data_7HVT
# 
_entry.id   7HVT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HVT         pdb_00007hvt 10.2210/pdb7hvt/pdb 
WWPDB D_1001407993 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HVT 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '1-methyl-N-[(2R)-1-(1,3-oxazol-4-yl)propan-2-yl]-1H-indazole-3-carboxamide' 284.313   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                   65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    2   ?         ? ? ? 
5 water       nat water                                                                        18.015    386 ?         ? ? ? 
# 
_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 '1-methyl-N-[(2R)-1-(1,3-oxazol-4-yl)propan-2-yl]-1H-indazole-3-carboxamide' A1BP1 
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 
A1BP1 non-polymer         . '1-methyl-N-[(2R)-1-(1,3-oxazol-4-yl)propan-2-yl]-1H-indazole-3-carboxamide' ? 'C15 H16 N4 O2'  
284.313 
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        A1BP1 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BP1 
_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 A1BP1 1   201 201 A1BP1 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 95  HOH   HOH A . 
H 5 HOH   2   302 351 HOH   HOH A . 
H 5 HOH   3   303 64  HOH   HOH A . 
H 5 HOH   4   304 134 HOH   HOH A . 
H 5 HOH   5   305 174 HOH   HOH A . 
H 5 HOH   6   306 348 HOH   HOH A . 
H 5 HOH   7   307 234 HOH   HOH A . 
H 5 HOH   8   308 277 HOH   HOH A . 
H 5 HOH   9   309 214 HOH   HOH A . 
H 5 HOH   10  310 181 HOH   HOH A . 
H 5 HOH   11  311 184 HOH   HOH A . 
H 5 HOH   12  312 224 HOH   HOH A . 
H 5 HOH   13  313 236 HOH   HOH A . 
H 5 HOH   14  314 265 HOH   HOH A . 
H 5 HOH   15  315 136 HOH   HOH A . 
H 5 HOH   16  316 133 HOH   HOH A . 
H 5 HOH   17  317 149 HOH   HOH A . 
H 5 HOH   18  318 97  HOH   HOH A . 
H 5 HOH   19  319 340 HOH   HOH A . 
H 5 HOH   20  320 112 HOH   HOH A . 
H 5 HOH   21  321 195 HOH   HOH A . 
H 5 HOH   22  322 347 HOH   HOH A . 
H 5 HOH   23  323 125 HOH   HOH A . 
H 5 HOH   24  324 50  HOH   HOH A . 
H 5 HOH   25  325 327 HOH   HOH A . 
H 5 HOH   26  326 367 HOH   HOH A . 
H 5 HOH   27  327 114 HOH   HOH A . 
H 5 HOH   28  328 13  HOH   HOH A . 
H 5 HOH   29  329 99  HOH   HOH A . 
H 5 HOH   30  330 36  HOH   HOH A . 
H 5 HOH   31  331 160 HOH   HOH A . 
H 5 HOH   32  332 10  HOH   HOH A . 
H 5 HOH   33  333 379 HOH   HOH A . 
H 5 HOH   34  334 173 HOH   HOH A . 
H 5 HOH   35  335 293 HOH   HOH A . 
H 5 HOH   36  336 328 HOH   HOH A . 
H 5 HOH   37  337 194 HOH   HOH A . 
H 5 HOH   38  338 111 HOH   HOH A . 
H 5 HOH   39  339 339 HOH   HOH A . 
H 5 HOH   40  340 5   HOH   HOH A . 
H 5 HOH   41  341 338 HOH   HOH A . 
H 5 HOH   42  342 272 HOH   HOH A . 
H 5 HOH   43  343 98  HOH   HOH A . 
H 5 HOH   44  344 57  HOH   HOH A . 
H 5 HOH   45  345 334 HOH   HOH A . 
H 5 HOH   46  346 138 HOH   HOH A . 
H 5 HOH   47  347 241 HOH   HOH A . 
H 5 HOH   48  348 330 HOH   HOH A . 
H 5 HOH   49  349 11  HOH   HOH A . 
H 5 HOH   50  350 6   HOH   HOH A . 
H 5 HOH   51  351 62  HOH   HOH A . 
H 5 HOH   52  352 71  HOH   HOH A . 
H 5 HOH   53  353 84  HOH   HOH A . 
H 5 HOH   54  354 263 HOH   HOH A . 
H 5 HOH   55  355 333 HOH   HOH A . 
H 5 HOH   56  356 243 HOH   HOH A . 
H 5 HOH   57  357 90  HOH   HOH A . 
H 5 HOH   58  358 190 HOH   HOH A . 
H 5 HOH   59  359 39  HOH   HOH A . 
H 5 HOH   60  360 86  HOH   HOH A . 
H 5 HOH   61  361 220 HOH   HOH A . 
H 5 HOH   62  362 78  HOH   HOH A . 
H 5 HOH   63  363 275 HOH   HOH A . 
H 5 HOH   64  364 156 HOH   HOH A . 
H 5 HOH   65  365 80  HOH   HOH A . 
H 5 HOH   66  366 253 HOH   HOH A . 
H 5 HOH   67  367 85  HOH   HOH A . 
H 5 HOH   68  368 209 HOH   HOH A . 
H 5 HOH   69  369 366 HOH   HOH A . 
H 5 HOH   70  370 294 HOH   HOH A . 
H 5 HOH   71  371 55  HOH   HOH A . 
H 5 HOH   72  372 19  HOH   HOH A . 
H 5 HOH   73  373 145 HOH   HOH A . 
H 5 HOH   74  374 269 HOH   HOH A . 
H 5 HOH   75  375 61  HOH   HOH A . 
H 5 HOH   76  376 255 HOH   HOH A . 
H 5 HOH   77  377 246 HOH   HOH A . 
H 5 HOH   78  378 38  HOH   HOH A . 
H 5 HOH   79  379 302 HOH   HOH A . 
H 5 HOH   80  380 329 HOH   HOH A . 
H 5 HOH   81  381 239 HOH   HOH A . 
H 5 HOH   82  382 44  HOH   HOH A . 
H 5 HOH   83  383 268 HOH   HOH A . 
H 5 HOH   84  384 344 HOH   HOH A . 
H 5 HOH   85  385 278 HOH   HOH A . 
H 5 HOH   86  386 53  HOH   HOH A . 
H 5 HOH   87  387 26  HOH   HOH A . 
H 5 HOH   88  388 60  HOH   HOH A . 
H 5 HOH   89  389 104 HOH   HOH A . 
H 5 HOH   90  390 211 HOH   HOH A . 
H 5 HOH   91  391 121 HOH   HOH A . 
H 5 HOH   92  392 213 HOH   HOH A . 
H 5 HOH   93  393 22  HOH   HOH A . 
H 5 HOH   94  394 92  HOH   HOH A . 
H 5 HOH   95  395 280 HOH   HOH A . 
H 5 HOH   96  396 152 HOH   HOH A . 
H 5 HOH   97  397 230 HOH   HOH A . 
H 5 HOH   98  398 82  HOH   HOH A . 
H 5 HOH   99  399 102 HOH   HOH A . 
H 5 HOH   100 400 382 HOH   HOH A . 
H 5 HOH   101 401 321 HOH   HOH A . 
H 5 HOH   102 402 238 HOH   HOH A . 
H 5 HOH   103 403 32  HOH   HOH A . 
H 5 HOH   104 404 323 HOH   HOH A . 
H 5 HOH   105 405 297 HOH   HOH A . 
H 5 HOH   106 406 335 HOH   HOH A . 
H 5 HOH   107 407 40  HOH   HOH A . 
H 5 HOH   108 408 381 HOH   HOH A . 
H 5 HOH   109 409 132 HOH   HOH A . 
H 5 HOH   110 410 219 HOH   HOH A . 
H 5 HOH   111 411 290 HOH   HOH A . 
H 5 HOH   112 412 172 HOH   HOH A . 
H 5 HOH   113 413 52  HOH   HOH A . 
H 5 HOH   114 414 182 HOH   HOH A . 
H 5 HOH   115 415 345 HOH   HOH A . 
H 5 HOH   116 416 309 HOH   HOH A . 
H 5 HOH   117 417 144 HOH   HOH A . 
H 5 HOH   118 418 197 HOH   HOH A . 
H 5 HOH   119 419 105 HOH   HOH A . 
H 5 HOH   120 420 12  HOH   HOH A . 
H 5 HOH   121 421 115 HOH   HOH A . 
H 5 HOH   122 422 154 HOH   HOH A . 
H 5 HOH   123 423 363 HOH   HOH A . 
H 5 HOH   124 424 69  HOH   HOH A . 
H 5 HOH   125 425 373 HOH   HOH A . 
H 5 HOH   126 426 242 HOH   HOH A . 
H 5 HOH   127 427 299 HOH   HOH A . 
H 5 HOH   128 428 166 HOH   HOH A . 
H 5 HOH   129 429 375 HOH   HOH A . 
H 5 HOH   130 430 76  HOH   HOH A . 
H 5 HOH   131 431 120 HOH   HOH A . 
H 5 HOH   132 432 2   HOH   HOH A . 
H 5 HOH   133 433 141 HOH   HOH A . 
H 5 HOH   134 434 215 HOH   HOH A . 
H 5 HOH   135 435 276 HOH   HOH A . 
H 5 HOH   136 436 320 HOH   HOH A . 
H 5 HOH   137 437 27  HOH   HOH A . 
H 5 HOH   138 438 341 HOH   HOH A . 
H 5 HOH   139 439 70  HOH   HOH A . 
H 5 HOH   140 440 63  HOH   HOH A . 
H 5 HOH   141 441 123 HOH   HOH A . 
H 5 HOH   142 442 8   HOH   HOH A . 
H 5 HOH   143 443 101 HOH   HOH A . 
H 5 HOH   144 444 370 HOH   HOH A . 
H 5 HOH   145 445 188 HOH   HOH A . 
H 5 HOH   146 446 17  HOH   HOH A . 
H 5 HOH   147 447 355 HOH   HOH A . 
H 5 HOH   148 448 185 HOH   HOH A . 
H 5 HOH   149 449 314 HOH   HOH A . 
H 5 HOH   150 450 365 HOH   HOH A . 
H 5 HOH   151 451 229 HOH   HOH A . 
H 5 HOH   152 452 205 HOH   HOH A . 
H 5 HOH   153 453 312 HOH   HOH A . 
H 5 HOH   154 454 372 HOH   HOH A . 
H 5 HOH   155 455 179 HOH   HOH A . 
H 5 HOH   156 456 317 HOH   HOH A . 
H 5 HOH   157 457 7   HOH   HOH A . 
H 5 HOH   158 458 250 HOH   HOH A . 
H 5 HOH   159 459 295 HOH   HOH A . 
H 5 HOH   160 460 336 HOH   HOH A . 
H 5 HOH   161 461 319 HOH   HOH A . 
H 5 HOH   162 462 221 HOH   HOH A . 
H 5 HOH   163 463 237 HOH   HOH A . 
H 5 HOH   164 464 387 HOH   HOH A . 
H 5 HOH   165 465 227 HOH   HOH A . 
H 5 HOH   166 466 313 HOH   HOH A . 
H 5 HOH   167 467 274 HOH   HOH A . 
H 5 HOH   168 468 208 HOH   HOH A . 
H 5 HOH   169 469 343 HOH   HOH A . 
H 5 HOH   170 470 244 HOH   HOH A . 
H 5 HOH   171 471 259 HOH   HOH A . 
H 5 HOH   172 472 189 HOH   HOH A . 
H 5 HOH   173 473 225 HOH   HOH A . 
H 5 HOH   174 474 332 HOH   HOH A . 
H 5 HOH   175 475 298 HOH   HOH A . 
H 5 HOH   176 476 47  HOH   HOH A . 
H 5 HOH   177 477 177 HOH   HOH A . 
H 5 HOH   178 478 117 HOH   HOH A . 
H 5 HOH   179 479 287 HOH   HOH A . 
H 5 HOH   180 480 261 HOH   HOH A . 
H 5 HOH   181 481 322 HOH   HOH A . 
H 5 HOH   182 482 288 HOH   HOH A . 
H 5 HOH   183 483 283 HOH   HOH A . 
H 5 HOH   184 484 380 HOH   HOH A . 
H 5 HOH   185 485 346 HOH   HOH A . 
H 5 HOH   186 486 262 HOH   HOH A . 
H 5 HOH   187 487 116 HOH   HOH A . 
H 5 HOH   188 488 342 HOH   HOH A . 
H 5 HOH   189 489 175 HOH   HOH A . 
H 5 HOH   190 490 75  HOH   HOH A . 
H 5 HOH   191 491 315 HOH   HOH A . 
H 5 HOH   192 492 137 HOH   HOH A . 
H 5 HOH   193 493 325 HOH   HOH A . 
H 5 HOH   194 494 291 HOH   HOH A . 
H 5 HOH   195 495 316 HOH   HOH A . 
H 5 HOH   196 496 186 HOH   HOH A . 
H 5 HOH   197 497 256 HOH   HOH A . 
H 5 HOH   198 498 324 HOH   HOH A . 
H 5 HOH   199 499 386 HOH   HOH A . 
H 5 HOH   200 500 210 HOH   HOH A . 
H 5 HOH   201 501 326 HOH   HOH A . 
I 5 HOH   1   301 198 HOH   HOH C . 
I 5 HOH   2   302 147 HOH   HOH C . 
I 5 HOH   3   303 350 HOH   HOH C . 
I 5 HOH   4   304 171 HOH   HOH C . 
I 5 HOH   5   305 353 HOH   HOH C . 
I 5 HOH   6   306 81  HOH   HOH C . 
I 5 HOH   7   307 286 HOH   HOH C . 
I 5 HOH   8   308 361 HOH   HOH C . 
I 5 HOH   9   309 124 HOH   HOH C . 
I 5 HOH   10  310 77  HOH   HOH C . 
I 5 HOH   11  311 233 HOH   HOH C . 
I 5 HOH   12  312 165 HOH   HOH C . 
I 5 HOH   13  313 42  HOH   HOH C . 
I 5 HOH   14  314 4   HOH   HOH C . 
I 5 HOH   15  315 87  HOH   HOH C . 
I 5 HOH   16  316 119 HOH   HOH C . 
I 5 HOH   17  317 232 HOH   HOH C . 
I 5 HOH   18  318 139 HOH   HOH C . 
I 5 HOH   19  319 31  HOH   HOH C . 
I 5 HOH   20  320 282 HOH   HOH C . 
I 5 HOH   21  321 187 HOH   HOH C . 
I 5 HOH   22  322 157 HOH   HOH C . 
I 5 HOH   23  323 122 HOH   HOH C . 
I 5 HOH   24  324 113 HOH   HOH C . 
I 5 HOH   25  325 226 HOH   HOH C . 
I 5 HOH   26  326 349 HOH   HOH C . 
I 5 HOH   27  327 151 HOH   HOH C . 
I 5 HOH   28  328 369 HOH   HOH C . 
I 5 HOH   29  329 202 HOH   HOH C . 
I 5 HOH   30  330 88  HOH   HOH C . 
I 5 HOH   31  331 354 HOH   HOH C . 
I 5 HOH   32  332 24  HOH   HOH C . 
I 5 HOH   33  333 34  HOH   HOH C . 
I 5 HOH   34  334 41  HOH   HOH C . 
I 5 HOH   35  335 66  HOH   HOH C . 
I 5 HOH   36  336 378 HOH   HOH C . 
I 5 HOH   37  337 260 HOH   HOH C . 
I 5 HOH   38  338 163 HOH   HOH C . 
I 5 HOH   39  339 14  HOH   HOH C . 
I 5 HOH   40  340 279 HOH   HOH C . 
I 5 HOH   41  341 273 HOH   HOH C . 
I 5 HOH   42  342 1   HOH   HOH C . 
I 5 HOH   43  343 223 HOH   HOH C . 
I 5 HOH   44  344 131 HOH   HOH C . 
I 5 HOH   45  345 337 HOH   HOH C . 
I 5 HOH   46  346 301 HOH   HOH C . 
I 5 HOH   47  347 65  HOH   HOH C . 
I 5 HOH   48  348 28  HOH   HOH C . 
I 5 HOH   49  349 371 HOH   HOH C . 
I 5 HOH   50  350 89  HOH   HOH C . 
I 5 HOH   51  351 72  HOH   HOH C . 
I 5 HOH   52  352 176 HOH   HOH C . 
I 5 HOH   53  353 228 HOH   HOH C . 
I 5 HOH   54  354 271 HOH   HOH C . 
I 5 HOH   55  355 33  HOH   HOH C . 
I 5 HOH   56  356 103 HOH   HOH C . 
I 5 HOH   57  357 110 HOH   HOH C . 
I 5 HOH   58  358 289 HOH   HOH C . 
I 5 HOH   59  359 49  HOH   HOH C . 
I 5 HOH   60  360 58  HOH   HOH C . 
I 5 HOH   61  361 362 HOH   HOH C . 
I 5 HOH   62  362 304 HOH   HOH C . 
I 5 HOH   63  363 252 HOH   HOH C . 
I 5 HOH   64  364 37  HOH   HOH C . 
I 5 HOH   65  365 266 HOH   HOH C . 
I 5 HOH   66  366 54  HOH   HOH C . 
I 5 HOH   67  367 352 HOH   HOH C . 
I 5 HOH   68  368 216 HOH   HOH C . 
I 5 HOH   69  369 218 HOH   HOH C . 
I 5 HOH   70  370 192 HOH   HOH C . 
I 5 HOH   71  371 167 HOH   HOH C . 
I 5 HOH   72  372 200 HOH   HOH C . 
I 5 HOH   73  373 204 HOH   HOH C . 
I 5 HOH   74  374 143 HOH   HOH C . 
I 5 HOH   75  375 377 HOH   HOH C . 
I 5 HOH   76  376 199 HOH   HOH C . 
I 5 HOH   77  377 142 HOH   HOH C . 
I 5 HOH   78  378 140 HOH   HOH C . 
I 5 HOH   79  379 245 HOH   HOH C . 
I 5 HOH   80  380 56  HOH   HOH C . 
I 5 HOH   81  381 159 HOH   HOH C . 
I 5 HOH   82  382 68  HOH   HOH C . 
I 5 HOH   83  383 106 HOH   HOH C . 
I 5 HOH   84  384 15  HOH   HOH C . 
I 5 HOH   85  385 257 HOH   HOH C . 
I 5 HOH   86  386 128 HOH   HOH C . 
I 5 HOH   87  387 74  HOH   HOH C . 
I 5 HOH   88  388 368 HOH   HOH C . 
I 5 HOH   89  389 93  HOH   HOH C . 
I 5 HOH   90  390 183 HOH   HOH C . 
I 5 HOH   91  391 18  HOH   HOH C . 
I 5 HOH   92  392 30  HOH   HOH C . 
I 5 HOH   93  393 46  HOH   HOH C . 
I 5 HOH   94  394 222 HOH   HOH C . 
I 5 HOH   95  395 20  HOH   HOH C . 
I 5 HOH   96  396 45  HOH   HOH C . 
I 5 HOH   97  397 94  HOH   HOH C . 
I 5 HOH   98  398 35  HOH   HOH C . 
I 5 HOH   99  399 25  HOH   HOH C . 
I 5 HOH   100 400 16  HOH   HOH C . 
I 5 HOH   101 401 308 HOH   HOH C . 
I 5 HOH   102 402 59  HOH   HOH C . 
I 5 HOH   103 403 118 HOH   HOH C . 
I 5 HOH   104 404 51  HOH   HOH C . 
I 5 HOH   105 405 161 HOH   HOH C . 
I 5 HOH   106 406 217 HOH   HOH C . 
I 5 HOH   107 407 48  HOH   HOH C . 
I 5 HOH   108 408 153 HOH   HOH C . 
I 5 HOH   109 409 356 HOH   HOH C . 
I 5 HOH   110 410 100 HOH   HOH C . 
I 5 HOH   111 411 73  HOH   HOH C . 
I 5 HOH   112 412 162 HOH   HOH C . 
I 5 HOH   113 413 96  HOH   HOH C . 
I 5 HOH   114 414 376 HOH   HOH C . 
I 5 HOH   115 415 251 HOH   HOH C . 
I 5 HOH   116 416 196 HOH   HOH C . 
I 5 HOH   117 417 191 HOH   HOH C . 
I 5 HOH   118 418 249 HOH   HOH C . 
I 5 HOH   119 419 21  HOH   HOH C . 
I 5 HOH   120 420 91  HOH   HOH C . 
I 5 HOH   121 421 170 HOH   HOH C . 
I 5 HOH   122 422 358 HOH   HOH C . 
I 5 HOH   123 423 248 HOH   HOH C . 
I 5 HOH   124 424 306 HOH   HOH C . 
I 5 HOH   125 425 240 HOH   HOH C . 
I 5 HOH   126 426 360 HOH   HOH C . 
I 5 HOH   127 427 206 HOH   HOH C . 
I 5 HOH   128 428 203 HOH   HOH C . 
I 5 HOH   129 429 43  HOH   HOH C . 
I 5 HOH   130 430 285 HOH   HOH C . 
I 5 HOH   131 431 79  HOH   HOH C . 
I 5 HOH   132 432 29  HOH   HOH C . 
I 5 HOH   133 433 357 HOH   HOH C . 
I 5 HOH   134 434 258 HOH   HOH C . 
I 5 HOH   135 435 23  HOH   HOH C . 
I 5 HOH   136 436 67  HOH   HOH C . 
I 5 HOH   137 437 109 HOH   HOH C . 
I 5 HOH   138 438 9   HOH   HOH C . 
I 5 HOH   139 439 126 HOH   HOH C . 
I 5 HOH   140 440 150 HOH   HOH C . 
I 5 HOH   141 441 3   HOH   HOH C . 
I 5 HOH   142 442 130 HOH   HOH C . 
I 5 HOH   143 443 254 HOH   HOH C . 
I 5 HOH   144 444 305 HOH   HOH C . 
I 5 HOH   145 445 135 HOH   HOH C . 
I 5 HOH   146 446 129 HOH   HOH C . 
I 5 HOH   147 447 169 HOH   HOH C . 
I 5 HOH   148 448 83  HOH   HOH C . 
I 5 HOH   149 449 364 HOH   HOH C . 
I 5 HOH   150 450 158 HOH   HOH C . 
I 5 HOH   151 451 383 HOH   HOH C . 
I 5 HOH   152 452 180 HOH   HOH C . 
I 5 HOH   153 453 331 HOH   HOH C . 
I 5 HOH   154 454 247 HOH   HOH C . 
I 5 HOH   155 455 311 HOH   HOH C . 
I 5 HOH   156 456 303 HOH   HOH C . 
I 5 HOH   157 457 108 HOH   HOH C . 
I 5 HOH   158 458 107 HOH   HOH C . 
I 5 HOH   159 459 310 HOH   HOH C . 
I 5 HOH   160 460 359 HOH   HOH C . 
I 5 HOH   161 461 385 HOH   HOH C . 
I 5 HOH   162 462 146 HOH   HOH C . 
I 5 HOH   163 463 267 HOH   HOH C . 
I 5 HOH   164 464 207 HOH   HOH C . 
I 5 HOH   165 465 270 HOH   HOH C . 
I 5 HOH   166 466 264 HOH   HOH C . 
I 5 HOH   167 467 164 HOH   HOH C . 
I 5 HOH   168 468 374 HOH   HOH C . 
I 5 HOH   169 469 155 HOH   HOH C . 
I 5 HOH   170 470 388 HOH   HOH C . 
I 5 HOH   171 471 307 HOH   HOH C . 
I 5 HOH   172 472 201 HOH   HOH C . 
I 5 HOH   173 473 389 HOH   HOH C . 
I 5 HOH   174 474 178 HOH   HOH C . 
I 5 HOH   175 475 296 HOH   HOH C . 
I 5 HOH   176 476 281 HOH   HOH C . 
I 5 HOH   177 477 212 HOH   HOH C . 
I 5 HOH   178 478 292 HOH   HOH C . 
I 5 HOH   179 479 168 HOH   HOH C . 
I 5 HOH   180 480 193 HOH   HOH C . 
I 5 HOH   181 481 148 HOH   HOH C . 
I 5 HOH   182 482 231 HOH   HOH C . 
I 5 HOH   183 483 384 HOH   HOH C . 
I 5 HOH   184 484 235 HOH   HOH C . 
I 5 HOH   185 485 318 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           7HVT 
_cell.length_a           87.022 
_cell.length_b           57.182 
_cell.length_c           65.051 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.68 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVT 
_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          7HVT 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.54 
_exptl_crystal.density_percent_sol   51.53 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-14 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVT 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             43.38 
_reflns.d_resolution_high            1.16 
_reflns.number_obs                   86574 
_reflns.percent_possible_obs         78.7 
_reflns.pdbx_Rmerge_I_obs            0.058 
_reflns.pdbx_netI_over_sigmaI        18.7 
_reflns.pdbx_redundancy              5.2 
_reflns.pdbx_Rrim_I_all              0.063 
_reflns.pdbx_Rpim_I_all              0.025 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     452047 
_reflns.pdbx_chi_squared             0.92 
_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                  1.16 
_reflns_shell.d_res_low                   1.18 
_reflns_shell.number_measured_all         544 
_reflns_shell.number_unique_obs           537 
_reflns_shell.Rmerge_I_obs                0.653 
_reflns_shell.pdbx_chi_squared            0.20 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        9.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             0.924 
_reflns_shell.pdbx_Rpim_I_all             0.653 
_reflns_shell.pdbx_CC_half                0.140 
_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                                 7HVT 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     86393 
_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                             43.37 
_refine.ls_d_res_high                            1.160 
_refine.ls_percent_reflns_obs                    78.7 
_refine.ls_R_factor_obs                          0.1840 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1835 
_refine.ls_R_factor_R_free                       0.1942 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.050 
_refine.ls_number_reflns_R_free                  4365 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.939 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.B_iso_mean                               18.78 
_refine.aniso_B[1][1]                            -0.41520 
_refine.aniso_B[2][2]                            0.15260 
_refine.aniso_B[3][3]                            0.26260 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.94930 
_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             0.042 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.042 
_refine.pdbx_overall_SU_R_Blow_DPI               0.045 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.044 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVT 
_refine_analyze.Luzzati_coordinate_error_obs    0.15 
_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         31 
_refine_hist.number_atoms_solvent             386 
_refine_hist.number_atoms_total               2583 
_refine_hist.d_res_high                       1.160 
_refine_hist.d_res_low                        43.37 
# 
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                  0.014 ? 2.00  2269 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.12  ? 2.00  3093 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  754  '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  416  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2269 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.17  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.40 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2112 '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                       1.16 
_refine_ls_shell.d_res_low                        1.21 
_refine_ls_shell.number_reflns_R_work             1619 
_refine_ls_shell.R_factor_R_work                  0.3189 
_refine_ls_shell.percent_reflns_obs               14.17 
_refine_ls_shell.R_factor_R_free                  0.3295 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.31 
_refine_ls_shell.number_reflns_R_free             109 
_refine_ls_shell.number_reflns_all                1728 
_refine_ls_shell.R_factor_all                     0.3196 
# 
_struct.entry_id                  7HVT 
_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-0032067-002 (A71EV2A-x3593)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVT 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I 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 7HVT A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HVT C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_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 ? ? ? ? ? ? ? 2.349 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.9 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
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_555 116.4 ? 
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_555 104.1 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.8 ? 
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_555 115.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.7 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.9 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.1 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.3 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.8 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 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 LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7HVT 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 408 ? ? O A HOH 446 ? ? 1.61 
2 1 O A HOH 404 ? ? O A HOH 457 ? ? 1.86 
3 1 O A HOH 438 ? ? O A HOH 492 ? ? 2.09 
4 1 O A HOH 358 ? ? O A HOH 450 ? ? 2.14 
5 1 O A HOH 355 ? ? O A HOH 435 ? ? 2.17 
# 
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 SER A 125 ? ? -135.02 -32.68 
2 1 SER C 125 ? ? -134.18 -30.47 
# 
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 15.0030 8.2311   14.5510 -0.0128 -0.0229 0.0030 0.0067 -0.0019 0.0115 1.4683 0.5788 0.5408 0.7690  
-0.5486 -0.2240 -0.0020 0.0761 0.1388 0.0291 0.0532 0.0251 -0.0052 -0.0495 -0.0512 
'X-RAY DIFFRACTION' 2 ? refined 25.9753 -20.2310 17.8161 -0.0169 -0.0165 0.0119 0.0057 -0.0038 0.0202 0.6778 0.7682 0.1692 -0.1087 
-0.1507 -0.1204 0.0089  0.0184 0.1185 0.0235 0.0377 0.0299 0.0327  0.0034  -0.0466 
# 
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 
A1BP1 N1   N  N N 1   
A1BP1 N3   N  Y N 2   
A1BP1 C4   C  Y N 3   
A1BP1 C5   C  Y N 4   
A1BP1 C6   C  N N 5   
A1BP1 C7   C  Y N 6   
A1BP1 C8   C  N N 7   
A1BP1 C10  C  Y N 8   
A1BP1 C13  C  Y N 9   
A1BP1 O1   O  N N 10  
A1BP1 C14  C  Y N 11  
A1BP1 C12  C  Y N 12  
A1BP1 C11  C  Y N 13  
A1BP1 C9   C  Y N 14  
A1BP1 N2   N  Y N 15  
A1BP1 C1   C  N S 16  
A1BP1 C    C  N N 17  
A1BP1 C2   C  N N 18  
A1BP1 C3   C  Y N 19  
A1BP1 N    N  Y N 20  
A1BP1 O    O  Y N 21  
A1BP1 H8   H  N N 22  
A1BP1 H6   H  N N 23  
A1BP1 H7   H  N N 24  
A1BP1 H10  H  N N 25  
A1BP1 H9   H  N N 26  
A1BP1 H11  H  N N 27  
A1BP1 H12  H  N N 28  
A1BP1 H15  H  N N 29  
A1BP1 H14  H  N N 30  
A1BP1 H13  H  N N 31  
A1BP1 H    H  N N 32  
A1BP1 H1   H  N N 33  
A1BP1 H2   H  N N 34  
A1BP1 H3   H  N N 35  
A1BP1 H4   H  N N 36  
A1BP1 H5   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1BP1 C   C1   sing N N 1   
A1BP1 C2  C1   sing N N 2   
A1BP1 C3  C2   sing N N 3   
A1BP1 C3  C4   doub Y N 4   
A1BP1 C4  O    sing Y N 5   
A1BP1 O   C5   sing Y N 6   
A1BP1 C5  N    doub Y N 7   
A1BP1 N   C3   sing Y N 8   
A1BP1 C1  N1   sing N N 9   
A1BP1 N1  C6   sing N N 10  
A1BP1 C6  O1   doub N N 11  
A1BP1 C7  C6   sing N N 12  
A1BP1 C7  N2   doub Y N 13  
A1BP1 N2  N3   sing Y N 14  
A1BP1 C8  N3   sing N N 15  
A1BP1 N3  C9   sing Y N 16  
A1BP1 C9  C10  doub Y N 17  
A1BP1 C10 C11  sing Y N 18  
A1BP1 C11 C12  doub Y N 19  
A1BP1 C12 C13  sing Y N 20  
A1BP1 C13 C14  doub Y N 21  
A1BP1 C14 C7   sing Y N 22  
A1BP1 C9  C14  sing Y N 23  
A1BP1 N1  H8   sing N N 24  
A1BP1 C4  H6   sing N N 25  
A1BP1 C5  H7   sing N N 26  
A1BP1 C8  H10  sing N N 27  
A1BP1 C8  H9   sing N N 28  
A1BP1 C8  H11  sing N N 29  
A1BP1 C10 H12  sing N N 30  
A1BP1 C13 H15  sing N N 31  
A1BP1 C12 H14  sing N N 32  
A1BP1 C11 H13  sing N N 33  
A1BP1 C1  H    sing N N 34  
A1BP1 C   H1   sing N N 35  
A1BP1 C   H2   sing N N 36  
A1BP1 C   H3   sing N N 37  
A1BP1 C2  H4   sing N N 38  
A1BP1 C2  H5   sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HVT 
_atom_sites.fract_transf_matrix[1][1]   0.011491 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000941 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017488 
_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]   0.015424 
_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   ? 17.695 8.041   24.941 1.00 15.03 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.953 8.157   24.153 1.00 14.94 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.089 6.952   23.204 1.00 14.76 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.358 5.956   23.373 1.00 14.63 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.162 8.206   25.107 1.00 17.48 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.231 6.974   25.801 1.00 20.79 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.998 7.021   22.236 1.00 13.85 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.284 5.919   21.324 1.00 12.88 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.690 6.397   19.940 1.00 11.68 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.379 7.530   19.558 1.00 13.15 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.382 5.572   19.219 1.00 10.99 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.862 5.926   17.878 1.00 11.19 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.838 4.693   16.987 1.00 11.34 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.740 3.552   17.471 1.00 12.02 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.306 6.457   17.995 1.00 13.03 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.924 4.920   15.677 1.00 10.66 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.157 3.894   14.650 1.00 10.25 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.621 3.981   14.267 1.00 11.01 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.103 5.097   13.986 1.00 11.30 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.284 4.106   13.409 1.00 10.47 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.778 4.254   13.757 1.00 12.25 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.491 2.924   12.452 1.00 12.38 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.967 4.815   12.562 1.00 13.40 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.320 2.843   14.220 1.00 10.92 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.739 2.822   13.835 1.00 11.76 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.860 2.007   12.565 1.00 12.05 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.828 0.757   12.641 1.00 12.80 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.644 2.236   14.958 1.00 13.00 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.674 3.128   16.175 1.00 12.67 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.528 4.236   16.239 1.00 13.15 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.815 2.909   17.247 1.00 13.90 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.519 5.103   17.335 1.00 13.68 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.826 3.759   18.371 1.00 14.42 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.650 4.880   18.378 1.00 14.07 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.630 5.749   19.472 1.00 16.96 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.883 2.660   11.417 1.00 12.44 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.968 2.000   10.105 1.00 12.64 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.198 2.491   9.365  1.00 14.08 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.440 3.707   9.324  1.00 13.38 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.662 2.242   9.259  1.00 13.92 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.316 3.735   9.142  1.00 15.19 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.820 1.620   7.874  1.00 15.23 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.061 1.580   8.873  1.00 14.63 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.302 2.022   8.231  1.00 15.37 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.123 2.909   9.157  1.00 14.46 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.254 2.618   10.358 1.00 14.11 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.575 4.063   8.636  1.00 13.93 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.277 5.044   9.476  1.00 13.29 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.367 6.235   9.797  1.00 12.52 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.859 7.367   9.920  1.00 13.78 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.627 5.481   8.881  1.00 15.70 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.685 4.407   8.994  1.00 18.93 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.452 4.338   9.983  1.00 21.84 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.730 3.534   8.024  1.00 18.27 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.090 5.954   10.024 1.00 12.24 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.126 6.984   10.406 1.00 11.35 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.460 6.655   11.740 1.00 11.29 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.192 5.467   12.073 1.00 12.37 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.016 7.059   9.329  1.00 12.08 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.518 7.453   7.960  1.00 13.41 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.162 8.671   7.753  1.00 14.90 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.331 6.621   6.876  1.00 15.99 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.604 9.050   6.487  1.00 15.77 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.734 7.010   5.601  1.00 17.11 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.355 8.220   5.415  1.00 17.86 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.818 8.617   4.166  1.00 21.25 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.142 7.712   12.481 1.00 11.14 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.345 7.656   13.699 1.00 11.18 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.105 8.517   13.477 1.00 11.17 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.230 9.731   13.180 1.00 10.97 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.165 8.187   14.912 1.00 11.77 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.362 8.556   16.168 1.00 11.72 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.305 8.936   17.335 1.00 13.15 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.752 10.011  18.167 1.00 13.41 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.080 9.827   19.304 1.00 13.78 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.773 8.594   19.717 1.00 15.95 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.641 10.872  19.992 1.00 15.24 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.909 7.908   13.556 1.00 10.53 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.640 8.627   13.319 1.00 10.16 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.963 8.842   14.653 1.00 10.80 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.667 7.851   15.363 1.00 11.21 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.706 7.852   12.390 1.00 10.62 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.486 8.699   12.031 1.00 11.91 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.404 7.337   11.132 1.00 12.59 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.725 10.108  15.019 1.00 10.11 ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.106 10.441  16.316 0.50 10.30 ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.155 10.426  16.334 0.50 12.14 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 20.003 11.422  16.140 1.00 11.08 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.854 12.070  15.063 1.00 11.56 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.140 11.025  17.333 0.50 10.31 ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.321 11.035  17.218 0.50 15.70 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.035 9.930   17.855 0.50 12.27 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.905 11.312  18.644 0.50 15.64 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.901 12.244  16.751 0.50 6.88  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.525 10.131  17.238 0.50 18.89 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.171 11.582  17.197 1.00 11.13 ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.176 12.666  17.164 1.00 11.67 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.985 13.993  17.171 1.00 11.14 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.944 14.156  17.965 1.00 11.67 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.310 12.680  18.441 1.00 11.11 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.426 11.452  18.542 1.00 11.22 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.813 10.429  19.127 1.00 11.83 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.264 11.497  17.916 1.00 12.43 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.596 14.940  16.303 1.00 11.40 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.345 16.224  16.256 1.00 12.35 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.320 16.906  17.614 1.00 13.95 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.339 17.456  18.049 1.00 14.83 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.726 17.118  15.198 1.00 13.11 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.525 18.442  14.940 1.00 12.73 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.753 19.304  13.946 1.00 14.70 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.473 20.509  13.498 1.00 15.67 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.485 21.660  14.160 1.00 17.32 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.913 21.758  15.354 1.00 17.68 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.049 22.743  13.616 1.00 18.62 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.184 16.775  18.354 1.00 13.33 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.096 17.462  19.643 1.00 15.22 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.989 16.876  20.753 1.00 15.86 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.143 17.499  21.820 1.00 17.80 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.641 17.610  20.142 1.00 16.87 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.994 16.342  20.629 1.00 15.55 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.351 15.491  19.758 1.00 15.05 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.876 15.850  21.898 1.00 16.55 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.854 14.487  20.519 1.00 15.46 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.157 14.662  21.804 1.00 16.86 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.522 15.637  20.530 1.00 14.60 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.417 14.956  21.463 1.00 14.06 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.863 14.914  20.974 1.00 14.74 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.720 14.327  21.627 1.00 15.81 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.925 13.537  21.772 1.00 13.78 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.533 13.517  22.399 1.00 14.70 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 18.069 12.072  22.630 1.00 15.09 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.504 14.294  23.756 1.00 17.27 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.166 15.597  19.855 1.00 14.39 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.548 15.589  19.336 1.00 14.55 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.525 16.259  20.294 1.00 15.23 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.195 17.258  20.933 1.00 15.41 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.618 16.284  17.970 1.00 14.54 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.693 15.666  20.424 1.00 14.78 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.763 16.178  21.304 1.00 14.51 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.686 17.185  20.579 1.00 15.48 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.654 17.313  19.337 1.00 14.19 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.633 15.015  21.822 1.00 16.33 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.343 14.462  20.719 1.00 16.39 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.806 13.886  22.485 1.00 17.35 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.625 17.837  21.320 1.00 14.93 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.614 18.678  20.679 1.00 15.53 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.439 17.858  19.700 1.00 14.60 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.719 18.330  18.597 1.00 15.53 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.567 19.310  21.733 1.00 17.45 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.826 19.932  21.114 1.00 23.53 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.787 21.121  20.402 1.00 27.89 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.078 19.395  20.972 1.00 26.75 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 33.033 21.375  20.025 1.00 28.19 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.845 20.327  20.275 1.00 28.84 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.827 16.594  20.074 1.00 14.57 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.596 15.787  19.154 1.00 14.30 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.823 15.505  17.858 1.00 13.77 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.423 15.528  16.773 1.00 14.13 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.046 14.449  19.763 1.00 15.78 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 33.012 13.736  18.838 1.00 23.32 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.178 14.175  18.660 1.00 26.50 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.545 12.653  18.192 1.00 24.69 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.488 15.292  17.950 1.00 13.29 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.698 15.109  16.743 1.00 12.40 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.756 16.360  15.845 1.00 12.09 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.977 16.237  14.628 1.00 13.07 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.216 14.825  17.088 1.00 13.03 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.961 13.465  17.686 1.00 14.48 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.596 12.482  17.232 1.00 13.69 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.148 13.388  18.628 1.00 13.84 