3380 -0.0029 0.0436  0.0278  85  GLU   C O   
1719 C CB  . GLU   B 79  ? 0.2830 0.2846 0.3669 -0.0035 0.0524  0.0266  85  GLU   C CB  
1720 C CG  . GLU   B 79  ? 0.3587 0.3663 0.4551 -0.0046 0.0539  0.0232  85  GLU   C CG  
1721 C CD  . GLU   B 79  ? 0.4632 0.4720 0.5762 -0.0081 0.0569  0.0227  85  GLU   C CD  
1722 O OE1 . GLU   B 79  ? 0.4966 0.5017 0.6120 -0.0090 0.0618  0.0275  85  GLU   C OE1 
1723 O OE2 . GLU   B 79  ? 0.4567 0.4697 0.5802 -0.0101 0.0539  0.0174  85  GLU   C OE2 
1724 N N   . ALA   B 80  ? 0.2731 0.2643 0.3542 -0.0045 0.0530  0.0343  86  ALA   C N   
1725 C CA  . ALA   B 80  ? 0.2837 0.2705 0.3581 -0.0033 0.0527  0.0398  86  ALA   C CA  
1726 C C   . ALA   B 80  ? 0.3089 0.2952 0.3680 -0.0009 0.0496  0.0420  86  ALA   C C   
1727 O O   . ALA   B 80  ? 0.3299 0.3177 0.3829 0.0003  0.0508  0.0419  86  ALA   C O   
1728 C CB  . ALA   B 80  ? 0.2907 0.2748 0.3706 -0.0038 0.0590  0.0462  86  ALA   C CB  
1729 N N   . SER   B 81  ? 0.3107 0.2948 0.3642 -0.0001 0.0454  0.0434  87  SER   C N   
1730 C CA  . SER   B 81  ? 0.3188 0.3020 0.3585 0.0017  0.0416  0.0455  87  SER   C CA  
1731 C C   . SER   B 81  ? 0.3289 0.3091 0.3657 0.0025  0.0412  0.0525  87  SER   C C   
1732 O O   . SER   B 81  ? 0.3176 0.2964 0.3634 0.0019  0.0446  0.0557  87  SER   C O   
1733 C CB  . SER   B 81  ? 0.3199 0.3044 0.3567 0.0019  0.0359  0.0403  87  SER   C CB  
1734 O OG  . SER   B 81  ? 0.3248 0.3080 0.3673 0.0013  0.0345  0.0408  87  SER   C OG  
1735 N N   . GLU   B 82  ? 0.3576 0.3367 0.3826 0.0037  0.0369  0.0552  88  GLU   C N   
1736 C CA  . GLU   B 82  ? 0.3834 0.3603 0.4065 0.0044  0.0355  0.0623  88  GLU   C CA  
1737 C C   . GLU   B 82  ? 0.3816 0.3587 0.4151 0.0041  0.0338  0.0626  88  GLU   C C   
1738 O O   . GLU   B 82  ? 0.3948 0.3705 0.4319 0.0048  0.0341  0.0687  88  GLU   C O   
1739 C CB  . GLU   B 82  ? 0.4484 0.4240 0.4563 0.0055  0.0305  0.0649  88  GLU   C CB  
1740 C CG  . GLU   B 82  ? 0.5294 0.5062 0.5333 0.0052  0.0241  0.0608  88  GLU   C CG  
1741 C CD  . GLU   B 82  ? 0.6120 0.5871 0.6022 0.0058  0.0187  0.0640  88  GLU   C CD  
1742 O OE1 . GLU   B 82  ? 0.6454 0.6179 0.6246 0.0065  0.0204  0.0660  88  GLU   C OE1 
1743 O OE2 . GLU   B 82  ? 0.6125 0.5884 0.6028 0.0054  0.0129  0.0644  88  GLU   C OE2 
1744 N N   . TYR   B 83  ? 0.3461 0.3248 0.3848 0.0033  0.0326  0.0562  89  TYR   C N   
1745 C CA  . TYR   B 83  ? 0.3286 0.3070 0.3754 0.0032  0.0314  0.0560  89  TYR   C CA  
1746 C C   . TYR   B 83  ? 0.3201 0.2975 0.3783 0.0020  0.0355  0.0514  89  TYR   C C   
1747 O O   . TYR   B 83  ? 0.3343 0.3103 0.3993 0.0022  0.0358  0.0516  89  TYR   C O   
1748 C CB  . TYR   B 83  ? 0.3108 0.2906 0.3520 0.0035  0.0258  0.0534  89  TYR   C CB  
1749 C CG  . TYR   B 83  ? 0.3089 0.2901 0.3433 0.0031  0.0241  0.0471  89  TYR   C CG  
1750 C CD1 . TYR   B 83  ? 0.3169 0.2982 0.3400 0.0035  0.0220  0.0475  89  TYR   C CD1 
1751 C CD2 . TYR   B 83  ? 0.2990 0.2808 0.3377 0.0024  0.0248  0.0408  89  TYR   C CD2 
1752 C CE1 . TYR   B 83  ? 0.3016 0.2838 0.3194 0.0035  0.0209  0.0420  89  TYR   C CE1 
1753 C CE2 . TYR   B 83  ? 0.3136 0.2968 0.3467 0.0023  0.0231  0.0356  89  TYR   C CE2 
1754 C CZ  . TYR   B 83  ? 0.3062 0.2897 0.3297 0.0030  0.0214  0.0364  89  TYR   C CZ  
1755 O OH  . TYR   B 83  ? 0.3052 0.2899 0.3243 0.0033  0.0201  0.0315  89  TYR   C OH  
1756 N N   . TYR   B 84  ? 0.2937 0.2719 0.3544 0.0007  0.0383  0.0472  90  TYR   C N   
1757 C CA  . TYR   B 84  ? 0.2811 0.2580 0.3524 -0.0009 0.0415  0.0426  90  TYR   C CA  
1758 C C   . TYR   B 84  ? 0.2823 0.2597 0.3589 -0.0023 0.0460  0.0429  90  TYR   C C   
1759 O O   . TYR   B 84  ? 0.2719 0.2515 0.3427 -0.0020 0.0462  0.0437  90  TYR   C O   
1760 C CB  . TYR   B 84  ? 0.2660 0.2446 0.3357 -0.0017 0.0385  0.0346  90  TYR   C CB  
1761 C CG  . TYR   B 84  ? 0.2453 0.2229 0.3123 -0.0008 0.0355  0.0332  90  TYR   C CG  
1762 C CD1 . TYR   B 84  ? 0.2441 0.2183 0.3178 -0.0006 0.0376  0.0341  90  TYR   C CD1 
1763 C CD2 . TYR   B 84  ? 0.2354 0.2149 0.2938 -0.0001 0.0311  0.0306  90  TYR   C CD2 
1764 C CE1 . TYR   B 84  ? 0.2393 0.2126 0.3113 0.0003  0.0359  0.0327  90  TYR   C CE1 
1765 C CE2 . TYR   B 84  ? 0.2345 0.2131 0.2911 0.0007  0.0290  0.0297  90  TYR   C CE2 
1766 C CZ  . TYR   B 84  ? 0.2458 0.2215 0.3093 0.0009  0.0316  0.0308  90  TYR   C CZ  
1767 O OH  . TYR   B 84  ? 0.2438 0.2187 0.3058 0.0018  0.0303  0.0302  90  TYR   C OH  
1768 N N   . PRO   B 85  ? 0.2949 0.2700 0.3828 -0.0041 0.0498  0.0414  91  PRO   C N   
1769 C CA  . PRO   B 85  ? 0.2936 0.2697 0.3887 -0.0060 0.0540  0.0407  91  PRO   C CA  
1770 C C   . PRO   B 85  ? 0.2834 0.2636 0.3790 -0.0074 0.0514  0.0331  91  PRO   C C   
1771 O O   . PRO   B 85  ? 0.2810 0.2624 0.3708 -0.0068 0.0467  0.0285  91  PRO   C O   
1772 C CB  . PRO   B 85  ? 0.3104 0.2820 0.4177 -0.0076 0.0579  0.0408  91  PRO   C CB  
1773 C CG  . PRO   B 85  ? 0.3157 0.2853 0.4220 -0.0075 0.0546  0.0358  91  PRO   C CG  
1774 C CD  . PRO   B 85  ? 0.2977 0.2690 0.3929 -0.0047 0.0506  0.0392  91  PRO   C CD  
1775 N N   . ALA   B 86  ? 0.2733 0.2557 0.3766 -0.0092 0.0546  0.0320  92  ALA   C N   
1776 C CA  . ALA   B 86  ? 0.2816 0.2685 0.3884 -0.0107 0.0520  0.0250  92  ALA   C CA  
1777 C C   . ALA   B 86  ? 0.2836 0.2681 0.3959 -0.0128 0.0494  0.0186  92  ALA   C C   
1778 O O   . ALA   B 86  ? 0.2990 0.2791 0.4190 -0.0144 0.0524  0.0191  92  ALA   C O   