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.558 17.534  16.426 1.00 12.32 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.575 18.779  15.641 1.00 12.42 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.978 19.029  15.046 1.00 12.69 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.076 19.602  13.958 1.00 13.48 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.137 19.963  16.519 1.00 13.85 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.642 20.057  16.660 1.00 12.82 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.899 19.762  17.768 1.00 14.73 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.695 20.478  15.648 1.00 13.65 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.554 19.945  17.501 1.00 14.19 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.409 20.436  16.221 1.00 14.63 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.834 20.918  14.322 1.00 14.79 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.255 20.791  15.488 1.00 15.95 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.718 21.231  13.604 1.00 16.58 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.465 21.263  14.199 1.00 16.81 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.041 18.638  15.778 1.00 11.92 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.401 18.854  15.290 1.00 12.78 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.819 17.848  14.197 1.00 13.90 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.869 17.996  13.562 1.00 15.52 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.379 18.778  16.460 1.00 15.95 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.011 16.775  13.991 1.00 13.56 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.276 15.717  12.988 1.00 13.88 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.016 15.551  12.127 1.00 12.75 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.630 14.426  11.796 1.00 13.05 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.689 14.396  13.678 1.00 14.77 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.045 14.564  14.327 1.00 16.62 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.064 14.507  13.637 1.00 19.63 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.070 14.848  15.622 1.00 17.27 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.360 16.644  11.805 1.00 12.59 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.078 16.616  11.139 1.00 12.51 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.124 16.148  9.728  1.00 13.99 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.970 16.594  8.941  1.00 15.42 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.476 18.041  11.209 1.00 12.88 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.087 18.184  10.606 1.00 13.16 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.040 17.404  11.458 1.00 13.89 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.658 19.660  10.569 1.00 16.04 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.185 15.259  9.350  1.00 12.87 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.023 14.835  7.948  1.00 13.76 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.766 15.518  7.368  1.00 13.25 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.803 16.080  6.266  1.00 15.11 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.914 13.300  7.842  1.00 12.84 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.525 12.890  6.412  1.00 15.49 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.212 12.643  8.306  1.00 14.17 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.628 15.500  8.110  1.00 12.74 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.372 16.041  7.603  1.00 13.03 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.402 16.260  8.759  1.00 13.22 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.436 15.479  9.712  1.00 12.76 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.759 15.039  6.584  1.00 14.31 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.337 15.306  6.145  1.00 15.10 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.915 16.175  5.175  1.00 17.32 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.145 14.700  6.684  1.00 14.54 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.544 16.101  5.038  1.00 18.08 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.040 15.226  5.981  1.00 16.26 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.910 13.775  7.693  1.00 15.68 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.715 14.761  6.202  1.00 18.23 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.617 13.306  7.889  1.00 16.07 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.537 13.840  7.199  1.00 17.89 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.556 17.287  8.711  1.00 13.74 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.547 17.482  9.739  1.00 14.30 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.317 18.117  9.135  1.00 15.23 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.428 18.913  8.185  1.00 16.20 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.083 18.277  10.916 1.00 16.07 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.676 19.644  10.559 1.00 16.79 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.722 20.828  10.394 1.00 17.43 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.050 21.785  9.649  1.00 18.62 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.621 20.818  10.989 1.00 16.96 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.165 17.827  9.716  1.00 15.20 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.910 18.389  9.236  1.00 14.94 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.963 18.583  10.402 1.00 14.68 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.451 17.599  10.968 1.00 14.51 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.322 17.488  8.132  1.00 17.26 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.046 17.981  7.492  1.00 20.63 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.209 18.555  8.208  1.00 22.39 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.850 17.729  6.297  1.00 24.30 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.737 19.831  10.815 1.00 14.79 ? 36  SER   A N   1 
ATOM   245  C  CA  . SER   A 1 30  ? 15.887 20.174  11.949 1.00 16.41 ? 36  SER   A CA  1 
ATOM   246  C  C   . SER   A 1 30  ? 14.429 19.748  11.714 1.00 17.28 ? 36  SER   A C   1 
ATOM   247  O  O   . SER   A 1 30  ? 13.790 19.225  12.654 1.00 17.15 ? 36  SER   A O   1 
ATOM   248  C  CB  . SER   A 1 30  ? 16.007 21.676  12.230 1.00 19.47 ? 36  SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 30  ? 15.164 22.063  13.304 1.00 21.84 ? 36  SER   A OG  1 
ATOM   250  N  N   . SER   A 1 31  ? 13.922 19.863  10.475 1.00 16.66 ? 37  SER   A N   1 
ATOM   251  C  CA  . SER   A 1 31  ? 12.549 19.448  10.203 1.00 17.38 ? 37  SER   A CA  1 
ATOM   252  C  C   . SER   A 1 31  ? 12.321 17.958  10.407 1.00 16.18 ? 37  SER   A C   1 
ATOM   253  O  O   . SER   A 1 31  ? 11.190 17.546  10.633 1.00 17.67 ? 37  SER   A O   1 
ATOM   254  C  CB  . SER   A 1 31  ? 12.105 19.855  8.799  1.00 19.47 ? 37  SER   A CB  1 
ATOM   255  O  OG  . SER   A 1 31  ? 12.648 19.058  7.766  1.00 25.10 ? 37  SER   A OG  1 
ATOM   256  N  N   . ARG   A 1 32  ? 13.377 17.142  10.330 1.00 15.03 ? 38  ARG   A N   1 
ATOM   257  C  CA  . ARG   A 1 32  ? 13.285 15.684  10.535 1.00 15.16 ? 38  ARG   A CA  1 
ATOM   258  C  C   . ARG   A 1 32  ? 13.754 15.246  11.936 1.00 14.61 ? 38  ARG   A C   1 
ATOM   259  O  O   . ARG   A 1 32  ? 13.660 14.047  12.260 1.00 13.49 ? 38  ARG   A O   1 
ATOM   260  C  CB  . ARG   A 1 32  ? 14.155 14.966  9.480  1.00 15.73 ? 38  ARG   A CB  1 
ATOM   261  C  CG  . ARG   A 1 32  ? 13.623 15.145  8.059  1.00 17.04 ? 38  ARG   A CG  1 
ATOM   262  C  CD  . ARG   A 1 32  ? 14.501 14.473  7.026  1.00 16.53 ? 38  ARG   A CD  1 
ATOM   263  N  NE  . ARG   A 1 32  ? 14.418 13.002  7.152  1.00 13.70 ? 38  ARG   A NE  1 
ATOM   264  C  CZ  . ARG   A 1 32  ? 14.575 12.167  6.129  1.00 14.26 ? 38  ARG   A CZ  1 
ATOM   265  N  NH1 . ARG   A 1 32  ? 14.842 12.633  4.912  1.00 17.63 ? 38  ARG   A NH1 1 
ATOM   266  N  NH2 . ARG   A 1 32  ? 14.443 10.849  6.309  1.00 14.83 ? 38  ARG   A NH2 1 
ATOM   267  N  N   . ASP   A 1 33  ? 14.328 16.151  12.760 1.00 13.47 ? 39  ASP   A N   1 
ATOM   268  C  CA  . ASP   A 1 33  ? 14.969 15.809  14.027 1.00 12.29 ? 39  ASP   A CA  1 
ATOM   269  C  C   . ASP   A 1 33  ? 16.108 14.791  13.853 1.00 12.70 ? 39  ASP   A C   1 
ATOM   270  O  O   . ASP   A 1 33  ? 16.316 13.943  14.727 1.00 12.65 ? 39  ASP   A O   1 
ATOM   271  C  CB  . ASP   A 1 33  ? 13.978 15.335  15.110 1.00 14.01 ? 39  ASP   A CB  1 
ATOM   272  C  CG  . ASP   A 1 33  ? 14.585 15.122  16.482 1.00 13.90 ? 39  ASP   A CG  1 
ATOM   273  O  OD1 . ASP   A 1 33  ? 15.455 15.931  16.922 1.00 14.17 ? 39  ASP   A OD1 1 
ATOM   274  O  OD2 . ASP   A 1 33  ? 14.184 14.133  17.178 1.00 15.10 ? 39  ASP   A OD2 1 
ATOM   275  N  N   . LEU   A 1 34  ? 16.905 14.936  12.762 1.00 12.48 ? 40  LEU   A N   1 
ATOM   276  C  CA  . LEU   A 1 34  ? 17.987 13.969  12.542 1.00 12.16 ? 40  LEU   A CA  1 
ATOM   277  C  C   . LEU   A 1 34  ? 19.332 14.691  12.384 1.00 11.85 ? 40  LEU   A C   1 
ATOM   278  O  O   . LEU   A 1 34  ? 19.405 15.800  11.798 1.00 12.64 ? 40  LEU   A O   1 
ATOM   279  C  CB  . LEU   A 1 34  ? 17.761 13.170  11.264 1.00 12.38 ? 40  LEU   A CB  1 
ATOM   280  C  CG  . LEU   A 1 34  ? 16.693 12.039  11.309 1.00 13.77 ? 40  LEU   A CG  1 
ATOM   281  C  CD1 . LEU   A 1 34  ? 16.623 11.344  9.969  1.00 13.86 ? 40  LEU   A CD1 1 
ATOM   282  C  CD2 . LEU   A 1 34  ? 16.947 11.033  12.456 1.00 13.95 ? 40  LEU   A CD2 1 
ATOM   283  N  N   . LEU   A 1 35  ? 20.387 14.040  12.844 1.00 11.24 ? 41  LEU   A N   1 
ATOM   284  C  CA  . LEU   A 1 35  ? 21.770 14.476  12.605 1.00 11.19 ? 41  LEU   A CA  1 
ATOM   285  C  C   . LEU   A 1 35  ? 22.610 13.243  12.442 1.00 10.65 ? 41  LEU   A C   1 
ATOM   286  O  O   . LEU   A 1 35  ? 22.436 12.228  13.156 1.00 11.17 ? 41  LEU   A O   1 
ATOM   287  C  CB  . LEU   A 1 35  ? 22.244 15.340  13.807 1.00 12.18 ? 41  LEU   A CB  1 
ATOM   288  C  CG  . LEU   A 1 35  ? 23.689 15.913  13.701 1.00 11.66 ? 41  LEU   A CG  1 
ATOM   289  C  CD1 . LEU   A 1 35  ? 23.770 17.280  14.375 1.00 13.62 ? 41  LEU   A CD1 1 
ATOM   290  C  CD2 . LEU   A 1 35  ? 24.724 14.989  14.342 1.00 12.55 ? 41  LEU   A CD2 1 
ATOM   291  N  N   . VAL   A 1 36  ? 23.588 13.323  11.516 1.00 11.34 ? 42  VAL   A N   1 
ATOM   292  C  CA  . VAL   A 1 36  ? 24.521 12.227  11.234 1.00 11.00 ? 42  VAL   A CA  1 
ATOM   293  C  C   . VAL   A 1 36  ? 25.931 12.750  11.380 1.00 10.65 ? 42  VAL   A C   1 
ATOM   294  O  O   . VAL   A 1 36  ? 26.253 13.794  10.794 1.00 11.71 ? 42  VAL   A O   1 
ATOM   295  C  CB  . VAL   A 1 36  ? 24.292 11.637  9.823  1.00 10.88 ? 42  VAL   A CB  1 
ATOM   296  C  CG1 . VAL   A 1 36  ? 25.309 10.527  9.532  1.00 12.89 ? 42  VAL   A CG1 1 
ATOM   297  C  CG2 . VAL   A 1 36  ? 22.842 11.110  9.684  1.00 12.31 ? 42  VAL   A CG2 1 
ATOM   298  N  N   . SER   A 1 37  ? 26.743 12.078  12.166 1.00 10.74 ? 43  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 37  ? 28.176 12.389  12.342 1.00 11.10 ? 43  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 37  ? 29.043 11.241  11.869 1.00 11.57 ? 43  SER   A C   1 
ATOM   301  O  O   . SER   A 1 37  ? 28.560 10.095  11.675 1.00 12.16 ? 43  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 37  ? 28.477 12.765  13.787 1.00 12.44 ? 43  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 37  ? 28.150 11.706  14.687 1.00 12.45 ? 43  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 38  ? 30.346 11.502  11.641 1.00 12.19 ? 44  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 38  ? 31.254 10.452  11.208 1.00 13.36 ? 44  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 38  ? 31.901 9.739   12.402 1.00 15.37 ? 44  SER   A C   1 
ATOM   307  O  O   . SER   A 1 38  ? 32.104 10.356  13.485 1.00 17.94 ? 44  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 38  ? 32.340 11.068  10.329 1.00 15.75 ? 44  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 38  ? 33.068 12.047  11.064 1.00 17.92 ? 44  SER   A OG  1 
ATOM   310  N  N   . THR   A 1 39  ? 32.260 8.440   12.218 1.00 15.05 ? 45  THR   A N   1 
ATOM   311  C  CA  . THR   A 1 39  ? 32.828 7.639   13.302 1.00 16.87 ? 45  THR   A CA  1 
ATOM   312  C  C   . THR   A 1 39  ? 34.166 7.057   12.859 1.00 19.01 ? 45  THR   A C   1 
ATOM   313  O  O   . THR   A 1 39  ? 34.394 6.813   11.668 1.00 18.80 ? 45  THR   A O   1 
ATOM   314  C  CB  . THR   A 1 39  ? 31.899 6.448   13.690 1.00 17.38 ? 45  THR   A CB  1 
ATOM   315  O  OG1 . THR   A 1 39  ? 31.792 5.544   12.595 1.00 17.91 ? 45  THR   A OG1 1 
ATOM   316  C  CG2 . THR   A 1 39  ? 30.483 6.913   14.087 1.00 17.97 ? 45  THR   A CG2 1 
ATOM   317  N  N   . THR   A 1 40  ? 35.033 6.792   13.848 1.00 19.92 ? 46  THR   A N   1 
ATOM   318  C  CA  . THR   A 1 40  ? 36.312 6.157   13.546 1.00 21.55 ? 46  THR   A CA  1 
ATOM   319  C  C   . THR   A 1 40  ? 36.092 4.638   13.358 1.00 21.14 ? 46  THR   A C   1 
ATOM   320  O  O   . THR   A 1 40  ? 36.611 4.061   12.394 1.00 22.80 ? 46  THR   A O   1 
ATOM   321  C  CB  . THR   A 1 40  ? 37.323 6.490   14.649 1.00 25.92 ? 46  THR   A CB  1 
ATOM   322  O  OG1 . THR   A 1 40  ? 36.846 5.989   15.875 1.00 31.35 ? 46  THR   A OG1 1 
ATOM   323  C  CG2 . THR   A 1 40  ? 37.525 7.973   14.800 1.00 26.56 ? 46  THR   A CG2 1 
ATOM   324  N  N   . ALA   A 1 41  ? 35.272 4.024   14.233 1.00 20.45 ? 47  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 41  ? 34.993 2.572   14.140 1.00 21.69 ? 47  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 41  ? 33.796 2.260   13.215 1.00 20.66 ? 47  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 41  ? 32.840 3.041   13.200 1.00 20.10 ? 47  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 41  ? 34.681 2.022   15.522 1.00 24.56 ? 47  ALA   A CB  1 
ATOM   329  N  N   . GLN   A 1 42  ? 33.791 1.121   12.530 1.00 18.23 ? 48  GLN   A N   1 
ATOM   330  C  CA  . GLN   A 1 42  ? 32.671 0.703   11.672 1.00 18.98 ? 48  GLN   A CA  1 
ATOM   331  C  C   . GLN   A 1 42  ? 31.564 0.125   12.533 1.00 19.21 ? 48  GLN   A C   1 
ATOM   332  O  O   . GLN   A 1 42  ? 31.816 -0.648  13.470 1.00 20.93 ? 48  GLN   A O   1 
ATOM   333  C  CB  . GLN   A 1 42  ? 33.133 -0.344  10.649 1.00 21.95 ? 48  GLN   A CB  1 
ATOM   334  C  CG  . GLN   A 1 42  ? 34.065 0.235   9.551  1.00 27.80 ? 48  GLN   A CG  1 
ATOM   335  C  CD  . GLN   A 1 42  ? 34.385 -0.821  8.535  1.00 34.78 ? 48  GLN   A CD  1 
ATOM   336  O  OE1 . GLN   A 1 42  ? 35.264 -1.659  8.746  1.00 33.21 ? 48  GLN   A OE1 1 
ATOM   337  N  NE2 . GLN   A 1 42  ? 33.632 -0.828  7.439  1.00 38.71 ? 48  GLN   A NE2 1 
ATOM   338  N  N   . GLY   A 1 43  ? 30.325 0.463   12.192 1.00 16.57 ? 49  GLY   A N   1 
ATOM   339  C  CA  . GLY   A 1 43  ? 29.166 -0.047  12.920 1.00 15.97 ? 49  GLY   A CA  1 
ATOM   340  C  C   . GLY   A 1 43  ? 28.566 -1.310  12.326 1.00 15.00 ? 49  GLY   A C   1 
ATOM   341  O  O   . GLY   A 1 43  ? 28.871 -1.684  11.183 1.00 15.75 ? 49  GLY   A O   1 
ATOM   342  N  N   . CYS   A 1 44  ? 27.642 -1.928  13.108 1.00 14.53 ? 50  CYS   A N   1 
ATOM   343  C  CA  . CYS   A 1 44  ? 27.034 -3.220  12.727 1.00 14.75 ? 50  CYS   A CA  1 
ATOM   344  C  C   . CYS   A 1 44  ? 25.572 -3.154  12.302 1.00 14.83 ? 50  CYS   A C   1 
ATOM   345  O  O   . CYS   A 1 44  ? 25.020 -4.193  11.911 1.00 15.76 ? 50  CYS   A O   1 
ATOM   346  C  CB  . CYS   A 1 44  ? 27.197 -4.245  13.855 1.00 15.97 ? 50  CYS   A CB  1 
ATOM   347  S  SG  . CYS   A 1 44  ? 28.905 -4.664  14.237 1.00 19.05 ? 50  CYS   A SG  1 
ATOM   348  N  N   . ASP   A 1 45  ? 24.912 -2.007  12.451 1.00 13.46 ? 51  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 45  ? 23.515 -1.902  12.029 1.00 12.99 ? 51  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 45  ? 23.444 -1.832  10.511 1.00 13.66 ? 51  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 45  ? 24.356 -1.278  9.860  1.00 15.47 ? 51  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 45  ? 22.885 -0.659  12.646 1.00 12.52 ? 51  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 45  ? 22.791 -0.713  14.164 1.00 13.47 ? 51  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 45  ? 22.440 -1.819  14.709 1.00 13.69 ? 51  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 45  ? 22.977 0.352   14.823 1.00 14.02 ? 51  ASP   A OD2 1 
ATOM   356  N  N   . THR   A 1 46  ? 22.385 -2.358  9.934  1.00 15.14 ? 52  THR   A N   1 
ATOM   357  C  CA  . THR   A 1 46  ? 22.110 -2.222  8.495  1.00 16.16 ? 52  THR   A CA  1 
ATOM   358  C  C   . THR   A 1 46  ? 20.742 -1.518  8.324  1.00 15.61 ? 52  THR   A C   1 
ATOM   359  O  O   . THR   A 1 46  ? 19.840 -1.667  9.164  1.00 16.20 ? 52  THR   A O   1 
ATOM   360  C  CB  . THR   A 1 46  ? 22.067 -3.576  7.830  1.00 20.69 ? 52  THR   A CB  1 
ATOM   361  O  OG1 . THR   A 1 46  ? 21.026 -4.303  8.435  1.00 24.41 ? 52  THR   A OG1 1 
ATOM   362  C  CG2 . THR   A 1 46  ? 23.432 -4.303  7.957  1.00 21.84 ? 52  THR   A CG2 1 
ATOM   363  N  N   . ILE   A 1 47  ? 20.626 -0.702  7.295  1.00 14.52 ? 53  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 47  ? 19.397 0.049   7.039  1.00 13.87 ? 53  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 47  ? 18.422 -0.710  6.162  1.00 14.17 ? 53  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 47  ? 18.802 -1.261  5.109  1.00 15.07 ? 53  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 47  ? 19.723 1.451   6.439  1.00 13.41 ? 53  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 47  ? 20.820 2.181   7.221  1.00 13.98 ? 53  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 47  ? 18.452 2.317   6.296  1.00 12.89 ? 53  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 47  ? 20.444 2.498   8.722  1.00 15.24 ? 53  ILE   A CD1 1 
ATOM   371  N  N   . ALA   A 1 48  ? 17.168 -0.763  6.558  1.00 12.81 ? 54  ALA   A N   1 
ATOM   372  C  CA  . ALA   A 1 48  ? 16.094 -1.350  5.752  1.00 13.20 ? 54  ALA   A CA  1 
ATOM   373  C  C   . ALA   A 1 48  ? 15.824 -0.496  4.499  1.00 14.20 ? 54  ALA   A C   1 
ATOM   374  O  O   . ALA   A 1 48  ? 15.837 0.753   4.546  1.00 14.37 ? 54  ALA   A O   1 
ATOM   375  C  CB  . ALA   A 1 48  ? 14.817 -1.384  6.597  1.00 12.39 ? 54  ALA   A CB  1 
ATOM   376  N  N   . ARG   A 1 49  ? 15.575 -1.175  3.359  1.00 15.88 ? 55  ARG   A N   1 
ATOM   377  C  CA  . ARG   A 1 49  ? 15.247 -0.495  2.099  1.00 17.08 ? 55  ARG   A CA  1 
ATOM   378  C  C   . ARG   A 1 49  ? 13.938 -1.126  1.619  1.00 19.62 ? 55  ARG   A C   1 
ATOM   379  O  O   . ARG   A 1 49  ? 13.969 -2.128  0.912  1.00 21.19 ? 55  ARG   A O   1 
ATOM   380  C  CB  . ARG   A 1 49  ? 16.441 -0.627  1.091  1.00 17.86 ? 55  ARG   A CB  1 
ATOM   381  C  CG  . ARG   A 1 49  ? 17.768 -0.038  1.599  1.00 18.34 ? 55  ARG   A CG  1 
ATOM   382  C  CD  . ARG   A 1 49  ? 17.766 1.483   1.865  1.00 17.08 ? 55  ARG   A CD  1 
ATOM   383  N  NE  . ARG   A 1 49  ? 19.100 1.936   2.362  1.00 16.81 ? 55  ARG   A NE  1 
ATOM   384  C  CZ  . ARG   A 1 49  ? 19.331 3.080   2.997  1.00 17.55 ? 55  ARG   A CZ  1 
ATOM   385  N  NH1 . ARG   A 1 49  ? 18.356 3.963   3.177  1.00 16.89 ? 55  ARG   A NH1 1 
ATOM   386  N  NH2 . ARG   A 1 49  ? 20.549 3.359   3.455  1.00 17.92 ? 55  ARG   A NH2 1 
ATOM   387  N  N   . CYS   A 1 50  ? 12.794 -0.530  2.038  1.00 18.85 ? 56  CYS   A N   1 
ATOM   388  C  CA  . CYS   A 1 50  ? 11.448 -1.145  1.931  1.00 19.05 ? 56  CYS   A CA  1 
ATOM   389  C  C   . CYS   A 1 50  ? 10.331 -0.135  2.283  1.00 19.25 ? 56  CYS   A C   1 
ATOM   390  O  O   . CYS   A 1 50  ? 10.558 1.009   2.682  1.00 21.34 ? 56  CYS   A O   1 
ATOM   391  C  CB  . CYS   A 1 50  ? 11.422 -2.305  2.919  1.00 18.07 ? 56  CYS   A CB  1 
ATOM   392  S  SG  . CYS   A 1 50  ? 11.379 -1.748  4.652  1.00 17.66 ? 56  CYS   A SG  1 
ATOM   393  N  N   . ASP   A 1 51  ? 9.033  -0.613  2.197  1.00 21.06 ? 57  ASP   A N   1 
ATOM   394  C  CA  . ASP   A 1 51  ? 7.887  0.188   2.608  1.00 23.52 ? 57  ASP   A CA  1 
ATOM   395  C  C   . ASP   A 1 51  ? 7.112  -0.580  3.680  1.00 22.92 ? 57  ASP   A C   1 
ATOM   396  O  O   . ASP   A 1 51  ? 5.891  -0.403  3.778  1.00 24.57 ? 57  ASP   A O   1 
ATOM   397  C  CB  . ASP   A 1 51  ? 6.952  0.576   1.435  1.00 29.04 ? 57  ASP   A CB  1 
ATOM   398  C  CG  . ASP   A 1 51  ? 6.320  -0.594  0.740  1.00 37.53 ? 57  ASP   A CG  1 
ATOM   399  O  OD1 . ASP   A 1 51  ? 6.666  -1.758  1.086  1.00 38.24 ? 57  ASP   A OD1 1 
ATOM   400  O  OD2 . ASP   A 1 51  ? 5.496  -0.363  -0.190 1.00 43.32 ? 57  ASP   A OD2 1 
ATOM   401  N  N   . CYS   A 1 52  ? 7.799  -1.391  4.544  1.00 19.17 ? 58  CYS   A N   1 
ATOM   402  C  CA  . CYS   A 1 52  ? 7.128  -2.059  5.697  1.00 17.27 ? 58  CYS   A CA  1 
ATOM   403  C  C   . CYS   A 1 52  ? 6.383  -1.037  6.532  1.00 17.89 ? 58  CYS   A C   1 
ATOM   404  O  O   . CYS   A 1 52  ? 6.847  0.100   6.734  1.00 17.49 ? 58  CYS   A O   1 
ATOM   405  C  CB  . CYS   A 1 52  ? 8.131  -2.790  6.584  1.00 18.43 ? 58  CYS   A CB  1 
ATOM   406  S  SG  . CYS   A 1 52  ? 8.852  -4.314  5.895  1.00 19.34 ? 58  CYS   A SG  1 
ATOM   407  N  N   . GLN   A 1 53  ? 5.276  -1.485  7.081  1.00 16.10 ? 59  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 53  ? 4.486  -0.744  8.048  1.00 15.53 ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.267  -1.560  9.310  1.00 14.02 ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.407  -1.196  10.087 1.00 14.09 ? 59  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 53  ? 3.117  -0.260  7.489  1.00 17.92 ? 59  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 53  ? 3.245  0.888   6.489  1.00 21.75 ? 59  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 53  ? 1.845  1.378   6.095  1.00 26.32 ? 59  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 53  ? 1.367  1.185   4.962  1.00 29.04 ? 59  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 53  ? 1.142  2.043   7.017  1.00 21.70 ? 59  GLN   A NE2 1 
ATOM   416  N  N   . THR   A 1 54  ? 5.034  -2.649  9.516  1.00 13.31 ? 60  THR   A N   1 
ATOM   417  C  CA  . THR   A 1 54  ? 5.057  -3.375  10.764 1.00 13.40 ? 60  THR   A CA  1 
ATOM   418  C  C   . THR   A 1 54  ? 6.517  -3.607  11.176 1.00 12.66 ? 60  THR   A C   1 
ATOM   419  O  O   . THR   A 1 54  ? 7.380  -3.790  10.304 1.00 13.87 ? 60  THR   A O   1 
ATOM   420  C  CB  . THR   A 1 54  ? 4.304  -4.682  10.750 1.00 16.67 ? 60  THR   A CB  1 
ATOM   421  O  OG1 . THR   A 1 54  ? 4.940  -5.575  9.895  1.00 22.40 ? 60  THR   A OG1 1 
ATOM   422  C  CG2 . THR   A 1 54  ? 2.864  -4.554  10.308 1.00 16.15 ? 60  THR   A CG2 1 
ATOM   423  N  N   . GLY   A 1 55  ? 6.773  -3.564  12.456 1.00 11.79 ? 61  GLY   A N   1 
ATOM   424  C  CA  . GLY   A 1 55  ? 8.139  -3.718  12.957 1.00 11.28 ? 61  GLY   A CA  1 
ATOM   425  C  C   . GLY   A 1 55  ? 8.143  -3.786  14.464 1.00 10.69 ? 61  GLY   A C   1 
ATOM   426  O  O   . GLY   A 1 55  ? 7.113  -4.046  15.085 1.00 11.45 ? 61  GLY   A O   1 
ATOM   427  N  N   . VAL   A 1 56  ? 9.325  -3.588  15.063 1.00 10.50 ? 62  VAL   A N   1 
ATOM   428  C  CA  . VAL   A 1 56  ? 9.502  -3.668  16.508 1.00 9.85  ? 62  VAL   A CA  1 
ATOM   429  C  C   . VAL   A 1 56  ? 10.351 -2.482  16.931 1.00 9.79  ? 62  VAL   A C   1 
ATOM   430  O  O   . VAL   A 1 56  ? 11.348 -2.181  16.265 1.00 10.70 ? 62  VAL   A O   1 
ATOM   431  C  CB  . VAL   A 1 56  ? 10.240 -5.001  16.838 1.00 11.20 ? 62  VAL   A CB  1 
ATOM   432  C  CG1 . VAL   A 1 56  ? 10.639 -5.109  18.300 1.00 14.09 ? 62  VAL   A CG1 1 
ATOM   433  C  CG2 . VAL   A 1 56  ? 9.355  -6.189  16.477 1.00 11.83 ? 62  VAL   A CG2 1 
ATOM   434  N  N   . TYR   A 1 57  ? 9.978  -1.823  18.050 1.00 9.36  ? 63  TYR   A N   1 
ATOM   435  C  CA  . TYR   A 1 57  ? 10.828 -0.726  18.560 1.00 9.57  ? 63  TYR   A CA  1 
ATOM   436  C  C   . TYR   A 1 57  ? 11.270 -0.968  20.002 1.00 9.42  ? 63  TYR   A C   1 
ATOM   437  O  O   . TYR   A 1 57  ? 10.581 -1.640  20.769 1.00 9.98  ? 63  TYR   A O   1 
ATOM   438  C  CB  . TYR   A 1 57  ? 10.129 0.690   18.429 1.00 9.91  ? 63  TYR   A CB  1 
ATOM   439  C  CG  . TYR   A 1 57  ? 9.135  1.009   19.524 1.00 10.03 ? 63  TYR   A CG  1 
ATOM   440  C  CD1 . TYR   A 1 57  ? 7.851  0.478   19.493 1.00 10.55 ? 63  TYR   A CD1 1 
ATOM   441  C  CD2 . TYR   A 1 57  ? 9.451  1.890   20.564 1.00 10.32 ? 63  TYR   A CD2 1 
ATOM   442  C  CE1 . TYR   A 1 57  ? 6.927  0.757   20.503 1.00 11.55 ? 63  TYR   A CE1 1 
ATOM   443  C  CE2 . TYR   A 1 57  ? 8.496  2.232   21.537 1.00 11.54 ? 63  TYR   A CE2 1 
ATOM   444  C  CZ  . TYR   A 1 57  ? 7.251  1.650   21.492 1.00 12.47 ? 63  TYR   A CZ  1 
ATOM   445  O  OH  . TYR   A 1 57  ? 6.241  1.850   22.453 1.00 14.40 ? 63  TYR   A OH  1 
ATOM   446  N  N   . TYR   A 1 58  ? 12.395 -0.352  20.375 1.00 9.74  ? 64  TYR   A N   1 
ATOM   447  C  CA  . TYR   A 1 58  ? 12.891 -0.403  21.741 1.00 9.94  ? 64  TYR   A CA  1 
ATOM   448  C  C   . TYR   A 1 58  ? 12.407 0.796   22.548 1.00 10.34 ? 64  TYR   A C   1 
ATOM   449  O  O   . TYR   A 1 58  ? 12.632 1.948   22.155 1.00 10.11 ? 64  TYR   A O   1 
ATOM   450  C  CB  . TYR   A 1 58  ? 14.442 -0.473  21.781 1.00 10.62 ? 64  TYR   A CB  1 
ATOM   451  C  CG  . TYR   A 1 58  ? 14.939 -0.632  23.195 1.00 10.50 ? 64  TYR   A CG  1 
ATOM   452  C  CD1 . TYR   A 1 58  ? 14.601 -1.742  23.941 1.00 11.52 ? 64  TYR   A CD1 1 
ATOM   453  C  CD2 . TYR   A 1 58  ? 15.650 0.399   23.832 1.00 11.45 ? 64  TYR   A CD2 1 
ATOM   454  C  CE1 . TYR   A 1 58  ? 14.993 -1.857  25.280 1.00 12.43 ? 64  TYR   A CE1 1 
ATOM   455  C  CE2 . TYR   A 1 58  ? 16.044 0.292   25.159 1.00 12.61 ? 64  TYR   A CE2 1 
ATOM   456  C  CZ  . TYR   A 1 58  ? 15.734 -0.851  25.866 1.00 12.94 ? 64  TYR   A CZ  1 
ATOM   457  O  OH  . TYR   A 1 58  ? 16.101 -0.978  27.207 1.00 16.41 ? 64  TYR   A OH  1 
ATOM   458  N  N   . CYS   A 1 59  ? 11.828 0.478   23.703 1.00 9.91  ? 65  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 59  ? 11.265 1.456   24.668 1.00 10.73 ? 65  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 59  ? 12.112 1.434   25.958 1.00 10.87 ? 65  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 59  ? 11.922 0.533   26.813 1.00 11.00 ? 65  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 59  ? 9.813  1.122   24.933 1.00 9.95  ? 65  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 59  ? 9.052  2.212   26.168 1.00 11.76 ? 65  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 60  ? 13.016 2.415   26.120 1.00 10.86 ? 66  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 60  ? 13.892 2.402   27.323 1.00 11.74 ? 66  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 60  ? 13.128 2.590   28.632 1.00 12.00 ? 66  SER   A C   1 
ATOM   467  O  O   . SER   A 1 60  ? 13.544 2.015   29.645 1.00 13.95 ? 66  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 60  ? 15.009 3.438   27.187 1.00 13.81 ? 66  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 60  ? 14.582 4.781   27.290 1.00 14.66 ? 66  SER   A OG  1 
ATOM   470  N  N   . SER   A 1 61  ? 11.987 3.330   28.591 1.00 10.73 ? 67  SER   A N   1 
ATOM   471  C  CA  . SER   A 1 61  ? 11.192 3.527   29.798 1.00 11.41 ? 67  SER   A CA  1 
ATOM   472  C  C   . SER   A 1 61  ? 10.399 2.305   30.234 1.00 12.13 ? 67  SER   A C   1 
ATOM   473  O  O   . SER   A 1 61  ? 9.739  2.347   31.282 1.00 12.04 ? 67  SER   A O   1 
ATOM   474  C  CB  . SER   A 1 61  ? 10.274 4.729   29.637 1.00 11.58 ? 67  SER   A CB  1 
ATOM   475  O  OG  . SER   A 1 61  ? 9.276  4.496   28.653 1.00 12.37 ? 67  SER   A OG  1 
ATOM   476  N  N   . ARG   A 1 62  ? 10.508 1.199   29.503 1.00 11.46 ? 68  ARG   A N   1 
ATOM   477  C  CA  . ARG   A 1 62  ? 9.942  -0.106  29.882 1.00 12.23 ? 68  ARG   A CA  1 
ATOM   478  C  C   . ARG   A 1 62  ? 11.001 -1.221  29.818 1.00 13.29 ? 68  ARG   A C   1 
ATOM   479  O  O   . ARG   A 1 62  ? 10.675 -2.386  30.112 1.00 13.55 ? 68  ARG   A O   1 
ATOM   480  C  CB  . ARG   A 1 62  ? 8.755  -0.445  28.955 1.00 12.43 ? 68  ARG   A CB  1 
ATOM   481  C  CG  . ARG   A 1 62  ? 7.562  0.503   29.103 1.00 12.26 ? 68  ARG   A CG  1 
ATOM   482  C  CD  . ARG   A 1 62  ? 6.826  0.169   30.395 1.00 12.48 ? 68  ARG   A CD  1 
ATOM   483  N  NE  . ARG   A 1 62  ? 5.653  1.045   30.561 1.00 14.40 ? 68  ARG   A NE  1 
ATOM   484  C  CZ  . ARG   A 1 62  ? 5.668  2.207   31.201 1.00 13.63 ? 68  ARG   A CZ  1 
ATOM   485  N  NH1 . ARG   A 1 62  ? 6.805  2.681   31.717 1.00 14.76 ? 68  ARG   A NH1 1 
ATOM   486  N  NH2 . ARG   A 1 62  ? 4.543  2.913   31.341 1.00 15.78 ? 68  ARG   A NH2 1 
ATOM   487  N  N   . ARG   A 1 63  ? 12.222 -0.943  29.340 1.00 14.20 ? 69  ARG   A N   1 
ATOM   488  C  CA  . ARG   A 1 63  ? 13.237 -1.979  29.047 1.00 14.83 ? 69  ARG   A CA  1 
ATOM   489  C  C   . ARG   A 1 63  ? 12.653 -3.106  28.179 1.00 16.36 ? 69  ARG   A C   1 
ATOM   490  O  O   . ARG   A 1 63  ? 12.870 -4.312  28.450 1.00 18.47 ? 69  ARG   A O   1 
ATOM   491  C  CB  . ARG   A 1 63  ? 13.852 -2.596  30.320 1.00 18.36 ? 69  ARG   A CB  1 
ATOM   492  C  CG  . ARG   A 1 63  ? 14.788 -1.676  30.935 1.00 19.32 ? 69  ARG   A CG  1 
ATOM   493  C  CD  . ARG   A 1 63  ? 15.524 -2.510  31.978 1.00 20.92 ? 69  ARG   A CD  1 
ATOM   494  N  NE  . ARG   A 1 63  ? 16.289 -1.583  32.772 1.00 21.87 ? 69  ARG   A NE  1 
ATOM   495  C  CZ  . ARG   A 1 63  ? 15.963 -1.177  33.996 1.00 17.02 ? 69  ARG   A CZ  1 
ATOM   496  N  NH1 . ARG   A 1 63  ? 14.906 -1.696  34.622 1.00 19.16 ? 69  ARG   A NH1 1 
ATOM   497  N  NH2 . ARG   A 1 63  ? 16.718 -0.289  34.624 1.00 19.37 ? 69  ARG   A NH2 1 
ATOM   498  N  N   . LYS   A 1 64  ? 11.846 -2.754  27.191 1.00 13.45 ? 70  LYS   A N   1 
ATOM   499  C  CA  . LYS   A 1 64  ? 11.164 -3.751  26.375 1.00 14.08 ? 70  LYS   A CA  1 
ATOM   500  C  C   . LYS   A 1 64  ? 11.126 -3.353  24.926 1.00 12.77 ? 70  LYS   A C   1 
ATOM   501  O  O   . LYS   A 1 64  ? 11.070 -2.154  24.594 1.00 12.44 ? 70  LYS   A O   1 
ATOM   502  C  CB  . LYS   A 1 64  ? 9.694  -3.891  26.892 1.00 16.70 ? 70  LYS   A CB  1 
ATOM   503  C  CG  . LYS   A 1 64  ? 9.561  -4.808  28.113 1.00 25.34 ? 70  LYS   A CG  1 
ATOM   504  C  CD  . LYS   A 1 64  ? 8.120  -5.101  28.478 1.00 33.76 ? 70  LYS   A CD  1 
ATOM   505  C  CE  . LYS   A 1 64  ? 8.028  -5.960  29.723 1.00 39.14 ? 70  LYS   A CE  1 
ATOM   506  N  NZ  . LYS   A 1 64  ? 8.702  -5.329  30.904 1.00 42.74 ? 70  LYS   A NZ  1 
ATOM   507  N  N   . HIS   A 1 65  ? 11.082 -4.353  24.057 1.00 12.64 ? 71  HIS   A N   1 
ATOM   508  C  CA  . HIS   A 1 65  ? 10.843 -4.194  22.622 1.00 11.66 ? 71  HIS   A CA  1 
ATOM   509  C  C   . HIS   A 1 65  ? 9.397  -4.520  22.368 1.00 12.62 ? 71  HIS   A C   1 
ATOM   510  O  O   . HIS   A 1 65  ? 8.904  -5.586  22.796 1.00 16.51 ? 71  HIS   A O   1 
ATOM   511  C  CB  . HIS   A 1 65  ? 11.756 -5.140  21.794 1.00 11.37 ? 71  HIS   A CB  1 
ATOM   512  C  CG  . HIS   A 1 65  ? 13.234 -4.815  21.929 1.00 12.08 ? 71  HIS   A CG  1 
ATOM   513  N  ND1 . HIS   A 1 65  ? 13.961 -4.131  20.964 1.00 15.40 ? 71  HIS   A ND1 1 
ATOM   514  C  CD2 . HIS   A 1 65  ? 14.066 -5.139  22.953 1.00 13.07 ? 71  HIS   A CD2 1 
ATOM   515  C  CE1 . HIS   A 1 65  ? 15.239 -4.106  21.416 1.00 13.63 ? 71  HIS   A CE1 1 
ATOM   516  N  NE2 . HIS   A 1 65  ? 15.326 -4.686  22.584 1.00 16.06 ? 71  HIS   A NE2 1 
ATOM   517  N  N   . TYR   A 1 66  ? 8.692  -3.680  21.600 1.00 10.78 ? 72  TYR   A N   1 
ATOM   518  C  CA  . TYR   A 1 66  ? 7.275  -3.883  21.308 1.00 11.14 ? 72  TYR   A CA  1 
ATOM   519  C  C   . TYR   A 1 66  ? 7.025  -3.979  19.833 1.00 11.06 ? 72  TYR   A C   1 
ATOM   520  O  O   . TYR   A 1 66  ? 7.531  -3.128  19.075 1.00 10.75 ? 72  TYR   A O   1 
ATOM   521  C  CB  . TYR   A 1 66  ? 6.430  -2.667  21.829 1.00 11.94 ? 72  TYR   A CB  1 
ATOM   522  C  CG  . TYR   A 1 66  ? 6.391  -2.523  23.347 1.00 12.28 ? 72  TYR   A CG  1 
ATOM   523  C  CD1 . TYR   A 1 66  ? 5.611  -3.377  24.125 1.00 13.38 ? 72  TYR   A CD1 1 
ATOM   524  C  CD2 . TYR   A 1 66  ? 7.121  -1.532  23.982 1.00 12.47 ? 72  TYR   A CD2 1 
ATOM   525  C  CE1 . TYR   A 1 66  ? 5.541  -3.248  25.505 1.00 14.16 ? 72  TYR   A CE1 1 
ATOM   526  C  CE2 . TYR   A 1 66  ? 7.039  -1.364  25.371 1.00 14.06 ? 72  TYR   A CE2 1 
ATOM   527  C  CZ  . TYR   A 1 66  ? 6.263  -2.241  26.121 1.00 14.94 ? 72  TYR   A CZ  1 
ATOM   528  O  OH  . TYR   A 1 66  ? 6.188  -2.041  27.491 1.00 16.64 ? 72  TYR   A OH  1 
ATOM   529  N  N   . PRO   A 1 67  ? 6.190  -4.933  19.399 1.00 11.17 ? 73  PRO   A N   1 
ATOM   530  C  CA  . PRO   A 1 67  ? 5.763  -4.955  17.991 1.00 11.39 ? 73  PRO   A CA  1 
ATOM   531  C  C   . PRO   A 1 67  ? 4.736  -3.863  17.703 1.00 12.77 ? 73  PRO   A C   1 
ATOM   532  O  O   . PRO   A 1 67  ? 3.809  -3.686  18.531 1.00 16.24 ? 73  PRO   A O   1 
ATOM   533  C  CB  . PRO   A 1 67  ? 5.170  -6.369  17.789 1.00 13.76 ? 73  PRO   A CB  1 
ATOM   534  C  CG  . PRO   A 1 67  ? 4.758  -6.800  19.178 1.00 14.80 ? 73  PRO   A CG  1 
ATOM   535  C  CD  . PRO   A 1 67  ? 5.629  -6.044  20.198 1.00 11.94 ? 73  PRO   A CD  1 
ATOM   536  N  N   . VAL   A 1 68  ? 4.861  -3.199  16.589 1.00 10.44 ? 74  VAL   A N   1 
ATOM   537  C  CA  . VAL   A 1 68  ? 3.948  -2.095  16.238 1.00 12.76 ? 74  VAL   A CA  1 
ATOM   538  C  C   . VAL   A 1 68  ? 3.592  -2.101  14.778 1.00 12.82 ? 74  VAL   A C   1 
ATOM   539  O  O   . VAL   A 1 68  ? 4.386  -2.476  13.931 1.00 12.14 ? 74  VAL   A O   1 
ATOM   540  C  CB  . VAL   A 1 68  ? 4.507  -0.716  16.605 1.00 16.19 ? 74  VAL   A CB  1 
ATOM   541  C  CG1 . VAL   A 1 68  ? 4.473  -0.525  18.125 1.00 18.28 ? 74  VAL   A CG1 1 
ATOM   542  C  CG2 . VAL   A 1 68  ? 5.895  -0.505  16.034 1.00 16.49 ? 74  VAL   A CG2 1 
ATOM   543  N  N   . SER   A 1 69  ? 2.402  -1.550  14.448 1.00 12.38 ? 75  SER   A N   1 
ATOM   544  C  CA  . SER   A 1 69  ? 2.023  -1.113  13.105 1.00 12.39 ? 75  SER   A CA  1 
ATOM   545  C  C   . SER   A 1 69  ? 2.253  0.397   13.051 1.00 11.66 ? 75  SER   A C   1 
ATOM   546  O  O   . SER   A 1 69  ? 1.885  1.096   14.017 1.00 13.02 ? 75  SER   A O   1 
ATOM   547  C  CB  . SER   A 1 69  ? 0.540  -1.360  12.884 1.00 16.40 ? 75  SER   A CB  1 
ATOM   548  O  OG  . SER   A 1 69  ? 0.314  -2.756  12.874 1.00 23.58 ? 75  SER   A OG  1 
ATOM   549  N  N   . PHE   A 1 70  ? 2.811  0.920   11.976 1.00 12.24 ? 76  PHE   A N   1 
ATOM   550  C  CA  . PHE   A 1 70  ? 3.124  2.343   11.920 1.00 12.96 ? 76  PHE   A CA  1 
ATOM   551  C  C   . PHE   A 1 70  ? 2.723  2.932   10.588 1.00 14.20 ? 76  PHE   A C   1 
ATOM   552  O  O   . PHE   A 1 70  ? 2.649  2.229   9.567  1.00 14.72 ? 76  PHE   A O   1 
ATOM   553  C  CB  . PHE   A 1 70  ? 4.632  2.606   12.275 1.00 13.24 ? 76  PHE   A CB  1 
ATOM   554  C  CG  . PHE   A 1 70  ? 5.655  1.816   11.468 1.00 12.02 ? 76  PHE   A CG  1 
ATOM   555  C  CD1 . PHE   A 1 70  ? 6.079  0.555   11.882 1.00 12.24 ? 76  PHE   A CD1 1 
ATOM   556  C  CD2 . PHE   A 1 70  ? 6.240  2.353   10.331 1.00 12.49 ? 76  PHE   A CD2 1 
ATOM   557  C  CE1 . PHE   A 1 70  ? 7.007  -0.157  11.153 1.00 12.33 ? 76  PHE   A CE1 1 
ATOM   558  C  CE2 . PHE   A 1 70  ? 7.185  1.619   9.594  1.00 13.25 ? 76  PHE   A CE2 1 
ATOM   559  C  CZ  . PHE   A 1 70  ? 7.557  0.364   10.013 1.00 12.50 ? 76  PHE   A CZ  1 
ATOM   560  N  N   . SER   A 1 71  ? 2.432  4.239   10.574 1.00 14.29 ? 77  SER   A N   1 
ATOM   561  C  CA  . SER   A 1 71  ? 2.040  4.927   9.356  1.00 14.66 ? 77  SER   A CA  1 
ATOM   562  C  C   . SER   A 1 71  ? 3.224  5.149   8.391  1.00 15.28 ? 77  SER   A C   1 
ATOM   563  O  O   . SER   A 1 71  ? 4.404  5.032   8.779  1.00 14.59 ? 77  SER   A O   1 
ATOM   564  C  CB  . SER   A 1 71  ? 1.337  6.257   9.698  1.00 16.57 ? 77  SER   A CB  1 
ATOM   565  O  OG  . SER   A 1 71  ? 2.215  7.136   10.389 1.00 18.21 ? 77  SER   A OG  1 
ATOM   566  N  N   . LYS   A 1 72  ? 2.937  5.497   7.168  1.00 15.41 ? 78  LYS   A N   1 
ATOM   567  C  CA  . LYS   A 1 72  ? 3.999  5.819   6.203  1.00 15.25 ? 78  LYS   A CA  1 
ATOM   568  C  C   . LYS   A 1 72  ? 4.621  7.174   6.532  1.00 16.47 ? 78  LYS   A C   1 
ATOM   569  O  O   . LYS   A 1 72  ? 3.923  8.056   7.071  1.00 17.69 ? 78  LYS   A O   1 
ATOM   570  C  CB  . LYS   A 1 72  ? 3.411  5.830   4.786  1.00 17.42 ? 78  LYS   A CB  1 
ATOM   571  C  CG  . LYS   A 1 72  ? 2.965  4.461   4.352  1.00 19.64 ? 78  LYS   A CG  1 
ATOM   572  C  CD  . LYS   A 1 72  ? 2.575  4.478   2.855  1.00 26.77 ? 78  LYS   A CD  1 
ATOM   573  C  CE  . LYS   A 1 72  ? 2.180  3.103   2.417  1.00 32.23 ? 78  LYS   A CE  1 
ATOM   574  N  NZ  . LYS   A 1 72  ? 2.263  2.958   0.929  1.00 36.30 ? 78  LYS   A NZ  1 
ATOM   575  N  N   . PRO   A 1 73  ? 5.902  7.413   6.211  1.00 15.79 ? 79  PRO   A N   1 
ATOM   576  C  CA  . PRO   A 1 73  ? 6.530  8.701   6.537  1.00 16.16 ? 79  PRO   A CA  1 
ATOM   577  C  C   . PRO   A 1 73  ? 5.750  9.875   5.969  1.00 17.66 ? 79  PRO   A C   1 
ATOM   578  O  O   . PRO   A 1 73  ? 5.423  9.879   4.780  1.00 20.11 ? 79  PRO   A O   1 
ATOM   579  C  CB  . PRO   A 1 73  ? 7.938  8.580   5.907  1.00 17.60 ? 79  PRO   A CB  1 
ATOM   580  C  CG  . PRO   A 1 73  ? 8.170  7.153   5.679  1.00 21.14 ? 79  PRO   A CG  1 
ATOM   581  C  CD  . PRO   A 1 73  ? 6.843  6.472   5.556  1.00 17.27 ? 79  PRO   A CD  1 
ATOM   582  N  N   . SER   A 1 74  ? 5.437  10.834  6.832  1.00 17.35 ? 80  SER   A N   1 
ATOM   583  C  CA  . SER   A 1 74  ? 4.576  11.952  6.431  1.00 18.87 ? 80  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 4.972  13.244  7.166  1.00 17.32 ? 80  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 5.788  13.255  8.090  1.00 16.81 ? 80  SER   A O   1 
ATOM   586  C  CB  . SER   A 1 74  ? 3.090  11.625  6.703  1.00 24.14 ? 80  SER   A CB  1 
ATOM   587  O  OG  . SER   A 1 74  ? 2.738  10.253  6.760  1.00 31.44 ? 80  SER   A OG  1 
ATOM   588  N  N   . LEU   A 1 75  ? 4.278  14.348  6.784  1.00 18.99 ? 81  LEU   A N   1 
ATOM   589  C  CA  . LEU   A 1 75  ? 4.456  15.658  7.360  1.00 20.37 ? 81  LEU   A CA  1 
ATOM   590  C  C   . LEU   A 1 75  ? 3.359  15.789  8.419  1.00 20.99 ? 81  LEU   A C   1 
ATOM   591  O  O   . LEU   A 1 75  ? 2.153  15.840  8.075  1.00 22.86 ? 81  LEU   A O   1 
ATOM   592  C  CB  . LEU   A 1 75  ? 4.271  16.718  6.252  1.00 21.79 ? 81  LEU   A CB  1 
ATOM   593  C  CG  . LEU   A 1 75  ? 4.613  18.130  6.640  1.00 24.15 ? 81  LEU   A CG  1 
ATOM   594  C  CD1 . LEU   A 1 75  ? 6.073  18.282  7.005  1.00 24.63 ? 81  LEU   A CD1 1 
ATOM   595  C  CD2 . LEU   A 1 75  ? 4.338  19.102  5.459  1.00 26.26 ? 81  LEU   A CD2 1 
ATOM   596  N  N   . ILE   A 1 76  ? 3.720  15.795  9.686  1.00 19.74 ? 82  ILE   A N   1 
ATOM   597  C  CA  . ILE   A 1 76  ? 2.810  15.810  10.835 1.00 20.52 ? 82  ILE   A CA  1 
ATOM   598  C  C   . ILE   A 1 76  ? 3.061  16.992  11.768 1.00 21.33 ? 82  ILE   A C   1 
ATOM   599  O  O   . ILE   A 1 76  ? 4.220  17.299  12.081 1.00 19.85 ? 82  ILE   A O   1 
ATOM   600  C  CB  . ILE   A 1 76  ? 2.980  14.490  11.610 1.00 21.58 ? 82  ILE   A CB  1 
ATOM   601  C  CG1 . ILE   A 1 76  ? 2.721  13.279  10.682 1.00 23.98 ? 82  ILE   A CG1 1 
ATOM   602  C  CG2 . ILE   A 1 76  ? 2.162  14.481  12.911 1.00 22.61 ? 82  ILE   A CG2 1 
ATOM   603  C  CD1 . ILE   A 1 76  ? 2.823  11.979  11.254 1.00 24.08 ? 82  ILE   A CD1 1 
ATOM   604  N  N   . PHE   A 1 77  ? 2.001  17.653  12.266 1.00 21.75 ? 83  PHE   A N   1 
ATOM   605  C  CA  . PHE   A 1 77  ? 2.165  18.728  13.229 1.00 22.66 ? 83  PHE   A CA  1 
ATOM   606  C  C   . PHE   A 1 77  ? 2.463  18.118  14.575 1.00 24.49 ? 83  PHE   A C   1 
ATOM   607  O  O   . PHE   A 1 77  ? 1.709  17.266  15.064 1.00 26.81 ? 83  PHE   A O   1 
ATOM   608  C  CB  . PHE   A 1 77  ? 0.873  19.561  13.332 1.00 23.79 ? 83  PHE   A CB  1 
ATOM   609  C  CG  . PHE   A 1 77  ? 1.114  20.849  14.070 1.00 25.99 ? 83  PHE   A CG  1 
ATOM   610  C  CD1 . PHE   A 1 77  ? 1.838  21.874  13.482 1.00 27.16 ? 83  PHE   A CD1 1 
ATOM   611  C  CD2 . PHE   A 1 77  ? 0.684  21.000  15.382 1.00 29.16 ? 83  PHE   A CD2 1 
ATOM   612  C  CE1 . PHE   A 1 77  ? 2.068  23.060  14.167 1.00 29.55 ? 83  PHE   A CE1 1 
ATOM   613  C  CE2 . PHE   A 1 77  ? 0.886  22.188  16.059 1.00 29.65 ? 83  PHE   A CE2 1 
ATOM   614  C  CZ  . PHE   A 1 77  ? 1.577  23.215  15.452 1.00 29.96 ? 83  PHE   A CZ  1 
ATOM   615  N  N   . VAL   A 1 78  ? 3.588  18.528  15.181 1.00 22.19 ? 84  VAL   A N   1 
ATOM   616  C  CA  . VAL   A 1 78  ? 4.030  18.016  16.477 1.00 21.12 ? 84  VAL   A CA  1 
ATOM   617  C  C   . VAL   A 1 78  ? 3.979  19.191  17.486 1.00 20.03 ? 84  VAL   A C   1 
ATOM   618  O  O   . VAL   A 1 78  ? 4.503  20.250  17.183 1.00 21.46 ? 84  VAL   A O   1 
ATOM   619  C  CB  . VAL   A 1 78  ? 5.473  17.429  16.352 1.00 19.73 ? 84  VAL   A CB  1 
ATOM   620  C  CG1 . VAL   A 1 78  ? 5.991  16.939  17.711 1.00 20.22 ? 84  VAL   A CG1 1 
ATOM   621  C  CG2 . VAL   A 1 78  ? 5.474  16.283  15.322 1.00 19.86 ? 84  VAL   A CG2 1 
ATOM   622  N  N   . GLU   A 1 79  ? 3.480  18.911  18.695 1.00 20.92 ? 85  GLU   A N   1 
ATOM   623  C  CA  . GLU   A 1 79  ? 3.377  19.939  19.734 1.00 21.99 ? 85  GLU   A CA  1 
ATOM   624  C  C   . GLU   A 1 79  ? 4.767  20.334  20.248 1.00 23.04 ? 85  GLU   A C   1 
ATOM   625  O  O   . GLU   A 1 79  ? 5.750  19.610  20.081 1.00 23.34 ? 85  GLU   A O   1 
ATOM   626  C  CB  . GLU   A 1 79  ? 2.530  19.414  20.898 1.00 24.15 ? 85  GLU   A CB  1 
ATOM   627  C  CG  . GLU   A 1 79  ? 1.042  19.246  20.547 1.00 29.53 ? 85  GLU   A CG  1 
ATOM   628  C  CD  . GLU   A 1 79  ? 0.363  20.490  19.999 1.00 38.02 ? 85  GLU   A CD  1 
ATOM   629  O  OE1 . GLU   A 1 79  ? 0.586  21.601  20.538 1.00 39.55 ? 85  GLU   A OE1 1 
ATOM   630  O  OE2 . GLU   A 1 79  ? -0.387 20.354  19.008 1.00 43.79 ? 85  GLU   A OE2 1 
ATOM   631  N  N   . ALA   A 1 80  ? 4.811  21.477  20.917 1.00 23.55 ? 86  ALA   A N   1 
ATOM   632  C  CA  . ALA   A 1 80  ? 6.035  22.001  21.479 1.00 24.37 ? 86  ALA   A CA  1 
ATOM   633  C  C   . ALA   A 1 80  ? 6.622  21.105  22.518 1.00 25.76 ? 86  ALA   A C   1 
ATOM   634  O  O   . ALA   A 1 80  ? 5.932  20.347  23.227 1.00 28.10 ? 86  ALA   A O   1 
ATOM   635  C  CB  . ALA   A 1 80  ? 5.761  23.359  22.115 1.00 25.79 ? 86  ALA   A CB  1 
ATOM   636  N  N   . SER   A 1 81  ? 7.956  21.157  22.604 1.00 23.57 ? 87  SER   A N   1 
ATOM   637  C  CA  A SER   A 1 81  ? 8.685  20.434  23.640 0.50 22.98 ? 87  SER   A CA  1 
ATOM   638  C  CA  B SER   A 1 81  ? 8.693  20.424  23.624 0.50 24.65 ? 87  SER   A CA  1 
ATOM   639  C  C   . SER   A 1 81  ? 9.797  21.393  24.112 1.00 25.08 ? 87  SER   A C   1 
ATOM   640  O  O   . SER   A 1 81  ? 9.868  22.528  23.616 1.00 26.27 ? 87  SER   A O   1 
ATOM   641  C  CB  A SER   A 1 81  ? 9.278  19.151  23.066 0.50 20.96 ? 87  SER   A CB  1 
ATOM   642  C  CB  B SER   A 1 81  ? 9.291  19.159  23.011 0.50 27.31 ? 87  SER   A CB  1 
ATOM   643  O  OG  A SER   A 1 81  ? 10.359 19.449  22.196 0.50 16.13 ? 87  SER   A OG  1 
ATOM   644  O  OG  B SER   A 1 81  ? 9.787  18.266  23.994 0.50 30.60 ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.700 20.952  25.042 1.00 25.98 ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.779 21.883  25.407 1.00 25.82 ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.799 21.971  24.234 1.00 23.65 ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.610 22.878  24.254 1.00 24.06 ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.464 21.517  26.722 1.00 29.64 ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 13.135 20.176  26.628 1.00 32.23 ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 14.004 19.804  27.813 1.00 41.06 ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 15.092 20.403  27.975 1.00 44.53 ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 13.597 18.895  28.573 1.00 41.80 ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.686 21.116  23.167 1.00 22.88 ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.686 21.145  22.096 1.00 21.49 ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.230 21.824  20.794 1.00 20.14 ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 14.064 22.295  20.020 1.00 20.24 ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 14.180 19.703  21.831 1.00 23.00 ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 15.012 19.158  22.983 1.00 25.23 ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 16.290 19.640  23.228 1.00 29.12 ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 14.471 18.277  23.898 1.00 28.70 ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 17.063 19.137  24.273 1.00 31.86 ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 15.231 17.763  24.945 1.00 30.56 ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 16.508 18.240  25.163 1.00 33.82 ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 17.261 17.766  26.221 1.00 39.08 ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.908 21.916  20.568 1.00 20.41 ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.393 22.546  19.364 1.00 20.51 ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 10.052 23.216  19.717 1.00 21.17 ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.286  22.657  20.516 1.00 21.21 ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 11.064 21.495  18.274 1.00 19.67 ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.242 20.684  17.742 1.00 17.47 ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 13.162 21.245  16.872 1.00 16.98 ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.438 19.361  18.137 1.00 17.16 ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.204 20.492  16.340 1.00 15.81 ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.515 18.613  17.665 1.00 17.30 ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.397 19.193  16.777 1.00 15.65 ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.465 18.473  16.300 1.00 15.54 ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.735  24.324  19.041 1.00 23.14 ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.374  24.875  19.170 1.00 23.93 ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.396  23.922  18.465 1.00 24.45 ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.848  22.999  17.718 1.00 23.55 ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.479  26.224  18.436 1.00 25.45 ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.524  26.006  17.393 1.00 26.01 ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.523 25.023  18.003 1.00 22.75 ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 6.086  24.136  18.594 1.00 25.64 ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.102  23.338  17.859 1.00 25.11 ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.344  23.638  16.352 1.00 24.77 ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.608  24.786  15.996 1.00 27.46 ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.698  23.770  18.277 1.00 25.83 ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.453  22.585  15.516 1.00 24.00 ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.814  22.779  14.115 1.00 22.85 ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.475  21.497  13.331 1.00 22.34 ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 5.174  20.471  13.924 1.00 23.80 ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.348  23.015  14.022 1.00 24.29 ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.138  21.687  14.251 1.00 26.38 ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.503  21.786  14.741 1.00 25.37 ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.404 20.702  14.337 1.00 22.52 ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.420 19.441  14.747 1.00 22.87 ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.429  18.962  15.520 1.00 22.34 ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.391 18.633  14.358 1.00 20.08 ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.601  21.563  11.996 1.00 21.90 ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.477  20.372  11.175 1.00 22.60 ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.816  19.653  11.116 1.00 20.81 ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.848  20.260  10.807 1.00 22.07 ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 5.034  20.747  9.766  1.00 23.36 ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.554  21.059  9.708  1.00 23.94 ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.612  20.042  9.674  1.00 24.59 ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 3.088  22.360  9.801  1.00 25.37 ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.252  20.305  9.676  1.00 26.01 ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.716  22.635  9.825  1.00 26.30 ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.806  21.599  9.750  1.00 26.83 ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.561 21.762  9.772  1.00 29.59 ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.787  18.344  11.437 1.00 18.35 ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.963  17.473  11.358 1.00 17.43 ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.771  16.584  10.136 1.00 16.88 ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.685  15.990  9.931  1.00 17.60 ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.168  16.682  12.651 1.00 17.02 ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.423  15.779  12.597 1.00 17.60 ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.944  15.346  13.958 1.00 15.56 ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 9.906  16.080  14.980 1.00 17.67 ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.504 14.137  14.000 1.00 14.92 ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.800  16.488  9.298  1.00 16.01 ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.743  15.715  8.097  1.00 15.29 ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.298  14.304  8.306  1.00 15.16 ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.069 14.051  9.248  1.00 15.30 ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.452  16.462  6.963  1.00 17.36 ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.828 16.541  7.285  1.00 19.99 ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.915  13.396  7.387  1.00 15.14 ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.382  12.008  7.335  1.00 14.90 ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.113  11.289  8.683  1.00 13.79 ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.943  10.435  9.112  1.00 14.58 ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.906 11.978  6.979  1.00 16.71 ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.240 12.578  5.633  1.00 17.46 ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.349 11.792  4.517  1.00 18.72 ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.389 13.877  5.274  1.00 20.03 ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.643 12.629  3.505  1.00 20.32 ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.642 13.891  3.913  1.00 21.45 ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.986  11.563  9.305  1.00 13.28 ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.632  11.036  10.630 1.00 13.29 ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.574  9.940   10.443 1.00 13.49 ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.656  10.091  9.625  1.00 14.24 ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.062  12.195  11.506 1.00 14.20 ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.732  11.802  12.972 1.00 15.60 ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 7.964  11.444  13.743 1.00 15.59 ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.015  12.990  13.714 1.00 18.94 ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.685  8.866   11.233 1.00 12.94 ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.736  7.723   11.203 1.00 12.41 ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.167  7.579   12.601 1.00 12.70 ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.928  7.609   13.582 1.00 13.59 ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.507  6.443   10.868 1.00 13.37 ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.188  6.551   9.484  1.00 14.65 ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.302  5.185   9.037  1.00 16.31 ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.556  5.426   10.256 1.00 19.56 ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.856  7.356   12.733 1.00 12.38 ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.242  7.221   14.052 1.00 13.31 ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.769  5.806   14.308 1.00 12.38 ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.315  5.088   13.379 1.00 13.10 ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 2.017  8.182   14.196 1.00 15.00 ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.294  9.675   14.099 1.00 18.58 ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 1.043  10.537  14.446 1.00 20.39 ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.365  10.111  15.036 1.00 21.13 ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.794  5.413   15.587 1.00 12.21 ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.280  4.102   16.005 1.00 11.42 ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.665  4.274   17.397 1.00 11.18 ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.948  5.244   18.114 1.00 11.85 ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.433  3.050   16.099 1.00 12.71 ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.865  3.290   17.787 1.00 11.12 ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.327  3.241   19.135 1.00 11.08 ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.343  2.440   19.988 1.00 12.68 ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.659  1.288   19.681 1.00 14.92 ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.031 2.519   19.119 1.00 11.64 ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.551 2.317   20.560 1.00 12.74 ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.032 3.323   18.291 1.00 11.62 ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.862  3.103   20.984 1.00 13.05 ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.863  2.478   21.848 1.00 14.12 ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.253  3.424   22.932 1.00 14.24 ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 3.082  4.627   22.813 1.00 14.55 ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.770  2.845   24.050 1.00 14.51 ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.219  3.693   25.138 1.00 15.11 ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.516  4.415   24.785 1.00 14.68 ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.440  3.791   24.228 1.00 14.25 ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.471  2.875   26.432 1.00 15.60 ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 4.919  3.754   27.557 1.00 16.09 ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.043  4.670   28.149 1.00 15.62 ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.150  3.929   28.117 1.00 16.26 ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.783  5.385   28.993 1.00 16.49 ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 6.043  4.930   29.046 1.00 16.77 ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.623  5.632   25.157 1.00 15.51 ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.837  6.391   25.089 1.00 14.21 ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 6.872  7.555   26.080 1.00 14.69 ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.802  8.073   26.429 1.00 16.91 ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.221  6.825   23.673 1.00 15.79 ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 6.324  7.788   23.135 1.00 15.94 ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.108  8.027   26.411 1.00 14.11 ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.430  9.193   27.250 1.00 14.33 ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.579  9.944   26.589 1.00 15.25 ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.261 9.387   25.694 1.00 14.00 ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 8.831  8.714   28.660 1.00 15.31 ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.668  7.970   29.303 1.00 17.12 ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 7.923  7.357   30.669 1.00 19.59 ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.756  7.918   31.415 1.00 24.76 ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.321  6.313   30.988 1.00 17.99 ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.838  11.210  26.936 1.00 15.24 ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.842 11.979  26.182 1.00 15.30 ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.217 11.314  26.030 1.00 15.04 ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.822 11.298  24.929 1.00 14.67 ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 10.901 13.329  26.942 1.00 17.29 ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.510  13.456  27.514 1.00 19.15 ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 9.107  12.057  27.911 1.00 16.78 ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.730 10.700  27.095 1.00 15.02 ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 14.039 10.038  27.082 1.00 14.46 ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 14.086 8.733   26.284 1.00 13.12 ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.156 8.150   26.112 1.00 13.57 ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.937 8.279   25.745 1.00 11.40 ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.930 7.107   24.839 1.00 11.00 ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.441 7.502   23.436 1.00 11.46 ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.705 6.593   22.624 1.00 10.82 ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.491 6.548   24.713 1.00 11.22 ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 11.103 5.803   25.977 1.00 11.51 ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 11.977 5.123   26.535 1.00 11.67 ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 9.885  5.853   26.362 1.00 12.40 ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.619 8.817   23.133 1.00 10.93 ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.167 9.179   21.811 1.00 11.29 ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.492 8.519   21.581 1.00 11.15 ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.337 8.416   22.477 1.00 11.52 ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.307 10.690  21.700 1.00 12.69 ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.696 11.549  21.495 1.00 13.46 ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.680 7.998   20.374 1.00 10.43 ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.879 7.290   19.975 1.00 10.95 ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.720 5.773   19.906 1.00 10.74 ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.566 5.078   19.327 1.00 11.22 ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.639 5.258   20.518 1.00 10.47 ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.372 3.830   20.422 1.00 10.27 ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.119 3.415   18.963 1.00 9.29  ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.415 4.135   18.216 1.00 9.82  ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.624 2.259   18.566 1.00 9.88  ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.474 1.814   17.172 1.00 10.02 ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.149 1.169   16.887 1.00 9.44  ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.676 0.331   17.677 1.00 9.39  ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.641 0.862   16.801 1.00 10.50 ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.912 1.715   16.556 1.00 11.75 ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.357 -0.049  15.590 1.00 11.96 ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.183 0.896   16.401 1.00 14.36 ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.567 1.502   15.739 1.00 9.10  ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.471 0.775   15.099 1.00 8.90  ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.097 -0.075  13.969 1.00 9.20  ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.857 0.481   13.148 1.00 10.24 ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.460 1.782   14.477 1.00 9.65  ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.348 1.152   13.608 1.00 9.91  ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.361  0.336   14.461 1.00 11.09 ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.572  2.275   12.850 1.00 12.74 ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.783 -1.367  13.926 1.00 9.77  ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.361 -2.252  12.888 1.00 10.02 ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.295 -3.149  12.321 1.00 11.21 ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.289 -3.472  12.969 1.00 11.53 ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.550 -3.072  13.493 1.00 11.48 ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 14.085 -4.047  14.576 1.00 11.40 ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.299 -4.773  15.165 1.00 12.97 ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.104 -3.895  16.003 1.00 13.66 ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.409 -3.715  15.916 1.00 13.71 ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 18.081 -4.142  14.842 1.00 14.71 ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 18.035 -2.980  16.812 1.00 15.02 ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.529 -3.610  11.095 1.00 13.58 ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.607 -4.538  10.404 1.00 16.08 ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.428 -5.703  9.959  1.00 17.61 ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.624 -5.853  10.303 1.00 16.64 ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.927 -3.826  9.232  1.00 15.13 ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.074 -3.463  7.866  1.00 15.17 ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.772 -6.621  9.193  1.00 18.85 ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.487 -7.773  8.675  1.00 20.74 ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.731 -7.423  7.818  1.00 22.37 ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.642 -8.239  7.731  1.00 24.71 ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.540 -8.719  7.875  1.00 24.95 ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.013 -8.100  6.585  1.00 29.50 ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.109 -9.058  5.838  1.00 35.76 ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 8.878  -8.972  5.928  1.00 38.14 ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.706 -9.976  5.076  1.00 36.68 ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.806 -6.227  7.242  1.00 19.37 ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 14.914 -5.825  6.337  1.00 18.98 ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.082 -5.103  7.038  1.00 18.88 ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.113 -4.826  6.417  1.00 20.82 ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.327 -4.926  5.232  1.00 19.88 ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.198 -5.604  4.475  1.00 22.19 ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.886 -5.213  4.620  1.00 20.53 ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.251 -6.575  3.520  1.00 24.71 ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.166 -5.999  3.831  1.00 24.30 ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 11.952 -6.825  3.137  1.00 26.50 ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.864 -4.629  8.287  1.00 16.99 ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.900 -3.875  8.982  1.00 15.79 ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.297 -2.702  9.764  1.00 13.28 ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.105 -2.701  10.099 1.00 13.56 ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.164 -1.691  10.066 1.00 12.38 ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.713 -0.514  10.822 1.00 11.60 ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.860 0.396   9.962  1.00 10.75 ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.275 0.771   8.850  1.00 11.68 ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.941 0.229   11.415 1.00 11.57 ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.543 1.553   12.082 1.00 12.78 ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.720 -0.670  12.392 1.00 12.79 ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.737 0.839   10.501 1.00 10.29 ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.776 1.677   9.808  1.00 11.00 ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.924 3.137   10.248 1.00 10.88 ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.778 4.073   9.443  1.00 11.88 ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.321 1.170   10.100 1.00 12.28 ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.237 2.148   9.590  1.00 14.09 ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.114 -0.223  9.532  1.00 13.53 ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.134 3.364   11.565 1.00 10.62 ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.200 4.744   12.060 1.00 11.20 ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.390 4.759   13.571 1.00 10.28 ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.703 3.696   14.152 1.00 10.31 ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.288 5.947   14.197 1.00 10.78 ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.512 6.083   15.649 1.00 9.88  ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.376 6.864   16.269 1.00 9.91  ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.782 7.755   15.619 1.00 10.95 ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.868 6.769   15.997 1.00 10.69 ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 16.025 8.094   15.255 1.00 12.45 ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 17.006 5.773   15.737 1.00 11.79 ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.299 8.896   15.756 1.00 12.26 ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.052 6.569   17.522 1.00 10.05 ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 12.031 7.314   18.255 1.00 10.00 ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.385 8.814   18.274 1.00 10.03 ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.554 9.176   18.571 1.00 10.64 ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.885 6.787   19.713 1.00 10.17 ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.926 7.649   20.543 1.00 10.47 ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.449 5.310   19.768 1.00 10.56 ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.390 9.672   18.005 1.00 10.72 ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.571 11.121  17.973 1.00 12.01 ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.460 11.877  18.706 1.00 12.46 ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.739 12.992  19.228 1.00 14.16 ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.743 11.561  16.534 1.00 13.02 ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.810 12.983  16.372 1.00 14.99 ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.214  11.373  18.706 1.00 12.73 ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.102  12.150  19.297 1.00 13.21 ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.186  11.176  20.103 1.00 14.63 ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.358  9.933   19.989 1.00 13.25 ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.235  12.823  18.180 1.00 14.21 ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.447  11.835  17.466 1.00 14.72 ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 8.043  13.704  17.224 1.00 14.69 ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.193  11.678  20.834 1.00 15.74 ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.220  10.790  21.464 1.00 17.26 ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.333  11.514  22.458 1.00 17.64 ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.437  12.727  22.636 1.00 19.08 ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.523  10.691  23.134 1.00 18.49 ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.605  11.121  24.198 1.00 19.43 ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.269  10.409  24.056 1.00 19.70 ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 0.855  10.058  22.936 1.00 20.29 ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.535  10.269  25.170 1.00 18.09 ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.834 9.709   25.190 1.00 18.75 ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -0.982 8.420   24.417 1.00 18.80 ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.046 8.197   23.806 1.00 19.57 ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.806 10.785  24.679 1.00 21.04 ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.787 12.005  25.546 1.00 25.39 ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -2.051 11.917  26.745 1.00 27.54 ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.482 13.155  24.946 1.00 25.98 ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.041 7.495   24.576 1.00 16.54 ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.147 6.202   23.956 1.00 15.85 ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.269  6.206   22.506 1.00 13.76 ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? 0.108  5.171   21.889 1.00 15.57 ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.852  7.300   21.995 1.00 14.68 ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.444  7.311   20.632 1.00 14.93 ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.975  7.391   20.736 1.00 15.72 ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.547  7.923   21.728 1.00 18.04 ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.945  8.505   19.842 1.00 16.08 ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.564 8.480   19.553 1.00 17.23 ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.090 9.896   19.208 1.00 20.43 ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.924 7.375   18.503 1.00 17.22 ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.635  6.882   19.703 1.00 11.84 ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.100  7.043   19.597 1.00 12.52 ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.342  7.408   18.102 1.00 12.36 ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.732  6.821   17.205 1.00 12.53 ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.844  5.762   20.069 1.00 12.69 ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.335  4.494   19.359 1.00 13.37 ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.372  5.916   19.903 1.00 13.33 ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.238  8.356   17.848 1.00 12.13 ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.600  8.783   16.497 1.00 12.34 ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.055  8.479   16.207 1.00 11.30 ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.921  8.670   17.076 1.00 12.22 ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.310  8.006   14.988 1.00 10.46 ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.679  7.609   14.548 1.00 11.18 ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.147 8.387   13.345 1.00 11.57 ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.371  8.561   12.391 1.00 11.95 ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.671  6.099   14.145 1.00 11.30 ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 9.058  5.168   15.180 1.00 10.19 ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.818  4.677   16.243 1.00 10.19 ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.740  4.762   15.065 1.00 11.61 ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.232  3.810   17.197 1.00 10.21 ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.181  3.898   16.001 1.00 11.91 ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.948  3.422   17.055 1.00 10.91 ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.382 8.889   13.436 1.00 10.97 ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 12.002 9.586   12.293 1.00 11.18 ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.509 8.509   11.321 1.00 10.94 ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.367 7.710   11.689 1.00 11.14 ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.149 10.428  12.823 1.00 11.53 ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.975 8.429   10.111 1.00 11.64 ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.388 7.448   9.104  1.00 12.06 ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.811 7.757   8.625  1.00 12.07 ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.176 8.935   8.488  1.00 12.32 ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.426 7.529   7.894  1.00 13.96 ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.721 6.534   6.827  1.00 18.11 ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.813 5.314   7.151  1.00 17.37 ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.976 6.976   5.677  1.00 21.63 ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.575 6.706   8.303  1.00 11.50 ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.904 6.838   7.659  1.00 11.64 ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 16.000 6.006   6.376  1.00 12.49 ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.063 6.036   5.740  1.00 12.14 ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.057 6.493   8.617  1.00 11.86 ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.073 7.408   9.852  1.00 13.28 ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.079 5.034   9.019  1.00 12.68 ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.913 5.322   5.941  1.00 12.47 ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 15.011 4.412   4.805  1.00 12.84 ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.265 5.112   3.485  1.00 14.12 ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.761 4.458   2.521  1.00 15.15 ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.757 3.549   4.690  1.00 13.48 ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.597 2.611   5.914  1.00 12.63 ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.302 1.820   5.791  1.00 14.49 ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.172 2.736   6.030  1.00 14.13 ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.897  2.355   6.122  1.00 15.90 ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.550  1.101   5.841  1.00 16.77 ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.966  3.238   6.447  1.00 17.44 ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.931 6.436   3.389  1.00 14.39 ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.196 7.151   2.147  1.00 15.11 ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.648 7.644   2.024  1.00 14.62 ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 17.029 8.155   0.955  1.00 16.47 ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.243 8.358   2.051  1.00 17.11 ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.488 9.388   3.138  1.00 21.21 ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.607 8.994   4.329  1.00 19.18 ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.523 10.608  2.820  1.00 22.93 ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.446 7.587   3.112  1.00 13.22 ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.823 8.128   3.126  1.00 13.97 ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.755 7.070   2.566  1.00 14.27 ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.470 6.367   3.298  1.00 13.77 ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.183 8.511   4.563  1.00 12.90 ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.237 9.550   5.221  1.00 15.07 ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.655 9.806   6.665  1.00 15.82 ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.244 10.874  4.478  1.00 18.26 ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.762 6.955   1.221  1.00 14.03 ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.506 5.869   0.584  1.00 15.26 ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.005 5.949   0.767  1.00 15.12 ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.711 4.919   0.825  1.00 16.22 ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.149 5.752   -0.940 1.00 16.69 ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.652 5.764   -1.253 1.00 17.82 ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.460 5.460   -2.753 1.00 21.05 ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.870 4.691   -0.433 1.00 18.21 ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.509 7.185   0.932  1.00 14.03 ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.933 7.444   1.109  1.00 14.16 ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.473 6.834   2.403  1.00 14.88 ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.697 6.684   2.536  1.00 15.64 ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.217 8.962   0.980  1.00 14.95 ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.399 9.781   1.928  1.00 14.05 ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.260 10.463  1.633  1.00 14.96 ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.744 10.117  3.281  1.00 13.89 ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.817 11.133  2.760  1.00 15.78 ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.731 10.950  3.773  1.00 14.51 ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.809 9.783   4.125  1.00 14.59 ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.744 11.445  5.092  1.00 15.96 ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.827 10.284  5.422  1.00 16.43 ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.817 11.115  5.878  1.00 16.48 ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.611 6.496   3.395  1.00 13.86 ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.125 5.829   4.607  1.00 14.76 ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.809 4.499   4.297  1.00 16.52 ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.643 4.029   5.111  1.00 17.66 ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.994 5.565   5.605  1.00 14.32 ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.436 6.796   6.292  1.00 13.70 ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.162 6.459   7.074  1.00 15.16 ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.532 7.445   7.241  1.00 14.51 ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.491 3.883   3.127  1.00 18.45 ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.045 2.565   2.736  1.00 21.59 ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.388 2.614   2.045  1.00 26.09 ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.911 1.546   1.681  1.00 27.81 ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.067 1.793   1.791  1.00 22.22 ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.709 1.468   2.353  1.00 25.28 ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.538 1.558   3.585  1.00 26.57 ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.776 1.124   1.557  1.00 31.38 ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.973 3.812   1.845  1.00 27.71 ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.288 3.875   1.161  1.00 31.94 ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.158 5.058   1.592  1.00 33.96 ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.757 5.814   2.480  1.00 33.60 ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 28.036 3.917   -0.346 1.00 37.10 ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.234 5.141   -0.731 1.00 46.38 ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.104 4.833   -1.686 1.00 57.68 ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 26.141 5.341   -2.829 1.00 61.72 ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.182 4.083   -1.296 1.00 61.23 ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.337 5.232   0.935  1.00 35.80 ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.291 6.344   1.071  1.00 38.23 ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 31.675 6.587   2.513  1.00 39.63 ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 31.851 7.728   2.957  1.00 39.83 ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.747 7.608   0.357  1.00 41.02 ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.316 8.977   0.731  1.00 49.08 ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.716 9.377   0.289  1.00 59.56 ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 32.983 10.600  0.234  1.00 61.53 ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.546 8.482   0.004  1.00 62.75 ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 22.041 -21.292 7.695  1.00 17.03 ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.917 -21.055 8.634  1.00 16.70 ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.869 -22.161 9.710  1.00 16.32 ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.531 -23.206 9.569  1.00 17.80 ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.591 -21.032 7.858  1.00 19.66 ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.407 -22.315 7.289  1.00 24.82 ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 20.104 -21.937 10.789 1.00 16.57 ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.923 -22.944 11.823 1.00 15.69 ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.667 -22.347 13.184 1.00 14.39 ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 20.063 -21.208 13.440 1.00 14.98 ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 19.016 -23.093 14.072 1.00 13.17 ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.705 -22.581 15.407 1.00 13.57 ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.818 -23.722 16.433 1.00 12.70 ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.882 -24.904 16.045 1.00 13.86 ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.265 -22.039 15.436 1.00 15.74 ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.861 -23.350 17.718 1.00 12.29 ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.759 -24.277 18.858 1.00 12.42 ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.356 -24.086 19.459 1.00 12.08 ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.917 -22.928 19.642 1.00 13.07 ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.803 -23.952 19.927 1.00 12.00 ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.242 -23.839 19.334 1.00 13.31 ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.740 -25.051 21.003 1.00 14.03 ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.223 -23.241 20.352 1.00 14.33 ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.666 -25.186 19.734 1.00 12.37 ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.311 -25.119 20.307 1.00 13.29 ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.378 -25.807 21.671 1.00 13.58 ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.438 -27.051 21.731 1.00 15.36 ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.247 -25.826 19.400 1.00 14.28 ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 14.062 -25.067 18.105 1.00 14.32 ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.236 -23.936 18.045 1.00 14.59 ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.789 -25.397 16.974 1.00 15.55 ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 13.102 -23.217 16.875 1.00 15.80 ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.652 -24.692 15.797 1.00 17.67 ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.819 -23.594 15.756 1.00 17.08 ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.750 -22.845 14.597 1.00 19.31 ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.412 -25.068 22.773 1.00 14.46 ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.492 -25.638 24.143 1.00 15.16 ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.383 -25.010 25.002 1.00 15.48 ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 14.194 -23.791 24.983 1.00 14.43 ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.902 -25.391 24.752 1.00 16.39 ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.290 -23.901 24.695 1.00 16.73 ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.940 -25.909 26.186 1.00 17.99 ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.539 -25.829 25.674 1.00 16.53 ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.437 -25.279 26.463 1.00 16.61 ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.525 -24.422 25.595 1.00 16.77 ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.218 -24.812 24.461 1.00 17.69 ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 11.186 -23.223 26.050 1.00 16.59 ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.389 -22.310 25.219 1.00 16.94 ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.259 -21.209 24.632 1.00 15.91 ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.816 -20.083 24.464 1.00 16.29 ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 9.140  -21.750 25.948 1.00 19.47 ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 8.066  -22.822 26.081 1.00 25.34 ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 7.203  -22.961 25.215 1.00 26.96 ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 8.159  -23.631 27.114 1.00 28.51 ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.485 -21.590 24.243 1.00 14.04 ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.456 -20.646 23.632 1.00 12.69 ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.915 -21.115 22.264 1.00 12.78 ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 14.107 -22.322 22.033 1.00 13.57 ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.702 -20.498 24.546 1.00 14.05 ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.397 -19.978 25.942 1.00 15.38 ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.817 -18.722 26.130 1.00 17.44 ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.695 -20.738 27.068 1.00 18.32 ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.561 -18.240 27.415 1.00 19.97 ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.458 -20.251 28.351 1.00 21.17 ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.923 -18.996 28.512 1.00 23.20 ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.640 -18.508 29.780 1.00 28.74 ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 14.166 -20.153 21.387 1.00 12.47 ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.778 -20.370 20.062 1.00 12.38 ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 16.052 -19.499 20.036 1.00 12.62 ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.962 -18.279 20.257 1.00 12.86 ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.809 -19.933 18.929 1.00 13.37 ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.442 -19.737 17.529 1.00 14.23 ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.361 -19.432 16.484 1.00 14.00 ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.813 -18.479 15.463 1.00 15.00 ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.332 -18.781 14.270 1.00 15.77 ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.580 -20.053 13.944 1.00 17.75 ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.693 -17.807 13.428 1.00 17.32 ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.223 -20.103 19.793 1.00 11.97 ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.517 -19.397 19.760 1.00 10.97 ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.963 -19.335 18.348 1.00 11.58 ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 19.126 -20.401 17.699 1.00 12.59 ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.587 -20.119 20.637 1.00 11.28 ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.840 -19.273 20.742 1.00 13.54 ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 19.042 -20.489 22.022 1.00 13.48 ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.213 -18.120 17.822 1.00 11.49 ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.663 -17.957 16.437 0.50 11.64 ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.612 -17.971 16.427 0.50 13.33 ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.793 -16.962 16.360 1.00 12.63 ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 21.055 -16.202 17.330 1.00 12.84 ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.510 -17.450 15.519 0.50 11.72 ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.345 -17.425 15.656 0.50 16.92 ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.542 -18.576 15.225 0.50 12.74 ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.585 -17.286 14.164 0.50 17.18 ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.851 -16.154 16.056 0.50 8.20  ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 17.149 -18.327 15.876 0.50 19.99 ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.500 -16.917 15.213 1.00 11.36 ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.486 -15.858 15.000 1.00 11.77 ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.697 -14.513 14.953 1.00 12.29 ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.677 -14.431 14.258 1.00 12.03 ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 23.206 -16.000 13.650 1.00 12.29 ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 24.056 -17.262 13.557 1.00 11.45 ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.600 -18.322 13.132 1.00 12.81 ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.277 -17.205 14.030 1.00 12.85 ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.195 -13.489 15.659 1.00 11.71 ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.456 -12.201 15.680 1.00 12.21 ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.321 -11.646 14.261 1.00 13.56 ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.230 -11.119 13.920 1.00 13.93 ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.224 -11.206 16.561 1.00 12.03 ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.425 -9.877  16.785 1.00 13.17 ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.281 -8.910  17.573 1.00 14.04 ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.599 -7.647  18.012 1.00 14.53 ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.468 -6.558  17.261 1.00 14.59 ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.842 -6.568  15.994 1.00 15.45 ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.955 -5.450  17.774 1.00 14.88 ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.320 -11.851 13.400 1.00 13.47 ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.226 -11.312 12.034 1.00 14.08 ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.229 -12.030 11.122 1.00 15.19 ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.915 -11.511 10.047 1.00 17.44 ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.626 -11.206 11.368 1.00 14.78 ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.208 -12.527 10.913 1.00 13.03 ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.948 -13.349 11.791 1.00 13.26 ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.187 -13.107 9.688  1.00 13.90 ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.345 -14.406 11.066 1.00 14.97 ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.922 -14.305 9.805  1.00 14.13 ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.690 -13.185 11.567 1.00 13.66 ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.674 -13.938 10.825 1.00 14.57 ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.302 -13.874 11.512 1.00 14.84 ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.366 -14.567 11.076 1.00 16.03 ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 20.130 -15.393 10.644 1.00 14.62 ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.407 -15.542 9.816  1.00 15.35 ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.848 -17.007 9.740  1.00 15.68 ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.294 -14.921 8.431  1.00 16.44 ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 18.162 -13.088 12.613 1.00 15.09 ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.872 -13.045 13.318 1.00 15.11 ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.753 -12.491 12.444 1.00 15.69 ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.994 -11.553 11.658 1.00 16.27 ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.984 -12.209 14.599 1.00 16.29 ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.559 -13.047 12.604 1.00 15.80 ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.394 -12.614 11.832 1.00 16.97 ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.581 -11.551 12.597 1.00 16.31 ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.799 -11.251 13.770 1.00 16.24 ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.475 -13.834 11.562 1.00 17.90 ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.940 -14.272 12.797 1.00 18.20 ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.203 -15.001 10.867 1.00 20.11 ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.546 -10.944 11.912 1.00 17.18 ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.620 -10.038 12.610 1.00 17.54 ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.936  -10.798 13.746 1.00 16.14 ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.816  -10.226 14.822 1.00 17.69 ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.492  -9.583  11.650 1.00 19.21 ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.350  -8.861  12.340 1.00 21.04 ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.500  -7.598  12.873 1.00 23.28 ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.149  -9.342  12.704 1.00 22.96 ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.309  -7.276  13.382 1.00 23.40 ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.479  -8.313  13.353 1.00 22.72 ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.518  -12.071 13.536 1.00 16.80 ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.889  -12.805 14.629 1.00 17.27 ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.814  -12.983 15.819 1.00 16.42 ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.378  -12.907 16.966 1.00 16.05 ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.359  -14.182 14.190 1.00 19.07 ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.541  -14.855 15.289 1.00 25.77 ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.421  -14.400 15.603 1.00 28.51 ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 8.101  -15.892 15.960 1.00 27.80 ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 11.141 -13.180 15.566 1.00 15.21 ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 12.090 -13.275 16.662 1.00 15.39 ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 12.127 -11.956 17.464 1.00 14.98 ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 12.066 -11.974 18.692 1.00 16.28 ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.518 -13.578 16.149 1.00 15.95 ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.714 -14.989 15.664 1.00 15.36 ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 13.144 -15.896 16.272 1.00 16.84 ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.404 -15.171 14.635 1.00 15.58 ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.229 -10.803 16.766 1.00 15.16 ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.267 -9.505  17.436 1.00 15.61 ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.934 -9.188  18.160 1.00 15.39 ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.951 -8.552  19.218 1.00 16.38 ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.644 -8.397  16.465 1.00 15.66 ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 14.125 -8.339  16.195 1.00 15.01 ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.772 -8.824  15.094 1.00 16.46 ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 15.143 -7.779  17.047 1.00 14.03 ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 16.126 -8.537  15.174 1.00 16.10 ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.369 -7.884  16.362 1.00 15.50 ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 15.120 -7.089  18.275 1.00 16.26 ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.546 -7.366  16.869 1.00 15.24 ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.302 -6.585  18.782 1.00 17.58 ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.494 -6.727  18.076 1.00 17.43 ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.818  -9.660  17.605 1.00 15.55 ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.496  -9.441  18.216 1.00 17.27 ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.259  -10.310 19.460 1.00 18.38 ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.267  -10.124 20.182 1.00 19.53 ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.400  -9.722  17.196 1.00 18.45 ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 9.131  -11.337 19.686 1.00 17.37 ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 9.017  -12.265 20.824 1.00 16.81 ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.398 -12.324 21.498 1.00 16.68 ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.834 -13.397 21.920 1.00 16.50 ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.560  -13.646 20.317 1.00 18.86 ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 7.130  -13.593 19.843 1.00 20.18 ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 6.183  -13.627 20.670 1.00 22.93 ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.942  -13.514 18.537 1.00 20.35 ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 11.097 -11.188 21.595 1.00 17.16 ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.477 -11.168 22.069 1.00 16.55 ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.601 -11.512 23.551 1.00 18.07 ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.813 -11.032 24.387 1.00 19.46 ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 13.053 -9.761  21.812 1.00 16.80 ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.510 -9.604  22.194 1.00 17.25 ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.421 -10.455 21.290 1.00 16.61 ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.917 -8.156  22.081 1.00 20.10 ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.601 -12.332 23.885 1.00 16.39 ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.954 -12.625 25.265 1.00 16.73 ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.291 -11.922 25.609 1.00 17.11 ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.417 -11.256 26.633 1.00 18.28 ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 14.087 -14.144 25.503 1.00 16.83 ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.677 -14.436 26.899 1.00 18.67 ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.741 -14.835 25.291 1.00 17.10 ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.302 -12.049 24.733 1.00 15.22 ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.627 -11.500 25.008 1.00 15.89 ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.435 -11.425 23.690 1.00 15.57 ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.251 -12.309 22.835 1.00 15.42 ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.377 -12.397 26.048 1.00 16.76 ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.850 -12.120 26.239 1.00 17.27 ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.430 -11.148 27.015 1.00 19.09 ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.927 -12.813 25.599 1.00 15.92 ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.814 -11.236 26.935 1.00 19.83 ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 22.139 -12.240 26.056 1.00 17.22 ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.994 -13.856 24.653 1.00 15.90 ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.400 -12.755 25.693 1.00 17.12 ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.251 -14.357 24.304 1.00 17.00 ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.423 -13.765 24.772 1.00 17.06 ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.279 -10.444 23.533 1.00 14.47 ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 20.133 -10.341 22.355 1.00 15.62 ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.430 -9.677  22.699 1.00 15.62 ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.457 -8.798  23.588 1.00 16.29 ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.431 -9.684  21.173 1.00 16.82 ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.882 -8.287  21.435 1.00 18.11 ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.863 -7.133  21.402 1.00 20.11 ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.591 -6.111  22.069 1.00 21.54 ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.863 -7.203  20.657 1.00 18.12 ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.497 -10.038 21.978 1.00 14.35 ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.798 -9.419  22.199 1.00 14.34 ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.560 -9.377  20.873 1.00 14.30 ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.979 -10.414 20.366 1.00 14.22 ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.530 -10.191 23.312 1.00 15.67 ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.880 -9.662  23.694 1.00 19.49 ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.619 -9.211  22.793 1.00 19.98 ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 26.255 -9.787  24.878 1.00 23.71 ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.726 -8.172  20.306 1.00 14.46 ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.430 -7.992  19.037 0.50 14.06 ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.400 -8.061  19.024 0.50 14.87 ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.887 -8.451  19.120 1.00 14.69 ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.399 -9.089  18.166 1.00 13.76 ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.403 -6.522  18.607 0.50 14.07 ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.212 -6.674  18.424 0.50 17.70 ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.326 -6.261  17.557 0.50 13.88 ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.750 -5.705  19.298 0.50 21.36 ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.569 -8.171  20.252 1.00 14.82 ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.980 -8.576  20.356 1.00 15.76 ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 29.160 -10.102 20.309 1.00 14.56 ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.245 -10.559 19.927 1.00 15.23 ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.610 -8.051  21.636 1.00 18.39 ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 29.228 -8.744  22.804 1.00 22.82 ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 28.120 -10.889 20.645 1.00 13.18 ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 28.183 -12.360 20.593 1.00 13.20 ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.545 -12.928 19.307 1.00 12.31 ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.548 -14.149 19.093 1.00 12.00 ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.436 -12.951 21.816 1.00 14.14 ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 28.122 -12.596 23.131 1.00 15.74 ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.365 -13.166 24.323 1.00 13.47 ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.417 -14.656 24.354 1.00 13.20 ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.400 -15.391 25.472 1.00 12.89 ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.307 -14.807 26.662 1.00 14.82 ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.539 -16.722 25.405 1.00 13.16 ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.877 -12.076 18.486 1.00 11.68 ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 26.087 -12.534 17.354 1.00 11.56 ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.978 -13.501 17.791 1.00 11.63 ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.667 -14.437 17.031 1.00 11.92 ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.905 -13.148 16.227 1.00 11.65 ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 26.105 -13.466 14.958 1.00 12.88 ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.215 -12.674 14.581 1.00 13.59 ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.418 -14.478 14.297 1.00 12.48 ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.319 -13.252 18.944 1.00 11.28 ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.245 -14.149 19.391 1.00 11.85 ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.941 -13.390 19.652 1.00 12.03 ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.961 -12.232 20.116 1.00 12.91 ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.621 -14.868 20.702 1.00 12.52 ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.678 -15.991 20.612 1.00 12.51 ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.934 -16.584 22.039 1.00 14.19 ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.248 -17.093 19.615 1.00 13.72 ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.837 -14.064 19.413 1.00 11.57 ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.507 -13.553 19.798 1.00 12.33 ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.674 -14.775 20.213 1.00 12.58 ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.731 -15.829 19.560 1.00 13.32 ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.846 -12.820 18.592 1.00 13.35 ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.456 -12.209 18.877 1.00 13.61 ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.274 -10.902 18.107 1.00 16.18 ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.342 -13.213 18.507 1.00 13.90 ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.882 -14.596 21.270 1.00 13.23 ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.973 -15.613 21.792 1.00 12.95 ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.545 -15.074 21.809 1.00 12.58 ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.313 -13.943 22.298 1.00 14.34 ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.396 -16.069 23.200 1.00 13.52 ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.437 -17.130 23.747 1.00 14.56 ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.846 -16.607 23.183 1.00 13.96 ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.632 -15.814 21.226 1.00 13.02 ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 13.199 -15.476 21.208 1.00 13.37 ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.403 -16.570 21.906 1.00 14.20 ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.892 -17.692 22.136 1.00 14.64 ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.711 -15.272 19.771 1.00 15.37 ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.887 -16.413 18.938 1.00 15.13 ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 11.156 -16.261 22.274 1.00 14.85 ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.284 -17.224 22.910 1.00 15.84 ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.460  -18.007 21.885 1.00 17.49 ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 9.114  -17.501 20.816 1.00 18.84 ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.387  -16.508 23.924 1.00 17.81 ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.554  -15.593 23.234 1.00 21.90 ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 9.106  -19.231 22.240 1.00 17.14 ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.350  -20.125 21.349 1.00 18.43 ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 7.055  -20.582 22.035 1.00 20.79 ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.984  -20.689 23.254 1.00 21.52 ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 9.202  -21.394 20.975 1.00 19.33 ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.436  -22.162 22.139 1.00 20.05 ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.577 -21.053 20.352 1.00 19.23 ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 6.074  -20.940 21.225 1.00 23.09 ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.822  -21.497 21.749 1.00 25.15 ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 5.038  -22.973 22.095 1.00 25.13 ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.639  -23.435 23.176 1.00 27.04 ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.702  -21.240 20.725 1.00 29.56 ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 4.073  -21.836 19.488 1.00 32.70 ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.525  -19.761 20.440 1.00 29.56 ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.695  -23.725 21.189 1.00 22.26 ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.946  -25.139 21.427 1.00 23.03 ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.272  -25.406 22.176 1.00 20.80 ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.223  -24.640 22.006 1.00 20.48 ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.963  -25.895 20.103 1.00 25.54 ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.367  -26.464 22.956 1.00 19.96 ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.591  -26.815 23.674 1.00 20.48 ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.587  -27.449 22.689 1.00 20.49 ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 9.203  -28.236 21.814 1.00 22.41 ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.289  -27.787 24.832 1.00 25.63 ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.601  -27.097 26.016 1.00 33.86 ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.548  -28.058 27.175 1.00 44.89 ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.679  -28.938 27.251 1.00 49.78 ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.484  -27.946 28.098 1.00 47.07 ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.855 -27.092 22.837 1.00 18.46 ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.953 -27.661 22.049 1.00 18.09 ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.609 -28.826 22.767 1.00 17.66 ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.405 -29.020 23.979 1.00 19.85 ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.432 -29.556 22.047 1.00 15.91 ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 14.006 -30.784 22.575 1.00 16.29 ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.509 -30.837 22.612 1.00 17.19 ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 16.067 -31.916 22.933 1.00 19.50 ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.445 -31.967 21.788 1.00 16.59 ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.641 -32.042 21.860 1.00 23.50 ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.205 -29.773 22.250 1.00 14.47 ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.654 -29.784 22.298 1.00 13.92 ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 18.062 -29.595 23.755 1.00 15.32 ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.345 -28.953 24.572 1.00 17.07 ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.230 -28.625 21.456 1.00 15.37 ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 18.047 -28.768 19.960 1.00 18.11 ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 18.042 -29.908 19.465 1.00 19.79 ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.905 -27.727 19.270 1.00 15.95 ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.181 -30.228 24.116 1.00 13.55 ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.796 -30.045 25.444 1.00 14.11 ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 21.071 -29.203 25.275 1.00 13.92 ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.893 -29.521 24.395 1.00 14.49 ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 20.168 -31.415 26.028 1.00 16.24 ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.959 -32.202 26.236 1.00 18.03 ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.973 -31.305 27.340 1.00 18.16 ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.254 -28.191 26.116 1.00 13.62 ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.466 -27.371 26.064 1.00 13.31 ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.567 -28.060 26.900 1.00 12.56 ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.344 -28.519 28.029 1.00 13.62 ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.213 -25.983 26.652 1.00 14.49 ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.997 -25.308 26.002 1.00 15.83 ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.469 -25.107 26.565 1.00 14.75 ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 21.204 -25.127 24.445 1.00 16.78 ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.766 -28.154 26.346 1.00 11.88 ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.909 -28.711 27.081 1.00 11.43 ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.278 -27.782 28.260 1.00 11.87 ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.256 -26.547 28.123 1.00 12.11 ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 27.093 -28.814 26.128 1.00 12.20 ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.638 -28.405 29.417 1.00 11.97 ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 27.087 -27.658 30.586 1.00 12.33 ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.404 -28.311 30.947 1.00 12.22 ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.435 -29.343 31.624 1.00 13.19 ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 26.050 -27.713 31.724 1.00 12.59 ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.695 -27.113 31.303 1.00 12.06 ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.725 -25.620 30.962 1.00 14.20 ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.367 -25.179 30.595 1.00 14.54 ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 23.104 -24.071 29.891 1.00 14.06 ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 24.078 -23.241 29.554 1.00 14.04 ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.845 -23.779 29.528 1.00 15.77 ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.520 -27.721 30.451 1.00 11.72 ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.865 -28.366 30.453 1.00 11.83 ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.915 -27.398 29.911 1.00 12.31 ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.582 -26.284 29.482 1.00 12.50 ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.791 -29.584 29.524 1.00 12.08 ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.631 -29.123 27.747 1.00 11.99 ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 33.200 -27.860 29.957 1.00 12.85 ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.297 -27.108 29.356 1.00 13.50 ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.977 -27.974 28.266 1.00 13.57 ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 36.180 -27.820 28.012 1.00 14.34 ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.339 -26.671 30.407 1.00 15.53 ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.997 -27.777 31.156 1.00 20.36 ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.676 -28.943 30.904 1.00 19.03 ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.939 -27.478 31.955 1.00 26.07 ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 34.199 -28.833 27.551 1.00 12.33 ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.775 -29.603 26.420 1.00 11.87 ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.437 -28.689 25.410 1.00 12.03 ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.973 -27.562 25.159 1.00 12.39 ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.681 -30.414 25.700 1.00 12.92 ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 33.061 -31.845 26.611 1.00 12.71 ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.454 -29.227 24.785 1.00 11.15 ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 37.136 -28.634 23.633 1.00 12.24 ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.193 -29.592 22.481 1.00 11.75 ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.942 -29.351 21.519 1.00 11.80 ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.564 -28.171 23.997 1.00 12.70 ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.566 -26.921 24.910 1.00 15.44 ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.963 -26.371 25.107 1.00 18.63 ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.495 -26.412 26.236 1.00 20.72 ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.562 -25.818 24.048 1.00 16.24 ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.378 -30.664 22.484 1.00 11.64 ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.266 -31.538 21.309 1.00 12.56 ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.766 -31.757 21.047 1.00 12.28 ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.996 -31.909 22.001 1.00 12.65 ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 37.000 -32.850 21.406 1.00 14.69 ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.431 -33.560 22.442 1.00 19.86 ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.475 -32.668 21.689 1.00 14.89 ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.372 -31.844 19.799 1.00 10.84 ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.971 -32.017 19.436 1.00 11.07 ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.835 -32.226 17.937 1.00 10.00 ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.822 -32.526 17.264 1.00 11.53 ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.610 -32.115 17.460 1.00 10.30 ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.309 -32.330 16.023 1.00 9.77  ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.389 -31.195 15.602 1.00 9.80  ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.449 -30.876 16.316 1.00 10.97 ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.556 -33.699 15.860 1.00 10.46 ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 30.048 -33.886 14.413 1.00 11.95 ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.471 -34.881 16.284 1.00 11.26 ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.649 -30.591 14.421 1.00 9.69  ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.753 -29.519 13.921 1.00 9.19  ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.189 -29.849 12.539 1.00 9.85  ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.861 -30.557 11.774 1.00 10.64 ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.447 -28.097 13.908 1.00 10.28 ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.322 -27.795 12.693 1.00 10.11 ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.610 -28.299 12.596 1.00 11.11 ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.874 -26.956 11.672 1.00 10.13 ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.424 -28.019 11.496 1.00 11.48 ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.706 -26.625 10.589 1.00 11.43 ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.972 -27.161 10.517 1.00 11.67 ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.816 -26.860 9.461  1.00 14.26 ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 28.039 -29.282 12.254 1.00 10.03 ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.419 -29.439 10.933 1.00 10.76 ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.809 -28.288 10.013 1.00 11.10 ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.578 -27.105 10.324 1.00 10.93 ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.897 -29.533 11.023 1.00 11.79 ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.282 -29.829 9.658  1.00 13.17 ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.626 -30.983 8.958  1.00 13.69 ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.467 -28.910 9.035  1.00 13.27 ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.133 -31.236 7.669  1.00 14.36 ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.937 -29.171 7.758  1.00 14.30 ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.284 -30.336 7.100  1.00 14.58 ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.796 -30.592 5.813  1.00 18.40 ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.323 -28.655 8.830  1.00 10.64 ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.739 -27.720 7.762  1.00 11.07 ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.805 -27.891 6.558  1.00 11.89 ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.965 -28.830 5.776  1.00 12.53 ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.181 -27.995 7.396  1.00 11.01 ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.776 -26.955 6.041  1.00 13.05 ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.819 -26.990 6.433  1.00 13.12 ? 66  SER   C N   1 