1779 C CB  . ALA   B 86  ? 0.2848 0.2749 0.4019 -0.0125 0.0564  0.0258  92  ALA   C CB  
1780 N N   . ARG   B 87  ? 0.2686 0.2551 0.3750 -0.0124 0.0440  0.0130  93  ARG   C N   
1781 C CA  . ARG   B 87  ? 0.2782 0.2617 0.3862 -0.0140 0.0414  0.0068  93  ARG   C CA  
1782 C C   . ARG   B 87  ? 0.2737 0.2605 0.3755 -0.0136 0.0354  0.0010  93  ARG   C C   
1783 O O   . ARG   B 87  ? 0.2555 0.2466 0.3513 -0.0117 0.0334  0.0022  93  ARG   C O   
1784 C CB  . ARG   B 87  ? 0.2826 0.2604 0.3854 -0.0123 0.0422  0.0092  93  ARG   C CB  
1785 C CG  . ARG   B 87  ? 0.2810 0.2603 0.3714 -0.0093 0.0388  0.0112  93  ARG   C CG  
1786 C CD  . ARG   B 87  ? 0.2774 0.2523 0.3645 -0.0076 0.0395  0.0139  93  ARG   C CD  
1787 N NE  . ARG   B 87  ? 0.2967 0.2733 0.3733 -0.0056 0.0355  0.0139  93  ARG   C NE  
1788 C CZ  . ARG   B 87  ? 0.3261 0.3001 0.3989 -0.0044 0.0345  0.0132  93  ARG   C CZ  
1789 N NH1 . ARG   B 87  ? 0.2884 0.2575 0.3663 -0.0048 0.0376  0.0123  93  ARG   C NH1 
1790 N NH2 . ARG   B 87  ? 0.3351 0.3109 0.3992 -0.0029 0.0310  0.0132  93  ARG   C NH2 
1791 N N   . TYR   B 88  ? 0.2922 0.2761 0.3939 -0.0151 0.0327  -0.0052 94  TYR   C N   
1792 C CA  . TYR   B 88  ? 0.3060 0.2920 0.3998 -0.0144 0.0269  -0.0102 94  TYR   C CA  
1793 C C   . TYR   B 88  ? 0.2835 0.2661 0.3656 -0.0117 0.0260  -0.0087 94  TYR   C C   
1794 O O   . TYR   B 88  ? 0.3041 0.2813 0.3859 -0.0115 0.0288  -0.0076 94  TYR   C O   
1795 C CB  . TYR   B 88  ? 0.3451 0.3290 0.4422 -0.0174 0.0238  -0.0179 94  TYR   C CB  
1796 C CG  . TYR   B 88  ? 0.4070 0.3960 0.5163 -0.0203 0.0228  -0.0201 94  TYR   C CG  
1797 C CD1 . TYR   B 88  ? 0.4412 0.4371 0.5508 -0.0200 0.0180  -0.0222 94  TYR   C CD1 
1798 C CD2 . TYR   B 88  ? 0.4428 0.4299 0.5646 -0.0232 0.0273  -0.0192 94  TYR   C CD2 
1799 C CE1 . TYR   B 88  ? 0.4609 0.4624 0.5839 -0.0227 0.0173  -0.0238 94  TYR   C CE1 
1800 C CE2 . TYR   B 88  ? 0.4638 0.4560 0.5986 -0.0262 0.0269  -0.0208 94  TYR   C CE2 
1801 C CZ  . TYR   B 88  ? 0.4851 0.4848 0.6209 -0.0259 0.0219  -0.0230 94  TYR   C CZ  
1802 O OH  . TYR   B 88  ? 0.5226 0.5277 0.6738 -0.0290 0.0221  -0.0240 94  TYR   C OH  
1803 N N   . GLN   B 89  ? 0.2610 0.2468 0.3347 -0.0095 0.0225  -0.0084 95  GLN   C N   
1804 C CA  . GLN   B 89  ? 0.2527 0.2356 0.3158 -0.0072 0.0213  -0.0073 95  GLN   C CA  
1805 C C   . GLN   B 89  ? 0.2427 0.2260 0.2993 -0.0070 0.0164  -0.0129 95  GLN   C C   
1806 O O   . GLN   B 89  ? 0.2457 0.2336 0.3034 -0.0073 0.0130  -0.0151 95  GLN   C O   
1807 C CB  . GLN   B 89  ? 0.2667 0.2522 0.3247 -0.0049 0.0213  -0.0018 95  GLN   C CB  
1808 C CG  . GLN   B 89  ? 0.2593 0.2424 0.3083 -0.0029 0.0200  -0.0001 95  GLN   C CG  
1809 C CD  . GLN   B 89  ? 0.2720 0.2560 0.3176 -0.0013 0.0205  0.0058  95  GLN   C CD  
1810 O OE1 . GLN   B 89  ? 0.2594 0.2436 0.3092 -0.0016 0.0233  0.0101  95  GLN   C OE1 
1811 N NE2 . GLN   B 89  ? 0.2505 0.2346 0.2881 0.0002  0.0176  0.0062  95  GLN   C NE2 
1812 N N   . SER   B 90  ? 0.2350 0.2133 0.2847 -0.0064 0.0163  -0.0148 96  SER   C N   
1813 C CA  . SER   B 90  ? 0.2387 0.2162 0.2803 -0.0061 0.0119  -0.0197 96  SER   C CA  
1814 C C   . SER   B 90  ? 0.2321 0.2103 0.2638 -0.0032 0.0100  -0.0171 96  SER   C C   
1815 O O   . SER   B 90  ? 0.2347 0.2130 0.2657 -0.0018 0.0122  -0.0121 96  SER   C O   
1816 C CB  . SER   B 90  ? 0.2707 0.2412 0.3094 -0.0072 0.0133  -0.0242 96  SER   C CB  
1817 O OG  . SER   B 90  ? 0.2823 0.2487 0.3178 -0.0054 0.0175  -0.0208 96  SER   C OG  
1818 N N   . HIS   B 91  ? 0.2253 0.2040 0.2496 -0.0025 0.0055  -0.0206 97  HIS   C N   
1819 C CA  . HIS   B 91  ? 0.2248 0.2034 0.2397 0.0001  0.0035  -0.0187 97  HIS   C CA  
1820 C C   . HIS   B 91  ? 0.2269 0.2098 0.2437 0.0014  0.0034  -0.0141 97  HIS   C C   
1821 O O   . HIS   B 91  ? 0.2270 0.2085 0.2384 0.0030  0.0039  -0.0108 97  HIS   C O   
1822 C CB  . HIS   B 91  ? 0.2473 0.2200 0.2555 0.0011  0.0066  -0.0175 97  HIS   C CB  
1823 C CG  . HIS   B 91  ? 0.2949 0.2621 0.2985 0.0002  0.0071  -0.0225 97  HIS   C CG  
1824 N ND1 . HIS   B 91  ? 0.3285 0.2930 0.3209 0.0013  0.0043  -0.0254 97  HIS   C ND1 
1825 C CD2 . HIS   B 91  ? 0.3141 0.2775 0.3223 -0.0016 0.0104  -0.0251 97  HIS   C CD2 
1826 C CE1 . HIS   B 91  ? 0.3367 0.2955 0.3260 0.0001  0.0059  -0.0299 97  HIS   C CE1 
1827 N NE2 . HIS   B 91  ? 0.3324 0.2902 0.3314 -0.0017 0.0097  -0.0301 97  HIS   C NE2 
1828 N N   . LEU   B 92  ? 0.2138 0.2014 0.2382 0.0006  0.0031  -0.0139 98  LEU   C N   
1829 C CA  . LEU   B 92  ? 0.2126 0.2035 0.2384 0.0019  0.0037  -0.0100 98  LEU   C CA  
1830 C C   . LEU   B 92  ? 0.2058 0.2007 0.2303 0.0034  -0.0001 -0.0115 98  LEU   C C   
1831 O O   . LEU   B 92  ? 0.2156 0.2132 0.2439 0.0027  -0.0029 -0.0151 98  LEU   C O   
1832 C CB  . LEU   B 92  ? 0.2286 0.2216 0.2642 0.0003  0.0074  -0.0082 98  LEU   C CB  
1833 C CG  . LEU   B 92  ? 0.2372 0.2321 0.2726 0.0015  0.0093  -0.0038 98  LEU   C CG  
1834 C CD1 . LEU   B 92  ? 0.2458 0.2372 0.2745 0.0025  0.0103  0.0002  98  LEU   C CD1 
1835 C CD2 . LEU   B 92  ? 0.2443 0.2413 0.2892 0.0000  0.0132  -0.0021 98  LEU   C CD2 
1836 N N   . MET   B 93  ? 0.1999 0.1949 0.2192 0.0055  -0.0004 -0.0088 99  MET   C N   
1837 C CA  . MET   B 93  ? 0.1883 0.1865 0.2066 0.0076  -0.0033 -0.0095 99  MET   C CA  
1838 C C   . MET   B 93  ? 0.1883 0.1886 0.2095 0.0084  -0.0005 -0.0067 99  MET   C C   