ATOM   1558 C  CA  A SER   B 1 60  ? 25.848 -27.170 5.365  0.50 14.83 ? 66  SER   C CA  1 
ATOM   1559 C  CA  B SER   B 1 60  ? 25.846 -27.119 5.358  0.50 14.02 ? 66  SER   C CA  1 
ATOM   1560 C  C   . SER   B 1 60  ? 26.475 -27.037 3.964  1.00 15.15 ? 66  SER   C C   1 
ATOM   1561 O  O   . SER   B 1 60  ? 26.035 -27.760 3.072  1.00 16.82 ? 66  SER   C O   1 
ATOM   1562 C  CB  A SER   B 1 60  ? 24.658 -26.259 5.564  0.50 18.09 ? 66  SER   C CB  1 
ATOM   1563 C  CB  B SER   B 1 60  ? 24.758 -26.074 5.493  0.50 14.89 ? 66  SER   C CB  1 
ATOM   1564 O  OG  A SER   B 1 60  ? 25.092 -24.913 5.588  0.50 21.68 ? 66  SER   C OG  1 
ATOM   1565 O  OG  B SER   B 1 60  ? 23.796 -26.295 4.469  0.50 13.89 ? 66  SER   C OG  1 
ATOM   1566 N  N   . SER   B 1 61  ? 27.497 -26.190 3.800  1.00 13.97 ? 67  SER   C N   1 
ATOM   1567 C  CA  . SER   B 1 61  ? 28.147 -26.020 2.482  1.00 13.84 ? 67  SER   C CA  1 
ATOM   1568 C  C   . SER   B 1 61  ? 28.970 -27.219 2.069  1.00 15.23 ? 67  SER   C C   1 
ATOM   1569 O  O   . SER   B 1 61  ? 29.460 -27.234 0.927  1.00 17.11 ? 67  SER   C O   1 
ATOM   1570 C  CB  . SER   B 1 61  ? 28.981 -24.752 2.449  1.00 14.98 ? 67  SER   C CB  1 
ATOM   1571 O  OG  . SER   B 1 61  ? 30.093 -24.876 3.323  1.00 15.43 ? 67  SER   C OG  1 
ATOM   1572 N  N   . ARG   B 1 62  ? 29.089 -28.274 2.899  1.00 13.58 ? 68  ARG   C N   1 
ATOM   1573 C  CA  . ARG   B 1 62  ? 29.715 -29.542 2.535  1.00 14.51 ? 68  ARG   C CA  1 
ATOM   1574 C  C   . ARG   B 1 62  ? 28.786 -30.743 2.759  1.00 15.66 ? 68  ARG   C C   1 
ATOM   1575 O  O   . ARG   B 1 62  ? 29.201 -31.888 2.567  1.00 16.73 ? 68  ARG   C O   1 
ATOM   1576 C  CB  . ARG   B 1 62  ? 31.009 -29.746 3.317  1.00 14.97 ? 68  ARG   C CB  1 
ATOM   1577 C  CG  . ARG   B 1 62  ? 32.050 -28.642 3.116  1.00 17.24 ? 68  ARG   C CG  1 
ATOM   1578 C  CD  . ARG   B 1 62  ? 32.721 -28.885 1.801  1.00 18.27 ? 68  ARG   C CD  1 
ATOM   1579 N  NE  . ARG   B 1 62  ? 33.776 -27.876 1.519  1.00 18.74 ? 68  ARG   C NE  1 
ATOM   1580 C  CZ  . ARG   B 1 62  ? 33.584 -26.721 0.910  1.00 20.71 ? 68  ARG   C CZ  1 
ATOM   1581 N  NH1 . ARG   B 1 62  ? 32.391 -26.412 0.416  1.00 22.28 ? 68  ARG   C NH1 1 
ATOM   1582 N  NH2 . ARG   B 1 62  ? 34.620 -25.918 0.641  1.00 23.24 ? 68  ARG   C NH2 1 
ATOM   1583 N  N   . ARG   B 1 63  ? 27.586 -30.496 3.302  1.00 16.76 ? 69  ARG   C N   1 
ATOM   1584 C  CA  . ARG   B 1 63  ? 26.617 -31.551 3.742  1.00 17.79 ? 69  ARG   C CA  1 
ATOM   1585 C  C   . ARG   B 1 63  ? 27.317 -32.584 4.612  1.00 18.46 ? 69  ARG   C C   1 
ATOM   1586 O  O   . ARG   B 1 63  ? 27.180 -33.801 4.400  1.00 19.88 ? 69  ARG   C O   1 
ATOM   1587 C  CB  . ARG   B 1 63  ? 25.980 -32.258 2.510  1.00 19.79 ? 69  ARG   C CB  1 
ATOM   1588 C  CG  . ARG   B 1 63  ? 25.132 -31.385 1.655  1.00 21.80 ? 69  ARG   C CG  1 
ATOM   1589 C  CD  . ARG   B 1 63  ? 23.912 -30.926 2.383  1.00 27.25 ? 69  ARG   C CD  1 
ATOM   1590 N  NE  . ARG   B 1 63  ? 22.908 -30.479 1.428  1.00 29.51 ? 69  ARG   C NE  1 
ATOM   1591 C  CZ  . ARG   B 1 63  ? 22.754 -29.229 1.025  1.00 29.53 ? 69  ARG   C CZ  1 
ATOM   1592 N  NH1 . ARG   B 1 63  ? 23.550 -28.271 1.484  1.00 26.37 ? 69  ARG   C NH1 1 
ATOM   1593 N  NH2 . ARG   B 1 63  ? 21.792 -28.921 0.169  1.00 30.24 ? 69  ARG   C NH2 1 
ATOM   1594 N  N   . LYS   B 1 64  ? 28.142 -32.107 5.554  1.00 15.40 ? 70  LYS   C N   1 
ATOM   1595 C  CA  . LYS   B 1 64  ? 28.953 -33.024 6.353  1.00 15.19 ? 70  LYS   C CA  1 
ATOM   1596 C  C   . LYS   B 1 64  ? 29.024 -32.550 7.795  1.00 13.69 ? 70  LYS   C C   1 
ATOM   1597 O  O   . LYS   B 1 64  ? 29.045 -31.328 8.041  1.00 13.82 ? 70  LYS   C O   1 
ATOM   1598 C  CB  . LYS   B 1 64  ? 30.394 -33.070 5.777  1.00 18.93 ? 70  LYS   C CB  1 
ATOM   1599 C  CG  . LYS   B 1 64  ? 30.544 -34.071 4.622  1.00 30.98 ? 70  LYS   C CG  1 
ATOM   1600 C  CD  . LYS   B 1 64  ? 31.986 -34.317 4.233  1.00 39.86 ? 70  LYS   C CD  1 
ATOM   1601 C  CE  . LYS   B 1 64  ? 32.086 -35.254 3.055  1.00 45.10 ? 70  LYS   C CE  1 
ATOM   1602 N  NZ  . LYS   B 1 64  ? 31.364 -34.723 1.867  1.00 49.18 ? 70  LYS   C NZ  1 
ATOM   1603 N  N   . HIS   B 1 65  ? 29.136 -33.510 8.703  1.00 13.40 ? 71  HIS   C N   1 
ATOM   1604 C  CA  . HIS   B 1 65  ? 29.449 -33.250 10.110 1.00 12.71 ? 71  HIS   C CA  1 
ATOM   1605 C  C   . HIS   B 1 65  ? 30.918 -33.526 10.278 1.00 14.41 ? 71  HIS   C C   1 
ATOM   1606 O  O   . HIS   B 1 65  ? 31.401 -34.627 9.949  1.00 17.67 ? 71  HIS   C O   1 
ATOM   1607 C  CB  . HIS   B 1 65  ? 28.616 -34.153 11.040 1.00 12.37 ? 71  HIS   C CB  1 
ATOM   1608 C  CG  . HIS   B 1 65  ? 27.140 -33.886 10.990 1.00 11.23 ? 71  HIS   C CG  1 
ATOM   1609 N  ND1 . HIS   B 1 65  ? 26.466 -33.127 11.953 1.00 14.70 ? 71  HIS   C ND1 1 
ATOM   1610 C  CD2 . HIS   B 1 65  ? 26.237 -34.299 10.074 1.00 12.09 ? 71  HIS   C CD2 1 
ATOM   1611 C  CE1 . HIS   B 1 65  ? 25.177 -33.139 11.597 1.00 12.48 ? 71  HIS   C CE1 1 
ATOM   1612 N  NE2 . HIS   B 1 65  ? 24.993 -33.837 10.502 1.00 15.86 ? 71  HIS   C NE2 1 
ATOM   1613 N  N   . TYR   B 1 66  ? 31.667 -32.586 10.881 1.00 11.83 ? 72  TYR   C N   1 
ATOM   1614 C  CA  . TYR   B 1 66  ? 33.119 -32.773 11.041 1.00 11.38 ? 72  TYR   C CA  1 
ATOM   1615 C  C   . TYR   B 1 66  ? 33.484 -32.829 12.514 1.00 10.77 ? 72  TYR   C C   1 
ATOM   1616 O  O   . TYR   B 1 66  ? 33.054 -31.944 13.281 1.00 10.52 ? 72  TYR   C O   1 
ATOM   1617 C  CB  . TYR   B 1 66  ? 33.857 -31.559 10.455 1.00 11.96 ? 72  TYR   C CB  1 
ATOM   1618 C  CG  . TYR   B 1 66  ? 33.822 -31.443 8.942  1.00 13.27 ? 72  TYR   C CG  1 
ATOM   1619 C  CD1 . TYR   B 1 66  ? 34.640 -32.227 8.149  1.00 14.51 ? 72  TYR   C CD1 1 
ATOM   1620 C  CD2 . TYR   B 1 66  ? 33.027 -30.499 8.311  1.00 13.90 ? 72  TYR   C CD2 1 
ATOM   1621 C  CE1 . TYR   B 1 66  ? 34.647 -32.092 6.766  1.00 16.30 ? 72  TYR   C CE1 1 
ATOM   1622 C  CE2 . TYR   B 1 66  ? 33.024 -30.353 6.928  1.00 15.08 ? 72  TYR   C CE2 1 
ATOM   1623 C  CZ  . TYR   B 1 66  ? 33.808 -31.176 6.159  1.00 16.01 ? 72  TYR   C CZ  1 
ATOM   1624 O  OH  . TYR   B 1 66  ? 33.795 -30.963 4.786  1.00 18.25 ? 72  TYR   C OH  1 
ATOM   1625 N  N   . PRO   B 1 67  ? 34.305 -33.792 12.925 1.00 11.06 ? 73  PRO   C N   1 
ATOM   1626 C  CA  . PRO   B 1 67  ? 34.847 -33.767 14.300 1.00 11.12 ? 73  PRO   C CA  1 
ATOM   1627 C  C   . PRO   B 1 67  ? 35.955 -32.697 14.406 1.00 11.87 ? 73  PRO   C C   1 
ATOM   1628 O  O   . PRO   B 1 67  ? 36.826 -32.643 13.515 1.00 13.52 ? 73  PRO   C O   1 
ATOM   1629 C  CB  . PRO   B 1 67  ? 35.424 -35.183 14.507 1.00 13.05 ? 73  PRO   C CB  1 
ATOM   1630 C  CG  . PRO   B 1 67  ? 35.742 -35.673 13.103 1.00 15.71 ? 73  PRO   C CG  1 
ATOM   1631 C  CD  . PRO   B 1 67  ? 34.790 -34.967 12.134 1.00 12.37 ? 73  PRO   C CD  1 
ATOM   1632 N  N   . VAL   B 1 68  ? 35.930 -31.901 15.462 1.00 10.51 ? 74  VAL   C N   1 
ATOM   1633 C  CA  . VAL   B 1 68  ? 36.897 -30.794 15.588 1.00 11.35 ? 74  VAL   C CA  1 
ATOM   1634 C  C   . VAL   B 1 68  ? 37.317 -30.629 17.021 1.00 11.35 ? 74  VAL   C C   1 
ATOM   1635 O  O   . VAL   B 1 68  ? 36.590 -30.944 17.968 1.00 11.42 ? 74  VAL   C O   1 
ATOM   1636 C  CB  . VAL   B 1 68  ? 36.284 -29.427 15.120 1.00 13.27 ? 74  VAL   C CB  1 
ATOM   1637 C  CG1 . VAL   B 1 68  ? 36.162 -29.348 13.570 1.00 16.00 ? 74  VAL   C CG1 1 
ATOM   1638 C  CG2 . VAL   B 1 68  ? 34.962 -29.108 15.819 1.00 13.79 ? 74  VAL   C CG2 1 
ATOM   1639 N  N   . SER   B 1 69  ? 38.531 -30.095 17.213 1.00 11.17 ? 75  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 69  ? 38.987 -29.490 18.461 1.00 11.52 ? 75  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 69  ? 38.709 -28.001 18.375 1.00 10.64 ? 75  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 69  ? 38.863 -27.395 17.301 1.00 11.01 ? 75  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 69  ? 40.485 -29.664 18.627 1.00 12.76 ? 75  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 69  ? 40.777 -31.041 18.764 1.00 18.52 ? 75  SER   C OG  1 
ATOM   1645 N  N   . PHE   B 1 70  ? 38.273 -27.376 19.444 1.00 10.30 ? 76  PHE   C N   1 
ATOM   1646 C  CA  . PHE   B 1 70  ? 37.918 -25.941 19.404 1.00 10.34 ? 76  PHE   C CA  1 
ATOM   1647 C  C   . PHE   B 1 70  ? 38.431 -25.219 20.662 1.00 11.03 ? 76  PHE   C C   1 
ATOM   1648 O  O   . PHE   B 1 70  ? 38.583 -25.838 21.717 1.00 11.31 ? 76  PHE   C O   1 
ATOM   1649 C  CB  . PHE   B 1 70  ? 36.398 -25.725 19.173 1.00 10.79 ? 76  PHE   C CB  1 
ATOM   1650 C  CG  . PHE   B 1 70  ? 35.500 -26.422 20.183 1.00 9.60  ? 76  PHE   C CG  1 
ATOM   1651 C  CD1 . PHE   B 1 70  ? 35.047 -27.721 19.962 1.00 10.38 ? 76  PHE   C CD1 1 
ATOM   1652 C  CD2 . PHE   B 1 70  ? 35.031 -25.750 21.310 1.00 11.14 ? 76  PHE   C CD2 1 
ATOM   1653 C  CE1 . PHE   B 1 70  ? 34.244 -28.363 20.883 1.00 10.17 ? 76  PHE   C CE1 1 
ATOM   1654 C  CE2 . PHE   B 1 70  ? 34.181 -26.406 22.224 1.00 11.02 ? 76  PHE   C CE2 1 
ATOM   1655 C  CZ  . PHE   B 1 70  ? 33.806 -27.710 22.023 1.00 10.97 ? 76  PHE   C CZ  1 
ATOM   1656 N  N   . SER   B 1 71  ? 38.682 -23.930 20.530 1.00 10.57 ? 77  SER   C N   1 
ATOM   1657 C  CA  . SER   B 1 71  ? 39.273 -23.155 21.604 1.00 11.51 ? 77  SER   C CA  1 
ATOM   1658 C  C   . SER   B 1 71  ? 38.287 -22.788 22.706 1.00 12.49 ? 77  SER   C C   1 
ATOM   1659 O  O   . SER   B 1 71  ? 37.081 -23.026 22.596 1.00 13.00 ? 77  SER   C O   1 
ATOM   1660 C  CB  . SER   B 1 71  ? 39.988 -21.932 21.027 1.00 12.08 ? 77  SER   C CB  1 
ATOM   1661 O  OG  . SER   B 1 71  ? 39.084 -21.030 20.393 1.00 13.84 ? 77  SER   C OG  1 
ATOM   1662 N  N   . LYS   B 1 72  ? 38.796 -22.141 23.757 1.00 13.68 ? 78  LYS   C N   1 
ATOM   1663 C  CA  . LYS   B 1 72  ? 37.938 -21.700 24.860 1.00 13.79 ? 78  LYS   C CA  1 
ATOM   1664 C  C   . LYS   B 1 72  ? 37.243 -20.382 24.489 1.00 13.71 ? 78  LYS   C C   1 
ATOM   1665 O  O   . LYS   B 1 72  ? 37.830 -19.557 23.765 1.00 15.78 ? 78  LYS   C O   1 
ATOM   1666 C  CB  . LYS   B 1 72  ? 38.839 -21.467 26.094 1.00 16.64 ? 78  LYS   C CB  1 
ATOM   1667 C  CG  . LYS   B 1 72  ? 39.550 -22.738 26.522 1.00 20.09 ? 78  LYS   C CG  1 
ATOM   1668 C  CD  . LYS   B 1 72  ? 40.049 -22.732 27.990 1.00 31.94 ? 78  LYS   C CD  1 
ATOM   1669 C  CE  . LYS   B 1 72  ? 39.933 -24.157 28.575 1.00 40.83 ? 78  LYS   C CE  1 
ATOM   1670 N  NZ  . LYS   B 1 72  ? 39.943 -24.201 30.069 1.00 46.17 ? 78  LYS   C NZ  1 
ATOM   1671 N  N   . PRO   B 1 73  ? 35.984 -20.154 24.937 1.00 12.94 ? 79  PRO   C N   1 
ATOM   1672 C  CA  . PRO   B 1 73  ? 35.249 -18.921 24.518 1.00 13.76 ? 79  PRO   C CA  1 
ATOM   1673 C  C   . PRO   B 1 73  ? 36.001 -17.658 24.909 1.00 14.59 ? 79  PRO   C C   1 
ATOM   1674 O  O   . PRO   B 1 73  ? 36.469 -17.516 26.064 1.00 16.25 ? 79  PRO   C O   1 
ATOM   1675 C  CB  . PRO   B 1 73  ? 33.936 -18.969 25.310 1.00 15.54 ? 79  PRO   C CB  1 
ATOM   1676 C  CG  . PRO   B 1 73  ? 33.779 -20.388 25.738 1.00 17.95 ? 79  PRO   C CG  1 
ATOM   1677 C  CD  . PRO   B 1 73  ? 35.173 -21.031 25.816 1.00 13.61 ? 79  PRO   C CD  1 
ATOM   1678 N  N   . SER   B 1 74  ? 36.254 -16.783 23.939 1.00 13.82 ? 80  SER   C N   1 
ATOM   1679 C  CA  . SER   B 1 74  ? 37.117 -15.600 24.162 1.00 15.02 ? 80  SER   C CA  1 
ATOM   1680 C  C   . SER   B 1 74  ? 36.729 -14.432 23.243 1.00 14.44 ? 80  SER   C C   1 
ATOM   1681 O  O   . SER   B 1 74  ? 35.852 -14.577 22.387 1.00 14.24 ? 80  SER   C O   1 
ATOM   1682 C  CB  . SER   B 1 74  ? 38.573 -15.974 23.855 1.00 17.96 ? 80  SER   C CB  1 
ATOM   1683 O  OG  . SER   B 1 74  ? 38.925 -17.096 24.653 1.00 27.34 ? 80  SER   C OG  1 
ATOM   1684 N  N   . LEU   B 1 75  ? 37.383 -13.287 23.429 1.00 15.39 ? 81  LEU   C N   1 
ATOM   1685 C  CA  . LEU   B 1 75  ? 37.193 -12.076 22.632 1.00 16.28 ? 81  LEU   C CA  1 
ATOM   1686 C  C   . LEU   B 1 75  ? 38.216 -12.137 21.490 1.00 17.02 ? 81  LEU   C C   1 
ATOM   1687 O  O   . LEU   B 1 75  ? 39.440 -12.084 21.759 1.00 19.35 ? 81  LEU   C O   1 
ATOM   1688 C  CB  . LEU   B 1 75  ? 37.431 -10.845 23.537 1.00 18.62 ? 81  LEU   C CB  1 
ATOM   1689 C  CG  . LEU   B 1 75  ? 37.178 -9.487  22.913 1.00 20.73 ? 81  LEU   C CG  1 
ATOM   1690 C  CD1 . LEU   B 1 75  ? 35.704 -9.297  22.627 1.00 19.85 ? 81  LEU   C CD1 1 
ATOM   1691 C  CD2 . LEU   B 1 75  ? 37.661 -8.355  23.870 1.00 23.60 ? 81  LEU   C CD2 1 
ATOM   1692 N  N   . ILE   B 1 76  ? 37.757 -12.302 20.266 1.00 17.38 ? 82  ILE   C N   1 
ATOM   1693 C  CA  . ILE   B 1 76  ? 38.582 -12.524 19.075 1.00 18.73 ? 82  ILE   C CA  1 
ATOM   1694 C  C   . ILE   B 1 76  ? 38.317 -11.471 18.013 1.00 18.37 ? 82  ILE   C C   1 
ATOM   1695 O  O   . ILE   B 1 76  ? 37.143 -11.172 17.731 1.00 16.84 ? 82  ILE   C O   1 
ATOM   1696 C  CB  . ILE   B 1 76  ? 38.272 -13.930 18.523 1.00 21.73 ? 82  ILE   C CB  1 
ATOM   1697 C  CG1 . ILE   B 1 76  ? 38.595 -15.009 19.578 1.00 24.27 ? 82  ILE   C CG1 1 
ATOM   1698 C  CG2 . ILE   B 1 76  ? 38.974 -14.201 17.176 1.00 24.00 ? 82  ILE   C CG2 1 
ATOM   1699 C  CD1 . ILE   B 1 76  ? 38.398 -16.324 19.197 1.00 24.37 ? 82  ILE   C CD1 1 
ATOM   1700 N  N   . PHE   B 1 77  ? 39.375 -10.955 17.358 1.00 18.75 ? 83  PHE   C N   1 
ATOM   1701 C  CA  . PHE   B 1 77  ? 39.172 -10.028 16.248 1.00 19.16 ? 83  PHE   C CA  1 
ATOM   1702 C  C   . PHE   B 1 77  ? 38.802 -10.906 15.028 1.00 19.70 ? 83  PHE   C C   1 
ATOM   1703 O  O   . PHE   B 1 77  ? 39.554 -11.815 14.647 1.00 21.60 ? 83  PHE   C O   1 
ATOM   1704 C  CB  . PHE   B 1 77  ? 40.470 -9.234  15.936 1.00 19.05 ? 83  PHE   C CB  1 
ATOM   1705 C  CG  . PHE   B 1 77  ? 40.177 -8.110  14.964 1.00 19.69 ? 83  PHE   C CG  1 
ATOM   1706 C  CD1 . PHE   B 1 77  ? 39.466 -6.999  15.361 1.00 20.51 ? 83  PHE   C CD1 1 
ATOM   1707 C  CD2 . PHE   B 1 77  ? 40.553 -8.206  13.626 1.00 21.51 ? 83  PHE   C CD2 1 
ATOM   1708 C  CE1 . PHE   B 1 77  ? 39.188 -5.965  14.459 1.00 22.05 ? 83  PHE   C CE1 1 
ATOM   1709 C  CE2 . PHE   B 1 77  ? 40.285 -7.167  12.737 1.00 22.11 ? 83  PHE   C CE2 1 
ATOM   1710 C  CZ  . PHE   B 1 77  ? 39.610 -6.057  13.161 1.00 21.89 ? 83  PHE   C CZ  1 
ATOM   1711 N  N   . VAL   B 1 78  ? 37.676 -10.595 14.384 1.00 17.22 ? 84  VAL   C N   1 
ATOM   1712 C  CA  . VAL   B 1 78  ? 37.161 -11.315 13.220 1.00 16.45 ? 84  VAL   C CA  1 
ATOM   1713 C  C   . VAL   B 1 78  ? 37.250 -10.360 12.012 1.00 16.22 ? 84  VAL   C C   1 
ATOM   1714 O  O   . VAL   B 1 78  ? 36.782 -9.229  12.112 1.00 16.49 ? 84  VAL   C O   1 
ATOM   1715 C  CB  . VAL   B 1 78  ? 35.680 -11.745 13.519 1.00 16.20 ? 84  VAL   C CB  1 
ATOM   1716 C  CG1 . VAL   B 1 78  ? 35.104 -12.500 12.328 1.00 16.55 ? 84  VAL   C CG1 1 
ATOM   1717 C  CG2 . VAL   B 1 78  ? 35.558 -12.567 14.826 1.00 16.67 ? 84  VAL   C CG2 1 
ATOM   1718 N  N   . GLU   B 1 79  ? 37.742 -10.836 10.867 1.00 14.92 ? 85  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 79  ? 37.785 -10.017 9.650  1.00 15.33 ? 85  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 79  ? 36.368 -9.774  9.114  1.00 15.08 ? 85  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 79  ? 35.397 -10.465 9.510  1.00 15.01 ? 85  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 79  ? 38.666 -10.684 8.569  1.00 17.29 ? 85  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 79  ? 40.149 -10.770 8.937  1.00 20.76 ? 85  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 79  ? 40.779 -9.396  9.136  1.00 25.82 ? 85  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 79  ? 40.416 -8.422  8.425  1.00 28.29 ? 85  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 79  ? 41.623 -9.272  10.053 1.00 27.45 ? 85  GLU   C OE2 1 
ATOM   1727 N  N   . ALA   B 1 80  ? 36.216 -8.784  8.235  1.00 16.15 ? 86  ALA   C N   1 
ATOM   1728 C  CA  . ALA   B 1 80  ? 34.927 -8.476  7.668  1.00 17.04 ? 86  ALA   C CA  1 
ATOM   1729 C  C   . ALA   B 1 80  ? 34.311 -9.662  6.955  1.00 17.62 ? 86  ALA   C C   1 
ATOM   1730 O  O   . ALA   B 1 80  ? 35.038 -10.449 6.334  1.00 19.13 ? 86  ALA   C O   1 
ATOM   1731 C  CB  . ALA   B 1 80  ? 35.070 -7.325  6.682  1.00 17.98 ? 86  ALA   C CB  1 
ATOM   1732 N  N   . SER   B 1 81  ? 33.000 -9.816  7.120  1.00 16.12 ? 87  SER   C N   1 
ATOM   1733 C  CA  . SER   B 1 81  ? 32.277 -10.835 6.424  1.00 17.07 ? 87  SER   C CA  1 
ATOM   1734 C  C   . SER   B 1 81  ? 31.164 -10.139 5.622  1.00 17.78 ? 87  SER   C C   1 
ATOM   1735 O  O   . SER   B 1 81  ? 30.998 -8.888  5.659  1.00 18.61 ? 87  SER   C O   1 
ATOM   1736 C  CB  . SER   B 1 81  ? 31.646 -11.812 7.426  1.00 16.35 ? 87  SER   C CB  1 
ATOM   1737 O  OG  . SER   B 1 81  ? 30.644 -11.122 8.166  1.00 16.70 ? 87  SER   C OG  1 
ATOM   1738 N  N   . GLU   B 1 82  ? 30.340 -10.948 4.969  1.00 19.11 ? 88  GLU   C N   1 
ATOM   1739 C  CA  . GLU   B 1 82  ? 29.239 -10.327 4.235  1.00 20.18 ? 88  GLU   C CA  1 
ATOM   1740 C  C   . GLU   B 1 82  ? 28.180 -9.684  5.176  1.00 20.45 ? 88  GLU   C C   1 
ATOM   1741 O  O   . GLU   B 1 82  ? 27.403 -8.826  4.732  1.00 21.98 ? 88  GLU   C O   1 
ATOM   1742 C  CB  . GLU   B 1 82  ? 28.636 -11.307 3.232  1.00 24.87 ? 88  GLU   C CB  1 
ATOM   1743 C  CG  . GLU   B 1 82  ? 27.768 -12.394 3.794  1.00 33.73 ? 88  GLU   C CG  1 
ATOM   1744 C  CD  . GLU   B 1 82  ? 27.110 -13.202 2.688  1.00 38.27 ? 88  GLU   C CD  1 
ATOM   1745 O  OE1 . GLU   B 1 82  ? 27.769 -13.415 1.642  1.00 37.62 ? 88  GLU   C OE1 1 
ATOM   1746 O  OE2 . GLU   B 1 82  ? 25.939 -13.614 2.866  1.00 39.44 ? 88  GLU   C OE2 1 
ATOM   1747 N  N   . TYR   B 1 83  ? 28.186 -10.039 6.460  1.00 17.67 ? 89  TYR   C N   1 
ATOM   1748 C  CA  . TYR   B 1 83  ? 27.170 -9.566  7.381  1.00 16.66 ? 89  TYR   C CA  1 
ATOM   1749 C  C   . TYR   B 1 83  ? 27.689 -8.715  8.569  1.00 17.23 ? 89  TYR   C C   1 
ATOM   1750 O  O   . TYR   B 1 83  ? 26.838 -8.135  9.279  1.00 17.72 ? 89  TYR   C O   1 
ATOM   1751 C  CB  . TYR   B 1 83  ? 26.302 -10.759 7.878  1.00 16.07 ? 89  TYR   C CB  1 
ATOM   1752 C  CG  . TYR   B 1 83  ? 27.143 -11.954 8.344  1.00 15.72 ? 89  TYR   C CG  1 
ATOM   1753 C  CD1 . TYR   B 1 83  ? 27.548 -12.949 7.453  1.00 15.19 ? 89  TYR   C CD1 1 
ATOM   1754 C  CD2 . TYR   B 1 83  ? 27.537 -12.081 9.668  1.00 15.79 ? 89  TYR   C CD2 1 
ATOM   1755 C  CE1 . TYR   B 1 83  ? 28.326 -14.037 7.879  1.00 14.75 ? 89  TYR   C CE1 1 
ATOM   1756 C  CE2 . TYR   B 1 83  ? 28.309 -13.152 10.102 1.00 15.75 ? 89  TYR   C CE2 1 
ATOM   1757 C  CZ  . TYR   B 1 83  ? 28.712 -14.129 9.201  1.00 15.04 ? 89  TYR   C CZ  1 
ATOM   1758 O  OH  . TYR   B 1 83  ? 29.517 -15.174 9.608  1.00 15.72 ? 89  TYR   C OH  1 
ATOM   1759 N  N   . TYR   B 1 84  ? 28.988 -8.600  8.817  1.00 15.23 ? 90  TYR   C N   1 
ATOM   1760 C  CA  . TYR   B 1 84  ? 29.530 -7.687  9.828  1.00 15.75 ? 90  TYR   C CA  1 
ATOM   1761 C  C   . TYR   B 1 84  ? 30.839 -7.061  9.285  1.00 15.89 ? 90  TYR   C C   1 
ATOM   1762 O  O   . TYR   B 1 84  ? 31.586 -7.720  8.550  1.00 15.82 ? 90  TYR   C O   1 
ATOM   1763 C  CB  . TYR   B 1 84  ? 29.905 -8.439  11.154 1.00 14.70 ? 90  TYR   C CB  1 
ATOM   1764 C  CG  . TYR   B 1 84  ? 28.729 -8.865  12.020 1.00 13.22 ? 90  TYR   C CG  1 
ATOM   1765 C  CD1 . TYR   B 1 84  ? 27.820 -7.923  12.535 1.00 13.34 ? 90  TYR   C CD1 1 
ATOM   1766 C  CD2 . TYR   B 1 84  ? 28.529 -10.186 12.330 1.00 13.12 ? 90  TYR   C CD2 1 
ATOM   1767 C  CE1 . TYR   B 1 84  ? 26.749 -8.317  13.347 1.00 14.06 ? 90  TYR   C CE1 1 
ATOM   1768 C  CE2 . TYR   B 1 84  ? 27.474 -10.588 13.145 1.00 13.49 ? 90  TYR   C CE2 1 
ATOM   1769 C  CZ  . TYR   B 1 84  ? 26.583 -9.657  13.648 1.00 13.61 ? 90  TYR   C CZ  1 
ATOM   1770 O  OH  . TYR   B 1 84  ? 25.531 -10.061 14.470 1.00 13.75 ? 90  TYR   C OH  1 
ATOM   1771 N  N   . PRO   B 1 85  ? 31.208 -5.856  9.750  1.00 16.52 ? 91  PRO   C N   1 
ATOM   1772 C  CA  . PRO   B 1 85  ? 32.557 -5.338  9.458  1.00 16.03 ? 91  PRO   C CA  1 
ATOM   1773 C  C   . PRO   B 1 85  ? 33.594 -6.126  10.293 1.00 16.05 ? 91  PRO   C C   1 
ATOM   1774 O  O   . PRO   B 1 85  ? 33.238 -6.930  11.202 1.00 15.79 ? 91  PRO   C O   1 
ATOM   1775 C  CB  . PRO   B 1 85  ? 32.460 -3.874  9.928  1.00 16.45 ? 91  PRO   C CB  1 
ATOM   1776 C  CG  . PRO   B 1 85  ? 31.519 -3.943  11.079 1.00 18.02 ? 91  PRO   C CG  1 
ATOM   1777 C  CD  . PRO   B 1 85  ? 30.453 -4.993  10.696 1.00 16.94 ? 91  PRO   C CD  1 
ATOM   1778 N  N   . ALA   B 1 86  ? 34.885 -5.859  10.072 1.00 15.95 ? 92  ALA   C N   1 
ATOM   1779 C  CA  . ALA   B 1 86  ? 35.939 -6.414  10.907 1.00 17.00 ? 92  ALA   C CA  1 
ATOM   1780 C  C   . ALA   B 1 86  ? 35.743 -5.843  12.332 1.00 17.78 ? 92  ALA   C C   1 
ATOM   1781 O  O   . ALA   B 1 86  ? 35.458 -4.630  12.466 1.00 19.36 ? 92  ALA   C O   1 
ATOM   1782 C  CB  . ALA   B 1 86  ? 37.309 -6.008  10.340 1.00 16.93 ? 92  ALA   C CB  1 
ATOM   1783 N  N   . ARG   B 1 87  ? 35.763 -6.706  13.355 1.00 17.27 ? 93  ARG   C N   1 
ATOM   1784 C  CA  . ARG   B 1 87  ? 35.445 -6.270  14.704 1.00 16.88 ? 93  ARG   C CA  1 
ATOM   1785 C  C   . ARG   B 1 87  ? 35.846 -7.345  15.711 1.00 17.02 ? 93  ARG   C C   1 
ATOM   1786 O  O   . ARG   B 1 87  ? 36.091 -8.487  15.326 1.00 16.40 ? 93  ARG   C O   1 
ATOM   1787 C  CB  . ARG   B 1 87  ? 33.915 -5.994  14.851 1.00 18.03 ? 93  ARG   C CB  1 
ATOM   1788 C  CG  . ARG   B 1 87  ? 33.097 -7.308  14.832 1.00 15.84 ? 93  ARG   C CG  1 
ATOM   1789 C  CD  . ARG   B 1 87  ? 31.599 -7.061  14.721 1.00 16.71 ? 93  ARG   C CD  1 
ATOM   1790 N  NE  . ARG   B 1 87  ? 30.903 -8.317  15.052 1.00 15.94 ? 93  ARG   C NE  1 
ATOM   1791 C  CZ  . ARG   B 1 87  ? 29.862 -8.487  15.859 1.00 16.39 ? 93  ARG   C CZ  1 
ATOM   1792 N  NH1 . ARG   B 1 87  ? 29.230 -7.437  16.383 1.00 17.72 ? 93  ARG   C NH1 1 
ATOM   1793 N  NH2 . ARG   B 1 87  ? 29.436 -9.719  16.151 1.00 16.82 ? 93  ARG   C NH2 1 
ATOM   1794 N  N   . TYR   B 1 88  ? 35.809 -7.001  17.009 1.00 17.85 ? 94  TYR   C N   1 
ATOM   1795 C  CA  . TYR   B 1 88  ? 35.948 -8.004  18.053 1.00 19.41 ? 94  TYR   C CA  1 
ATOM   1796 C  C   . TYR   B 1 88  ? 34.584 -8.646  18.338 1.00 16.97 ? 94  TYR   C C   1 
ATOM   1797 O  O   . TYR   B 1 88  ? 33.563 -7.952  18.480 1.00 17.74 ? 94  TYR   C O   1 
ATOM   1798 C  CB  . TYR   B 1 88  ? 36.447 -7.379  19.378 1.00 22.22 ? 94  TYR   C CB  1 
ATOM   1799 C  CG  . TYR   B 1 88  ? 37.903 -7.027  19.286 1.00 23.87 ? 94  TYR   C CG  1 
ATOM   1800 C  CD1 . TYR   B 1 88  ? 38.875 -7.989  19.478 1.00 25.03 ? 94  TYR   C CD1 1 
ATOM   1801 C  CD2 . TYR   B 1 88  ? 38.304 -5.738  18.920 1.00 24.53 ? 94  TYR   C CD2 1 
ATOM   1802 C  CE1 . TYR   B 1 88  ? 40.226 -7.679  19.337 1.00 25.92 ? 94  TYR   C CE1 1 
ATOM   1803 C  CE2 . TYR   B 1 88  ? 39.636 -5.419  18.763 1.00 25.55 ? 94  TYR   C CE2 1 
ATOM   1804 C  CZ  . TYR   B 1 88  ? 40.597 -6.385  18.989 1.00 26.19 ? 94  TYR   C CZ  1 
ATOM   1805 O  OH  . TYR   B 1 88  ? 41.909 -6.006  18.825 1.00 29.29 ? 94  TYR   C OH  1 
ATOM   1806 N  N   . GLN   B 1 89  ? 34.574 -9.973  18.383 1.00 16.02 ? 95  GLN   C N   1 
ATOM   1807 C  CA  . GLN   B 1 89  ? 33.386 -10.727 18.755 1.00 14.37 ? 95  GLN   C CA  1 
ATOM   1808 C  C   . GLN   B 1 89  ? 33.693 -11.464 20.068 1.00 14.35 ? 95  GLN   C C   1 
ATOM   1809 O  O   . GLN   B 1 89  ? 34.784 -12.062 20.206 1.00 15.22 ? 95  GLN   C O   1 
ATOM   1810 C  CB  . GLN   B 1 89  ? 33.016 -11.673 17.610 1.00 15.27 ? 95  GLN   C CB  1 
ATOM   1811 C  CG  . GLN   B 1 89  ? 31.755 -12.489 17.928 1.00 15.91 ? 95  GLN   C CG  1 
ATOM   1812 C  CD  . GLN   B 1 89  ? 31.034 -13.034 16.707 1.00 14.02 ? 95  GLN   C CD  1 
ATOM   1813 O  OE1 . GLN   B 1 89  ? 30.988 -12.442 15.602 1.00 14.93 ? 95  GLN   C OE1 1 
ATOM   1814 N  NE2 . GLN   B 1 89  ? 30.477 -14.189 16.904 1.00 13.57 ? 95  GLN   C NE2 1 
ATOM   1815 N  N   . SER   B 1 90  ? 32.792 -11.439 21.016 1.00 13.31 ? 96  SER   C N   1 
ATOM   1816 C  CA  . SER   B 1 90  ? 32.961 -12.063 22.309 1.00 13.39 ? 96  SER   C CA  1 
ATOM   1817 C  C   . SER   B 1 90  ? 32.379 -13.491 22.368 1.00 12.85 ? 96  SER   C C   1 
ATOM   1818 O  O   . SER   B 1 90  ? 31.505 -13.846 21.563 1.00 12.54 ? 96  SER   C O   1 
ATOM   1819 C  CB  . SER   B 1 90  ? 32.409 -11.184 23.452 1.00 15.15 ? 96  SER   C CB  1 
ATOM   1820 O  OG  . SER   B 1 90  ? 31.003 -11.164 23.332 1.00 15.79 ? 96  SER   C OG  1 
ATOM   1821 N  N   . HIS   B 1 91  ? 32.825 -14.269 23.369 1.00 12.95 ? 97  HIS   C N   1 
ATOM   1822 C  CA  . HIS   B 1 91  ? 32.348 -15.628 23.640 1.00 12.63 ? 97  HIS   C CA  1 
ATOM   1823 C  C   . HIS   B 1 91  ? 32.438 -16.506 22.360 1.00 12.57 ? 97  HIS   C C   1 
ATOM   1824 O  O   . HIS   B 1 91  ? 31.532 -17.326 22.111 1.00 13.20 ? 97  HIS   C O   1 
ATOM   1825 C  CB  . HIS   B 1 91  ? 30.896 -15.593 24.184 1.00 13.66 ? 97  HIS   C CB  1 
ATOM   1826 C  CG  . HIS   B 1 91  ? 30.760 -14.854 25.499 1.00 14.32 ? 97  HIS   C CG  1 
ATOM   1827 N  ND1 . HIS   B 1 91  ? 30.734 -15.518 26.706 1.00 16.70 ? 97  HIS   C ND1 1 
ATOM   1828 C  CD2 . HIS   B 1 91  ? 30.683 -13.510 25.736 1.00 15.16 ? 97  HIS   C CD2 1 
ATOM   1829 C  CE1 . HIS   B 1 91  ? 30.623 -14.590 27.650 1.00 17.15 ? 97  HIS   C CE1 1 
ATOM   1830 N  NE2 . HIS   B 1 91  ? 30.575 -13.368 27.112 1.00 17.14 ? 97  HIS   C NE2 1 
ATOM   1831 N  N   . LEU   B 1 92  ? 33.516 -16.352 21.628 1.00 11.45 ? 98  LEU   C N   1 
ATOM   1832 C  CA  . LEU   B 1 92  ? 33.717 -17.025 20.352 1.00 11.62 ? 98  LEU   C CA  1 
ATOM   1833 C  C   . LEU   B 1 92  ? 34.782 -18.108 20.535 1.00 11.52 ? 98  LEU   C C   1 
ATOM   1834 O  O   . LEU   B 1 92  ? 35.766 -17.907 21.260 1.00 11.65 ? 98  LEU   C O   1 
ATOM   1835 C  CB  . LEU   B 1 92  ? 34.185 -16.003 19.254 1.00 13.01 ? 98  LEU   C CB  1 
ATOM   1836 C  CG  . LEU   B 1 92  ? 34.294 -16.569 17.842 1.00 13.65 ? 98  LEU   C CG  1 
ATOM   1837 C  CD1 . LEU   B 1 92  ? 32.949 -16.929 17.278 1.00 13.52 ? 98  LEU   C CD1 1 
ATOM   1838 C  CD2 . LEU   B 1 92  ? 34.966 -15.542 16.881 1.00 16.11 ? 98  LEU   C CD2 1 
ATOM   1839 N  N   . MET   B 1 93  ? 34.611 -19.265 19.872 1.00 10.86 ? 99  MET   C N   1 
ATOM   1840 C  CA  . MET   B 1 93  ? 35.556 -20.392 19.921 1.00 9.99  ? 99  MET   C CA  1 
ATOM   1841 C  C   . MET   B 1 93  ? 35.953 -20.720 18.486 1.00 11.22 ? 99  MET   C C   1 
ATOM   1842 O  O   . MET   B 1 93  ? 35.075 -20.758 17.616 1.00 12.20 ? 99  MET   C O   1 
ATOM   1843 C  CB  . MET   B 1 93  ? 34.831 -21.611 20.488 1.00 11.90 ? 99  MET   C CB  1 
ATOM   1844 C  CG  . MET   B 1 93  ? 34.336 -21.348 21.920 1.00 12.98 ? 99  MET   C CG  1 
ATOM   1845 S  SD  . MET   B 1 93  ? 33.332 -22.661 22.579 1.00 13.87 ? 99  MET   C SD  1 
ATOM   1846 C  CE  . MET   B 1 93  ? 31.886 -22.563 21.493 1.00 14.54 ? 99  MET   C CE  1 
ATOM   1847 N  N   . LEU   B 1 94  ? 37.223 -20.987 18.216 1.00 11.04 ? 100 LEU   C N   1 
ATOM   1848 C  CA  . LEU   B 1 94  ? 37.673 -21.286 16.858 1.00 11.58 ? 100 LEU   C CA  1 
ATOM   1849 C  C   . LEU   B 1 94  ? 38.111 -22.743 16.707 1.00 11.01 ? 100 LEU   C C   1 
ATOM   1850 O  O   . LEU   B 1 94  ? 38.635 -23.346 17.656 1.00 11.90 ? 100 LEU   C O   1 
ATOM   1851 C  CB  . LEU   B 1 94  ? 38.917 -20.414 16.473 1.00 12.24 ? 100 LEU   C CB  1 
ATOM   1852 C  CG  . LEU   B 1 94  ? 38.730 -18.904 16.436 1.00 13.57 ? 100 LEU   C CG  1 
ATOM   1853 C  CD1 . LEU   B 1 94  ? 40.039 -18.210 15.981 1.00 17.24 ? 100 LEU   C CD1 1 
ATOM   1854 C  CD2 . LEU   B 1 94  ? 37.529 -18.494 15.578 1.00 15.78 ? 100 LEU   C CD2 1 
ATOM   1855 N  N   . ALA   B 1 95  ? 37.961 -23.253 15.498 1.00 11.15 ? 101 ALA   C N   1 
ATOM   1856 C  CA  . ALA   B 1 95  ? 38.474 -24.566 15.099 1.00 11.28 ? 101 ALA   C CA  1 
ATOM   1857 C  C   . ALA   B 1 95  ? 39.016 -24.444 13.667 1.00 11.38 ? 101 ALA   C C   1 
ATOM   1858 O  O   . ALA   B 1 95  ? 38.644 -23.519 12.937 1.00 11.12 ? 101 ALA   C O   1 
ATOM   1859 C  CB  . ALA   B 1 95  ? 37.366 -25.648 15.146 1.00 12.14 ? 101 ALA   C CB  1 
ATOM   1860 N  N   . VAL   B 1 96  ? 39.865 -25.364 13.270 1.00 11.41 ? 102 VAL   C N   1 
ATOM   1861 C  CA  . VAL   B 1 96  ? 40.325 -25.465 11.881 1.00 12.64 ? 102 VAL   C CA  1 
ATOM   1862 C  C   . VAL   B 1 96  ? 39.264 -26.197 11.058 1.00 13.03 ? 102 VAL   C C   1 
ATOM   1863 O  O   . VAL   B 1 96  ? 38.933 -27.374 11.359 1.00 14.79 ? 102 VAL   C O   1 
ATOM   1864 C  CB  . VAL   B 1 96  ? 41.699 -26.202 11.847 1.00 13.70 ? 102 VAL   C CB  1 
ATOM   1865 C  CG1 . VAL   B 1 96  ? 42.182 -26.353 10.400 1.00 15.99 ? 102 VAL   C CG1 1 
ATOM   1866 C  CG2 . VAL   B 1 96  ? 42.714 -25.437 12.691 1.00 14.79 ? 102 VAL   C CG2 1 
ATOM   1867 N  N   . GLY   B 1 97  ? 38.660 -25.502 10.120 1.00 13.75 ? 103 GLY   C N   1 
ATOM   1868 C  CA  . GLY   B 1 97  ? 37.592 -26.125 9.340  1.00 14.49 ? 103 GLY   C CA  1 
ATOM   1869 C  C   . GLY   B 1 97  ? 36.927 -25.162 8.432  1.00 14.43 ? 103 GLY   C C   1 
ATOM   1870 O  O   . GLY   B 1 97  ? 37.198 -23.945 8.477  1.00 16.34 ? 103 GLY   C O   1 
ATOM   1871 N  N   . HIS   B 1 98  ? 36.060 -25.666 7.582  1.00 14.36 ? 104 HIS   C N   1 
ATOM   1872 C  CA  . HIS   B 1 98  ? 35.365 -24.854 6.618  1.00 14.41 ? 104 HIS   C CA  1 
ATOM   1873 C  C   . HIS   B 1 98  ? 34.106 -24.151 7.147  1.00 13.31 ? 104 HIS   C C   1 
ATOM   1874 O  O   . HIS   B 1 98  ? 33.287 -24.782 7.835  1.00 13.61 ? 104 HIS   C O   1 
ATOM   1875 C  CB  . HIS   B 1 98  ? 35.024 -25.718 5.430  1.00 17.34 ? 104 HIS   C CB  1 
ATOM   1876 C  CG  . HIS   B 1 98  ? 34.467 -24.916 4.325  1.00 19.01 ? 104 HIS   C CG  1 
ATOM   1877 N  ND1 . HIS   B 1 98  ? 35.237 -23.966 3.649  1.00 20.90 ? 104 HIS   C ND1 1 
ATOM   1878 C  CD2 . HIS   B 1 98  ? 33.199 -24.896 3.854  1.00 21.06 ? 104 HIS   C CD2 1 
ATOM   1879 C  CE1 . HIS   B 1 98  ? 34.385 -23.364 2.828  1.00 22.71 ? 104 HIS   C CE1 1 
ATOM   1880 N  NE2 . HIS   B 1 98  ? 33.164 -23.921 2.884  1.00 23.22 ? 104 HIS   C NE2 1 
ATOM   1881 N  N   . SER   B 1 99  ? 33.901 -22.869 6.771  1.00 13.55 ? 105 SER   C N   1 
ATOM   1882 C  CA  . SER   B 1 99  ? 32.676 -22.119 7.157  1.00 14.33 ? 105 SER   C CA  1 
ATOM   1883 C  C   . SER   B 1 99  ? 32.448 -20.971 6.173  1.00 15.54 ? 105 SER   C C   1 
ATOM   1884 O  O   . SER   B 1 99  ? 33.317 -20.098 6.040  1.00 18.19 ? 105 SER   C O   1 
ATOM   1885 C  CB  . SER   B 1 99  ? 32.907 -21.513 8.546  1.00 15.38 ? 105 SER   C CB  1 
ATOM   1886 O  OG  . SER   B 1 99  ? 31.798 -20.692 8.920  1.00 16.23 ? 105 SER   C OG  1 
ATOM   1887 N  N   . GLU   B 1 100 ? 31.335 -20.982 5.491  1.00 14.66 ? 106 GLU   C N   1 
ATOM   1888 C  CA  . GLU   B 1 100 ? 30.898 -19.895 4.591  1.00 16.02 ? 106 GLU   C CA  1 
ATOM   1889 C  C   . GLU   B 1 100 ? 29.717 -19.220 5.254  1.00 14.51 ? 106 GLU   C C   1 
ATOM   1890 O  O   . GLU   B 1 100 ? 29.149 -19.759 6.206  1.00 14.41 ? 106 GLU   C O   1 
ATOM   1891 C  CB  . GLU   B 1 100 ? 30.387 -20.527 3.295  1.00 20.28 ? 106 GLU   C CB  1 
ATOM   1892 C  CG  . GLU   B 1 100 ? 31.491 -21.101 2.462  1.00 29.46 ? 106 GLU   C CG  1 
ATOM   1893 C  CD  . GLU   B 1 100 ? 30.989 -21.872 1.266  1.00 32.63 ? 106 GLU   C CD  1 
ATOM   1894 O  OE1 . GLU   B 1 100 ? 29.914 -21.533 0.717  1.00 36.58 ? 106 GLU   C OE1 1 
ATOM   1895 O  OE2 . GLU   B 1 100 ? 31.708 -22.805 0.865  1.00 33.10 ? 106 GLU   C OE2 1 
ATOM   1896 N  N   . PRO   B 1 101 ? 29.295 -18.018 4.780  1.00 15.43 ? 107 PRO   C N   1 
ATOM   1897 C  CA  . PRO   B 1 101 ? 28.179 -17.340 5.468  1.00 14.73 ? 107 PRO   C CA  1 
ATOM   1898 C  C   . PRO   B 1 101 ? 26.920 -18.200 5.638  1.00 15.42 ? 107 PRO   C C   1 
ATOM   1899 O  O   . PRO   B 1 101 ? 26.307 -18.143 6.712  1.00 15.50 ? 107 PRO   C O   1 
ATOM   1900 C  CB  . PRO   B 1 101 ? 27.921 -16.091 4.568  1.00 17.50 ? 107 PRO   C CB  1 
ATOM   1901 C  CG  . PRO   B 1 101 ? 29.247 -15.791 4.035  1.00 21.15 ? 107 PRO   C CG  1 
ATOM   1902 C  CD  . PRO   B 1 101 ? 29.944 -17.132 3.768  1.00 18.30 ? 107 PRO   C CD  1 
ATOM   1903 N  N   . GLY   B 1 102 ? 26.596 -19.023 4.625  1.00 14.85 ? 108 GLY   C N   1 
ATOM   1904 C  CA  . GLY   B 1 102 ? 25.387 -19.861 4.706  1.00 15.82 ? 108 GLY   C CA  1 
ATOM   1905 C  C   . GLY   B 1 102 ? 25.467 -20.969 5.745  1.00 14.67 ? 108 GLY   C C   1 
ATOM   1906 O  O   . GLY   B 1 102 ? 24.469 -21.635 6.063  1.00 15.36 ? 108 GLY   C O   1 
ATOM   1907 N  N   . ASP   B 1 103 ? 26.675 -21.235 6.299  1.00 13.15 ? 109 ASP   C N   1 
ATOM   1908 C  CA  . ASP   B 1 103 ? 26.836 -22.270 7.340  1.00 12.34 ? 109 ASP   C CA  1 
ATOM   1909 C  C   . ASP   B 1 103 ? 26.467 -21.764 8.711  1.00 12.50 ? 109 ASP   C C   1 
ATOM   1910 O  O   . ASP   B 1 103 ? 26.361 -22.555 9.644  1.00 12.32 ? 109 ASP   C O   1 
ATOM   1911 C  CB  . ASP   B 1 103 ? 28.306 -22.726 7.364  1.00 13.26 ? 109 ASP   C CB  1 
ATOM   1912 C  CG  . ASP   B 1 103 ? 28.633 -23.512 6.119  1.00 14.67 ? 109 ASP   C CG  1 
ATOM   1913 O  OD1 . ASP   B 1 103 ? 27.788 -24.283 5.668  1.00 14.91 ? 109 ASP   C OD1 1 
ATOM   1914 O  OD2 . ASP   B 1 103 ? 29.778 -23.365 5.584  1.00 15.13 ? 109 ASP   C OD2 1 
ATOM   1915 N  N   . CYS   B 1 104 ? 26.274 -20.433 8.905  1.00 11.48 ? 110 CYS   C N   1 
ATOM   1916 C  CA  . CYS   B 1 104 ? 25.870 -19.894 10.193 1.00 11.43 ? 110 CYS   C CA  1 
ATOM   1917 C  C   . CYS   B 1 104 ? 24.622 -20.603 10.696 1.00 11.69 ? 110 CYS   C C   1 
ATOM   1918 O  O   . CYS   B 1 104 ? 23.667 -20.810 9.926  1.00 13.29 ? 110 CYS   C O   1 
ATOM   1919 C  CB  . CYS   B 1 104 ? 25.639 -18.380 10.116 1.00 11.53 ? 110 CYS   C CB  1 
ATOM   1920 S  SG  . CYS   B 1 104 ? 27.179 -17.414 10.015 1.00 13.70 ? 110 CYS   C SG  1 
ATOM   1921 N  N   . GLY   B 1 105 ? 24.617 -20.943 11.966 1.00 10.71 ? 111 GLY   C N   1 
ATOM   1922 C  CA  . GLY   B 1 105 ? 23.484 -21.603 12.605 1.00 11.79 ? 111 GLY   C CA  1 
ATOM   1923 C  C   . GLY   B 1 105 ? 23.676 -23.107 12.723 1.00 11.45 ? 111 GLY   C C   1 
ATOM   1924 O  O   . GLY   B 1 105 ? 22.912 -23.765 13.453 1.00 12.47 ? 111 GLY   C O   1 
ATOM   1925 N  N   . GLY   B 1 106 ? 24.700 -23.669 12.054 1.00 11.61 ? 112 GLY   C N   1 
ATOM   1926 C  CA  . GLY   B 1 106 ? 24.999 -25.101 12.224 1.00 12.19 ? 112 GLY   C CA  1 
ATOM   1927 C  C   . GLY   B 1 106 ? 25.401 -25.414 13.664 1.00 11.17 ? 112 GLY   C C   1 
ATOM   1928 O  O   . GLY   B 1 106 ? 26.136 -24.632 14.297 1.00 10.95 ? 112 GLY   C O   1 
ATOM   1929 N  N   . ILE   B 1 107 ? 24.937 -26.541 14.185 1.00 10.94 ? 113 ILE   C N   1 
ATOM   1930 C  CA  . ILE   B 1 107 ? 25.214 -26.880 15.586 1.00 10.77 ? 113 ILE   C CA  1 
ATOM   1931 C  C   . ILE   B 1 107 ? 26.577 -27.526 15.765 1.00 10.23 ? 113 ILE   C C   1 
ATOM   1932 O  O   . ILE   B 1 107 ? 27.018 -28.368 14.978 1.00 10.17 ? 113 ILE   C O   1 
ATOM   1933 C  CB  . ILE   B 1 107 ? 24.089 -27.845 16.093 1.00 13.50 ? 113 ILE   C CB  1 
ATOM   1934 C  CG1 . ILE   B 1 107 ? 22.880 -26.879 16.536 1.00 16.90 ? 113 ILE   C CG1 1 
ATOM   1935 C  CG2 . ILE   B 1 107 ? 24.547 -28.685 17.326 1.00 13.72 ? 113 ILE   C CG2 1 
ATOM   1936 C  CD1 . ILE   B 1 107 ? 21.530 -27.552 16.936 1.00 20.65 ? 113 ILE   C CD1 1 
ATOM   1937 N  N   . LEU   B 1 108 ? 27.269 -27.080 16.852 1.00 9.49  ? 114 LEU   C N   1 
ATOM   1938 C  CA  . LEU   B 1 108 ? 28.450 -27.751 17.417 1.00 9.44  ? 114 LEU   C CA  1 
ATOM   1939 C  C   . LEU   B 1 108 ? 27.955 -28.525 18.665 1.00 9.36  ? 114 LEU   C C   1 
ATOM   1940 O  O   . LEU   B 1 108 ? 27.309 -27.928 19.530 1.00 10.11 ? 114 LEU   C O   1 
ATOM   1941 C  CB  . LEU   B 1 108 ? 29.504 -26.714 17.826 1.00 9.43  ? 114 LEU   C CB  1 
ATOM   1942 C  CG  . LEU   B 1 108 ? 30.702 -27.253 18.608 1.00 9.96  ? 114 LEU   C CG  1 
ATOM   1943 C  CD1 . LEU   B 1 108 ? 31.594 -28.165 17.729 1.00 11.30 ? 114 LEU   C CD1 1 
ATOM   1944 C  CD2 . LEU   B 1 108 ? 31.552 -26.071 19.117 1.00 11.05 ? 114 LEU   C CD2 1 
ATOM   1945 N  N   . ARG   B 1 109 ? 28.227 -29.836 18.712 1.00 9.81  ? 115 ARG   C N   1 
ATOM   1946 C  CA  . ARG   B 1 109 ? 27.770 -30.650 19.868 1.00 10.11 ? 115 ARG   C CA  1 
ATOM   1947 C  C   . ARG   B 1 109 ? 28.904 -31.482 20.429 1.00 10.86 ? 115 ARG   C C   1 
ATOM   1948 O  O   . ARG   B 1 109 ? 29.804 -31.933 19.699 1.00 11.54 ? 115 ARG   C O   1 
ATOM   1949 C  CB  . ARG   B 1 109 ? 26.603 -31.551 19.394 1.00 13.85 ? 115 ARG   C CB  1 
ATOM   1950 C  CG  . ARG   B 1 109 ? 27.022 -32.571 18.367 1.00 17.22 ? 115 ARG   C CG  1 
ATOM   1951 C  CD  . ARG   B 1 109 ? 25.847 -33.442 17.875 1.00 21.93 ? 115 ARG   C CD  1 
ATOM   1952 N  NE  . ARG   B 1 109 ? 24.962 -32.702 16.969 1.00 29.18 ? 115 ARG   C NE  1 
ATOM   1953 C  CZ  . ARG   B 1 109 ? 23.668 -32.484 17.192 1.00 37.92 ? 115 ARG   C CZ  1 
ATOM   1954 N  NH1 . ARG   B 1 109 ? 23.096 -32.926 18.306 1.00 40.65 ? 115 ARG   C NH1 1 
ATOM   1955 N  NH2 . ARG   B 1 109 ? 22.944 -31.797 16.316 1.00 40.33 ? 115 ARG   C NH2 1 
ATOM   1956 N  N   . CYS   B 1 110 ? 28.817 -31.731 21.735 1.00 10.46 ? 116 CYS   C N   1 
ATOM   1957 C  CA  . CYS   B 1 110 ? 29.774 -32.622 22.428 1.00 11.34 ? 116 CYS   C CA  1 
ATOM   1958 C  C   . CYS   B 1 110 ? 28.928 -33.706 23.118 1.00 12.98 ? 116 CYS   C C   1 
ATOM   1959 O  O   . CYS   B 1 110 ? 27.704 -33.808 22.917 1.00 12.80 ? 116 CYS   C O   1 
ATOM   1960 C  CB  . CYS   B 1 110 ? 30.593 -31.815 23.427 1.00 11.11 ? 116 CYS   C CB  1 
ATOM   1961 S  SG  . CYS   B 1 110 ? 29.582 -31.172 24.804 1.00 11.53 ? 116 CYS   C SG  1 
ATOM   1962 N  N   . GLN   B 1 111 ? 29.572 -34.559 23.949 1.00 13.86 ? 117 GLN   C N   1 
ATOM   1963 C  CA  . GLN   B 1 111 ? 28.824 -35.605 24.642 1.00 15.62 ? 117 GLN   C CA  1 
ATOM   1964 C  C   . GLN   B 1 111 ? 27.759 -35.051 25.575 1.00 15.41 ? 117 GLN   C C   1 
ATOM   1965 O  O   . GLN   B 1 111 ? 26.808 -35.779 25.919 1.00 17.19 ? 117 GLN   C O   1 
ATOM   1966 C  CB  . GLN   B 1 111 ? 29.753 -36.547 25.473 1.00 17.91 ? 117 GLN   C CB  1 
ATOM   1967 C  CG  . GLN   B 1 111 ? 30.500 -35.837 26.595 1.00 20.48 ? 117 GLN   C CG  1 
ATOM   1968 C  CD  . GLN   B 1 111 ? 31.444 -36.736 27.354 1.00 31.02 ? 117 GLN   C CD  1 
ATOM   1969 O  OE1 . GLN   B 1 111 ? 32.641 -36.787 27.067 1.00 34.88 ? 117 GLN   C OE1 1 
ATOM   1970 N  NE2 . GLN   B 1 111 ? 30.909 -37.429 28.341 1.00 30.65 ? 117 GLN   C NE2 1 
ATOM   1971 N  N   . HIS   B 1 112 ? 27.844 -33.757 25.980 1.00 12.94 ? 118 HIS   C N   1 
ATOM   1972 C  CA  . HIS   B 1 112 ? 26.891 -33.190 26.929 1.00 12.97 ? 118 HIS   C CA  1 
ATOM   1973 C  C   . HIS   B 1 112 ? 25.682 -32.514 26.281 1.00 13.99 ? 118 HIS   C C   1 
ATOM   1974 O  O   . HIS   B 1 112 ? 24.760 -32.079 26.974 1.00 15.10 ? 118 HIS   C O   1 
ATOM   1975 C  CB  . HIS   B 1 112 ? 27.625 -32.220 27.867 1.00 14.23 ? 118 HIS   C CB  1 
ATOM   1976 C  CG  . HIS   B 1 112 ? 28.798 -32.859 28.562 1.00 13.66 ? 118 HIS   C CG  1 
ATOM   1977 N  ND1 . HIS   B 1 112 ? 30.102 -32.581 28.181 1.00 11.93 ? 118 HIS   C ND1 1 
ATOM   1978 C  CD2 . HIS   B 1 112 ? 28.826 -33.687 29.633 1.00 15.70 ? 118 HIS   C CD2 1 
ATOM   1979 C  CE1 . HIS   B 1 112 ? 30.889 -33.301 28.974 1.00 13.50 ? 118 HIS   C CE1 1 
ATOM   1980 N  NE2 . HIS   B 1 112 ? 30.160 -33.948 29.878 1.00 15.89 ? 118 HIS   C NE2 1 
ATOM   1981 N  N   . GLY   B 1 113 ? 25.758 -32.245 24.973 1.00 13.15 ? 119 GLY   C N   1 
ATOM   1982 C  CA  . GLY   B 1 113 ? 24.692 -31.553 24.261 1.00 12.58 ? 119 GLY   C CA  1 
ATOM   1983 C  C   . GLY   B 1 113 ? 25.231 -30.503 23.320 1.00 11.86 ? 119 GLY   C C   1 
ATOM   1984 O  O   . GLY   B 1 113 ? 26.359 -30.607 22.815 1.00 11.37 ? 119 GLY   C O   1 
ATOM   1985 N  N   . VAL   B 1 114 ? 24.372 -29.479 23.060 1.00 10.95 ? 120 VAL   C N   1 
ATOM   1986 C  CA  . VAL   B 1 114 ? 24.718 -28.412 22.124 1.00 10.86 ? 120 VAL   C CA  1 
ATOM   1987 C  C   . VAL   B 1 114 ? 25.658 -27.423 22.801 1.00 11.33 ? 120 VAL   C C   1 
ATOM   1988 O  O   . VAL   B 1 114 ? 25.345 -26.845 23.864 1.00 11.73 ? 120 VAL   C O   1 
ATOM   1989 C  CB  . VAL   B 1 114 ? 23.420 -27.726 21.637 1.00 11.95 ? 120 VAL   C CB  1 
ATOM   1990 C  CG1 . VAL   B 1 114 ? 23.754 -26.491 20.792 1.00 13.40 ? 120 VAL   C CG1 1 
ATOM   1991 C  CG2 . VAL   B 1 114 ? 22.516 -28.716 20.875 1.00 13.55 ? 120 VAL   C CG2 1 
ATOM   1992 N  N   . VAL   B 1 115 ? 26.800 -27.182 22.168 1.00 9.89  ? 121 VAL   C N   1 
ATOM   1993 C  CA  . VAL   B 1 115 ? 27.817 -26.235 22.672 1.00 10.73 ? 121 VAL   C CA  1 
ATOM   1994 C  C   . VAL   B 1 115 ? 27.595 -24.807 22.159 1.00 11.87 ? 121 VAL   C C   1 
ATOM   1995 O  O   . VAL   B 1 115 ? 27.833 -23.825 22.886 1.00 11.80 ? 121 VAL   C O   1 
ATOM   1996 C  CB  . VAL   B 1 115 ? 29.223 -26.766 22.271 1.00 10.81 ? 121 VAL   C CB  1 
ATOM   1997 C  CG1 . VAL   B 1 115 ? 30.319 -25.753 22.610 1.00 12.62 ? 121 VAL   C CG1 1 
ATOM   1998 C  CG2 . VAL   B 1 115 ? 29.485 -28.153 22.884 1.00 11.52 ? 121 VAL   C CG2 1 
ATOM   1999 N  N   . GLY   B 1 116 ? 27.209 -24.703 20.889 1.00 10.49 ? 122 GLY   C N   1 
ATOM   2000 C  CA  . GLY   B 1 116 ? 27.003 -23.395 20.281 1.00 12.10 ? 122 GLY   C CA  1 
ATOM   2001 C  C   . GLY   B 1 116 ? 26.683 -23.570 18.805 1.00 10.62 ? 122 GLY   C C   1 
ATOM   2002 O  O   . GLY   B 1 116 ? 26.369 -24.679 18.360 1.00 10.84 ? 122 GLY   C O   1 
ATOM   2003 N  N   . ILE   B 1 117 ? 26.699 -22.417 18.070 1.00 10.53 ? 123 ILE   C N   1 
ATOM   2004 C  CA  . ILE   B 1 117 ? 26.323 -22.445 16.650 1.00 10.30 ? 123 ILE   C CA  1 
ATOM   2005 C  C   . ILE   B 1 117 ? 27.374 -21.698 15.855 1.00 10.42 ? 123 ILE   C C   1 
ATOM   2006 O  O   . ILE   B 1 117 ? 28.035 -20.750 16.341 1.00 10.90 ? 123 ILE   C O   1 
ATOM   2007 C  CB  . ILE   B 1 117 ? 24.913 -21.799 16.399 1.00 11.54 ? 123 ILE   C CB  1 
ATOM   2008 C  CG1 . ILE   B 1 117 ? 24.826 -20.401 17.046 1.00 12.90 ? 123 ILE   C CG1 1 
ATOM   2009 C  CG2 . ILE   B 1 117 ? 23.792 -22.748 16.837 1.00 13.27 ? 123 ILE   C CG2 1 
ATOM   2010 C  CD1 . ILE   B 1 117 ? 23.472 -19.600 16.589 1.00 13.53 ? 123 ILE   C CD1 1 
ATOM   2011 N  N   . VAL   B 1 118 ? 27.557 -22.133 14.599 1.00 9.79  ? 124 VAL   C N   1 
ATOM   2012 C  CA  . VAL   B 1 118 ? 28.484 -21.447 13.684 1.00 10.67 ? 124 VAL   C CA  1 
ATOM   2013 C  C   . VAL   B 1 118 ? 28.115 -19.959 13.581 1.00 10.55 ? 124 VAL   C C   1 
ATOM   2014 O  O   . VAL   B 1 118 ? 26.920 -19.631 13.367 1.00 10.77 ? 124 VAL   C O   1 
ATOM   2015 C  CB  . VAL   B 1 118 ? 28.475 -22.112 12.282 1.00 10.37 ? 124 VAL   C CB  1 
ATOM   2016 C  CG1 . VAL   B 1 118 ? 29.321 -21.348 11.276 1.00 11.06 ? 124 VAL   C CG1 1 
ATOM   2017 C  CG2 . VAL   B 1 118 ? 28.923 -23.576 12.330 1.00 10.78 ? 124 VAL   C CG2 1 
ATOM   2018 N  N   . SER   B 1 119 ? 29.152 -19.095 13.655 1.00 10.71 ? 125 SER   C N   1 
ATOM   2019 C  CA  . SER   B 1 119 ? 28.970 -17.649 13.543 1.00 10.09 ? 125 SER   C CA  1 
ATOM   2020 C  C   . SER   B 1 119 ? 29.960 -16.968 12.624 1.00 10.88 ? 125 SER   C C   1 
ATOM   2021 O  O   . SER   B 1 119 ? 29.634 -15.874 12.100 1.00 11.72 ? 125 SER   C O   1 
ATOM   2022 C  CB  . SER   B 1 119 ? 28.972 -17.049 14.944 1.00 11.22 ? 125 SER   C CB  1 
ATOM   2023 O  OG  . SER   B 1 119 ? 28.876 -15.612 14.916 1.00 12.47 ? 125 SER   C OG  1 
ATOM   2024 N  N   . THR   B 1 120 ? 31.199 -17.508 12.510 1.00 11.31 ? 126 THR   C N   1 
ATOM   2025 C  CA  . THR   B 1 120 ? 32.219 -16.822 11.693 1.00 11.60 ? 126 THR   C CA  1 
ATOM   2026 C  C   . THR   B 1 120 ? 32.930 -17.843 10.800 1.00 10.93 ? 126 THR   C C   1 
ATOM   2027 O  O   . THR   B 1 120 ? 32.846 -19.074 11.028 1.00 11.37 ? 126 THR   C O   1 
ATOM   2028 C  CB  . THR   B 1 120 ? 33.295 -16.108 12.577 1.00 11.52 ? 126 THR   C CB  1 
ATOM   2029 O  OG1 . THR   B 1 120 ? 34.136 -17.068 13.237 1.00 12.27 ? 126 THR   C OG1 1 
ATOM   2030 C  CG2 . THR   B 1 120 ? 32.700 -15.158 13.602 1.00 13.17 ? 126 THR   C CG2 1 
ATOM   2031 N  N   . GLY   B 1 121 ? 33.628 -17.356 9.802  1.00 12.41 ? 127 GLY   C N   1 
ATOM   2032 C  CA  . GLY   B 1 121 ? 34.425 -18.192 8.900  1.00 13.62 ? 127 GLY   C CA  1 
ATOM   2033 C  C   . GLY   B 1 121 ? 35.464 -17.354 8.175  1.00 16.32 ? 127 GLY   C C   1 
ATOM   2034 O  O   . GLY   B 1 121 ? 35.199 -16.210 7.798  1.00 19.10 ? 127 GLY   C O   1 
ATOM   2035 N  N   . GLY   B 1 122 ? 36.596 -17.923 7.889  1.00 19.58 ? 128 GLY   C N   1 
ATOM   2036 C  CA  . GLY   B 1 122 ? 37.651 -17.211 7.163  1.00 21.36 ? 128 GLY   C CA  1 
ATOM   2037 C  C   . GLY   B 1 122 ? 39.002 -17.771 7.464  1.00 21.58 ? 128 GLY   C C   1 
ATOM   2038 O  O   . GLY   B 1 122 ? 39.235 -18.254 8.557  1.00 21.32 ? 128 GLY   C O   1 
ATOM   2039 N  N   . ASN   B 1 123 ? 39.946 -17.645 6.511  1.00 20.43 ? 129 ASN   C N   1 
ATOM   2040 C  CA  . ASN   B 1 123 ? 41.332 -18.081 6.709  1.00 20.74 ? 129 ASN   C CA  1 
ATOM   2041 C  C   . ASN   B 1 123 ? 41.393 -19.548 7.133  1.00 18.90 ? 129 ASN   C C   1 
ATOM   2042 O  O   . ASN   B 1 123 ? 42.327 -19.934 7.849  1.00 21.59 ? 129 ASN   C O   1 
ATOM   2043 C  CB  . ASN   B 1 123 ? 42.121 -17.149 7.710  1.00 24.75 ? 129 ASN   C CB  1 
ATOM   2044 C  CG  . ASN   B 1 123 ? 42.953 -16.031 7.087  1.00 30.82 ? 129 ASN   C CG  1 
ATOM   2045 O  OD1 . ASN   B 1 123 ? 43.265 -16.031 5.884  1.00 32.44 ? 129 ASN   C OD1 1 
ATOM   2046 N  ND2 . ASN   B 1 123 ? 43.329 -15.021 7.882  1.00 32.86 ? 129 ASN   C ND2 1 
ATOM   2047 N  N   . GLY   B 1 124 ? 40.459 -20.385 6.661  1.00 17.33 ? 130 GLY   C N   1 
ATOM   2048 C  CA  . GLY   B 1 124 ? 40.476 -21.804 7.057  1.00 17.08 ? 130 GLY   C CA  1 
ATOM   2049 C  C   . GLY   B 1 124 ? 40.061 -22.108 8.491  1.00 15.40 ? 130 GLY   C C   1 
ATOM   2050 O  O   . GLY   B 1 124 ? 40.313 -23.229 8.987  1.00 15.59 ? 130 GLY   C O   1 
ATOM   2051 N  N   . LEU   B 1 125 ? 39.433 -21.145 9.136  1.00 13.96 ? 131 LEU   C N   1 
ATOM   2052 C  CA  . LEU   B 1 125 ? 38.953 -21.302 10.503 1.00 13.65 ? 131 LEU   C CA  1 
ATOM   2053 C  C   . LEU   B 1 125 ? 37.431 -21.175 10.531 1.00 13.46 ? 131 LEU   C C   1 
ATOM   2054 O  O   . LEU   B 1 125 ? 36.827 -20.430 9.712  1.00 16.58 ? 131 LEU   C O   1 
ATOM   2055 C  CB  . LEU   B 1 125 ? 39.582 -20.223 11.445 1.00 15.39 ? 131 LEU   C CB  1 
ATOM   2056 C  CG  . LEU   B 1 125 ? 41.125 -20.288 11.526 1.00 17.89 ? 131 LEU   C CG  1 
ATOM   2057 C  CD1 . LEU   B 1 125 ? 41.765 -18.956 11.934 1.00 22.72 ? 131 LEU   C CD1 1 
ATOM   2058 C  CD2 . LEU   B 1 125 ? 41.618 -21.489 12.262 1.00 19.40 ? 131 LEU   C CD2 1 
ATOM   2059 N  N   . VAL   B 1 126 ? 36.814 -21.861 11.461 1.00 11.01 ? 132 VAL   C N   1 
ATOM   2060 C  CA  . VAL   B 1 126 ? 35.373 -21.732 11.685 1.00 10.57 ? 132 VAL   C CA  1 
ATOM   2061 C  C   . VAL   B 1 126 ? 35.217 -21.272 13.151 1.00 10.44 ? 132 VAL   C C   1 
ATOM   2062 O  O   . VAL   B 1 126 ? 35.881 -21.797 14.071 1.00 11.15 ? 132 VAL   C O   1 
ATOM   2063 C  CB  . VAL   B 1 126 ? 34.620 -23.058 11.450 1.00 11.18 ? 132 VAL   C CB  1 
ATOM   2064 C  CG1 . VAL   B 1 126 ? 35.225 -24.260 12.146 1.00 13.40 ? 132 VAL   C CG1 1 
ATOM   2065 C  CG2 . VAL   B 1 126 ? 33.105 -22.936 11.785 1.00 11.71 ? 132 VAL   C CG2 1 
ATOM   2066 N  N   . GLY   B 1 127 ? 34.335 -20.314 13.357 1.00 10.38 ? 133 GLY   C N   1 
ATOM   2067 C  CA  . GLY   B 1 127 ? 34.096 -19.793 14.698 1.00 10.79 ? 133 GLY   C CA  1 
ATOM   2068 C  C   . GLY   B 1 127 ? 32.669 -20.095 15.158 1.00 10.37 ? 133 GLY   C C   1 
ATOM   2069 O  O   . GLY   B 1 127 ? 31.710 -19.951 14.366 1.00 11.07 ? 133 GLY   C O   1 
ATOM   2070 N  N   . PHE   B 1 128 ? 32.548 -20.484 16.429 1.00 9.82  ? 134 PHE   C N   1 
ATOM   2071 C  CA  . PHE   B 1 128 ? 31.250 -20.849 17.062 1.00 9.95  ? 134 PHE   C CA  1 
ATOM   2072 C  C   . PHE   B 1 128 ? 30.910 -19.915 18.215 1.00 9.90  ? 134 PHE   C C   1 
ATOM   2073 O  O   . PHE   B 1 128 ? 31.783 -19.644 19.058 1.00 10.33 ? 134 PHE   C O   1 
ATOM   2074 C  CB  . PHE   B 1 128 ? 31.315 -22.290 17.638 1.00 10.27 ? 134 PHE   C CB  1 
ATOM   2075 C  CG  . PHE   B 1 128 ? 31.832 -23.301 16.616 1.00 10.12 ? 134 PHE   C CG  1 
ATOM   2076 C  CD1 . PHE   B 1 128 ? 30.969 -23.896 15.699 1.00 10.84 ? 134 PHE   C CD1 1 
ATOM   2077 C  CD2 . PHE   B 1 128 ? 33.160 -23.689 16.629 1.00 10.81 ? 134 PHE   C CD2 1 
ATOM   2078 C  CE1 . PHE   B 1 128 ? 31.459 -24.862 14.790 1.00 10.78 ? 134 PHE   C CE1 1 
ATOM   2079 C  CE2 . PHE   B 1 128 ? 33.651 -24.645 15.715 1.00 11.30 ? 134 PHE   C CE2 1 
ATOM   2080 C  CZ  . PHE   B 1 128 ? 32.794 -25.222 14.817 1.00 11.42 ? 134 PHE   C CZ  1 
ATOM   2081 N  N   . ALA   B 1 129 ? 29.663 -19.415 18.242 1.00 10.72 ? 135 ALA   C N   1 
ATOM   2082 C  CA  . ALA   B 1 129 ? 29.184 -18.602 19.346 1.00 10.13 ? 135 ALA   C CA  1 
ATOM   2083 C  C   . ALA   B 1 129 ? 28.781 -19.596 20.476 1.00 10.52 ? 135 ALA   C C   1 
ATOM   2084 O  O   . ALA   B 1 129 ? 27.885 -20.433 20.313 1.00 10.85 ? 135 ALA   C O   1 
ATOM   2085 C  CB  . ALA   B 1 129 ? 27.946 -17.820 18.878 1.00 11.41 ? 135 ALA   C CB  1 
ATOM   2086 N  N   . ASP   B 1 130 ? 29.489 -19.532 21.603 1.00 10.37 ? 136 ASP   C N   1 
ATOM   2087 C  CA  . ASP   B 1 130 ? 29.192 -20.410 22.751 1.00 10.84 ? 136 ASP   C CA  1 
ATOM   2088 C  C   . ASP   B 1 130 ? 27.838 -20.056 23.356 1.00 11.48 ? 136 ASP   C C   1 
ATOM   2089 O  O   . ASP   B 1 130 ? 27.467 -18.861 23.432 1.00 11.75 ? 136 ASP   C O   1 
ATOM   2090 C  CB  . ASP   B 1 130 ? 30.296 -20.182 23.822 1.00 11.83 ? 136 ASP   C CB  1 
ATOM   2091 C  CG  . ASP   B 1 130 ? 30.155 -21.109 25.019 1.00 14.49 ? 136 ASP   C CG  1 
ATOM   2092 O  OD1 . ASP   B 1 130 ? 30.021 -22.334 24.821 1.00 14.04 ? 136 ASP   C OD1 1 
ATOM   2093 O  OD2 . ASP   B 1 130 ? 30.095 -20.584 26.176 1.00 17.48 ? 136 ASP   C OD2 1 
ATOM   2094 N  N   . VAL   B 1 131 ? 27.143 -21.061 23.869 1.00 11.11 ? 137 VAL   C N   1 
ATOM   2095 C  CA  . VAL   B 1 131 ? 25.897 -20.872 24.650 1.00 11.35 ? 137 VAL   C CA  1 
ATOM   2096 C  C   . VAL   B 1 131 ? 25.970 -21.562 25.997 1.00 12.63 ? 137 VAL   C C   1 
ATOM   2097 O  O   . VAL   B 1 131 ? 24.993 -21.482 26.774 1.00 12.88 ? 137 VAL   C O   1 
ATOM   2098 C  CB  . VAL   B 1 131 ? 24.609 -21.302 23.898 1.00 12.24 ? 137 VAL   C CB  1 
ATOM   2099 C  CG1 . VAL   B 1 131 ? 24.445 -20.478 22.596 1.00 12.82 ? 137 VAL   C CG1 1 
ATOM   2100 C  CG2 . VAL   B 1 131 ? 24.610 -22.781 23.583 1.00 12.60 ? 137 VAL   C CG2 1 
ATOM   2101 N  N   . ARG   B 1 132 ? 27.102 -22.224 26.351 1.00 11.57 ? 138 ARG   C N   1 
ATOM   2102 C  CA  . ARG   B 1 132 ? 27.162 -23.006 27.599 1.00 12.35 ? 138 ARG   C CA  1 
ATOM   2103 C  C   . ARG   B 1 132 ? 27.131 -22.180 28.863 1.00 11.96 ? 138 ARG   C C   1 
ATOM   2104 O  O   . ARG   B 1 132 ? 26.772 -22.753 29.919 1.00 14.00 ? 138 ARG   C O   1 
ATOM   2105 C  CB  . ARG   B 1 132 ? 28.397 -23.874 27.589 1.00 11.60 ? 138 ARG   C CB  1 
ATOM   2106 C  CG  . ARG   B 1 132 ? 28.404 -24.913 26.433 1.00 11.83 ? 138 ARG   C CG  1 
ATOM   2107 C  CD  . ARG   B 1 132 ? 29.721 -25.692 26.459 1.00 11.58 ? 138 ARG   C CD  1 
ATOM   2108 N  NE  . ARG   B 1 132 ? 30.813 -24.793 26.048 1.00 11.09 ? 138 ARG   C NE  1 
ATOM   2109 C  CZ  . ARG   B 1 132 ? 32.071 -25.177 25.904 1.00 11.73 ? 138 ARG   C CZ  1 
ATOM   2110 N  NH1 . ARG   B 1 132 ? 32.445 -26.429 26.219 1.00 12.03 ? 138 ARG   C NH1 1 
ATOM   2111 N  NH2 . ARG   B 1 132 ? 32.975 -24.324 25.427 1.00 11.97 ? 138 ARG   C NH2 1 
ATOM   2112 N  N   . ASP   B 1 133 ? 27.432 -20.887 28.787 1.00 11.71 ? 139 ASP   C N   1 
ATOM   2113 C  CA  . ASP   B 1 133 ? 27.375 -20.033 29.965 1.00 13.18 ? 139 ASP   C CA  1 
ATOM   2114 C  C   . ASP   B 1 133 ? 25.950 -19.488 30.214 1.00 14.29 ? 139 ASP   C C   1 
ATOM   2115 O  O   . ASP   B 1 133 ? 25.744 -18.883 31.271 1.00 15.44 ? 139 ASP   C O   1 
ATOM   2116 C  CB  . ASP   B 1 133 ? 28.331 -18.831 29.803 1.00 14.93 ? 139 ASP   C CB  1 
ATOM   2117 C  CG  . ASP   B 1 133 ? 27.957 -17.911 28.668 1.00 14.79 ? 139 ASP   C CG  1 
ATOM   2118 O  OD1 . ASP   B 1 133 ? 27.614 -18.414 27.572 1.00 15.17 ? 139 ASP   C OD1 1 
ATOM   2119 O  OD2 . ASP   B 1 133 ? 27.988 -16.664 28.874 1.00 17.11 ? 139 ASP   C OD2 1 
ATOM   2120 N  N   . LEU   B 1 134 ? 25.009 -19.656 29.267 1.00 13.50 ? 140 LEU   C N   1 
ATOM   2121 C  CA  . LEU   B 1 134 ? 23.646 -19.088 29.391 1.00 13.66 ? 140 LEU   C CA  1 
ATOM   2122 C  C   . LEU   B 1 134 ? 22.795 -20.070 30.161 1.00 13.78 ? 140 LEU   C C   1 
ATOM   2123 O  O   . LEU   B 1 134 ? 21.967 -20.794 29.610 1.00 13.48 ? 140 LEU   C O   1 
ATOM   2124 C  CB  . LEU   B 1 134 ? 23.081 -18.819 27.996 1.00 13.50 ? 140 LEU   C CB  1 
ATOM   2125 C  CG  . LEU   B 1 134 ? 23.942 -17.859 27.125 1.00 13.93 ? 140 LEU   C CG  1 
ATOM   2126 C  CD1 . LEU   B 1 134 ? 23.333 -17.750 25.683 1.00 15.05 ? 140 LEU   C CD1 1 
ATOM   2127 C  CD2 . LEU   B 1 134 ? 24.037 -16.459 27.756 1.00 16.29 ? 140 LEU   C CD2 1 
ATOM   2128 N  N   . LEU   B 1 135 ? 22.992 -20.098 31.502 1.00 14.65 ? 141 LEU   C N   1 
ATOM   2129 C  CA  . LEU   B 1 135 ? 22.359 -21.128 32.318 1.00 14.86 ? 141 LEU   C CA  1 
ATOM   2130 C  C   . LEU   B 1 135 ? 20.832 -21.050 32.353 1.00 14.31 ? 141 LEU   C C   1 
ATOM   2131 O  O   . LEU   B 1 135 ? 20.144 -22.065 32.535 1.00 16.44 ? 141 LEU   C O   1 
ATOM   2132 C  CB  . LEU   B 1 135 ? 22.925 -21.164 33.764 1.00 15.34 ? 141 LEU   C CB  1 
ATOM   2133 C  CG  . LEU   B 1 135 ? 24.464 -21.168 33.851 1.00 15.29 ? 141 LEU   C CG  1 
ATOM   2134 C  CD1 . LEU   B 1 135 ? 24.951 -21.198 35.313 1.00 16.73 ? 141 LEU   C CD1 1 
ATOM   2135 C  CD2 . LEU   B 1 135 ? 25.089 -22.349 33.066 1.00 16.33 ? 141 LEU   C CD2 1 
ATOM   2136 N  N   . TRP   B 1 136 ? 20.316 -19.834 32.169 1.00 14.42 ? 142 TRP   C N   1 
ATOM   2137 C  CA  . TRP   B 1 136 ? 18.865 -19.565 32.205 1.00 15.90 ? 142 TRP   C CA  1 
ATOM   2138 C  C   . TRP   B 1 136 ? 18.140 -20.245 31.050 1.00 17.18 ? 142 TRP   C C   1 
ATOM   2139 O  O   . TRP   B 1 136 ? 16.909 -20.386 31.106 1.00 18.46 ? 142 TRP   C O   1 
ATOM   2140 C  CB  . TRP   B 1 136 ? 18.618 -18.047 32.203 1.00 16.24 ? 142 TRP   C CB  1 
ATOM   2141 C  CG  . TRP   B 1 136 ? 19.316 -17.299 31.102 1.00 15.79 ? 142 TRP   C CG  1 
ATOM   2142 C  CD1 . TRP   B 1 136 ? 20.493 -16.624 31.186 1.00 16.93 ? 142 TRP   C CD1 1 
ATOM   2143 C  CD2 . TRP   B 1 136 ? 18.803 -17.057 29.777 1.00 15.81 ? 142 TRP   C CD2 1 
ATOM   2144 N  NE1 . TRP   B 1 136 ? 20.798 -16.038 29.955 1.00 16.77 ? 142 TRP   C NE1 1 
ATOM   2145 C  CE2 . TRP   B 1 136 ? 19.753 -16.274 29.086 1.00 16.70 ? 142 TRP   C CE2 1 
ATOM   2146 C  CE3 . TRP   B 1 136 ? 17.638 -17.450 29.116 1.00 15.54 ? 142 TRP   C CE3 1 
ATOM   2147 C  CZ2 . TRP   B 1 136 ? 19.568 -15.887 27.746 1.00 16.15 ? 142 TRP   C CZ2 1 
ATOM   2148 C  CZ3 . TRP   B 1 136 ? 17.430 -17.015 27.815 1.00 15.97 ? 142 TRP   C CZ3 1 
ATOM   2149 C  CH2 . TRP   B 1 136 ? 18.401 -16.282 27.137 1.00 16.50 ? 142 TRP   C CH2 1 
ATOM   2150 N  N   . LEU   B 1 137 ? 18.843 -20.697 29.994 1.00 15.87 ? 143 LEU   C N   1 
ATOM   2151 C  CA  . LEU   B 1 137 ? 18.161 -21.447 28.924 1.00 15.94 ? 143 LEU   C CA  1 
ATOM   2152 C  C   . LEU   B 1 137 ? 17.546 -22.745 29.461 1.00 18.75 ? 143 LEU   C C   1 
ATOM   2153 O  O   . LEU   B 1 137 ? 16.616 -23.289 28.835 1.00 21.05 ? 143 LEU   C O   1 
ATOM   2154 C  CB  . LEU   B 1 137 ? 19.096 -21.808 27.761 1.00 15.47 ? 143 LEU   C CB  1 
ATOM   2155 C  CG  . LEU   B 1 137 ? 19.561 -20.622 26.907 1.00 14.92 ? 143 LEU   C CG  1 
ATOM   2156 C  CD1 . LEU   B 1 137 ? 20.739 -21.034 26.001 1.00 15.76 ? 143 LEU   C CD1 1 
ATOM   2157 C  CD2 . LEU   B 1 137 ? 18.403 -20.054 26.056 1.00 16.37 ? 143 LEU   C CD2 1 
ATOM   2158 N  N   . ASP   B 1 138 ? 18.064 -23.274 30.607 1.00 17.63 ? 144 ASP   C N   1 
ATOM   2159 C  CA  . ASP   B 1 138 ? 17.614 -24.556 31.185 1.00 18.86 ? 144 ASP   C CA  1 
ATOM   2160 C  C   . ASP   B 1 138 ? 16.339 -24.439 32.040 1.00 21.51 ? 144 ASP   C C   1 
ATOM   2161 O  O   . ASP   B 1 138 ? 15.883 -25.484 32.556 1.00 22.83 ? 144 ASP   C O   1 
ATOM   2162 C  CB  . ASP   B 1 138 ? 18.709 -25.234 32.055 1.00 18.67 ? 144 ASP   C CB  1 
ATOM   2163 C  CG  . ASP   B 1 138 ? 19.952 -25.658 31.286 1.00 19.47 ? 144 ASP   C CG  1 
ATOM   2164 O  OD1 . ASP   B 1 138 ? 19.915 -25.672 30.041 1.00 20.01 ? 144 ASP   C OD1 1 
ATOM   2165 O  OD2 . ASP   B 1 138 ? 20.995 -25.967 31.949 1.00 22.03 ? 144 ASP   C OD2 1 
ATOM   2166 N  N   . GLU   B 1 139 ? 15.768 -23.232 32.194 1.00 21.94 ? 145 GLU   C N   1 
ATOM   2167 C  CA  . GLU   B 1 139 ? 14.561 -23.101 33.032 1.00 26.41 ? 145 GLU   C CA  1 
ATOM   2168 C  C   . GLU   B 1 139 ? 13.637 -21.932 32.637 1.00 31.08 ? 145 GLU   C C   1 
ATOM   2169 O  O   . GLU   B 1 139 ? 13.907 -21.240 31.659 1.00 31.85 ? 145 GLU   C O   1 
ATOM   2170 C  CB  . GLU   B 1 139 ? 15.030 -22.940 34.482 1.00 30.69 ? 145 GLU   C CB  1 
ATOM   2171 C  CG  . GLU   B 1 139 ? 15.861 -21.690 34.653 1.00 36.74 ? 145 GLU   C CG  1 
ATOM   2172 C  CD  . GLU   B 1 139 ? 17.112 -21.914 35.474 1.00 48.46 ? 145 GLU   C CD  1 
ATOM   2173 O  OE1 . GLU   B 1 139 ? 17.205 -21.320 36.569 1.00 47.11 ? 145 GLU   C OE1 1 
ATOM   2174 O  OE2 . GLU   B 1 139 ? 17.994 -22.687 35.027 1.00 54.03 ? 145 GLU   C OE2 1 
ATOM   2175 N  N   . GLU   B 1 140 ? 12.562 -21.684 33.444 1.00 34.06 ? 146 GLU   C N   1 
ATOM   2176 C  CA  . GLU   B 1 140 ? 11.619 -20.549 33.362 1.00 36.57 ? 146 GLU   C CA  1 
ATOM   2177 C  C   . GLU   B 1 140 ? 11.021 -20.414 31.993 1.00 37.88 ? 146 GLU   C C   1 
ATOM   2178 O  O   . GLU   B 1 140 ? 10.796 -19.314 31.494 1.00 38.78 ? 146 GLU   C O   1 
ATOM   2179 C  CB  . GLU   B 1 140 ? 12.295 -19.248 33.866 1.00 39.66 ? 146 GLU   C CB  1 
ATOM   2180 C  CG  . GLU   B 1 140 ? 11.709 -17.892 33.461 1.00 48.96 ? 146 GLU   C CG  1 
ATOM   2181 C  CD  . GLU   B 1 140 ? 10.406 -17.402 34.074 1.00 57.42 ? 146 GLU   C CD  1 
ATOM   2182 O  OE1 . GLU   B 1 140 ? 10.190 -16.169 34.063 1.00 60.23 ? 146 GLU   C OE1 1 
ATOM   2183 O  OE2 . GLU   B 1 140 ? 9.600  -18.234 34.549 1.00 60.76 ? 146 GLU   C OE2 1 
HETATM 2184 N  N1  . A1BP1 C 2 .   ? 10.205 14.829  21.910 1.00 20.86 ? 201 A1BP1 A N1  1 
HETATM 2185 N  N3  . A1BP1 C 2 .   ? 8.604  11.211  23.028 1.00 16.01 ? 201 A1BP1 A N3  1 
HETATM 2186 C  C4  . A1BP1 C 2 .   ? 10.451 16.278  18.528 1.00 24.45 ? 201 A1BP1 A C4  1 
HETATM 2187 C  C5  . A1BP1 C 2 .   ? 9.379  18.043  19.074 1.00 24.25 ? 201 A1BP1 A C5  1 
HETATM 2188 C  C6  . A1BP1 C 2 .   ? 9.324  14.720  22.913 1.00 20.11 ? 201 A1BP1 A C6  1 
HETATM 2189 C  C7  . A1BP1 C 2 .   ? 8.777  13.362  23.174 1.00 17.32 ? 201 A1BP1 A C7  1 
HETATM 2190 C  C8  . A1BP1 C 2 .   ? 9.032  9.866   22.663 1.00 15.60 ? 201 A1BP1 A C8  1 
HETATM 2191 C  C10 . A1BP1 C 2 .   ? 6.766  10.808  24.679 1.00 17.15 ? 201 A1BP1 A C10 1 
HETATM 2192 C  C13 . A1BP1 C 2 .   ? 6.857  13.604  24.959 1.00 17.70 ? 201 A1BP1 A C13 1 
HETATM 2193 O  O1  . A1BP1 C 2 .   ? 8.981  15.687  23.619 1.00 21.21 ? 201 A1BP1 A O1  1 
HETATM 2194 C  C14 . A1BP1 C 2 .   ? 7.715  12.965  24.064 1.00 17.20 ? 201 A1BP1 A C14 1 
HETATM 2195 C  C12 . A1BP1 C 2 .   ? 5.967  12.841  25.705 1.00 18.74 ? 201 A1BP1 A C12 1 
HETATM 2196 C  C11 . A1BP1 C 2 .   ? 5.930  11.458  25.579 1.00 17.60 ? 201 A1BP1 A C11 1 
HETATM 2197 C  C9  . A1BP1 C 2 .   ? 7.645  11.570  23.928 1.00 16.07 ? 201 A1BP1 A C9  1 
HETATM 2198 N  N2  . A1BP1 C 2 .   ? 9.286  12.303  22.541 1.00 17.07 ? 201 A1BP1 A N2  1 
HETATM 2199 C  C1  . A1BP1 C 2 .   ? 11.245 15.851  22.057 1.00 22.90 ? 201 A1BP1 A C1  1 
HETATM 2200 C  C   . A1BP1 C 2 .   ? 12.291 15.442  23.079 1.00 24.35 ? 201 A1BP1 A C   1 
HETATM 2201 C  C2  . A1BP1 C 2 .   ? 11.840 16.086  20.677 1.00 22.38 ? 201 A1BP1 A C2  1 
HETATM 2202 C  C3  . A1BP1 C 2 .   ? 10.847 16.677  19.744 1.00 23.34 ? 201 A1BP1 A C3  1 
HETATM 2203 N  N   . A1BP1 C 2 .   ? 10.147 17.838  20.082 1.00 23.09 ? 201 A1BP1 A N   1 
HETATM 2204 O  O   . A1BP1 C 2 .   ? 9.512  17.158  18.061 1.00 24.97 ? 201 A1BP1 A O   1 
HETATM 2205 ZN ZN  . ZN    D 3 .   ? 11.056 -3.744  5.847  1.00 18.89 2 202 ZN    A ZN  1 
HETATM 2206 S  S   . DMS   E 4 .   ? 19.499 -1.794  24.207 1.00 83.91 ? 203 DMS   A S   1 
HETATM 2207 O  O   . DMS   E 4 .   ? 18.418 -2.087  23.210 1.00 83.74 ? 203 DMS   A O   1 
HETATM 2208 C  C1  . DMS   E 4 .   ? 19.564 -3.192  25.362 1.00 83.93 ? 203 DMS   A C1  1 
HETATM 2209 C  C2  . DMS   E 4 .   ? 21.102 -2.133  23.426 1.00 83.90 ? 203 DMS   A C2  1 
HETATM 2210 ZN ZN  . ZN    F 3 .   ? 30.815 -31.238 26.754 1.00 12.23 2 201 ZN    C ZN  1 
HETATM 2211 S  S   . DMS   G 4 .   ? 21.044 -32.155 9.535  1.00 82.22 ? 202 DMS   C S   1 
HETATM 2212 O  O   . DMS   G 4 .   ? 22.227 -32.567 8.723  1.00 82.42 ? 202 DMS   C O   1 
HETATM 2213 C  C1  . DMS   G 4 .   ? 21.455 -32.398 11.271 1.00 82.13 ? 202 DMS   C C1  1 
HETATM 2214 C  C2  . DMS   G 4 .   ? 20.999 -30.346 9.597  1.00 82.14 ? 202 DMS   C C2  1 
HETATM 2215 O  O   . HOH   H 5 .   ? 35.517 -3.909  7.876  1.00 21.90 ? 301 HOH   A O   1 
HETATM 2216 O  O   . HOH   H 5 .   ? 2.294  22.996  21.594 1.00 29.61 ? 302 HOH   A O   1 
HETATM 2217 O  O   . HOH   H 5 .   ? 11.268 9.022   4.446  1.00 23.46 ? 303 HOH   A O   1 
HETATM 2218 O  O   . HOH   H 5 .   ? 3.003  9.378   9.090  1.00 27.38 ? 304 HOH   A O   1 
HETATM 2219 O  O   . HOH   H 5 .   ? 27.843 8.013   1.694  1.00 34.05 ? 305 HOH   A O   1 
HETATM 2220 O  O   . HOH   H 5 .   ? 31.785 7.072   5.402  1.00 28.56 ? 306 HOH   A O   1 
HETATM 2221 O  O   . HOH   H 5 .   ? 37.519 15.049  13.970 1.00 43.52 ? 307 HOH   A O   1 
HETATM 2222 O  O   . HOH   H 5 .   ? 8.822  -3.074  0.659  1.00 31.70 ? 308 HOH   A O   1 
HETATM 2223 O  O   . HOH   H 5 .   ? 29.655 22.288  19.434 1.00 25.23 ? 309 HOH   A O   1 
HETATM 2224 O  O   . HOH   H 5 .   ? 28.126 3.202   4.887  1.00 30.89 ? 310 HOH   A O   1 
HETATM 2225 O  O   . HOH   H 5 .   ? 2.724  -3.097  20.851 1.00 28.14 ? 311 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 8.512  16.738  25.982 1.00 29.99 ? 312 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 21.807 2.418   -0.735 1.00 30.65 ? 313 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 33.866 14.181  9.730  1.00 28.20 ? 314 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 8.583  -2.906  31.949 1.00 23.89 ? 315 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 14.008 2.928   1.266  1.00 20.26 ? 316 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 12.539 22.366  13.140 1.00 25.74 ? 317 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 17.514 0.972   28.324 1.00 23.49 ? 318 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 0.387  -1.027  19.396 1.00 23.70 ? 319 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 23.485 21.660  7.401  1.00 22.66 ? 320 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 25.016 5.075   21.494 1.00 31.82 ? 321 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 16.092 24.117  14.753 1.00 35.42 ? 322 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 30.475 10.432  15.614 1.00 27.09 ? 323 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 10.906 5.771   3.519  1.00 21.26 ? 324 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 10.175 18.611  26.637 1.00 41.19 ? 325 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 28.938 11.160  3.269  1.00 49.72 ? 326 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 35.349 10.847  11.882 1.00 44.52 ? 327 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 19.417 10.061  19.764 1.00 12.34 ? 328 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 4.858  -3.781  29.090 1.00 24.90 ? 329 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 30.048 11.612  18.399 1.00 27.94 ? 330 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 8.551  24.887  23.892 1.00 27.49 ? 331 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? -0.076 1.270   15.890 1.00 12.06 ? 332 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 36.794 2.595   10.111 1.00 41.13 ? 333 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 4.211  9.339   28.237 1.00 30.15 ? 334 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 7.360  -2.434  -1.458 1.00 43.41 ? 335 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 12.132 16.767  27.705 1.00 32.04 ? 336 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 33.701 11.205  15.533 1.00 33.66 ? 337 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 10.511 10.010  31.539 1.00 22.23 ? 338 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? 16.146 -6.777  10.826 1.00 33.83 ? 339 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 22.688 0.885   17.492 1.00 15.25 ? 340 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 20.651 -0.862  3.079  1.00 30.57 ? 341 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 17.056 -3.468  27.861 1.00 29.33 ? 342 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 7.529  20.276  17.522 1.00 20.92 ? 343 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 21.061 -4.162  14.288 1.00 15.49 ? 344 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 29.476 12.004  21.216 1.00 30.90 ? 345 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 26.935 -1.175  8.901  1.00 22.50 ? 346 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 23.328 12.999  23.965 1.00 40.41 ? 347 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 1.448  5.212   27.382 1.00 25.96 ? 348 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? 28.957 3.388   12.674 1.00 15.71 ? 349 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 13.817 3.965   23.629 1.00 11.58 ? 350 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 16.682 3.798   23.809 1.00 15.79 ? 351 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 6.207  2.658   5.895  1.00 26.92 ? 352 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 31.670 20.016  11.730 1.00 20.34 ? 353 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 7.248  26.476  14.526 1.00 34.64 ? 354 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 23.566 11.706  21.998 1.00 30.06 ? 355 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 33.958 -2.407  13.679 1.00 33.91 ? 356 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 5.506  5.263   32.818 1.00 19.04 ? 357 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 19.896 19.924  5.641  1.00 39.07 ? 358 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 11.335 12.772  11.389 1.00 15.19 ? 359 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 18.438 21.889  9.618  1.00 18.57 ? 360 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 36.558 17.896  14.316 1.00 26.51 ? 361 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 6.724  -6.956  23.889 1.00 22.69 ? 362 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 13.876 25.010  26.047 1.00 35.53 ? 363 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 28.861 15.933  4.373  1.00 29.02 ? 364 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 14.628 13.381  24.240 1.00 20.87 ? 365 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 3.457  20.882  24.440 1.00 42.73 ? 366 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 20.085 -4.208  11.079 1.00 28.43 ? 367 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 17.481 -4.993  12.234 1.00 31.29 ? 368 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? -1.834 13.825  22.240 1.00 44.16 ? 369 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 21.783 4.855   24.795 1.00 36.72 ? 370 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 30.574 3.015   14.866 1.00 21.02 ? 371 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 13.277 11.442  9.395  1.00 13.85 ? 372 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 3.870  12.950  17.681 1.00 25.69 ? 373 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 31.863 -2.732  15.364 1.00 50.87 ? 374 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 20.883 -2.573  16.939 1.00 14.38 ? 375 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 24.233 -3.399  16.224 1.00 28.27 ? 376 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 3.383  0.055   29.191 1.00 31.69 ? 377 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 12.089 10.996  29.837 1.00 18.30 ? 378 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 1.284  12.167  21.095 1.00 38.70 ? 379 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 5.947  17.737  24.331 1.00 58.01 ? 380 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 30.309 -1.382  8.755  1.00 31.12 ? 381 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 17.727 19.989  17.232 1.00 17.01 ? 382 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 17.976 17.795  4.414  1.00 37.31 ? 383 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 9.299  3.528   3.071  1.00 27.36 ? 384 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 32.801 16.635  9.215  1.00 29.68 ? 385 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 22.874 -0.610  5.412  1.00 21.00 ? 386 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 9.615  3.959   33.642 1.00 13.08 ? 387 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 30.399 4.524   5.817  1.00 22.52 ? 388 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 11.497 -7.079  24.829 1.00 26.66 ? 389 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 23.486 -6.601  12.155 1.00 28.30 ? 390 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 17.054 6.233   27.230 1.00 24.70 ? 391 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 25.527 19.673  21.724 1.00 24.86 ? 392 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 19.501 2.962   19.433 1.00 17.34 ? 393 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 17.866 10.556  26.314 1.00 22.30 ? 394 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 16.617 21.232  19.250 1.00 29.24 ? 395 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 0.292  6.022   6.170  1.00 24.16 ? 396 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 31.074 15.651  22.780 1.00 23.85 ? 397 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 27.472 -1.258  15.900 1.00 24.67 ? 398 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 25.297 18.074  4.839  1.00 27.50 ? 399 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 16.618 23.290  20.899 1.00 45.79 ? 400 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 3.302  14.631  24.478 1.00 37.05 ? 401 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 35.961 15.069  10.945 1.00 37.80 ? 402 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 4.124  -0.023  24.231 1.00 17.16 ? 403 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 6.478  17.062  21.253 1.00 38.08 ? 404 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 32.269 1.877   6.143  1.00 34.16 ? 405 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 29.169 6.919   20.251 1.00 40.74 ? 406 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 14.538 -2.414  18.064 1.00 16.53 ? 407 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 15.006 21.798  8.590  1.00 26.93 ? 408 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 1.878  10.985  27.652 1.00 31.92 ? 409 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 3.671  -8.180  10.182 1.00 47.10 ? 410 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 4.799  -5.644  14.311 1.00 38.82 ? 411 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 2.513  16.214  19.289 1.00 26.85 ? 412 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 3.926  -3.889  6.093  1.00 25.22 ? 413 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 28.111 17.596  24.201 1.00 23.94 ? 414 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 5.031  8.137   2.445  1.00 35.09 ? 415 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 34.008 18.725  10.710 1.00 27.33 ? 416 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 36.354 -0.326  12.680 1.00 29.79 ? 417 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 5.332  26.488  20.213 1.00 26.63 ? 418 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 3.246  7.570   24.647 1.00 26.07 ? 419 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 17.577 0.866   20.294 1.00 18.35 ? 420 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 32.041 8.779   7.607  1.00 22.17 ? 421 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 2.068  14.813  16.679 1.00 29.78 ? 422 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 23.384 17.052  23.775 1.00 46.15 ? 423 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 8.292  6.494   33.978 1.00 18.20 ? 424 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 3.562  26.912  16.425 1.00 42.18 ? 425 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 8.682  -6.409  9.711  1.00 24.83 ? 426 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 6.377  24.061  10.558 1.00 35.12 ? 427 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 22.613 19.633  19.762 1.00 31.23 ? 428 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 17.362 23.685  17.047 1.00 61.79 ? 429 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 7.380  13.911  4.862  1.00 24.06 ? 430 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 15.596 15.369  3.936  1.00 29.68 ? 431 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 0.502  -1.321  16.768 1.00 19.11 ? 432 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 19.863 13.397  2.436  1.00 30.49 ? 433 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 14.465 24.370  17.860 1.00 36.94 ? 434 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 25.213 10.695  22.988 1.00 34.55 ? 435 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 19.459 -0.436  33.330 1.00 34.09 ? 436 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 23.223 19.135  6.395  1.00 18.05 ? 437 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 3.368  -0.449  21.498 1.00 29.14 ? 438 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 23.511 8.334   21.740 1.00 22.57 ? 439 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 22.766 3.439   20.901 1.00 19.74 ? 440 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? -1.320 -3.095  15.428 1.00 28.10 ? 441 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 21.107 9.858   22.021 1.00 15.82 ? 442 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 17.221 -2.383  19.699 1.00 21.97 ? 