1839 O O   . MET   B 93  ? 0.2143 0.2116 0.2317 0.0083  0.0019  -0.0037 99  MET   C O   
1840 C CB  . MET   B 93  ? 0.2207 0.2153 0.2286 0.0097  -0.0057 -0.0088 99  MET   C CB  
1841 C CG  . MET   B 93  ? 0.2306 0.2221 0.2338 0.0091  -0.0075 -0.0110 99  MET   C CG  
1842 S SD  . MET   B 93  ? 0.2595 0.2461 0.2510 0.0112  -0.0088 -0.0093 99  MET   C SD  
1843 C CE  . MET   B 93  ? 0.2524 0.2362 0.2432 0.0106  -0.0053 -0.0055 99  MET   C CE  
1844 N N   . LEU   B 94  ? 0.1788 0.1837 0.2060 0.0094  -0.0008 -0.0075 100 LEU   C N   
1845 C CA  . LEU   B 94  ? 0.1984 0.2045 0.2273 0.0105  0.0029  -0.0050 100 LEU   C CA  
1846 C C   . LEU   B 94  ? 0.1962 0.2025 0.2209 0.0136  0.0016  -0.0050 100 LEU   C C   
1847 O O   . LEU   B 94  ? 0.2077 0.2160 0.2332 0.0150  -0.0021 -0.0068 100 LEU   C O   
1848 C CB  . LEU   B 94  ? 0.2112 0.2230 0.2528 0.0093  0.0054  -0.0057 100 LEU   C CB  
1849 C CG  . LEU   B 94  ? 0.2440 0.2558 0.2923 0.0061  0.0076  -0.0057 100 LEU   C CG  
1850 C CD1 . LEU   B 94  ? 0.2832 0.3008 0.3450 0.0050  0.0102  -0.0060 100 LEU   C CD1 
1851 C CD2 . LEU   B 94  ? 0.2694 0.2762 0.3117 0.0055  0.0111  -0.0020 100 LEU   C CD2 
1852 N N   . ALA   B 95  ? 0.2056 0.2096 0.2258 0.0148  0.0048  -0.0027 101 ALA   C N   
1853 C CA  . ALA   B 95  ? 0.2075 0.2109 0.2245 0.0180  0.0051  -0.0027 101 ALA   C CA  
1854 C C   . ALA   B 95  ? 0.2133 0.2174 0.2322 0.0187  0.0105  -0.0011 101 ALA   C C   
1855 O O   . ALA   B 95  ? 0.2135 0.2169 0.2329 0.0168  0.0136  0.0007  101 ALA   C O   
1856 C CB  . ALA   B 95  ? 0.2233 0.2202 0.2283 0.0189  0.0032  -0.0019 101 ALA   C CB  
1857 N N   . VAL   B 96  ? 0.2123 0.2171 0.2319 0.0218  0.0122  -0.0015 102 VAL   C N   
1858 C CA  . VAL   B 96  ? 0.2356 0.2394 0.2541 0.0229  0.0183  0.0000  102 VAL   C CA  
1859 C C   . VAL   B 96  ? 0.2458 0.2414 0.2495 0.0232  0.0185  0.0010  102 VAL   C C   
1860 O O   . VAL   B 96  ? 0.2657 0.2573 0.2625 0.0249  0.0159  -0.0002 102 VAL   C O   
1861 C CB  . VAL   B 96  ? 0.2410 0.2487 0.2669 0.0263  0.0206  -0.0009 102 VAL   C CB  
1862 C CG1 . VAL   B 96  ? 0.2583 0.2635 0.2810 0.0279  0.0279  0.0006  102 VAL   C CG1 
1863 C CG2 . VAL   B 96  ? 0.2344 0.2510 0.2764 0.0256  0.0191  -0.0018 102 VAL   C CG2 
1864 N N   . GLY   B 97  ? 0.2690 0.2620 0.2678 0.0214  0.0212  0.0031  103 GLY   C N   
1865 C CA  . GLY   B 97  ? 0.2765 0.2620 0.2613 0.0212  0.0205  0.0040  103 GLY   C CA  
1866 C C   . GLY   B 97  ? 0.2906 0.2742 0.2712 0.0190  0.0223  0.0070  103 GLY   C C   
1867 O O   . GLY   B 97  ? 0.3142 0.3018 0.3030 0.0175  0.0245  0.0086  103 GLY   C O   
1868 N N   . HIS   B 98  ? 0.2931 0.2702 0.2610 0.0188  0.0212  0.0078  104 HIS   C N   
1869 C CA  . HIS   B 98  ? 0.2959 0.2705 0.2577 0.0171  0.0222  0.0111  104 HIS   C CA  
1870 C C   . HIS   B 98  ? 0.3019 0.2771 0.2656 0.0144  0.0177  0.0130  104 HIS   C C   
1871 O O   . HIS   B 98  ? 0.3000 0.2738 0.2620 0.0138  0.0130  0.0118  104 HIS   C O   
1872 C CB  . HIS   B 98  ? 0.3112 0.2782 0.2574 0.0178  0.0220  0.0109  104 HIS   C CB  
1873 C CG  . HIS   B 98  ? 0.3613 0.3257 0.3001 0.0166  0.0234  0.0145  104 HIS   C CG  
1874 N ND1 . HIS   B 98  ? 0.3906 0.3572 0.3329 0.0171  0.0296  0.0170  104 HIS   C ND1 
1875 C CD2 . HIS   B 98  ? 0.3971 0.3574 0.3267 0.0147  0.0190  0.0166  104 HIS   C CD2 
1876 C CE1 . HIS   B 98  ? 0.4213 0.3847 0.3551 0.0159  0.0289  0.0207  104 HIS   C CE1 
1877 N NE2 . HIS   B 98  ? 0.4280 0.3876 0.3538 0.0144  0.0222  0.0204  104 HIS   C NE2 
1878 N N   . SER   B 99  ? 0.2974 0.2742 0.2643 0.0129  0.0196  0.0165  105 SER   C N   
1879 C CA  . SER   B 99  ? 0.2994 0.2767 0.2692 0.0107  0.0161  0.0190  105 SER   C CA  
1880 C C   . SER   B 99  ? 0.3118 0.2886 0.2808 0.0098  0.0187  0.0237  105 SER   C C   
1881 O O   . SER   B 99  ? 0.3342 0.3139 0.3108 0.0098  0.0233  0.0248  105 SER   C O   
1882 C CB  . SER   B 99  ? 0.3026 0.2848 0.2850 0.0100  0.0159  0.0173  105 SER   C CB  
1883 O OG  . SER   B 99  ? 0.3518 0.3341 0.3377 0.0082  0.0136  0.0194  105 SER   C OG  
1884 N N   . GLU   B 100 ? 0.2950 0.2682 0.2551 0.0090  0.0155  0.0267  106 GLU   C N   
1885 C CA  . GLU   B 100 ? 0.2810 0.2533 0.2392 0.0083  0.0166  0.0320  106 GLU   C CA  
1886 C C   . GLU   B 100 ? 0.2759 0.2506 0.2432 0.0067  0.0134  0.0342  106 GLU   C C   
1887 O O   . GLU   B 100 ? 0.2769 0.2524 0.2474 0.0062  0.0098  0.0318  106 GLU   C O   
1888 C CB  . GLU   B 100 ? 0.3214 0.2883 0.2640 0.0083  0.0133  0.0339  106 GLU   C CB  
1889 C CG  . GLU   B 100 ? 0.4117 0.3741 0.3420 0.0099  0.0157  0.0313  106 GLU   C CG  
1890 C CD  . GLU   B 100 ? 0.4918 0.4529 0.4178 0.0112  0.0223  0.0339  106 GLU   C CD  
1891 O OE1 . GLU   B 100 ? 0.5327 0.4895 0.4477 0.0128  0.0253  0.0319  106 GLU   C OE1 
1892 O OE2 . GLU   B 100 ? 0.4870 0.4509 0.4207 0.0107  0.0251  0.0379  106 GLU   C OE2 
1893 N N   . PRO   B 101 ? 0.2757 0.2509 0.2468 0.0062  0.0148  0.0391  107 PRO   C N   
1894 C CA  . PRO   B 101 ? 0.2713 0.2484 0.2516 0.0052  0.0124  0.0414  107 PRO   C CA  
1895 C C   . PRO   B 101 ? 0.2840 0.2603 0.2609 0.0044  0.0060  0.0414  107 PRO   C C   
1896 O O   . PRO   B 101 ? 0.2943 0.2725 0.2794 0.0039  0.0047  0.0403  107 PRO   C O   
1897 C CB  . PRO   B 101 ? 0.3058 0.2821 0.2871 0.0052  0.0145  0.0478  107 PRO   C CB  
1898 C CG  . PRO   B 101 ? 0.3315 0.3066 0.3081 0.0061  0.0199  0.0480  107 PRO   C CG  
1899 C CD  . PRO   B 101 ? 0.2963 0.2702 0.2642 0.0069  0.0196  0.0431  107 PRO   C CD  