443 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 36.646 16.119  16.675 1.00 37.82 ? 444 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 0.443  -1.443  9.362  1.00 38.36 ? 445 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 15.798 21.408  7.241  1.00 25.44 ? 446 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 3.332  13.811  19.978 1.00 40.00 ? 447 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 31.043 19.477  9.010  1.00 36.85 ? 448 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 1.259  -5.118  17.543 1.00 34.67 ? 449 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 19.393 21.551  6.930  1.00 38.28 ? 450 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 33.958 5.276   16.769 1.00 31.44 ? 451 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 6.134  -3.666  31.657 1.00 25.57 ? 452 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 7.816  10.908  31.737 1.00 34.79 ? 453 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 7.803  11.622  3.630  1.00 41.25 ? 454 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 17.072 -3.947  2.987  1.00 28.13 ? 455 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 34.075 7.866   16.684 1.00 31.78 ? 456 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 6.037  15.410  21.988 1.00 23.41 ? 457 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 0.695  7.652   27.882 1.00 43.97 ? 458 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? -0.064 11.954  29.493 1.00 48.39 ? 459 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 25.407 -0.946  16.878 1.00 37.35 ? 460 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 7.548  -4.611  2.802  1.00 39.27 ? 461 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 14.631 13.163  28.769 1.00 28.30 ? 462 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 17.584 8.837   28.615 1.00 28.52 ? 463 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 31.731 9.239   17.381 1.00 40.80 ? 464 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 2.922  -0.715  26.741 1.00 27.69 ? 465 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 2.352  -5.412  14.549 1.00 40.60 ? 466 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 33.547 -4.245  5.851  1.00 37.79 ? 467 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 21.673 19.694  4.240  1.00 33.73 ? 468 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 16.919 -5.004  34.472 1.00 28.00 ? 469 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 6.562  3.434   3.396  1.00 33.40 ? 470 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 18.259 14.257  27.601 1.00 30.60 ? 471 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 18.603 2.078   22.947 1.00 37.18 ? 472 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 29.731 0.786   16.550 1.00 32.00 ? 473 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 16.357 12.663  26.412 1.00 25.32 ? 474 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 11.900 24.450  14.876 1.00 36.43 ? 475 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 0.090  0.024   23.277 1.00 26.21 ? 476 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 23.889 1.026   19.927 1.00 29.68 ? 477 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 14.259 14.893  26.656 1.00 33.97 ? 478 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 9.640  8.157   2.379  1.00 38.44 ? 479 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 11.466 23.284  10.876 1.00 38.68 ? 480 HOH   A O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 2.282  14.010  26.688 1.00 49.82 ? 481 HOH   A O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 30.322 7.118   17.886 1.00 34.24 ? 482 HOH   A O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 21.393 2.902   23.201 1.00 29.09 ? 483 HOH   A O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 34.972 -2.100  16.087 1.00 54.52 ? 484 HOH   A O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 17.843 24.416  10.258 1.00 32.19 ? 485 HOH   A O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 38.021 -4.568  6.919  1.00 29.15 ? 486 HOH   A O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 31.323 4.627   17.027 1.00 24.61 ? 487 HOH   A O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 12.443 -5.114  33.246 1.00 30.27 ? 488 HOH   A O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 21.520 11.164  24.494 1.00 30.51 ? 489 HOH   A O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 21.359 -1.058  19.049 1.00 31.17 ? 490 HOH   A O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? -0.403 13.750  16.993 1.00 29.17 ? 491 HOH   A O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 2.564  -1.762  22.916 1.00 25.42 ? 492 HOH   A O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 6.167  11.397  29.692 1.00 30.05 ? 493 HOH   A O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 3.011  25.666  21.767 1.00 43.71 ? 494 HOH   A O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 39.347 -2.557  10.863 1.00 36.59 ? 495 HOH   A O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 20.026 11.847  26.562 1.00 34.16 ? 496 HOH   A O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 28.995 1.577   18.980 1.00 40.50 ? 497 HOH   A O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 7.046  15.948  28.156 1.00 40.13 ? 498 HOH   A O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 9.929  25.915  13.861 1.00 43.69 ? 499 HOH   A O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 26.719 0.397   19.953 1.00 47.42 ? 500 HOH   A O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 5.954  14.096  29.476 1.00 47.14 ? 501 HOH   A O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 17.595 -33.434 24.171 1.00 35.99 ? 301 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 31.171 -23.810 -1.351 1.00 20.94 ? 302 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 38.740 -18.681 21.613 1.00 26.09 ? 303 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 10.385 -20.044 29.127 1.00 31.08 ? 304 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 14.898 -18.903 31.946 1.00 39.18 ? 305 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 38.463 -7.408  7.057  1.00 20.33 ? 306 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 18.862 -32.352 19.882 1.00 44.01 ? 307 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 16.398 -16.099 9.143  1.00 33.24 ? 308 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 19.920 -4.136  20.329 1.00 21.70 ? 309 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 30.998 -18.213 26.962 1.00 17.17 ? 310 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 24.840 -5.962  15.363 1.00 24.42 ? 311 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 27.905 -4.168  18.064 1.00 43.97 ? 312 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 18.011 -27.523 16.607 1.00 17.26 ? 313 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 20.913 -18.720 12.941 1.00 13.96 ? 314 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 36.288 -17.709 11.780 1.00 22.41 ? 315 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 26.749 -15.361 30.858 1.00 24.49 ? 316 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 36.347 -2.529  11.061 1.00 29.71 ? 317 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 21.887 -26.242 34.466 1.00 24.00 ? 318 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 23.174 -5.947  21.234 1.00 20.16 ? 319 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 38.805 -27.530 28.548 1.00 45.67 ? 320 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 18.011 -6.099  24.253 1.00 24.32 ? 321 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 37.437 -18.820 28.222 1.00 22.58 ? 322 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 42.802 -11.400 11.248 1.00 22.74 ? 323 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 10.451 -17.611 18.460 1.00 25.15 ? 324 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 37.323 -10.423 4.873  1.00 37.01 ? 325 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 16.688 -17.195 11.120 1.00 37.75 ? 326 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 14.881 -23.961 12.394 1.00 31.47 ? 327 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 32.702 -5.376  18.511 1.00 36.78 ? 328 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 18.819 -8.797  13.879 1.00 27.77 ? 329 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 40.180 -29.713 11.972 1.00 24.58 ? 330 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 14.162 -24.357 29.343 1.00 32.63 ? 331 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 31.202 -21.582 28.460 1.00 14.93 ? 332 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 32.679 -23.800 29.221 1.00 15.92 ? 333 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 37.465 -31.940 10.957 1.00 22.33 ? 334 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 24.910 -15.761 7.483  1.00 18.30 ? 335 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 22.130 -21.655 4.626  1.00 44.32 ? 336 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 35.087 -32.900 3.331  1.00 34.45 ? 337 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 36.270 -26.456 34.416 1.00 30.53 ? 338 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 26.169 -25.275 8.835  1.00 13.08 ? 339 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 24.651 -9.764  27.117 1.00 37.13 ? 340 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 16.995 -9.226  27.633 1.00 35.60 ? 341 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 40.701 -27.335 15.240 1.00 11.77 ? 342 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 31.347 -6.153  5.876  1.00 34.33 ? 343 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 9.401  -8.124  21.473 1.00 27.54 ? 344 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 26.731 -5.475  10.058 1.00 19.53 ? 345 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 36.163 -28.523 2.801  1.00 38.98 ? 346 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 24.068 -8.151  9.583  1.00 20.84 ? 347 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 30.102 -15.325 19.661 1.00 14.67 ? 348 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 6.125  -16.825 22.619 1.00 43.94 ? 349 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 32.190 -10.481 13.842 1.00 17.47 ? 350 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 10.665 -16.851 15.395 1.00 30.72 ? 351 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 34.793 -35.020 18.073 1.00 24.12 ? 352 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 20.577 -23.750 34.888 1.00 27.42 ? 353 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 13.500 -11.225 28.672 1.00 35.48 ? 354 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 12.110 -24.275 21.828 1.00 17.28 ? 355 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 10.042 -8.901  23.977 1.00 27.97 ? 356 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 26.011 -37.932 24.314 1.00 29.22 ? 357 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 7.011  -17.041 19.022 1.00 43.33 ? 358 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 19.397 -27.789 28.275 1.00 18.01 ? 359 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 20.889 -25.650 13.936 1.00 19.04 ? 360 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 42.633 -17.028 3.335  1.00 49.09 ? 361 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 28.260 -37.565 29.269 1.00 55.43 ? 362 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 34.270 -33.790 24.238 1.00 32.32 ? 363 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 35.400 -13.203 8.834  1.00 17.36 ? 364 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 14.723 -28.901 25.610 1.00 35.16 ? 365 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 29.956 -13.116 13.057 1.00 14.09 ? 366 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 10.826 -16.860 12.546 1.00 29.63 ? 367 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 17.655 -24.022 8.725  1.00 39.86 ? 368 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 7.450  -30.440 22.158 1.00 32.01 ? 369 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 23.799 -33.665 29.124 1.00 27.47 ? 370 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 27.293 -35.700 20.834 1.00 24.70 ? 371 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 11.298 -21.669 13.765 1.00 36.42 ? 372 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 7.150  -9.380  22.928 1.00 34.75 ? 373 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 22.056 -28.532 4.895  1.00 28.21 ? 374 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 5.296  -11.981 14.583 1.00 51.76 ? 375 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 13.239 -29.384 19.201 1.00 31.26 ? 376 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 4.001  -8.344  14.782 1.00 28.75 ? 377 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 32.000 -34.851 31.879 1.00 33.96 ? 378 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 11.067 -6.411  13.347 1.00 22.86 ? 379 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 23.143 -8.491  14.166 1.00 15.17 ? 380 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 36.494 -21.388 7.022  1.00 22.27 ? 381 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 37.715 -31.633 25.729 1.00 27.79 ? 382 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 40.264 -25.415 7.117  1.00 33.10 ? 383 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 33.155 -9.859  11.213 1.00 13.97 ? 384 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 22.379 -23.700 6.151  1.00 35.71 ? 385 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 8.980  -13.267 10.970 1.00 22.55 ? 386 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 22.881 -33.313 5.524  1.00 31.21 ? 387 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 32.331 -34.779 24.772 1.00 33.16 ? 388 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 4.423  -10.432 19.781 1.00 30.82 ? 389 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 11.676 -22.494 28.803 1.00 25.85 ? 390 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 28.322 -16.409 22.160 1.00 12.95 ? 391 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 31.464 -12.183 10.728 1.00 14.60 ? 392 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 10.224 -24.830 19.923 1.00 19.84 ? 393 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 24.068 -3.345  19.140 1.00 40.59 ? 394 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 28.992 -36.276 7.827  1.00 19.69 ? 395 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 23.355 -25.384 8.957  1.00 19.81 ? 396 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 27.026 -12.145 27.799 1.00 24.17 ? 397 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 43.457 -25.759 23.763 1.00 20.33 ? 398 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 23.108 -28.207 12.653 1.00 21.19 ? 399 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 34.567 -13.537 25.588 1.00 18.62 ? 400 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 30.238 -15.996 30.603 1.00 30.75 ? 401 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 35.790 -24.733 24.762 1.00 16.92 ? 402 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 21.847 -18.949 5.958  1.00 25.87 ? 403 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 26.216 -31.124 30.943 1.00 17.59 ? 404 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 31.739 -13.467 4.398  1.00 33.13 ? 405 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 22.648 -13.774 29.635 1.00 34.42 ? 406 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 26.841 -6.080  22.192 1.00 25.98 ? 407 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 14.825 -18.288 10.526 1.00 30.30 ? 408 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 16.942 -18.547 35.603 1.00 44.51 ? 409 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 37.087 -29.320 10.135 1.00 21.57 ? 410 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 35.878 -28.600 7.835  1.00 18.29 ? 411 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 27.163 -19.174 1.732  1.00 25.88 ? 412 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 26.537 -31.282 14.892 1.00 18.56 ? 413 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 17.098 -8.866  12.229 1.00 37.58 ? 414 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 10.628 -30.939 25.370 1.00 29.94 ? 415 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 42.456 -12.138 14.098 1.00 29.79 ? 416 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 34.737 -23.306 -0.786 1.00 33.23 ? 417 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 4.770  -27.882 23.320 1.00 33.79 ? 418 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 17.452 -25.313 12.836 1.00 22.36 ? 419 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 22.616 -10.994 7.647  1.00 41.54 ? 420 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 30.530 -18.025 8.471  1.00 25.21 ? 421 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 41.832 -13.805 10.173 1.00 28.70 ? 422 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 39.161 -16.785 3.738  1.00 40.15 ? 423 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 10.084 -18.344 26.810 1.00 31.26 ? 424 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 39.068 -14.640 13.721 1.00 35.20 ? 425 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 23.584 -31.035 13.467 1.00 36.33 ? 426 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 15.218 -30.356 18.483 1.00 41.78 ? 427 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 39.026 -13.059 25.966 1.00 26.64 ? 428 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 33.191 -30.475 31.722 1.00 17.78 ? 429 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 10.953 -11.866 9.085  1.00 30.57 ? 430 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 37.876 -13.786 10.166 1.00 26.51 ? 431 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 18.781 -8.346  25.669 1.00 20.09 ? 432 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 37.828 -20.166 5.161  1.00 37.62 ? 433 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 35.118 -4.135  17.737 1.00 28.73 ? 434 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 33.009 -14.394 9.542  1.00 13.96 ? 435 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 16.564 -20.479 11.682 1.00 21.55 ? 436 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 35.361 -13.704 6.077  1.00 32.31 ? 437 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 18.959 -19.111 10.970 1.00 17.68 ? 438 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 6.700  -22.924 18.370 1.00 30.86 ? 439 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 41.945 -12.463 18.048 1.00 24.59 ? 440 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 40.202 -30.015 14.651 1.00 16.14 ? 441 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 20.449 -32.328 22.256 1.00 26.43 ? 442 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 38.170 -23.589 4.524  1.00 35.97 ? 443 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 24.458 -14.047 5.538  1.00 42.76 ? 444 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 6.674  -20.101 18.315 1.00 32.80 ? 445 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 34.218 -15.725 27.261 1.00 29.11 ? 446 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 33.939 -36.145 8.833  1.00 35.08 ? 447 HOH   C O   1 
HETATM 2563 O  O   . HOH   I 5 .   ? 23.643 -17.681 33.443 1.00 19.88 ? 448 HOH   C O   1 
HETATM 2564 O  O   . HOH   I 5 .   ? 6.052  -12.031 23.412 1.00 40.93 ? 449 HOH   C O   1 
HETATM 2565 O  O   . HOH   I 5 .   ? 31.817 -15.750 7.245  1.00 32.31 ? 450 HOH   C O   1 
HETATM 2566 O  O   . HOH   I 5 .   ? 30.669 -4.386  17.117 1.00 42.97 ? 451 HOH   C O   1 
HETATM 2567 O  O   . HOH   I 5 .   ? 36.749 -24.450 27.304 1.00 30.37 ? 452 HOH   C O   1 
HETATM 2568 O  O   . HOH   I 5 .   ? 43.869 -25.479 26.219 1.00 30.46 ? 453 HOH   C O   1 
HETATM 2569 O  O   . HOH   I 5 .   ? 41.325 -29.817 22.293 1.00 40.15 ? 454 HOH   C O   1 
HETATM 2570 O  O   . HOH   I 5 .   ? 23.925 -15.816 31.559 1.00 27.27 ? 455 HOH   C O   1 
HETATM 2571 O  O   . HOH   I 5 .   ? 24.283 -16.680 3.375  1.00 35.84 ? 456 HOH   C O   1 
HETATM 2572 O  O   . HOH   I 5 .   ? 34.398 -31.957 29.550 1.00 21.50 ? 457 HOH   C O   1 
HETATM 2573 O  O   . HOH   I 5 .   ? 26.207 -35.308 7.465  1.00 23.87 ? 458 HOH   C O   1 
HETATM 2574 O  O   . HOH   I 5 .   ? 21.424 -17.548 34.741 1.00 23.66 ? 459 HOH   C O   1 
HETATM 2575 O  O   . HOH   I 5 .   ? 39.801 -14.329 8.511  1.00 30.25 ? 460 HOH   C O   1 
HETATM 2576 O  O   . HOH   I 5 .   ? 28.331 -4.051  21.308 1.00 41.67 ? 461 HOH   C O   1 
HETATM 2577 O  O   . HOH   I 5 .   ? 21.601 -26.895 10.334 1.00 31.90 ? 462 HOH   C O   1 
HETATM 2578 O  O   . HOH   I 5 .   ? 23.013 -16.696 5.493  1.00 40.54 ? 463 HOH   C O   1 
HETATM 2579 O  O   . HOH   I 5 .   ? 16.655 -27.561 14.254 1.00 29.56 ? 464 HOH   C O   1 
HETATM 2580 O  O   . HOH   I 5 .   ? 28.103 -12.732 30.291 1.00 42.00 ? 465 HOH   C O   1 
HETATM 2581 O  O   . HOH   I 5 .   ? 34.190 -34.482 30.369 1.00 48.79 ? 466 HOH   C O   1 
HETATM 2582 O  O   . HOH   I 5 .   ? 18.663 -26.113 10.272 1.00 34.44 ? 467 HOH   C O   1 
HETATM 2583 O  O   . HOH   I 5 .   ? 30.372 -5.093  19.951 1.00 44.72 ? 468 HOH   C O   1 
HETATM 2584 O  O   . HOH   I 5 .   ? 32.775 -19.512 29.195 1.00 28.19 ? 469 HOH   C O   1 
HETATM 2585 O  O   . HOH   I 5 .   ? 41.730 -15.340 13.882 1.00 30.52 ? 470 HOH   C O   1 
HETATM 2586 O  O   . HOH   I 5 .   ? 17.100 -28.954 28.805 1.00 35.33 ? 471 HOH   C O   1 
HETATM 2587 O  O   . HOH   I 5 .   ? 40.710 -28.125 7.482  1.00 46.04 ? 472 HOH   C O   1 
HETATM 2588 O  O   . HOH   I 5 .   ? 10.251 -21.200 16.485 1.00 33.13 ? 473 HOH   C O   1 
HETATM 2589 O  O   . HOH   I 5 .   ? 18.233 -17.942 8.513  1.00 29.20 ? 474 HOH   C O   1 
HETATM 2590 O  O   . HOH   I 5 .   ? 1.052  -19.205 17.523 1.00 74.25 ? 475 HOH   C O   1 
HETATM 2591 O  O   . HOH   I 5 .   ? 39.685 -11.271 5.018  1.00 47.13 ? 476 HOH   C O   1 
HETATM 2592 O  O   . HOH   I 5 .   ? 9.283  -23.373 17.769 1.00 28.30 ? 477 HOH   C O   1 
HETATM 2593 O  O   . HOH   I 5 .   ? 27.298 -15.364 33.702 1.00 32.86 ? 478 HOH   C O   1 
HETATM 2594 O  O   . HOH   I 5 .   ? 35.414 -23.112 29.080 1.00 25.76 ? 479 HOH   C O   1 
HETATM 2595 O  O   . HOH   I 5 .   ? 35.589 -20.404 29.490 1.00 33.05 ? 480 HOH   C O   1 
HETATM 2596 O  O   . HOH   I 5 .   ? 3.237  -8.888  22.132 1.00 40.77 ? 481 HOH   C O   1 
HETATM 2597 O  O   . HOH   I 5 .   ? 19.538 -17.572 5.956  1.00 38.32 ? 482 HOH   C O   1 
HETATM 2598 O  O   . HOH   I 5 .   ? 44.674 -2.099  17.661 1.00 40.77 ? 483 HOH   C O   1 
HETATM 2599 O  O   . HOH   I 5 .   ? 3.441  -9.497  17.104 1.00 33.29 ? 484 HOH   C O   1 
HETATM 2600 O  O   . HOH   I 5 .   ? 19.913 -15.169 34.763 1.00 30.38 ? 485 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   ? 0.1997 0.1869 0.1844 -0.0105 -0.0042 -0.0108 7   SER   A N   
2    C CA  . SER   A 1   ? 0.1969 0.1850 0.1858 -0.0085 -0.0066 -0.0088 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1940 0.1813 0.1855 -0.0037 -0.0094 -0.0034 7   SER   A C   
4    O O   . SER   A 1   ? 0.1933 0.1801 0.1825 -0.0027 -0.0102 -0.0011 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2278 0.2228 0.2134 -0.0134 -0.0095 -0.0088 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2694 0.2692 0.2512 -0.0143 -0.0136 -0.0039 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1808 0.1680 0.1772 -0.0013 -0.0104 -0.0020 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1678 0.1543 0.1674 0.0022  -0.0118 0.0017  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1515 0.1363 0.1560 0.0042  -0.0104 0.0012  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1703 0.1535 0.1760 0.0039  -0.0082 -0.0009 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1414 0.1267 0.1494 0.0060  -0.0112 0.0032  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1429 0.1276 0.1547 0.0070  -0.0097 0.0025  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1443 0.1280 0.1583 0.0082  -0.0085 0.0034  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1531 0.1361 0.1675 0.0090  -0.0089 0.0050  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1640 0.1516 0.1794 0.0064  -0.0110 0.0023  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1352 0.1191 0.1508 0.0078  -0.0066 0.0023  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1292 0.1128 0.1473 0.0075  -0.0041 0.0015  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1365 0.1216 0.1603 0.0079  -0.0038 0.0009  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1394 0.1263 0.1635 0.0073  -0.0045 0.0005  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1325 0.1175 0.1477 0.0051  -0.0021 0.0006  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1567 0.1416 0.1673 0.0047  -0.0027 0.0019  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1563 0.1410 0.1729 0.0032  0.0014  -0.0018 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1704 0.1595 0.1795 0.0021  -0.0018 0.0030  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1337 0.1179 0.1632 0.0090  -0.0021 0.0009  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1413 0.1274 0.1783 0.0097  -0.0012 0.0005  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1444 0.1291 0.1846 0.0080  0.0042  -0.0030 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1532 0.1350 0.1983 0.0089  0.0072  -0.0032 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1540 0.1417 0.1982 0.0124  -0.0034 0.0044  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1502 0.1412 0.1902 0.0121  -0.0083 0.0069  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1548 0.1495 0.1953 0.0110  -0.0101 0.0063  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1676 0.1581 0.2026 0.0119  -0.0106 0.0090  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1620 0.1597 0.1979 0.0092  -0.0136 0.0071  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1745 0.1686 0.2048 0.0101  -0.0142 0.0100  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1689 0.1663 0.1994 0.0085  -0.0153 0.0085  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2061 0.2068 0.2315 0.0054  -0.0177 0.0080  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1495 0.1363 0.1868 0.0049  0.0059  -0.0057 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1516 0.1386 0.1900 0.0013  0.0115  -0.0102 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1673 0.1573 0.2104 0.0002  0.0132  -0.0121 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1583 0.1513 0.1987 0.0000  0.0099  -0.0104 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1702 0.1595 0.1993 -0.0033 0.0122  -0.0114 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1866 0.1798 0.2108 -0.0039 0.0080  -0.0081 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1861 0.1775 0.2150 -0.0090 0.0182  -0.0167 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1718 0.1608 0.2232 -0.0002 0.0186  -0.0155 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1784 0.1705 0.2352 -0.0012 0.0204  -0.0174 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1651 0.1593 0.2252 0.0027  0.0149  -0.0130 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1596 0.1528 0.2237 0.0068  0.0116  -0.0089 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1580 0.1559 0.2152 0.0006  0.0134  -0.0133 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1487 0.1487 0.2075 0.0030  0.0085  -0.0099 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1421 0.1419 0.1917 0.0021  0.0044  -0.0078 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1577 0.1593 0.2068 0.0016  0.0023  -0.0069 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1759 0.1797 0.2409 0.0019  0.0102  -0.0116 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2122 0.2168 0.2902 0.0044  0.0135  -0.0122 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2457 0.2528 0.3312 0.0078  0.0105  -0.0084 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2032 0.2061 0.2848 0.0024  0.0202  -0.0168 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1414 0.1386 0.1852 0.0022  0.0038  -0.0069 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1324 0.1289 0.1698 0.0019  0.0008  -0.0046 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1332 0.1271 0.1688 0.0045  -0.0018 -0.0028 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1470 0.1392 0.1838 0.0058  -0.0010 -0.0028 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1432 0.1408 0.1750 -0.0013 0.0024  -0.0045 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1587 0.1605 0.1905 -0.0053 0.0047  -0.0057 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1764 0.1800 0.2097 -0.0059 0.0036  -0.0042 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1911 0.1954 0.2211 -0.0094 0.0085  -0.0085 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1862 0.1942 0.2190 -0.0101 0.0056  -0.0046 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2039 0.2135 0.2325 -0.0144 0.0107  -0.0096 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2124 0.2239 0.2424 -0.0146 0.0089  -0.0071 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2538 0.2711 0.2825 -0.0199 0.0109  -0.0077 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1323 0.1257 0.1652 0.0047  -0.0042 -0.0016 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1346 0.1261 0.1642 0.0058  -0.0062 -0.0005 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1362 0.1261 0.1620 0.0050  -0.0056 0.0001  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1333 0.1232 0.1603 0.0041  -0.0050 0.0004  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1410 0.1344 0.1718 0.0056  -0.0087 -0.0004 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1422 0.1345 0.1684 0.0049  -0.0100 -0.0004 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1589 0.1553 0.1855 0.0029  -0.0124 -0.0007 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1640 0.1590 0.1863 0.0001  -0.0116 -0.0033 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1702 0.1656 0.1879 -0.0014 -0.0123 -0.0037 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1976 0.1945 0.2141 0.0000  -0.0144 -0.0007 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1901 0.1841 0.2049 -0.0047 -0.0102 -0.0074 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1297 0.1182 0.1522 0.0054  -0.0052 0.0009  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1257 0.1137 0.1465 0.0050  -0.0046 0.0026  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1353 0.1208 0.1543 0.0059  -0.0052 0.0021  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1416 0.1264 0.1579 0.0065  -0.0060 0.0017  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1317 0.1217 0.1502 0.0038  -0.0036 0.0037  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1473 0.1391 0.1662 0.0034  -0.0033 0.0071  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1555 0.1485 0.1745 0.0015  -0.0021 0.0026  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1264 0.1104 0.1474 0.0056  -0.0041 0.0019  18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1301 0.1118 0.1495 0.0054  -0.0034 0.0001  18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1534 0.1351 0.1727 0.0054  -0.0035 0.0000  18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1392 0.1191 0.1625 0.0059  -0.0006 0.0014  18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1434 0.1244 0.1715 0.0064  0.0004  0.0047  18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1303 0.1119 0.1494 0.0034  -0.0036 -0.0032 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1983 0.1802 0.2178 0.0034  -0.0038 -0.0031 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1550 0.1398 0.1714 0.0030  -0.0068 -0.0031 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.1990 0.1799 0.2153 0.0012  -0.0028 -0.0062 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0856 0.0665 0.1095 0.0025  -0.0019 -0.0038 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2379 0.2231 0.2566 0.0034  -0.0067 -0.0027 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1410 0.1187 0.1633 0.0056  0.0011  -0.0006 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1463 0.1218 0.1753 0.0063  0.0051  0.0004  19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1386 0.1114 0.1732 0.0052  0.0079  -0.0015 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1467 0.1187 0.1780 0.0025  0.0078  -0.0062 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1407 0.1138 0.1679 0.0053  0.0076  -0.0032 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1430 0.1182 0.1650 0.0061  0.0054  -0.0015 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1528 0.1291 0.1675 0.0050  0.0025  -0.0030 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1564 0.1330 0.1828 0.0080  0.0064  0.0023  19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1392 0.1112 0.1828 0.0067  0.0104  0.0027  20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1501 0.1187 0.2003 0.0056  0.0137  0.0012  20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1719 0.1355 0.2229 0.0030  0.0186  -0.0060 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1839 0.1458 0.2339 -0.0001 0.0200  -0.0108 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1559 0.1248 0.2176 0.0080  0.0160  0.0083  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1496 0.1146 0.2194 0.0070  0.0197  0.0082  20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1698 0.1358 0.2531 0.0097  0.0220  0.0173  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1802 0.1429 0.2723 0.0090  0.0252  0.0191  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2005 0.1554 0.3023 0.0085  0.0323  0.0154  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2065 0.1563 0.3091 0.0079  0.0371  0.0085  20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2147 0.1667 0.3261 0.0082  0.0355  0.0183  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1643 0.1263 0.2159 0.0033  0.0213  -0.0077 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1895 0.1471 0.2418 -0.0004 0.0272  -0.0157 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2008 0.1611 0.2407 -0.0056 0.0246  -0.0222 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2264 0.1846 0.2652 -0.0107 0.0294  -0.0297 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2093 0.1645 0.2672 0.0008  0.0321  -0.0163 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1945 0.1535 0.2428 0.0008  0.0282  -0.0162 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.1870 0.1500 0.2348 0.0047  0.0236  -0.0090 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2100 0.1697 0.2493 -0.0033 0.0287  -0.0224 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.1944 0.1593 0.2335 0.0035  0.0217  -0.0111 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2145 0.1777 0.2483 -0.0012 0.0243  -0.0186 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.1859 0.1516 0.2172 -0.0047 0.0173  -0.0191 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1807 0.1511 0.2022 -0.0089 0.0135  -0.0223 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.1886 0.1622 0.2092 -0.0094 0.0098  -0.0210 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2024 0.1815 0.2169 -0.0124 0.0060  -0.0219 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1783 0.1523 0.1927 -0.0076 0.0090  -0.0194 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.1909 0.1626 0.2050 -0.0078 0.0125  -0.0213 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.1970 0.1720 0.2043 -0.0066 0.0080  -0.0180 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2246 0.1955 0.2362 -0.0144 0.0177  -0.0293 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1825 0.1537 0.2103 -0.0069 0.0111  -0.0185 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1836 0.1579 0.2112 -0.0075 0.0080  -0.0176 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.1925 0.1686 0.2178 -0.0135 0.0094  -0.0235 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.1953 0.1675 0.2226 -0.0171 0.0151  -0.0289 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1818 0.1535 0.2171 -0.0046 0.0095  -0.0137 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.1859 0.1684 0.2074 -0.0150 0.0046  -0.0226 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1818 0.1690 0.2005 -0.0215 0.0047  -0.0273 24  THR   A CA  
140  C C   . THR   A 18  ? 0.1928 0.1783 0.2171 -0.0224 0.0068  -0.0286 24  THR   A C   