1900 N N   . GLY   B 102 ? 0.2694 0.2427 0.2345 0.0042  0.0021  0.0426  108 GLY   C N   
1901 C CA  . GLY   B 102 ? 0.2641 0.2368 0.2271 0.0030  -0.0044 0.0427  108 GLY   C CA  
1902 C C   . GLY   B 102 ? 0.2559 0.2285 0.2198 0.0028  -0.0057 0.0374  108 GLY   C C   
1903 O O   . GLY   B 102 ? 0.2758 0.2480 0.2399 0.0016  -0.0104 0.0374  108 GLY   C O   
1904 N N   . ASP   B 103 ? 0.2553 0.2280 0.2192 0.0040  -0.0017 0.0331  109 ASP   C N   
1905 C CA  . ASP   B 103 ? 0.2496 0.2220 0.2142 0.0043  -0.0027 0.0285  109 ASP   C CA  
1906 C C   . ASP   B 103 ? 0.2310 0.2066 0.2068 0.0040  -0.0021 0.0279  109 ASP   C C   
1907 O O   . ASP   B 103 ? 0.2322 0.2074 0.2085 0.0040  -0.0036 0.0251  109 ASP   C O   
1908 C CB  . ASP   B 103 ? 0.2591 0.2308 0.2206 0.0060  0.0008  0.0244  109 ASP   C CB  
1909 C CG  . ASP   B 103 ? 0.2888 0.2561 0.2377 0.0066  0.0006  0.0239  109 ASP   C CG  
1910 O OD1 . ASP   B 103 ? 0.3080 0.2718 0.2496 0.0056  -0.0039 0.0242  109 ASP   C OD1 
1911 O OD2 . ASP   B 103 ? 0.3073 0.2743 0.2539 0.0081  0.0051  0.0231  109 ASP   C OD2 
1912 N N   . CYS   B 104 ? 0.2216 0.1996 0.2058 0.0037  0.0003  0.0306  110 CYS   C N   
1913 C CA  . CYS   B 104 ? 0.2237 0.2037 0.2176 0.0035  0.0015  0.0297  110 CYS   C CA  
1914 C C   . CYS   B 104 ? 0.2319 0.2114 0.2265 0.0028  -0.0021 0.0304  110 CYS   C C   
1915 O O   . CYS   B 104 ? 0.2470 0.2259 0.2395 0.0019  -0.0055 0.0339  110 CYS   C O   
1916 C CB  . CYS   B 104 ? 0.2358 0.2173 0.2381 0.0033  0.0045  0.0330  110 CYS   C CB  
1917 S SG  . CYS   B 104 ? 0.2543 0.2368 0.2601 0.0037  0.0098  0.0311  110 CYS   C SG  
1918 N N   . GLY   B 105 ? 0.2039 0.1834 0.2008 0.0031  -0.0015 0.0274  111 GLY   C N   
1919 C CA  . GLY   B 105 ? 0.2165 0.1953 0.2147 0.0024  -0.0039 0.0283  111 GLY   C CA  
1920 C C   . GLY   B 105 ? 0.2262 0.2026 0.2172 0.0025  -0.0064 0.0255  111 GLY   C C   
1921 O O   . GLY   B 105 ? 0.2380 0.2135 0.2303 0.0020  -0.0076 0.0256  111 GLY   C O   
1922 N N   . GLY   B 106 ? 0.2331 0.2080 0.2167 0.0031  -0.0069 0.0233  112 GLY   C N   
1923 C CA  . GLY   B 106 ? 0.2280 0.1998 0.2048 0.0036  -0.0087 0.0204  112 GLY   C CA  
1924 C C   . GLY   B 106 ? 0.2177 0.1898 0.1967 0.0048  -0.0073 0.0178  112 GLY   C C   
1925 O O   . GLY   B 106 ? 0.2176 0.1919 0.2002 0.0057  -0.0046 0.0163  112 GLY   C O   
1926 N N   . ILE   B 107 ? 0.2103 0.1796 0.1867 0.0047  -0.0091 0.0172  113 ILE   C N   
1927 C CA  . ILE   B 107 ? 0.2145 0.1835 0.1915 0.0060  -0.0078 0.0152  113 ILE   C CA  
1928 C C   . ILE   B 107 ? 0.2126 0.1809 0.1852 0.0081  -0.0077 0.0119  113 ILE   C C   
1929 O O   . ILE   B 107 ? 0.2214 0.1872 0.1889 0.0086  -0.0089 0.0110  113 ILE   C O   
1930 C CB  . ILE   B 107 ? 0.2541 0.2203 0.2311 0.0050  -0.0092 0.0169  113 ILE   C CB  
1931 C CG1 . ILE   B 107 ? 0.3065 0.2749 0.2914 0.0038  -0.0075 0.0200  113 ILE   C CG1 
1932 C CG2 . ILE   B 107 ? 0.2566 0.2204 0.2301 0.0068  -0.0086 0.0149  113 ILE   C CG2 
1933 C CD1 . ILE   B 107 ? 0.3618 0.3287 0.3498 0.0024  -0.0084 0.0228  113 ILE   C CD1 
1934 N N   . LEU   B 108 ? 0.1990 0.1692 0.1736 0.0094  -0.0063 0.0100  114 LEU   C N   
1935 C CA  . LEU   B 108 ? 0.1883 0.1583 0.1602 0.0116  -0.0068 0.0074  114 LEU   C CA  
1936 C C   . LEU   B 108 ? 0.2111 0.1783 0.1802 0.0123  -0.0076 0.0076  114 LEU   C C   
1937 O O   . LEU   B 108 ? 0.2006 0.1680 0.1714 0.0117  -0.0065 0.0082  114 LEU   C O   
1938 C CB  . LEU   B 108 ? 0.2017 0.1760 0.1780 0.0122  -0.0056 0.0053  114 LEU   C CB  
1939 C CG  . LEU   B 108 ? 0.2158 0.1913 0.1913 0.0144  -0.0069 0.0028  114 LEU   C CG  
1940 C CD1 . LEU   B 108 ? 0.2179 0.1931 0.1916 0.0163  -0.0072 0.0021  114 LEU   C CD1 
1941 C CD2 . LEU   B 108 ? 0.2237 0.2036 0.2047 0.0142  -0.0064 0.0006  114 LEU   C CD2 
1942 N N   . ARG   B 109 ? 0.2151 0.1792 0.1797 0.0138  -0.0091 0.0072  115 ARG   C N   
1943 C CA  . ARG   B 109 ? 0.2426 0.2032 0.2038 0.0147  -0.0095 0.0081  115 ARG   C CA  
1944 C C   . ARG   B 109 ? 0.2485 0.2083 0.2064 0.0177  -0.0109 0.0066  115 ARG   C C   
1945 O O   . ARG   B 109 ? 0.2348 0.1950 0.1926 0.0191  -0.0116 0.0053  115 ARG   C O   
1946 C CB  . ARG   B 109 ? 0.2837 0.2400 0.2437 0.0130  -0.0100 0.0104  115 ARG   C CB  
1947 C CG  . ARG   B 109 ? 0.3589 0.3119 0.3157 0.0134  -0.0116 0.0096  115 ARG   C CG  
1948 C CD  . ARG   B 109 ? 0.4599 0.4085 0.4162 0.0110  -0.0127 0.0116  115 ARG   C CD  
1949 N NE  . ARG   B 109 ? 0.5420 0.4926 0.5018 0.0081  -0.0133 0.0131  115 ARG   C NE  
1950 C CZ  . ARG   B 109 ? 0.6215 0.5729 0.5862 0.0060  -0.0130 0.0159  115 ARG   C CZ  
1951 N NH1 . ARG   B 109 ? 0.6127 0.5625 0.5784 0.0065  -0.0113 0.0173  115 ARG   C NH1 
1952 N NH2 . ARG   B 109 ? 0.6304 0.5842 0.5993 0.0036  -0.0141 0.0176  115 ARG   C NH2 
1953 N N   . CYS   B 110 ? 0.2401 0.1983 0.1951 0.0189  -0.0112 0.0072  116 CYS   C N   
1954 C CA  . CYS   B 110 ? 0.2415 0.1985 0.1929 0.0220  -0.0130 0.0067  116 CYS   C CA  
1955 C C   . CYS   B 110 ? 0.2675 0.2183 0.2138 0.0225  -0.0127 0.0093  116 CYS   C C   
1956 O O   . CYS   B 110 ? 0.2732 0.2215 0.2203 0.0203  -0.0111 0.0112  116 CYS   C O   
1957 C CB  . CYS   B 110 ? 0.2420 0.2029 0.1935 0.0232  -0.0142 0.0048  116 CYS   C CB  
1958 S SG  . CYS   B 110 ? 0.2442 0.2029 0.1913 0.0221  -0.0127 0.0056  116 CYS   C SG  
1959 N N   . GLN   B 111 ? 0.2724 0.2212 0.2146 0.0255  -0.0142 0.0099  117 GLN   C N   
1960 C CA  . GLN   B 111 ? 0.3028 0.2452 0.2402 0.0262  -0.0134 0.0130  117 GLN   C CA  
1961 C C   . GLN   B 111 ? 0.3043 0.2452 0.2393 0.0247  -0.0109 0.0148  117 GLN   C C   
1962 O O   . GLN   B 111 ? 0.3299 0.2658 0.2630 0.0241  -0.0089 0.0178  117 GLN   C O   
1963 C CB  . GLN   B 111 ? 0.3327 0.2731 0.2657 0.0302  -0.0157 0.0138  117 GLN   C CB  
1964 C CG  . GLN   B 111 ? 0.3766 0.3204 0.3062 0.0319  -0.0175 0.0130  117 GLN   C CG  
1965 C CD  . GLN   B 111 ? 0.4969 0.4392 0.4224 0.0360  -0.0206 0.0144  117 GLN   C CD  
1966 O OE1 . GLN   B 111 ? 0.5480 0.4945 0.4774 0.0381  -0.0234 0.0128  117 GLN   C OE1 
1967 N NE2 . GLN   B 111 ? 0.4963 0.4329 0.4144 0.0374  -0.0199 0.0178  117 GLN   C NE2 
1968 N N   . HIS   B 112 ? 0.2860 0.2310 0.2215 0.0239  -0.0104 0.0129  118 HIS   C N   
1969 C CA  . HIS   B 112 ? 0.2740 0.2172 0.2069 0.0229  -0.0072 0.0142  118 HIS   C CA  
1970 C C   . HIS   B 112 ? 0.2988 0.2432 0.2383 0.0197  -0.0042 0.0150  118 HIS   C C   
1971 O O   . HIS   B 112 ? 0.3114 0.2538 0.2501 0.0190  -0.0006 0.0167  118 HIS   C O   
1972 C CB  . HIS   B 112 ? 0.2764 0.2220 0.2052 0.0240  -0.0083 0.0114  118 HIS   C CB  
1973 C CG  . HIS   B 112 ? 0.2923 0.2377 0.2153 0.0272  -0.0124 0.0109  118 HIS   C CG  
1974 N ND1 . HIS   B 112 ? 0.2698 0.2205 0.1964 0.0281  -0.0163 0.0080  118 HIS   C ND1 
1975 C CD2 . HIS   B 112 ? 0.3093 0.2500 0.2238 0.0296  -0.0129 0.0133  118 HIS   C CD2 
1976 C CE1 . HIS   B 112 ? 0.3113 0.2608 0.2321 0.0312  -0.0196 0.0088  118 HIS   C CE1 
1977 N NE2 . HIS   B 112 ? 0.3297 0.2730 0.2424 0.0322  -0.0178 0.0120  118 HIS   C NE2 
1978 N N   . GLY   B 113 ? 0.2779 0.2255 0.2238 0.0181  -0.0054 0.0139  119 GLY   C N   
1979 C CA  . GLY   B 113 ? 0.2596 0.2088 0.2121 0.0153  -0.0034 0.0152  119 GLY   C CA  
1980 C C   . GLY   B 113 ? 0.2411 0.1954 0.1986 0.0142  -0.0043 0.0129  119 GLY   C C   
1981 O O   . GLY   B 113 ? 0.2449 0.2011 0.2017 0.0152  -0.0066 0.0107  119 GLY   C O   
1982 N N   . VAL   B 114 ? 0.2251 0.1814 0.1883 0.0123  -0.0021 0.0139  120 VAL   C N   
1983 C CA  . VAL   B 114 ? 0.2373 0.1977 0.2055 0.0112  -0.0025 0.0127  120 VAL   C CA  
1984 C C   . VAL   B 114 ? 0.2285 0.1910 0.1957 0.0122  -0.0019 0.0095  120 VAL   C C   
1985 O O   . VAL   B 114 ? 0.2422 0.2033 0.2077 0.0126  0.0003  0.0089  120 VAL   C O   
1986 C CB  . VAL   B 114 ? 0.2525 0.2143 0.2278 0.0091  -0.0005 0.0154  120 VAL   C CB  
1987 C CG1 . VAL   B 114 ? 0.2642 0.2299 0.2444 0.0083  -0.0004 0.0146  120 VAL   C CG1 
1988 C CG2 . VAL   B 114 ? 0.2735 0.2338 0.2507 0.0075  -0.0023 0.0184  120 VAL   C CG2 
1989 N N   . VAL   B 115 ? 0.2081 0.1737 0.1765 0.0126  -0.0039 0.0072  121 VAL   C N   
1990 C CA  . VAL   B 115 ? 0.2165 0.1847 0.1856 0.0130  -0.0041 0.0039  121 VAL   C CA  
1991 C C   . VAL   B 115 ? 0.2332 0.2038 0.2091 0.0112  -0.0019 0.0037  121 VAL   C C   
1992 O O   . VAL   B 115 ? 0.2304 0.2013 0.2074 0.0109  -0.0007 0.0015  121 VAL   C O   
1993 C CB  . VAL   B 115 ? 0.2098 0.1805 0.1787 0.0145  -0.0070 0.0021  121 VAL   C CB  
1994 C CG1 . VAL   B 115 ? 0.2145 0.1890 0.1867 0.0144  -0.0078 -0.0012 121 VAL   C CG1 
1995 C CG2 . VAL   B 115 ? 0.2295 0.1974 0.1922 0.0167  -0.0091 0.0026  121 VAL   C CG2 
1996 N N   . GLY   B 116 ? 0.2207 0.1926 0.2006 0.0101  -0.0016 0.0060  122 GLY   C N   
1997 C CA  . GLY   B 116 ? 0.2213 0.1953 0.2077 0.0087  0.0005  0.0067  122 GLY   C CA  
1998 C C   . GLY   B 116 ? 0.2151 0.1901 0.2036 0.0078  0.0000  0.0096  122 GLY   C C   
1999 O O   . GLY   B 116 ? 0.2180 0.1914 0.2028 0.0080  -0.0019 0.0109  122 GLY   C O   
2000 N N   . ILE   B 117 ? 0.1907 0.1677 0.1846 0.0068  0.0016  0.0107  123 ILE   C N   
2001 C CA  . ILE   B 117 ? 0.1883 0.1659 0.1827 0.0060  0.0008  0.0138  123 ILE   C CA  
2002 C C   . ILE   B 117 ? 0.1907 0.1705 0.1873 0.0060  0.0021  0.0132  123 ILE   C C   
2003 O O   . ILE   B 117 ? 0.2083 0.1896 0.2094 0.0058  0.0040  0.0114  123 ILE   C O   
2004 C CB  . ILE   B 117 ? 0.2178 0.1954 0.2174 0.0049  0.0017  0.0178  123 ILE   C CB  
2005 C CG1 . ILE   B 117 ? 0.2279 0.2060 0.2340 0.0048  0.0053  0.0174  123 ILE   C CG1 
2006 C CG2 . ILE   B 117 ? 0.2355 0.2113 0.2340 0.0046  0.0003  0.0195  123 ILE   C CG2 
2007 C CD1 . ILE   B 117 ? 0.2416 0.2202 0.2548 0.0041  0.0066  0.0222  123 ILE   C CD1 
2008 N N   . VAL   B 118 ? 0.1963 0.1760 0.1895 0.0060  0.0011  0.0148  124 VAL   C N   
2009 C CA  . VAL   B 118 ? 0.1876 0.1691 0.1826 0.0060  0.0033  0.0151  124 VAL   C CA  
2010 C C   . VAL   B 118 ? 0.2123 0.1950 0.2145 0.0050  0.0058  0.0174  124 VAL   C C   
2011 O O   . VAL   B 118 ? 0.2155 0.1974 0.2194 0.0043  0.0053  0.0207  124 VAL   C O   
2012 C CB  . VAL   B 118 ? 0.1980 0.1779 0.1862 0.0062  0.0021  0.0169  124 VAL   C CB  
2013 C CG1 . VAL   B 118 ? 0.2202 0.2014 0.2095 0.0064  0.0053  0.0181  124 VAL   C CG1 
2014 C CG2 . VAL   B 118 ? 0.2163 0.1942 0.1977 0.0075  0.0003  0.0142  124 VAL   C CG2 
2015 N N   . SER   B 119 ? 0.1993 0.1840 0.2069 0.0048  0.0085  0.0158  125 SER   C N   
2016 C CA  . SER   B 119 ? 0.2173 0.2023 0.2323 0.0038  0.0114  0.0177  125 SER   C CA  
2017 C C   . SER   B 119 ? 0.2286 0.2151 0.2468 0.0036  0.0144  0.0188  125 SER   C C   
2018 O O   . SER   B 119 ? 0.2370 0.2230 0.2597 0.0029  0.0169  0.0222  125 SER   C O   
2019 C CB  . SER   B 119 ? 0.2213 0.2061 0.2413 0.0034  0.0123  0.0142  125 SER   C CB  
2020 O OG  . SER   B 119 ? 0.2473 0.2315 0.2750 0.0024  0.0156  0.0156  125 SER   C OG  
2021 N N   . THR   B 120 ? 0.2168 0.2051 0.2336 0.0042  0.0148  0.0163  126 THR   C N   
2022 C CA  . THR   B 120 ? 0.2218 0.2119 0.2431 0.0040  0.0186  0.0174  126 THR   C CA  
2023 C C   . THR   B 120 ? 0.2226 0.2129 0.2372 0.0055  0.0190  0.0173  126 THR   C C   
2024 O O   . THR   B 120 ? 0.2279 0.2174 0.2359 0.0067  0.0160  0.0154  126 THR   C O   
2025 C CB  . THR   B 120 ? 0.2373 0.2302 0.2686 0.0029  0.0201  0.0135  126 THR   C CB  
2026 O OG1 . THR   B 120 ? 0.2535 0.2489 0.2841 0.0038  0.0178  0.0094  126 THR   C OG1 
2027 C CG2 . THR   B 120 ? 0.2465 0.2381 0.2831 0.0015  0.0199  0.0122  126 THR   C CG2 
2028 N N   . GLY   B 121 ? 0.2411 0.2321 0.2574 0.0056  0.0232  0.0196  127 GLY   C N   
2029 C CA  . GLY   B 121 ? 0.2683 0.2593 0.2788 0.0073  0.0249  0.0193  127 GLY   C CA  
2030 C C   . GLY   B 121 ? 0.3105 0.3034 0.3272 0.0072  0.0308  0.0213  127 GLY   C C   
2031 O O   . GLY   B 121 ? 0.3177 0.3102 0.3394 0.0058  0.0333  0.0244  127 GLY   C O   
2032 N N   . GLY   B 122 ? 0.3579 0.3522 0.3741 0.0087  0.0335  0.0199  128 GLY   C N   
2033 C CA  . GLY   B 122 ? 0.3837 0.3803 0.4069 0.0087  0.0400  0.0219  128 GLY   C CA  
2034 C C   . GLY   B 122 ? 0.3799 0.3813 0.4113 0.0098  0.0417  0.0186  128 GLY   C C   
2035 O O   . GLY   B 122 ? 0.3718 0.3760 0.4077 0.0099  0.0374  0.0147  128 GLY   C O   
2036 N N   . ASN   B 123 ? 0.3710 0.3732 0.4044 0.0109  0.0484  0.0207  129 ASN   C N   
2037 C CA  . ASN   B 123 ? 0.3793 0.3868 0.4222 0.0124  0.0513  0.0185  129 ASN   C CA  
2038 C C   . ASN   B 123 ? 0.3532 0.3605 0.3904 0.0150  0.0475  0.0149  129 ASN   C C   
2039 O O   . ASN   B 123 ? 0.3729 0.3858 0.4211 0.0157  0.0467  0.0122  129 ASN   C O   
2040 C CB  . ASN   B 123 ? 0.4226 0.4367 0.4842 0.0099  0.0507  0.0168  129 ASN   C CB  
2041 C CG  . ASN   B 123 ? 0.5127 0.5272 0.5822 0.0079  0.0568  0.0206  129 ASN   C CG  
2042 O OD1 . ASN   B 123 ? 0.5265 0.5419 0.5988 0.0090  0.0640  0.0232  129 ASN   C OD1 
2043 N ND2 . ASN   B 123 ? 0.5472 0.5602 0.6202 0.0050  0.0549  0.0213  129 ASN   C ND2 
2044 N N   . GLY   B 124 ? 0.3180 0.3190 0.3393 0.0163  0.0452  0.0150  130 GLY   C N   
2045 C CA  . GLY   B 124 ? 0.2973 0.2971 0.3131 0.0188  0.0419  0.0118  130 GLY   C CA  
2046 C C   . GLY   B 124 ? 0.2770 0.2787 0.2960 0.0178  0.0345  0.0089  130 GLY   C C   
2047 O O   . GLY   B 124 ? 0.2785 0.2804 0.2963 0.0198  0.0317  0.0063  130 GLY   C O   
2048 N N   . LEU   B 125 ? 0.2543 0.2568 0.2770 0.0149  0.0317  0.0094  131 LEU   C N   
2049 C CA  . LEU   B 125 ? 0.2395 0.2430 0.2640 0.0139  0.0254  0.0068  131 LEU   C CA  
2050 C C   . LEU   B 125 ? 0.2437 0.2421 0.2589 0.0125  0.0224  0.0083  131 LEU   C C   
2051 O O   . LEU   B 125 ? 0.2793 0.2749 0.2904 0.0116  0.0247  0.0115  131 LEU   C O   
2052 C CB  . LEU   B 125 ? 0.2611 0.2700 0.2995 0.0116  0.0246  0.0054  131 LEU   C CB  
2053 C CG  . LEU   B 125 ? 0.3081 0.3236 0.3595 0.0122  0.0266  0.0040  131 LEU   C CG  
2054 C CD1 . LEU   B 125 ? 0.3451 0.3646 0.4096 0.0090  0.0265  0.0030  131 LEU   C CD1 
2055 C CD2 . LEU   B 125 ? 0.3357 0.3537 0.3878 0.0146  0.0226  0.0011  131 LEU   C CD2 
2056 N N   . VAL   B 126 ? 0.2067 0.2038 0.2181 0.0128  0.0175  0.0063  132 VAL   C N   
2057 C CA  . VAL   B 126 ? 0.2032 0.1964 0.2085 0.0114  0.0146  0.0076  132 VAL   C CA  
2058 C C   . VAL   B 126 ? 0.1990 0.1942 0.2102 0.0101  0.0116  0.0053  132 VAL   C C   
2059 O O   . VAL   B 126 ? 0.2063 0.2039 0.2203 0.0111  0.0094  0.0024  132 VAL   C O   
2060 C CB  . VAL   B 126 ? 0.2195 0.2080 0.2135 0.0126  0.0118  0.0076  132 VAL   C CB  
2061 C CG1 . VAL   B 126 ? 0.2519 0.2410 0.2456 0.0147  0.0098  0.0046  132 VAL   C CG1 
2062 C CG2 . VAL   B 126 ? 0.2289 0.2144 0.2190 0.0110  0.0086  0.0091  132 VAL   C CG2 
2063 N N   . GLY   B 127 ? 0.1902 0.1841 0.2030 0.0082  0.0117  0.0068  133 GLY   C N   
2064 C CA  . GLY   B 127 ? 0.1893 0.1839 0.2062 0.0071  0.0096  0.0043  133 GLY   C CA  
2065 C C   . GLY   B 127 ? 0.2043 0.1951 0.2153 0.0069  0.0075  0.0053  133 GLY   C C   
2066 O O   . GLY   B 127 ? 0.2074 0.1959 0.2153 0.0065  0.0082  0.0087  133 GLY   C O   
2067 N N   . PHE   B 128 ? 0.1855 0.1758 0.1950 0.0072  0.0050  0.0027  134 PHE   C N   
2068 C CA  . PHE   B 128 ? 0.1916 0.1784 0.1961 0.0072  0.0037  0.0037  134 PHE   C CA  
2069 C C   . PHE   B 128 ? 0.2032 0.1890 0.2108 0.0061  0.0043  0.0018  134 PHE   C C   
2070 O O   . PHE   B 128 ? 0.2165 0.2037 0.2260 0.0060  0.0032  -0.0018 134 PHE   C O   
2071 C CB  . PHE   B 128 ? 0.1913 0.1767 0.1890 0.0089  0.0006  0.0024  134 PHE   C CB  
2072 C CG  . PHE   B 128 ? 0.1959 0.1814 0.1902 0.0103  0.0001  0.0031  134 PHE   C CG  
2073 C CD1 . PHE   B 128 ? 0.1929 0.1755 0.1821 0.0102  0.0000  0.0057  134 PHE   C CD1 
2074 C CD2 . PHE   B 128 ? 0.2113 0.1998 0.2077 0.0118  -0.0002 0.0010  134 PHE   C CD2 
2075 C CE1 . PHE   B 128 ? 0.2064 0.1877 0.1910 0.0115  -0.0002 0.0056  134 PHE   C CE1 
2076 C CE2 . PHE   B 128 ? 0.2185 0.2062 0.2115 0.0135  0.0002  0.0014  134 PHE   C CE2 
2077 C CZ  . PHE   B 128 ? 0.2125 0.1961 0.1988 0.0133  0.0003  0.0035  134 PHE   C CZ  
2078 N N   . ALA   B 129 ? 0.2010 0.1843 0.2088 0.0055  0.0058  0.0041  135 ALA   C N   
2079 C CA  . ALA   B 129 ? 0.1976 0.1787 0.2071 0.0048  0.0072  0.0023  135 ALA   C CA  
2080 C C   . ALA   B 129 ? 0.2115 0.1902 0.2136 0.0060  0.0053  0.0009  135 ALA   C C   
2081 O O   . ALA   B 129 ? 0.2173 0.1946 0.2159 0.0067  0.0049  0.0036  135 ALA   C O   
2082 C CB  . ALA   B 129 ? 0.2165 0.1959 0.2301 0.0042  0.0101  0.0060  135 ALA   C CB  
2083 N N   . ASP   B 130 ? 0.2166 0.1948 0.2164 0.0062  0.0041  -0.0033 136 ASP   C N   
2084 C CA  . ASP   B 130 ? 0.2154 0.1909 0.2069 0.0075  0.0023  -0.0044 136 ASP   C CA  
2085 C C   . ASP   B 130 ? 0.2267 0.1980 0.2165 0.0075  0.0057  -0.0031 136 ASP   C C   
2086 O O   . ASP   B 130 ? 0.2406 0.2105 0.2348 0.0065  0.0088  -0.0037 136 ASP   C O   
2087 C CB  . ASP   B 130 ? 0.2206 0.1965 0.2097 0.0075  -0.0002 -0.0092 136 ASP   C CB  
2088 C CG  . ASP   B 130 ? 0.2916 0.2648 0.2709 0.0092  -0.0027 -0.0103 136 ASP   C CG  
2089 O OD1 . ASP   B 130 ? 0.2921 0.2651 0.2676 0.0108  -0.0039 -0.0078 136 ASP   C OD1 
2090 O OD2 . ASP   B 130 ? 0.3503 0.3209 0.3251 0.0090  -0.0032 -0.0137 136 ASP   C OD2 
2091 N N   . VAL   B 131 ? 0.2043 0.1730 0.1877 0.0087  0.0055  -0.0015 137 VAL   C N   
2092 C CA  . VAL   B 131 ? 0.2240 0.1886 0.2056 0.0090  0.0094  -0.0003 137 VAL   C CA  
2093 C C   . VAL   B 131 ? 0.2467 0.2075 0.2181 0.0105  0.0089  -0.0021 137 VAL   C C   
2094 O O   . VAL   B 131 ? 0.2607 0.2175 0.2292 0.0110  0.0127  -0.0011 137 VAL   C O   
2095 C CB  . VAL   B 131 ? 0.2278 0.1927 0.2137 0.0088  0.0111  0.0050  137 VAL   C CB  
2096 C CG1 . VAL   B 131 ? 0.2264 0.1945 0.2216 0.0076  0.0117  0.0072  137 VAL   C CG1 
2097 C CG2 . VAL   B 131 ? 0.2350 0.2003 0.2169 0.0094  0.0080  0.0070  137 VAL   C CG2 
2098 N N   . ARG   B 132 ? 0.2435 0.2054 0.2095 0.0113  0.0045  -0.0044 138 ARG   C N   
2099 C CA  . ARG   B 132 ? 0.2362 0.1943 0.1913 0.0130  0.0033  -0.0052 138 ARG   C CA  
2100 C C   . ARG   B 132 ? 0.2594 0.2130 0.2077 0.0130  0.0052  -0.0088 138 ARG   C C   
2101 O O   . ARG   B 132 ? 0.2829 0.2320 0.2209 0.0146  0.0057  -0.0087 138 ARG   C O   
2102 C CB  . ARG   B 132 ? 0.2285 0.1894 0.1807 0.0142  -0.0023 -0.0064 138 ARG   C CB  
2103 C CG  . ARG   B 132 ? 0.2187 0.1820 0.1747 0.0146  -0.0036 -0.0030 138 ARG   C CG  
2104 C CD  . ARG   B 132 ? 0.2272 0.1931 0.1813 0.0162  -0.0085 -0.0043 138 ARG   C CD  
2105 N NE  . ARG   B 132 ? 0.2389 0.2099 0.2000 0.0152  -0.0103 -0.0073 138 ARG   C NE  
2106 C CZ  . ARG   B 132 ? 0.2602 0.2351 0.2236 0.0162  -0.0141 -0.0085 138 ARG   C CZ  
2107 N NH1 . ARG   B 132 ? 0.2351 0.2092 0.1935 0.0187  -0.0169 -0.0073 138 ARG   C NH1 
2108 N NH2 . ARG   B 132 ? 0.2607 0.2404 0.2322 0.0149  -0.0149 -0.0108 138 ARG   C NH2 
2109 N N   . ASP   B 133 ? 0.2540 0.2081 0.2071 0.0114  0.0062  -0.0121 139 ASP   C N   
2110 C CA  . ASP   B 133 ? 0.2675 0.2163 0.2139 0.0112  0.0082  -0.0163 139 ASP   C CA  
2111 C C   . ASP   B 133 ? 0.2895 0.2334 0.2364 0.0115  0.0155  -0.0145 139 ASP   C C   
2112 O O   . ASP   B 133 ? 0.2951 0.2330 0.2344 0.0117  0.0184  -0.0179 139 ASP   C O   
2113 C CB  . ASP   B 133 ? 0.2853 0.2360 0.2373 0.0090  0.0059  -0.0212 139 ASP   C CB  
2114 C CG  . ASP   B 133 ? 0.3116 0.2647 0.2765 0.0075  0.0094  -0.0194 139 ASP   C CG  
2115 O OD1 . ASP   B 133 ? 0.3011 0.2581 0.2724 0.0078  0.0098  -0.0148 139 ASP   C OD1 
2116 O OD2 . ASP   B 133 ? 0.3510 0.3011 0.3188 0.0060  0.0122  -0.0226 139 ASP   C OD2 
2117 N N   . LEU   B 134 ? 0.2762 0.2225 0.2321 0.0115  0.0185  -0.0095 140 LEU   C N   
2118 C CA  . LEU   B 134 ? 0.2639 0.2070 0.2240 0.0118  0.0255  -0.0071 140 LEU   C CA  
2119 C C   . LEU   B 134 ? 0.2754 0.2148 0.2280 0.0136  0.0285  -0.0042 140 LEU   C C   
2120 O O   . LEU   B 134 ? 0.2871 0.2287 0.2453 0.0138  0.0296  0.0009  140 LEU   C O   
2121 C CB  . LEU   B 134 ? 0.2562 0.2043 0.2302 0.0108  0.0262  -0.0027 140 LEU   C CB  
2122 C CG  . LEU   B 134 ? 0.2753 0.2270 0.2567 0.0091  0.0238  -0.0047 140 LEU   C CG  
2123 C CD1 . LEU   B 134 ? 0.2763 0.2326 0.2694 0.0085  0.0242  0.0005  140 LEU   C CD1 
2124 C CD2 . LEU   B 134 ? 0.2901 0.2374 0.2722 0.0085  0.0273  -0.0090 140 LEU   C CD2 
2125 N N   . LEU   B 135 ? 0.2833 0.2167 0.2226 0.0148  0.0295  -0.0075 141 LEU   C N   
2126 C CA  . LEU   B 135 ? 0.2982 0.2277 0.2285 0.0167  0.0321  -0.0046 141 LEU   C CA  
2127 C C   . LEU   B 135 ? 0.3019 0.2294 0.2383 0.0174  0.0402  -0.0003 141 LEU   C C   
2128 O O   . LEU   B 135 ? 0.3107 0.2373 0.2457 0.0183  0.0423  0.0042  141 LEU   C O   
2129 C CB  . LEU   B 135 ? 0.3105 0.2336 0.2232 0.0180  0.0312  -0.0088 141 LEU   C CB  
2130 C CG  . LEU   B 135 ? 0.3261 0.2516 0.2341 0.0172  0.0228  -0.0135 141 LEU   C CG  
2131 C CD1 . LEU   B 135 ? 0.3435 0.2623 0.2332 0.0184  0.0212  -0.0177 141 LEU   C CD1 
2132 C CD2 . LEU   B 135 ? 0.3153 0.2472 0.2277 0.0173  0.0165  -0.0105 141 LEU   C CD2 
2133 N N   . TRP   B 136 ? 0.3060 0.2327 0.2503 0.0169  0.0449  -0.0013 142 TRP   C N   
2134 C CA  . TRP   B 136 ? 0.3194 0.2448 0.2719 0.0178  0.0531  0.0029  142 TRP   C CA  
2135 C C   . TRP   B 136 ? 0.3161 0.2482 0.2826 0.0169  0.0518  0.0094  142 TRP   C C   
2136 O O   . TRP   B 136 ? 0.3251 0.2570 0.2987 0.0177  0.0577  0.0139  142 TRP   C O   
2137 C CB  . TRP   B 136 ? 0.3228 0.2456 0.2812 0.0178  0.0581  0.0001  142 TRP   C CB  
2138 C CG  . TRP   B 136 ? 0.2996 0.2275 0.2678 0.0158  0.0533  -0.0012 142 TRP   C CG  
2139 C CD1 . TRP   B 136 ? 0.3167 0.2438 0.2804 0.0145  0.0491  -0.0070 142 TRP   C CD1 
2140 C CD2 . TRP   B 136 ? 0.2939 0.2285 0.2783 0.0149  0.0523  0.0036  142 TRP   C CD2 
2141 N NE1 . TRP   B 136 ? 0.3208 0.2532 0.2971 0.0130  0.0466  -0.0059 142 TRP   C NE1 
2142 C CE2 . TRP   B 136 ? 0.3076 0.2444 0.2957 0.0133  0.0484  0.0006  142 TRP   C CE2 
2143 C CE3 . TRP   B 136 ? 0.2991 0.2379 0.2954 0.0151  0.0544  0.0102  142 TRP   C CE3 
2144 C CZ2 . TRP   B 136 ? 0.3001 0.2427 0.3016 0.0123  0.0466  0.0044  142 TRP   C CZ2 
2145 C CZ3 . TRP   B 136 ? 0.3030 0.2476 0.3127 0.0140  0.0520  0.0136  142 TRP   C CZ3 
2146 C CH2 . TRP   B 136 ? 0.2984 0.2447 0.3098 0.0127  0.0482  0.0108  142 TRP   C CH2 
2147 N N   . LEU   B 137 ? 0.2956 0.2334 0.2658 0.0154  0.0443  0.0100  143 LEU   C N   
2148 C CA  . LEU   B 137 ? 0.2961 0.2395 0.2776 0.0143  0.0424  0.0157  143 LEU   C CA  
2149 C C   . LEU   B 137 ? 0.3292 0.2705 0.3065 0.0150  0.0439  0.0192  143 LEU   C C   
2150 O O   . LEU   B 137 ? 0.3454 0.2900 0.3328 0.0141  0.0443  0.0241  143 LEU   C O   
2151 C CB  . LEU   B 137 ? 0.2857 0.2341 0.2687 0.0128  0.0344  0.0149  143 LEU   C CB  
2152 C CG  . LEU   B 137 ? 0.2952 0.2467 0.2854 0.0117  0.0328  0.0133  143 LEU   C CG  
2153 C CD1 . LEU   B 137 ? 0.2842 0.2397 0.2731 0.0107  0.0258  0.0120  143 LEU   C CD1 
2154 C CD2 . LEU   B 137 ? 0.2809 0.2358 0.2852 0.0112  0.0354  0.0180  143 LEU   C CD2 
2155 N N   . ASP   B 138 ? 0.3285 0.2645 0.2913 0.0165  0.0446  0.0168  144 ASP   C N   
2156 C CA  . ASP   B 138 ? 0.3476 0.2808 0.3054 0.0173  0.0462  0.0204  144 ASP   C CA  
2157 C C   . ASP   B 138 ? 0.3947 0.3235 0.3530 0.0186  0.0556  0.0233  144 ASP   C C   
2158 O O   . ASP   B 138 ? 0.4040 0.3299 0.3582 0.0193  0.0580  0.0266  144 ASP   C O   
2159 C CB  . ASP   B 138 ? 0.3487 0.2777 0.2897 0.0186  0.0426  0.0174  144 ASP   C CB  
2160 C CG  . ASP   B 138 ? 0.3751 0.3081 0.3151 0.0178  0.0338  0.0153  144 ASP   C CG  
2161 O OD1 . ASP   B 138 ? 0.3814 0.3198 0.3323 0.0161  0.0305  0.0167  144 ASP   C OD1 
2162 O OD2 . ASP   B 138 ? 0.3902 0.3209 0.3182 0.0191  0.0302  0.0124  144 ASP   C OD2 
2163 N N   . GLU   B 139 ? 0.4187 0.3462 0.3813 0.0193  0.0613  0.0219  145 GLU   C N   
2164 C CA  . GLU   B 139 ? 0.4770 0.3997 0.4395 0.0211  0.0715  0.0242  145 GLU   C CA  
2165 C C   . GLU   B 139 ? 0.5299 0.4559 0.5096 0.0210  0.0769  0.0266  145 GLU   C C   
2166 O O   . GLU   B 139 ? 0.5311 0.4627 0.5215 0.0195  0.0724  0.0264  145 GLU   C O   
2167 C CB  . GLU   B 139 ? 0.5212 0.4354 0.4649 0.0231  0.0746  0.0185  145 GLU   C CB  
2168 C CG  . GLU   B 139 ? 0.5884 0.5022 0.5326 0.0227  0.0734  0.0128  145 GLU   C CG  
2169 C CD  . GLU   B 139 ? 0.6741 0.5803 0.5995 0.0238  0.0733  0.0060  145 GLU   C CD  
2170 O OE1 . GLU   B 139 ? 0.6633 0.5673 0.5894 0.0235  0.0747  0.0013  145 GLU   C OE1 
2171 O OE2 . GLU   B 139 ? 0.7227 0.6248 0.6326 0.0248  0.0715  0.0053  145 GLU   C OE2 
2172 N N   . GLU   B 140 ? 0.5622 0.4842 0.5441 0.0229  0.0872  0.0290  146 GLU   C N   
2173 C CA  . GLU   B 140 ? 0.5895 0.5136 0.5875 0.0237  0.0940  0.0315  146 GLU   C CA  
2174 C C   . GLU   B 140 ? 0.6041 0.5379 0.6231 0.0216  0.0896  0.0370  146 GLU   C C   
2175 O O   . GLU   B 140 ? 0.6131 0.5499 0.6477 0.0221  0.0953  0.0423  146 GLU   C O   
2176 C CB  . GLU   B 140 ? 0.6278 0.5477 0.6211 0.0247  0.0959  0.0254  146 GLU   C CB  
2177 C CG  . GLU   B 140 ? 0.7154 0.6387 0.7270 0.0252  0.0999  0.0275  146 GLU   C CG  
2178 C CD  . GLU   B 140 ? 0.8114 0.7304 0.8288 0.0280  0.1124  0.0297  146 GLU   C CD  
2179 O OE1 . GLU   B 140 ? 0.8207 0.7404 0.8501 0.0290  0.1164  0.0300  146 GLU   C OE1 
2180 O OE2 . GLU   B 140 ? 0.8571 0.7717 0.8675 0.0295  0.1189  0.0314  146 GLU   C OE2 
2181 N N1  . A1B5X C .   ? 0.3859 0.3314 0.3884 0.0149  0.0499  -0.0276 201 A1B5X A N1  
2182 N N3  . A1B5X C .   ? 0.3002 0.2497 0.3179 0.0230  0.0218  0.0023  201 A1B5X A N3  
2183 C C4  . A1B5X C .   ? 0.3872 0.3399 0.3873 0.0123  0.0564  -0.0309 201 A1B5X A C4  
2184 C C5  . A1B5X C .   ? 0.3852 0.3367 0.3818 0.0133  0.0486  -0.0266 201 A1B5X A C5  
2185 C C6  . A1B5X C .   ? 0.3654 0.3010 0.3687 0.0154  0.0452  -0.0265 201 A1B5X A C6  
2186 C C7  . A1B5X C .   ? 0.3758 0.3105 0.3718 0.0138  0.0384  -0.0243 201 A1B5X A C7  
2187 C C8  . A1B5X C .   ? 0.3634 0.2981 0.3710 0.0181  0.0358  -0.0175 201 A1B5X A C8  
2188 C C10 . A1B5X C .   ? 0.3312 0.2754 0.3553 0.0244  0.0285  -0.0019 201 A1B5X A C10 
2189 O O2  . A1B5X C .   ? 0.3350 0.2764 0.3727 0.0273  0.0316  0.0008  201 A1B5X A O2  
2190 C C9  . A1B5X C .   ? 0.3485 0.2908 0.3634 0.0217  0.0325  -0.0100 201 A1B5X A C9  
2191 C C11 . A1B5X C .   ? 0.3476 0.2909 0.3719 0.0240  0.0389  -0.0115 201 A1B5X A C11 
2192 N N2  . A1B5X C .   ? 0.3673 0.3101 0.3797 0.0199  0.0419  -0.0187 201 A1B5X A N2  
2193 S S1  . A1B5X C .   ? 0.3693 0.3155 0.3891 0.0214  0.0480  -0.0201 201 A1B5X A S1  
2194 O O   . A1B5X C .   ? 0.3671 0.3081 0.4014 0.0240  0.0566  -0.0232 201 A1B5X A O   
2195 O O1  . A1B5X C .   ? 0.3709 0.3254 0.3951 0.0238  0.0427  -0.0124 201 A1B5X A O1  
2196 C C1  . A1B5X C .   ? 0.3703 0.3263 0.3577 0.0120  0.0404  -0.0219 201 A1B5X A C1  
2197 S S   . A1B5X C .   ? 0.3593 0.3142 0.3434 0.0129  0.0320  -0.0173 201 A1B5X A S   
2198 C C   . A1B5X C .   ? 0.3659 0.3255 0.3391 0.0104  0.0249  -0.0138 201 A1B5X A C   
2199 N N   . A1B5X C .   ? 0.3933 0.3515 0.3874 0.0100  0.0558  -0.0303 201 A1B5X A N   
2200 C C3  . A1B5X C .   ? 0.3848 0.3467 0.3696 0.0088  0.0473  -0.0253 201 A1B5X A C3  
2201 C C2  . A1B5X C .   ? 0.3732 0.3339 0.3549 0.0099  0.0397  -0.0212 201 A1B5X A C2  
# 