141  O O   . THR   A 18  ? 0.1758 0.1578 0.2056 -0.0177 0.0071  -0.0246 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2031 0.2002 0.2170 -0.0226 -0.0021 -0.0241 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2019 0.2004 0.2202 -0.0179 -0.0053 -0.0191 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2171 0.2163 0.2259 -0.0215 -0.0047 -0.0215 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.1852 0.1747 0.2075 -0.0292 0.0079  -0.0336 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.1914 0.1802 0.2185 -0.0305 0.0094  -0.0347 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.1774 0.1709 0.2064 -0.0259 0.0038  -0.0284 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.1885 0.1785 0.2230 -0.0233 0.0052  -0.0266 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2150 0.2098 0.2381 -0.0397 0.0106  -0.0412 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.2900 0.2868 0.3172 -0.0413 0.0105  -0.0416 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3459 0.3338 0.3801 -0.0411 0.0166  -0.0438 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3277 0.3342 0.3544 -0.0419 0.0047  -0.0384 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3475 0.3402 0.3832 -0.0432 0.0148  -0.0436 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3534 0.3574 0.3851 -0.0432 0.0075  -0.0402 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1755 0.1771 0.2009 -0.0248 -0.0022 -0.0248 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1696 0.1750 0.1988 -0.0205 -0.0061 -0.0197 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1640 0.1627 0.1964 -0.0144 -0.0048 -0.0163 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1672 0.1661 0.2037 -0.0125 -0.0049 -0.0144 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.1858 0.2001 0.2136 -0.0198 -0.0117 -0.0155 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2780 0.2960 0.3121 -0.0159 -0.0142 -0.0113 26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3155 0.3384 0.3531 -0.0182 -0.0147 -0.0119 26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.2955 0.3111 0.3317 -0.0105 -0.0149 -0.0076 26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1603 0.1540 0.1907 -0.0122 -0.0034 -0.0157 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1496 0.1389 0.1826 -0.0077 -0.0022 -0.0123 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1453 0.1304 0.1835 -0.0081 0.0014  -0.0122 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1567 0.1426 0.1975 -0.0062 0.0010  -0.0089 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1597 0.1452 0.1904 -0.0060 -0.0011 -0.0116 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1784 0.1672 0.2046 -0.0048 -0.0045 -0.0102 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1670 0.1593 0.1939 -0.0029 -0.0073 -0.0076 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1719 0.1595 0.1944 -0.0059 -0.0039 -0.0117 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1491 0.1300 0.1892 -0.0110 0.0055  -0.0158 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1495 0.1258 0.1965 -0.0112 0.0097  -0.0149 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1514 0.1311 0.1998 -0.0130 0.0084  -0.0150 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1603 0.1384 0.2136 -0.0120 0.0099  -0.0116 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1686 0.1387 0.2188 -0.0144 0.0157  -0.0199 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1562 0.1213 0.2094 -0.0117 0.0188  -0.0183 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.1821 0.1463 0.2315 -0.0130 0.0201  -0.0221 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1652 0.1269 0.2267 -0.0076 0.0209  -0.0117 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1747 0.1346 0.2299 -0.0094 0.0231  -0.0188 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1780 0.1365 0.2413 -0.0061 0.0236  -0.0121 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.1773 0.1394 0.2451 -0.0056 0.0207  -0.0051 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.1925 0.1488 0.2649 -0.0021 0.0258  -0.0053 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.1979 0.1586 0.2734 -0.0022 0.0223  0.0020  28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2007 0.1583 0.2797 -0.0004 0.0252  0.0020  28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1409 0.1264 0.1856 -0.0159 0.0057  -0.0183 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1496 0.1395 0.1964 -0.0178 0.0046  -0.0186 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1622 0.1562 0.2098 -0.0142 0.0013  -0.0143 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1807 0.1781 0.2310 -0.0152 0.0009  -0.0141 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1886 0.1851 0.2323 -0.0226 0.0026  -0.0227 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1586 0.1528 0.2040 -0.0106 -0.0006 -0.0114 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1613 0.1588 0.2074 -0.0080 -0.0023 -0.0086 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1484 0.1426 0.1935 -0.0059 -0.0011 -0.0053 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1523 0.1481 0.1956 -0.0040 -0.0023 -0.0040 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1712 0.1737 0.2165 -0.0066 -0.0056 -0.0085 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1917 0.2002 0.2395 -0.0092 -0.0073 -0.0100 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2272 0.2393 0.2793 -0.0093 -0.0072 -0.0098 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2002 0.2108 0.2452 -0.0119 -0.0086 -0.0117 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1470 0.1372 0.1942 -0.0064 0.0014  -0.0037 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1465 0.1351 0.1938 -0.0048 0.0022  0.0006  31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1640 0.1570 0.2107 -0.0053 0.0016  0.0040  31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1806 0.1760 0.2294 -0.0073 0.0022  0.0046  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1510 0.1346 0.2039 -0.0051 0.0056  0.0025  31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1538 0.1368 0.2093 -0.0033 0.0064  0.0085  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1647 0.1465 0.2167 -0.0012 0.0056  0.0071  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1889 0.1670 0.2536 -0.0032 0.0105  0.0116  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1501 0.1449 0.1938 -0.0043 0.0007  0.0061  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1602 0.1604 0.2023 -0.0064 0.0007  0.0091  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1526 0.1542 0.1966 -0.0067 0.0009  0.0159  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1741 0.1802 0.2199 -0.0094 0.0012  0.0207  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1493 0.1516 0.1868 -0.0063 0.0001  0.0063  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1818 0.1904 0.2165 -0.0101 0.0009  0.0086  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1658 0.1680 0.2046 -0.0056 0.0001  0.0014  32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1470 0.1455 0.1916 -0.0042 0.0008  0.0171  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1486 0.1496 0.1970 -0.0040 0.0010  0.0244  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1519 0.1472 0.2031 -0.0006 0.0021  0.0238  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1487 0.1410 0.1952 0.0006  0.0015  0.0182  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1639 0.1730 0.2067 -0.0068 -0.0007 0.0271  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1713 0.1854 0.2171 -0.0069 -0.0014 0.0350  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1953 0.2160 0.2467 -0.0089 -0.0019 0.0444  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1648 0.1786 0.2092 -0.0051 -0.0020 0.0353  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2024 0.2282 0.2563 -0.0085 -0.0030 0.0508  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1823 0.2035 0.2320 -0.0061 -0.0028 0.0449  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1824 0.1913 0.2222 -0.0030 -0.0020 0.0291  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2063 0.2304 0.2559 -0.0052 -0.0036 0.0476  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1869 0.1979 0.2258 -0.0023 -0.0026 0.0314  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2058 0.2239 0.2499 -0.0031 -0.0032 0.0402  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1561 0.1503 0.2157 0.0008  0.0039  0.0297  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1635 0.1528 0.2269 0.0036  0.0059  0.0289  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1710 0.1639 0.2437 0.0049  0.0068  0.0384  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1797 0.1764 0.2594 0.0040  0.0070  0.0459  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1877 0.1685 0.2545 0.0043  0.0096  0.0226  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.1948 0.1725 0.2706 0.0035  0.0128  0.0249  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.1990 0.1740 0.2891 0.0056  0.0171  0.0319  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2113 0.1865 0.3098 0.0051  0.0188  0.0376  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1924 0.1653 0.2866 0.0078  0.0192  0.0323  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1704 0.1627 0.2447 0.0070  0.0075  0.0389  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1619 0.1587 0.2470 0.0087  0.0084  0.0487  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1588 0.1494 0.2496 0.0118  0.0121  0.0459  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1592 0.1502 0.2421 0.0119  0.0107  0.0416  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1892 0.1980 0.2686 0.0060  0.0036  0.0550  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2255 0.2426 0.3158 0.0069  0.0032  0.0671  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2457 0.2584 0.3468 0.0107  0.0067  0.0688  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2687 0.2977 0.3569 0.0031  -0.0004 0.0747  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1576 0.1419 0.2623 0.0140  0.0177  0.0475  36  SER   A N   
245  C CA  . SER   A 30  ? 0.1780 0.1557 0.2898 0.0164  0.0230  0.0437  36  SER   A CA  
246  C C   . SER   A 30  ? 0.1852 0.1697 0.3017 0.0185  0.0217  0.0508  36  SER   A C   
247  O O   . SER   A 30  ? 0.1857 0.1675 0.2986 0.0191  0.0232  0.0451  36  SER   A O   
248  C CB  . SER   A 30  ? 0.2140 0.1836 0.3422 0.0178  0.0305  0.0443  36  SER   A CB  
249  O OG  . SER   A 30  ? 0.2435 0.2063 0.3799 0.0196  0.0372  0.0399  36  SER   A OG  
250  N N   . SER   A 31  ? 0.1717 0.1666 0.2946 0.0187  0.0185  0.0632  37  SER   A N   
251  C CA  . SER   A 31  ? 0.1764 0.1800 0.3038 0.0199  0.0167  0.0707  37  SER   A CA  
252  C C   . SER   A 31  ? 0.1656 0.1730 0.2760 0.0176  0.0122  0.0648  37  SER   A C   
253  O O   . SER   A 31  ? 0.1825 0.1939 0.2950 0.0186  0.0121  0.0670  37  SER   A O   
254  C CB  . SER   A 31  ? 0.1953 0.2120 0.3324 0.0193  0.0133  0.0862  37  SER   A CB  
255  O OG  . SER   A 31  ? 0.2680 0.2944 0.3912 0.0143  0.0070  0.0878  37  SER   A OG  
256  N N   . ARG   A 32  ? 0.1567 0.1629 0.2514 0.0145  0.0090  0.0575  38  ARG   A N   
257  C CA  . ARG   A 32  ? 0.1627 0.1710 0.2422 0.0123  0.0056  0.0516  38  ARG   A CA  
258  C C   . ARG   A 32  ? 0.1619 0.1598 0.2336 0.0130  0.0076  0.0399  38  ARG   A C   
259  O O   . ARG   A 32  ? 0.1511 0.1497 0.2119 0.0117  0.0053  0.0353  38  ARG   A O   
260  C CB  . ARG   A 32  ? 0.1715 0.1859 0.2402 0.0080  0.0013  0.0515  38  ARG   A CB  
261  C CG  . ARG   A 32  ? 0.1823 0.2101 0.2551 0.0051  -0.0015 0.0628  38  ARG   A CG  
262  C CD  . ARG   A 32  ? 0.1774 0.2113 0.2392 -0.0003 -0.0045 0.0614  38  ARG   A CD  
263  N NE  . ARG   A 32  ? 0.1456 0.1802 0.1946 -0.0030 -0.0058 0.0541  38  ARG   A NE  
264  C CZ  . ARG   A 32  ? 0.1528 0.1960 0.1930 -0.0090 -0.0077 0.0539  38  ARG   A CZ  
265  N NH1 . ARG   A 32  ? 0.1919 0.2449 0.2333 -0.0135 -0.0092 0.0604  38  ARG   A NH1 
266  N NH2 . ARG   A 32  ? 0.1635 0.2059 0.1939 -0.0113 -0.0076 0.0469  38  ARG   A NH2 
267  N N   . ASP   A 33  ? 0.1486 0.1378 0.2254 0.0143  0.0118  0.0351  39  ASP   A N   
268  C CA  . ASP   A 33  ? 0.1390 0.1206 0.2075 0.0134  0.0131  0.0247  39  ASP   A CA  
269  C C   . ASP   A 33  ? 0.1480 0.1310 0.2036 0.0111  0.0087  0.0206  39  ASP   A C   
270  O O   . ASP   A 33  ? 0.1509 0.1317 0.1978 0.0102  0.0076  0.0147  39  ASP   A O   
271  C CB  . ASP   A 33  ? 0.1622 0.1417 0.2286 0.0139  0.0150  0.0208  39  ASP   A CB  
272  C CG  . ASP   A 33  ? 0.1653 0.1387 0.2239 0.0120  0.0165  0.0111  39  ASP   A CG  
273  O OD1 . ASP   A 33  ? 0.1698 0.1384 0.2303 0.0105  0.0193  0.0067  39  ASP   A OD1 
274  O OD2 . ASP   A 33  ? 0.1832 0.1572 0.2334 0.0111  0.0149  0.0079  39  ASP   A OD2 
275  N N   . LEU   A 34  ? 0.1440 0.1305 0.1996 0.0100  0.0066  0.0239  40  LEU   A N   
276  C CA  . LEU   A 34  ? 0.1429 0.1307 0.1886 0.0080  0.0034  0.0200  40  LEU   A CA  
277  C C   . LEU   A 34  ? 0.1391 0.1245 0.1864 0.0070  0.0040  0.0181  40  LEU   A C   
278  O O   . LEU   A 34  ? 0.1464 0.1320 0.2018 0.0072  0.0057  0.0224  40  LEU   A O   
279  C CB  . LEU   A 34  ? 0.1443 0.1400 0.1862 0.0061  0.0005  0.0244  40  LEU   A CB  
280  C CG  . LEU   A 34  ? 0.1625 0.1614 0.1992 0.0056  -0.0008 0.0247  40  LEU   A CG  
281  C CD1 . LEU   A 34  ? 0.1623 0.1696 0.1948 0.0019  -0.0028 0.0278  40  LEU   A CD1 
282  C CD2 . LEU   A 34  ? 0.1689 0.1625 0.1985 0.0062  -0.0011 0.0178  40  LEU   A CD2 
283  N N   . LEU   A 35  ? 0.1341 0.1181 0.1747 0.0060  0.0024  0.0126  41  LEU   A N   
284  C CA  . LEU   A 35  ? 0.1334 0.1170 0.1746 0.0047  0.0023  0.0106  41  LEU   A CA  
285  C C   . LEU   A 35  ? 0.1279 0.1141 0.1625 0.0038  -0.0004 0.0079  41  LEU   A C   
286  O O   . LEU   A 35  ? 0.1362 0.1219 0.1662 0.0044  -0.0017 0.0055  41  LEU   A O   
287  C CB  . LEU   A 35  ? 0.1471 0.1253 0.1904 0.0041  0.0049  0.0056  41  LEU   A CB  
288  C CG  . LEU   A 35  ? 0.1403 0.1182 0.1846 0.0021  0.0050  0.0031  41  LEU   A CG  
289  C CD1 . LEU   A 35  ? 0.1649 0.1375 0.2151 0.0008  0.0095  0.0003  41  LEU   A CD1 
290  C CD2 . LEU   A 35  ? 0.1529 0.1331 0.1908 0.0010  0.0021  -0.0011 41  LEU   A CD2 
291  N N   . VAL   A 36  ? 0.1355 0.1245 0.1708 0.0024  -0.0009 0.0085  42  VAL   A N   
292  C CA  . VAL   A 36  ? 0.1315 0.1229 0.1635 0.0016  -0.0022 0.0059  42  VAL   A CA  
293  C C   . VAL   A 36  ? 0.1263 0.1176 0.1607 0.0008  -0.0021 0.0035  42  VAL   A C   
294  O O   . VAL   A 36  ? 0.1386 0.1301 0.1763 -0.0004 -0.0010 0.0051  42  VAL   A O   
295  C CB  . VAL   A 36  ? 0.1289 0.1253 0.1591 -0.0005 -0.0020 0.0081  42  VAL   A CB  
296  C CG1 . VAL   A 36  ? 0.1544 0.1522 0.1832 -0.0015 -0.0016 0.0043  42  VAL   A CG1 
297  C CG2 . VAL   A 36  ? 0.1474 0.1454 0.1750 -0.0006 -0.0022 0.0106  42  VAL   A CG2 
298  N N   . SER   A 37  ? 0.1278 0.1191 0.1612 0.0013  -0.0034 0.0004  43  SER   A N   
299  C CA  . SER   A 37  ? 0.1309 0.1239 0.1669 0.0003  -0.0038 -0.0017 43  SER   A CA  
300  C C   . SER   A 37  ? 0.1353 0.1316 0.1728 0.0007  -0.0042 -0.0024 43  SER   A C   
301  O O   . SER   A 37  ? 0.1432 0.1395 0.1794 0.0017  -0.0039 -0.0022 43  SER   A O   
302  C CB  . SER   A 37  ? 0.1483 0.1406 0.1838 -0.0003 -0.0049 -0.0039 43  SER   A CB  
303  O OG  . SER   A 37  ? 0.1490 0.1421 0.1817 0.0009  -0.0068 -0.0038 43  SER   A OG  
304  N N   . SER   A 38  ? 0.1410 0.1401 0.1823 -0.0003 -0.0041 -0.0036 44  SER   A N   
305  C CA  . SER   A 38  ? 0.1534 0.1556 0.1987 0.0003  -0.0035 -0.0045 44  SER   A CA  
306  C C   . SER   A 38  ? 0.1769 0.1814 0.2257 0.0021  -0.0058 -0.0039 44  SER   A C   
307  O O   . SER   A 38  ? 0.2094 0.2152 0.2570 0.0013  -0.0082 -0.0036 44  SER   A O   
308  C CB  . SER   A 38  ? 0.1815 0.1866 0.2303 -0.0018 -0.0020 -0.0056 44  SER   A CB  
309  O OG  . SER   A 38  ? 0.2082 0.2144 0.2585 -0.0027 -0.0036 -0.0060 44  SER   A OG  
310  N N   . THR   A 39  ? 0.1708 0.1765 0.2247 0.0040  -0.0047 -0.0035 45  THR   A N   
311  C CA  . THR   A 39  ? 0.1909 0.1998 0.2502 0.0061  -0.0071 -0.0008 45  THR   A CA  
312  C C   . THR   A 39  ? 0.2131 0.2262 0.2832 0.0072  -0.0054 -0.0005 45  THR   A C   
313  O O   . THR   A 39  ? 0.2099 0.2217 0.2827 0.0066  -0.0012 -0.0034 45  THR   A O   
314  C CB  . THR   A 39  ? 0.1987 0.2045 0.2572 0.0083  -0.0068 0.0008  45  THR   A CB  
315  O OG1 . THR   A 39  ? 0.2052 0.2083 0.2671 0.0088  -0.0022 -0.0012 45  THR   A OG1 
316  C CG2 . THR   A 39  ? 0.2108 0.2126 0.2595 0.0074  -0.0080 0.0005  45  THR   A CG2 
317  N N   . THR   A 40  ? 0.2204 0.2395 0.2972 0.0084  -0.0085 0.0032  46  THR   A N   
318  C CA  . THR   A 40  ? 0.2350 0.2590 0.3249 0.0101  -0.0069 0.0048  46  THR   A CA  
319  C C   . THR   A 40  ? 0.2279 0.2489 0.3264 0.0137  -0.0034 0.0064  46  THR   A C   
320  O O   . THR   A 40  ? 0.2465 0.2662 0.3535 0.0145  0.0020  0.0038  46  THR   A O   
321  C CB  . THR   A 40  ? 0.2855 0.3190 0.3803 0.0095  -0.0119 0.0093  46  THR   A CB  
322  O OG1 . THR   A 40  ? 0.3539 0.3899 0.4473 0.0102  -0.0159 0.0143  46  THR   A OG1 
323  C CG2 . THR   A 40  ? 0.2957 0.3312 0.3824 0.0052  -0.0140 0.0064  46  THR   A CG2 
324  N N   . ALA   A 41  ? 0.2206 0.2398 0.3165 0.0151  -0.0057 0.0099  47  ALA   A N   
325  C CA  . ALA   A 41  ? 0.2348 0.2502 0.3392 0.0183  -0.0020 0.0118  47  ALA   A CA  
326  C C   . ALA   A 41  ? 0.2273 0.2340 0.3236 0.0170  0.0028  0.0060  47  ALA   A C   
327  O O   . ALA   A 41  ? 0.2254 0.2298 0.3084 0.0146  0.0008  0.0038  47  ALA   A O   
328  C CB  . ALA   A 41  ? 0.2697 0.2880 0.3753 0.0201  -0.0067 0.0190  47  ALA   A CB  
329  N N   . GLN   A 42  ? 0.1953 0.1976 0.2998 0.0181  0.0093  0.0038  48  GLN   A N   
330  C CA  . GLN   A 42  ? 0.2095 0.2051 0.3065 0.0156  0.0141  -0.0018 48  GLN   A CA  
331  C C   . GLN   A 42  ? 0.2152 0.2074 0.3075 0.0169  0.0118  0.0014  48  GLN   A C   
332  O O   . GLN   A 42  ? 0.2337 0.2266 0.3349 0.0204  0.0103  0.0074  48  GLN   A O   
333  C CB  . GLN   A 42  ? 0.2446 0.2369 0.3527 0.0151  0.0231  -0.0066 48  GLN   A CB  
334  C CG  . GLN   A 42  ? 0.3168 0.3123 0.4272 0.0123  0.0267  -0.0117 48  GLN   A CG  
335  C CD  . GLN   A 42  ? 0.4031 0.3950 0.5235 0.0105  0.0369  -0.0180 48  GLN   A CD  
336  O OE1 . GLN   A 42  ? 0.3776 0.3690 0.5154 0.0142  0.0411  -0.0163 48  GLN   A OE1 
337  N NE2 . GLN   A 42  ? 0.4570 0.4467 0.5671 0.0045  0.0415  -0.0253 48  GLN   A NE2 
338  N N   . GLY   A 43  ? 0.1871 0.1762 0.2663 0.0140  0.0115  -0.0018 49  GLY   A N   
339  C CA  . GLY   A 43  ? 0.1824 0.1682 0.2561 0.0147  0.0098  0.0005  49  GLY   A CA  
340  C C   . GLY   A 43  ? 0.1711 0.1510 0.2477 0.0137  0.0164  -0.0029 49  GLY   A C   
341  O O   . GLY   A 43  ? 0.1799 0.1583 0.2602 0.0112  0.0230  -0.0086 49  GLY   A O   
342  N N   . CYS   A 44  ? 0.1671 0.1440 0.2409 0.0148  0.0150  0.0000  50  CYS   A N   
343  C CA  . CYS   A 44  ? 0.1708 0.1416 0.2481 0.0139  0.0215  -0.0028 50  CYS   A CA  
344  C C   . CYS   A 44  ? 0.1769 0.1458 0.2408 0.0097  0.0221  -0.0067 50  CYS   A C   
345  O O   . CYS   A 44  ? 0.1896 0.1538 0.2552 0.0077  0.0279  -0.0101 50  CYS   A O   
346  C CB  . CYS   A 44  ? 0.1834 0.1520 0.2712 0.0182  0.0209  0.0041  50  CYS   A CB  
347  S SG  . CYS   A 44  ? 0.2146 0.1864 0.3228 0.0231  0.0216  0.0101  50  CYS   A SG  
348  N N   . ASP   A 45  ? 0.1622 0.1347 0.2144 0.0084  0.0165  -0.0059 51  ASP   A N   
349  C CA  . ASP   A 45  ? 0.1600 0.1323 0.2011 0.0046  0.0168  -0.0085 51  ASP   A CA  
350  C C   . ASP   A 45  ? 0.1689 0.1433 0.2069 -0.0010 0.0217  -0.0146 51  ASP   A C   
351  O O   . ASP   A 45  ? 0.1900 0.1673 0.2306 -0.0019 0.0225  -0.0162 51  ASP   A O   
352  C CB  . ASP   A 45  ? 0.1559 0.1316 0.1883 0.0053  0.0103  -0.0052 51  ASP   A CB  
353  C CG  . ASP   A 45  ? 0.1680 0.1429 0.2010 0.0089  0.0058  -0.0001 51  ASP   A CG  
354  O OD1 . ASP   A 45  ? 0.1711 0.1424 0.2068 0.0100  0.0072  0.0014  51  ASP   A OD1 
355  O OD2 . ASP   A 45  ? 0.1749 0.1527 0.2050 0.0099  0.0012  0.0021  51  ASP   A OD2 
356  N N   . THR   A 46  ? 0.1896 0.1638 0.2217 -0.0056 0.0248  -0.0179 52  THR   A N   
357  C CA  . THR   A 46  ? 0.2029 0.1819 0.2293 -0.0128 0.0287  -0.0232 52  THR   A CA  
358  C C   . THR   A 46  ? 0.1977 0.1823 0.2130 -0.0158 0.0244  -0.0208 52  THR   A C   
359  O O   . THR   A 46  ? 0.2068 0.1894 0.2194 -0.0135 0.0216  -0.0178 52  THR   A O   
360  C CB  . THR   A 46  ? 0.2604 0.2357 0.2902 -0.0175 0.0375  -0.0301 52  THR   A CB  
361  O OG1 . THR   A 46  ? 0.3095 0.2812 0.3368 -0.0172 0.0375  -0.0292 52  THR   A OG1 
362  C CG2 . THR   A 46  ? 0.2720 0.2416 0.3161 -0.0140 0.0428  -0.0320 52  THR   A CG2 
363  N N   . ILE   A 47  ? 0.1832 0.1754 0.1932 -0.0207 0.0236  -0.0210 53  ILE   A N   
364  C CA  . ILE   A 47  ? 0.1751 0.1745 0.1773 -0.0233 0.0194  -0.0171 53  ILE   A CA  
365  C C   . ILE   A 47  ? 0.1794 0.1838 0.1752 -0.0315 0.0231  -0.0207 53  ILE   A C   
366  O O   . ILE   A 47  ? 0.1902 0.1974 0.1849 -0.0384 0.0288  -0.0267 53  ILE   A O   
367  C CB  . ILE   A 47  ? 0.1673 0.1737 0.1683 -0.0241 0.0159  -0.0132 53  ILE   A CB  
368  C CG1 . ILE   A 47  ? 0.1741 0.1757 0.1812 -0.0174 0.0132  -0.0110 53  ILE   A CG1 
369  C CG2 . ILE   A 47  ? 0.1599 0.1737 0.1562 -0.0255 0.0114  -0.0069 53  ILE   A CG2 
370  C CD1 . ILE   A 47  ? 0.1913 0.1877 0.2000 -0.0106 0.0089  -0.0071 53  ILE   A CD1 
371  N N   . ALA   A 48  ? 0.1629 0.1692 0.1546 -0.0316 0.0206  -0.0177 54  ALA   A N   
372  C CA  . ALA   A 48  ? 0.1677 0.1811 0.1526 -0.0400 0.0230  -0.0200 54  ALA   A CA  
373  C C   . ALA   A 48  ? 0.1776 0.2047 0.1573 -0.0472 0.0211  -0.0172 54  ALA   A C   
374  O O   . ALA   A 48  ? 0.1777 0.2092 0.1589 -0.0439 0.0157  -0.0101 54  ALA   A O   
375  C CB  . ALA   A 48  ? 0.1582 0.1713 0.1410 -0.0373 0.0195  -0.0158 54  ALA   A CB  
376  N N   . ARG   A 49  ? 0.1983 0.2329 0.1721 -0.0579 0.0258  -0.0226 55  ARG   A N   
377  C CA  . ARG   A 49  ? 0.2102 0.2606 0.1780 -0.0668 0.0239  -0.0193 55  ARG   A CA  
378  C C   . ARG   A 49  ? 0.2417 0.3018 0.2021 -0.0757 0.0248  -0.0202 55  ARG   A C   
379  O O   . ARG   A 49  ? 0.2626 0.3245 0.2181 -0.0852 0.0316  -0.0290 55  ARG   A O   
380  C CB  . ARG   A 49  ? 0.2197 0.2719 0.1868 -0.0730 0.0292  -0.0259 55  ARG   A CB  
381  C CG  . ARG   A 49  ? 0.2263 0.2693 0.2013 -0.0642 0.0284  -0.0251 55  ARG   A CG  
382  C CD  . ARG   A 49  ? 0.2081 0.2550 0.1857 -0.0582 0.0205  -0.0146 55  ARG   A CD  
383  N NE  . ARG   A 49  ? 0.2053 0.2434 0.1900 -0.0508 0.0205  -0.0154 55  ARG   A NE  
384  C CZ  . ARG   A 49  ? 0.2140 0.2498 0.2032 -0.0434 0.0152  -0.0086 55  ARG   A CZ  
385  N NH1 . ARG   A 49  ? 0.2040 0.2451 0.1928 -0.0417 0.0099  -0.0002 55  ARG   A NH1 
386  N NH2 . ARG   A 49  ? 0.2191 0.2476 0.2142 -0.0380 0.0156  -0.0102 55  ARG   A NH2 
387  N N   . CYS   A 50  ? 0.2299 0.2960 0.1903 -0.0728 0.0186  -0.0113 56  CYS   A N   
388  C CA  . CYS   A 50  ? 0.2317 0.3053 0.1868 -0.0789 0.0186  -0.0110 56  CYS   A CA  
389  C C   . CYS   A 50  ? 0.2303 0.3128 0.1883 -0.0747 0.0109  0.0011  56  CYS   A C   
390  O O   . CYS   A 50  ? 0.2550 0.3362 0.2196 -0.0668 0.0063  0.0087  56  CYS   A O   
391  C CB  . CYS   A 50  ? 0.2238 0.2822 0.1807 -0.0745 0.0232  -0.0183 56  CYS   A CB  
392  S SG  . CYS   A 50  ? 0.2203 0.2654 0.1854 -0.0590 0.0181  -0.0121 56  CYS   A SG  
393  N N   . ASP   A 51  ? 0.2517 0.3428 0.2057 -0.0801 0.0102  0.0025  57  ASP   A N   
394  C CA  . ASP   A 51  ? 0.2786 0.3777 0.2373 -0.0758 0.0040  0.0135  57  ASP   A CA  
395  C C   . ASP   A 51  ? 0.2739 0.3640 0.2329 -0.0717 0.0054  0.0104  57  ASP   A C   
396  O O   . ASP   A 51  ? 0.2913 0.3910 0.2514 -0.0727 0.0022  0.0166  57  ASP   A O   
397  C CB  . ASP   A 51  ? 0.3418 0.4643 0.2973 -0.0862 0.0004  0.0217  57  ASP   A CB  
398  C CG  . ASP   A 51  ? 0.4496 0.5815 0.3949 -0.0993 0.0041  0.0150  57  ASP   A CG  
399  O OD1 . ASP   A 51  ? 0.4643 0.5831 0.4055 -0.1005 0.0106  0.0030  57  ASP   A OD1 
400  O OD2 . ASP   A 51  ? 0.5170 0.6702 0.4589 -0.1091 0.0008  0.0218  57  ASP   A OD2 
401  N N   . CYS   A 52  ? 0.2323 0.3044 0.1916 -0.0665 0.0097  0.0018  58  CYS   A N   
402  C CA  . CYS   A 52  ? 0.2111 0.2738 0.1714 -0.0617 0.0106  -0.0001 58  CYS   A CA  
403  C C   . CYS   A 52  ? 0.2162 0.2805 0.1829 -0.0536 0.0052  0.0090  58  CYS   A C   
404  O O   . CYS   A 52  ? 0.2095 0.2729 0.1823 -0.0473 0.0020  0.0144  58  CYS   A O   
405  C CB  . CYS   A 52  ? 0.2312 0.2754 0.1936 -0.0556 0.0147  -0.0072 58  CYS   A CB  
406  S SG  . CYS   A 52  ? 0.2461 0.2842 0.2044 -0.0640 0.0238  -0.0194 58  CYS   A SG  
407  N N   . GLN   A 53  ? 0.1936 0.2589 0.1594 -0.0538 0.0050  0.0096  59  GLN   A N   
408  C CA  . GLN   A 53  ? 0.1844 0.2492 0.1566 -0.0463 0.0016  0.0162  59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.1699 0.2218 0.1410 -0.0420 0.0038  0.0113  59  GLN   A C   
410  O O   . GLN   A 53  ? 0.1694 0.2219 0.1442 -0.0379 0.0021  0.0151  59  GLN   A O   
411  C CB  . GLN   A 53  ? 0.2078 0.2905 0.1826 -0.0504 -0.0018 0.0246  59  GLN   A CB  
412  C CG  . GLN   A 53  ? 0.2502 0.3464 0.2298 -0.0522 -0.0055 0.0334  59  GLN   A CG  
413  C CD  . GLN   A 53  ? 0.3003 0.4146 0.2852 -0.0551 -0.0091 0.0437  59  GLN   A CD  
414  O OE1 . GLN   A 53  ? 0.3302 0.4620 0.3111 -0.0650 -0.0107 0.0472  59  GLN   A OE1 
415  N NE2 . GLN   A 53  ? 0.2393 0.3512 0.2341 -0.0470 -0.0104 0.0492  59  GLN   A NE2 
416  N N   . THR   A 54  ? 0.1660 0.2065 0.1330 -0.0431 0.0080  0.0033  60  THR   A N   
417  C CA  . THR   A 54  ? 0.1715 0.1991 0.1385 -0.0384 0.0098  0.0000  60  THR   A CA  
418  C C   . THR   A 54  ? 0.1656 0.1806 0.1347 -0.0339 0.0117  -0.0036 60  THR   A C   
419  O O   . THR   A 54  ? 0.1810 0.1963 0.1496 -0.0372 0.0140  -0.0069 60  THR   A O   
420  C CB  . THR   A 54  ? 0.2149 0.2417 0.1769 -0.0443 0.0136  -0.0047 60  THR   A CB  
421  O OG1 . THR   A 54  ? 0.2891 0.3139 0.2479 -0.0507 0.0185  -0.0113 60  THR   A OG1 
422  C CG2 . THR   A 54  ? 0.2043 0.2450 0.1642 -0.0497 0.0118  -0.0012 60  THR   A CG2 
423  N N   . GLY   A 55  ? 0.1568 0.1625 0.1285 -0.0271 0.0106  -0.0027 61  GLY   A N   
424  C CA  . GLY   A 55  ? 0.1527 0.1484 0.1275 -0.0226 0.0115  -0.0045 61  GLY   A CA  
425  C C   . GLY   A 55  ? 0.1473 0.1355 0.1234 -0.0170 0.0099  -0.0027 61  GLY   A C   
426  O O   . GLY   A 55  ? 0.1575 0.1462 0.1313 -0.0173 0.0096  -0.0017 61  GLY   A O   
427  N N   . VAL   A 56  ? 0.1457 0.1279 0.1253 -0.0124 0.0090  -0.0021 62  VAL   A N   
428  C CA  . VAL   A 56  ? 0.1392 0.1158 0.1194 -0.0083 0.0072  0.0000  62  VAL   A CA  
429  C C   . VAL   A 56  ? 0.1374 0.1144 0.1202 -0.0044 0.0041  0.0019  62  VAL   A C   
430  O O   . VAL   A 56  ? 0.1479 0.1251 0.1336 -0.0039 0.0042  0.0012  62  VAL   A O   
431  C CB  . VAL   A 56  ? 0.1579 0.1268 0.1409 -0.0079 0.0100  -0.0010 62  VAL   A CB  
432  C CG1 . VAL   A 56  ? 0.1954 0.1604 0.1796 -0.0043 0.0075  0.0027  62  VAL   A CG1 
433  C CG2 . VAL   A 56  ? 0.1671 0.1344 0.1479 -0.0123 0.0141  -0.0036 62  VAL   A CG2 
434  N N   . TYR   A 57  ? 0.1322 0.1095 0.1139 -0.0023 0.0019  0.0037  63  TYR   A N   
435  C CA  . TYR   A 57  ? 0.1342 0.1114 0.1180 0.0004  -0.0003 0.0046  63  TYR   A CA  
436  C C   . TYR   A 57  ? 0.1337 0.1081 0.1161 0.0015  -0.0018 0.0057  63  TYR   A C   
437  O O   . TYR   A 57  ? 0.1422 0.1155 0.1216 0.0004  -0.0016 0.0064  63  TYR   A O   
438  C CB  . TYR   A 57  ? 0.1365 0.1182 0.1218 0.0009  -0.0007 0.0051  63  TYR   A CB  
439  C CG  . TYR   A 57  ? 0.1385 0.1204 0.1221 0.0010  -0.0004 0.0050  63  TYR   A CG  
440  C CD1 . TYR   A 57  ? 0.1450 0.1290 0.1268 -0.0007 0.0008  0.0053  63  TYR   A CD1 
441  C CD2 . TYR   A 57  ? 0.1424 0.1232 0.1264 0.0019  -0.0006 0.0041  63  TYR   A CD2 
442  C CE1 . TYR   A 57  ? 0.1578 0.1423 0.1386 -0.0008 0.0017  0.0048  63  TYR   A CE1 
443  C CE2 . TYR   A 57  ? 0.1581 0.1394 0.1409 0.0011  0.0009  0.0029  63  TYR   A CE2 
444  C CZ  . TYR   A 57  ? 0.1698 0.1528 0.1513 0.0000  0.0020  0.0034  63  TYR   A CZ  
445  O OH  . TYR   A 57  ? 0.1943 0.1781 0.1747 -0.0011 0.0039  0.0020  63  TYR   A OH  
446  N N   . TYR   A 58  ? 0.1371 0.1116 0.1215 0.0029  -0.0036 0.0062  64  TYR   A N   
447  C CA  . TYR   A 58  ? 0.1401 0.1146 0.1228 0.0026  -0.0057 0.0079  64  TYR   A CA  
448  C C   . TYR   A 58  ? 0.1454 0.1223 0.1253 0.0014  -0.0058 0.0059  64  TYR   A C   
449  O O   . TYR   A 58  ? 0.1413 0.1191 0.1236 0.0020  -0.0052 0.0041  64  TYR   A O   
450  C CB  . TYR   A 58  ? 0.1473 0.1222 0.1342 0.0039  -0.0076 0.0098  64  TYR   A CB  
451  C CG  . TYR   A 58  ? 0.1455 0.1229 0.1304 0.0026  -0.0104 0.0129  64  TYR   A CG  
452  C CD1 . TYR   A 58  ? 0.1591 0.1360 0.1426 0.0017  -0.0110 0.0166  64  TYR   A CD1 
453  C CD2 . TYR   A 58  ? 0.1567 0.1380 0.1404 0.0012  -0.0123 0.0122  64  TYR   A CD2 
454  C CE1 . TYR   A 58  ? 0.1700 0.1514 0.1509 -0.0006 -0.0142 0.0205  64  TYR   A CE1 
455  C CE2 . TYR   A 58  ? 0.1709 0.1569 0.1514 -0.0017 -0.0151 0.0150  64  TYR   A CE2 
456  C CZ  . TYR   A 58  ? 0.1753 0.1620 0.1545 -0.0026 -0.0164 0.0197  64  TYR   A CZ  
457  O OH  . TYR   A 58  ? 0.2182 0.2116 0.1938 -0.0065 -0.0197 0.0237  64  TYR   A OH  
458  N N   . CYS   A 59  ? 0.1412 0.1188 0.1165 -0.0008 -0.0060 0.0063  65  CYS   A N   
459  C CA  . CYS   A 59  ? 0.1520 0.1316 0.1241 -0.0032 -0.0048 0.0033  65  CYS   A CA  
460  C C   . CYS   A 59  ? 0.1540 0.1368 0.1220 -0.0065 -0.0072 0.0043  65  CYS   A C   
461  O O   . CYS   A 59  ? 0.1566 0.1410 0.1204 -0.0087 -0.0087 0.0072  65  CYS   A O   
462  C CB  . CYS   A 59  ? 0.1431 0.1224 0.1125 -0.0043 -0.0027 0.0024  65  CYS   A CB  
463  S SG  . CYS   A 59  ? 0.1663 0.1477 0.1328 -0.0079 0.0005  -0.0023 65  CYS   A SG  
464  N N   . SER   A 60  ? 0.1530 0.1377 0.1220 -0.0075 -0.0076 0.0024  66  SER   A N   
465  C CA  . SER   A 60  ? 0.1637 0.1538 0.1284 -0.0118 -0.0104 0.0038  66  SER   A CA  
466  C C   . SER   A 60  ? 0.1684 0.1619 0.1257 -0.0176 -0.0089 0.0011  66  SER   A C   
467  O O   . SER   A 60  ? 0.1928 0.1920 0.1452 -0.0217 -0.0121 0.0047  66  SER   A O   
468  C CB  . SER   A 60  ? 0.1885 0.1806 0.1557 -0.0126 -0.0108 0.0016  66  SER   A CB  
469  O OG  . SER   A 60  ? 0.1997 0.1904 0.1668 -0.0146 -0.0065 -0.0050 66  SER   A OG  
470  N N   . SER   A 61  ? 0.1532 0.1438 0.1106 -0.0180 -0.0040 -0.0045 67  SER   A N   
471  C CA  . SER   A 61  ? 0.1631 0.1565 0.1140 -0.0238 -0.0014 -0.0083 67  SER   A CA  
472  C C   . SER   A 61  ? 0.1734 0.1676 0.1198 -0.0246 -0.0028 -0.0045 67  SER   A C   
473  O O   . SER   A 61  ? 0.1734 0.1707 0.1135 -0.0300 -0.0008 -0.0072 67  SER   A O   
474  C CB  . SER   A 61  ? 0.1650 0.1549 0.1199 -0.0237 0.0053  -0.0154 67  SER   A CB  
475  O OG  . SER   A 61  ? 0.1744 0.1602 0.1352 -0.0183 0.0068  -0.0139 67  SER   A OG  
476  N N   . ARG   A 62  ? 0.1648 0.1564 0.1141 -0.0200 -0.0057 0.0015  68  ARG   A N   
477  C CA  . ARG   A 62  ? 0.1756 0.1674 0.1217 -0.0207 -0.0073 0.0062  68  ARG   A CA  
478  C C   . ARG   A 62  ? 0.1878 0.1806 0.1364 -0.0190 -0.0119 0.0142  68  ARG   A C   
479  O O   . ARG   A 62  ? 0.1916 0.1839 0.1393 -0.0192 -0.0131 0.0193  68  ARG   A O   
480  C CB  . ARG   A 62  ? 0.1788 0.1653 0.1281 -0.0169 -0.0044 0.0049  68  ARG   A CB  
481  C CG  . ARG   A 62  ? 0.1768 0.1633 0.1259 -0.0182 0.0005  -0.0014 68  ARG   A CG  
482  C CD  . ARG   A 62  ? 0.1809 0.1706 0.1225 -0.0238 0.0016  -0.0024 68  ARG   A CD  
483  N NE  . ARG   A 62  ? 0.2048 0.1944 0.1480 -0.0249 0.0072  -0.0087 68  ARG   A NE  
484  C CZ  . ARG   A 62  ? 0.1946 0.1858 0.1376 -0.0285 0.0111  -0.0149 68  ARG   A CZ  
485  N NH1 . ARG   A 62  ? 0.2091 0.2029 0.1490 -0.0319 0.0096  -0.0159 68  ARG   A NH1 
486  N NH2 . ARG   A 62  ? 0.2207 0.2112 0.1675 -0.0291 0.0172  -0.0202 68  ARG   A NH2 
487  N N   . ARG   A 63  ? 0.1975 0.1909 0.1510 -0.0167 -0.0141 0.0158  69  ARG   A N   
488  C CA  . ARG   A 63  ? 0.2034 0.1969 0.1631 -0.0137 -0.0174 0.0234  69  ARG   A CA  
489  C C   . ARG   A 63  ? 0.2236 0.2100 0.1879 -0.0097 -0.0153 0.0252  69  ARG   A C   
490  O O   . ARG   A 63  ? 0.2495 0.2354 0.2170 -0.0091 -0.0166 0.0319  69  ARG   A O   
491  C CB  . ARG   A 63  ? 0.2463 0.2477 0.2035 -0.0179 -0.0217 0.0311  69  ARG   A CB  
492  C CG  . ARG   A 63  ? 0.2567 0.2661 0.2113 -0.0220 -0.0242 0.0304  69  ARG   A CG  
493  C CD  . ARG   A 63  ? 0.2738 0.2926 0.2285 -0.0254 -0.0295 0.0408  69  ARG   A CD  
494  N NE  . ARG   A 63  ? 0.2841 0.3132 0.2337 -0.0318 -0.0320 0.0397  69  ARG   A NE  
495  C CZ  . ARG   A 63  ? 0.2233 0.2611 0.1623 -0.0406 -0.0327 0.0379  69  ARG   A CZ  
496  N NH1 . ARG   A 63  ? 0.2526 0.2902 0.1853 -0.0437 -0.0315 0.0384  69  ARG   A NH1 
497  N NH2 . ARG   A 63  ? 0.2515 0.2988 0.1858 -0.0473 -0.0343 0.0356  69  ARG   A NH2 
498  N N   . LYS   A 64  ? 0.1882 0.1698 0.1530 -0.0076 -0.0118 0.0197  70  LYS   A N   
499  C CA  . LYS   A 64  ? 0.1971 0.1732 0.1646 -0.0055 -0.0094 0.0200  70  LYS   A CA  
500  C C   . LYS   A 64  ? 0.1802 0.1533 0.1517 -0.0028 -0.0070 0.0159  70  LYS   A C   
501  O O   . LYS   A 64  ? 0.1756 0.1504 0.1467 -0.0025 -0.0066 0.0121  70  LYS   A O   
502  C CB  . LYS   A 64  ? 0.2325 0.2086 0.1937 -0.0082 -0.0075 0.0179  70  LYS   A CB  
503  C CG  . LYS   A 64  ? 0.3424 0.3204 0.3000 -0.0112 -0.0092 0.0232  70  LYS   A CG  
504  C CD  . LYS   A 64  ? 0.4510 0.4284 0.4032 -0.0138 -0.0069 0.0211  70  LYS   A CD  
505  C CE  . LYS   A 64  ? 0.5197 0.4997 0.4678 -0.0174 -0.0087 0.0269  70  LYS   A CE  
506  N NZ  . LYS   A 64  ? 0.5642 0.5519 0.5077 -0.0213 -0.0120 0.0289  70  LYS   A NZ  
507  N N   . HIS   A 65  ? 0.1787 0.1475 0.1542 -0.0014 -0.0049 0.0164  71  HIS   A N   
508  C CA  . HIS   A 65  ? 0.1660 0.1332 0.1438 -0.0006 -0.0022 0.0125  71  HIS   A CA  
509  C C   . HIS   A 65  ? 0.1795 0.1465 0.1535 -0.0027 0.0001  0.0103  71  HIS   A C   
510  O O   . HIS   A 65  ? 0.2299 0.1944 0.2028 -0.0041 0.0013  0.0119  71  HIS   A O   
511  C CB  . HIS   A 65  ? 0.1613 0.1245 0.1462 0.0007  -0.0002 0.0134  71  HIS   A CB  
512  C CG  . HIS   A 65  ? 0.1682 0.1324 0.1585 0.0031  -0.0023 0.0158  71  HIS   A CG  
513  N ND1 . HIS   A 65  ? 0.2089 0.1740 0.2023 0.0042  -0.0019 0.0132  71  HIS   A ND1 
514  C CD2 . HIS   A 65  ? 0.1792 0.1448 0.1725 0.0040  -0.0051 0.0214  71  HIS   A CD2 
515  C CE1 . HIS   A 65  ? 0.1843 0.1506 0.1830 0.0061  -0.0041 0.0168  71  HIS   A CE1 
516  N NE2 . HIS   A 65  ? 0.2147 0.1819 0.2136 0.0060  -0.0062 0.0220  71  HIS   A NE2 
517  N N   . TYR   A 66  ? 0.1554 0.1257 0.1285 -0.0032 0.0010  0.0074  72  TYR   A N   
518  C CA  . TYR   A 66  ? 0.1602 0.1326 0.1306 -0.0055 0.0028  0.0059  72  TYR   A CA  
519  C C   . TYR   A 66  ? 0.1579 0.1325 0.1298 -0.0070 0.0046  0.0040  72  TYR   A C   
520  O O   . TYR   A 66  ? 0.1521 0.1295 0.1267 -0.0060 0.0038  0.0037  72  TYR   A O   
521  C CB  . TYR   A 66  ? 0.1693 0.1460 0.1385 -0.0052 0.0022  0.0052  72  TYR   A CB  
522  C CG  . TYR   A 66  ? 0.1749 0.1510 0.1407 -0.0058 0.0013  0.0057  72  TYR   A CG  
523  C CD1 . TYR   A 66  ? 0.1904 0.1657 0.1521 -0.0080 0.0020  0.0064  72  TYR   A CD1 
524  C CD2 . TYR   A 66  ? 0.1768 0.1538 0.1431 -0.0050 0.0001  0.0052  72  TYR   A CD2 
525  C CE1 . TYR   A 66  ? 0.2015 0.1776 0.1590 -0.0097 0.0013  0.0068  72  TYR   A CE1 
526  C CE2 . TYR   A 66  ? 0.1981 0.1761 0.1600 -0.0073 -0.0003 0.0048  72  TYR   A CE2 
527  C CZ  . TYR   A 66  ? 0.2108 0.1887 0.1681 -0.0097 0.0002  0.0059  72  TYR   A CZ  
528  O OH  . TYR   A 66  ? 0.2333 0.2135 0.1854 -0.0131 -0.0001 0.0054  72  TYR   A OH  
529  N N   . PRO   A 67  ? 0.1599 0.1346 0.1299 -0.0103 0.0071  0.0027  73  PRO   A N   
530  C CA  . PRO   A 67  ? 0.1610 0.1407 0.1310 -0.0137 0.0087  0.0008  73  PRO   A CA  
531  C C   . PRO   A 67  ? 0.1754 0.1640 0.1457 -0.0140 0.0071  0.0024  73  PRO   A C   
532  O O   . PRO   A 67  ? 0.2193 0.2091 0.1886 -0.0135 0.0067  0.0034  73  PRO   A O   
533  C CB  . PRO   A 67  ? 0.1927 0.1698 0.1603 -0.0180 0.0124  -0.0016 73  PRO   A CB  
534  C CG  . PRO   A 67  ? 0.2079 0.1807 0.1737 -0.0164 0.0118  0.0004  73  PRO   A CG  
535  C CD  . PRO   A 67  ? 0.1719 0.1426 0.1392 -0.0118 0.0085  0.0032  73  PRO   A CD  
536  N N   . VAL   A 68  ? 0.1432 0.1380 0.1156 -0.0151 0.0065  0.0031  74  VAL   A N   
537  C CA  . VAL   A 68  ? 0.1683 0.1724 0.1439 -0.0149 0.0049  0.0065  74  VAL   A CA  
538  C C   . VAL   A 68  ? 0.1659 0.1799 0.1414 -0.0199 0.0049  0.0076  74  VAL   A C   
539  O O   . VAL   A 68  ? 0.1580 0.1715 0.1318 -0.0226 0.0059  0.0054  74  VAL   A O   
540  C CB  . VAL   A 68  ? 0.2103 0.2137 0.1912 -0.0100 0.0031  0.0087  74  VAL   A CB  
541  C CG1 . VAL   A 68  ? 0.2389 0.2362 0.2194 -0.0069 0.0034  0.0077  74  VAL   A CG1 
542  C CG2 . VAL   A 68  ? 0.2147 0.2153 0.1964 -0.0092 0.0026  0.0079  74  VAL   A CG2 
543  N N   . SER   A 69  ? 0.1558 0.1803 0.1342 -0.0213 0.0037  0.0118  75  SER   A N   
544  C CA  . SER   A 69  ? 0.1509 0.1886 0.1313 -0.0256 0.0022  0.0158  75  SER   A CA  
545  C C   . SER   A 69  ? 0.1377 0.1785 0.1268 -0.0206 0.0000  0.0216  75  SER   A C   
546  O O   . SER   A 69  ? 0.1541 0.1917 0.1489 -0.0154 0.0002  0.0232  75  SER   A O   
547  C CB  . SER   A 69  ? 0.1980 0.2466 0.1786 -0.0297 0.0019  0.0187  75  SER   A CB  
548  O OG  . SER   A 69  ? 0.2926 0.3381 0.2652 -0.0351 0.0046  0.0130  75  SER   A OG  
549  N N   . PHE   A 70  ? 0.1425 0.1895 0.1332 -0.0225 -0.0014 0.0244  76  PHE   A N   
550  C CA  . PHE   A 70  ? 0.1479 0.1967 0.1478 -0.0177 -0.0029 0.0300  76  PHE   A CA  
551  C C   . PHE   A 70  ? 0.1570 0.2214 0.1611 -0.0218 -0.0053 0.0378  76  PHE   A C   
552  O O   . PHE   A 70  ? 0.1630 0.2360 0.1604 -0.0294 -0.0058 0.0372  76  PHE   A O   
553  C CB  . PHE   A 70  ? 0.1556 0.1928 0.1544 -0.0140 -0.0023 0.0258  76  PHE   A CB  
554  C CG  . PHE   A 70  ? 0.1431 0.1787 0.1348 -0.0184 -0.0016 0.0213  76  PHE   A CG  
555  C CD1 . PHE   A 70  ? 0.1511 0.1780 0.1360 -0.0197 0.0007  0.0144  76  PHE   A CD1 
556  C CD2 . PHE   A 70  ? 0.1465 0.1888 0.1394 -0.0210 -0.0028 0.0241  76  PHE   A CD2 
557  C CE1 . PHE   A 70  ? 0.1543 0.1792 0.1351 -0.0235 0.0026  0.0099  76  PHE   A CE1 
558  C CE2 . PHE   A 70  ? 0.1586 0.1993 0.1455 -0.0255 -0.0011 0.0189  76  PHE   A CE2 
559  C CZ  . PHE   A 70  ? 0.1539 0.1857 0.1354 -0.0266 0.0019  0.0115  76  PHE   A CZ  
560  N N   . SER   A 71  ? 0.1526 0.2218 0.1687 -0.0175 -0.0065 0.0457  77  SER   A N   
561  C CA  . SER   A 71  ? 0.1498 0.2351 0.1723 -0.0208 -0.0094 0.0557  77  SER   A CA  
562  C C   . SER   A 71  ? 0.1584 0.2450 0.1772 -0.0238 -0.0105 0.0557  77  SER   A C   
563  O O   . SER   A 71  ? 0.1555 0.2292 0.1699 -0.0213 -0.0088 0.0486  77  SER   A O   
564  C CB  . SER   A 71  ? 0.1671 0.2561 0.2065 -0.0145 -0.0094 0.0650  77  SER   A CB  
565  O OG  . SER   A 71  ? 0.1903 0.2664 0.2353 -0.0079 -0.0072 0.0627  77  SER   A OG  
566  N N   . LYS   A 72  ? 0.1539 0.2567 0.1749 -0.0294 -0.0133 0.0640  78  LYS   A N   
567  C CA  . LYS   A 72  ? 0.1518 0.2576 0.1699 -0.0328 -0.0143 0.0649  78  LYS   A CA  
568  C C   . LYS   A 72  ? 0.1656 0.2647 0.1953 -0.0250 -0.0143 0.0697  78  LYS   A C   
569  O O   . LYS   A 72  ? 0.1766 0.2760 0.2195 -0.0190 -0.0141 0.0764  78  LYS   A O   
570  C CB  . LYS   A 72  ? 0.1724 0.3002 0.1892 -0.0423 -0.0177 0.0736  78  LYS   A CB  
571  C CG  . LYS   A 72  ? 0.2027 0.3370 0.2064 -0.0520 -0.0168 0.0670  78  LYS   A CG  
572  C CD  . LYS   A 72  ? 0.2864 0.4441 0.2866 -0.0637 -0.0201 0.0746  78  LYS   A CD  
573  C CE  . LYS   A 72  ? 0.3581 0.5218 0.3447 -0.0746 -0.0180 0.0663  78  LYS   A CE  
574  N NZ  . LYS   A 72  ? 0.4057 0.5891 0.3843 -0.0882 -0.0196 0.0690  78  LYS   A NZ  
575  N N   . PRO   A 73  ? 0.1602 0.2533 0.1866 -0.0251 -0.0138 0.0663  79  PRO   A N   
576  C CA  . PRO   A 73  ? 0.1636 0.2498 0.2008 -0.0183 -0.0132 0.0701  79  PRO   A CA  
577  C C   . PRO   A 73  ? 0.1733 0.2724 0.2254 -0.0171 -0.0153 0.0846  79  PRO   A C   
578  O O   . PRO   A 73  ? 0.1989 0.3149 0.2503 -0.0239 -0.0186 0.0928  79  PRO   A O   
579  C CB  . PRO   A 73  ? 0.1854 0.2684 0.2150 -0.0215 -0.0131 0.0652  79  PRO   A CB  
580  C CG  . PRO   A 73  ? 0.2351 0.3174 0.2508 -0.0276 -0.0120 0.0559  79  PRO   A CG  
581  C CD  . PRO   A 73  ? 0.1836 0.2756 0.1969 -0.0317 -0.0129 0.0581  79  PRO   A CD  
582  N N   . SER   A 74  ? 0.1671 0.2589 0.2331 -0.0092 -0.0131 0.0878  80  SER   A N   
583  C CA  . SER   A 74  ? 0.1766 0.2795 0.2608 -0.0068 -0.0140 0.1023  80  SER   A CA  
584  C C   . SER   A 74  ? 0.1562 0.2466 0.2554 0.0014  -0.0098 0.1035  80  SER   A C   
585  O O   . SER   A 74  ? 0.1567 0.2308 0.2514 0.0048  -0.0064 0.0926  80  SER   A O   
586  C CB  . SER   A 74  ? 0.2385 0.3502 0.3285 -0.0066 -0.0144 0.1070  80  SER   A CB  
587  O OG  . SER   A 74  ? 0.3355 0.4492 0.4101 -0.0119 -0.0154 0.0991  80  SER   A OG  
588  N N   . LEU   A 75  ? 0.1678 0.2671 0.2868 0.0044  -0.0097 0.1175  81  LEU   A N   
589  C CA  . LEU   A 75  ? 0.1827 0.2717 0.3197 0.0117  -0.0046 0.1203  81  LEU   A CA  
590  C C   . LEU   A 75  ? 0.1883 0.2727 0.3366 0.0169  0.0000  0.1190  81  LEU   A C   
591  O O   . LEU   A 75  ? 0.2037 0.3017 0.3633 0.0170  -0.0015 0.1298  81  LEU   A O   
592  C CB  . LEU   A 75  ? 0.1905 0.2930 0.3444 0.0115  -0.0067 0.1378  81  LEU   A CB  
593  C CG  . LEU   A 75  ? 0.2174 0.3092 0.3909 0.0183  -0.0010 0.1415  81  LEU   A CG  
594  C CD1 . LEU   A 75  ? 0.2322 0.3082 0.3953 0.0184  0.0013  0.1295  81  LEU   A CD1 
595  C CD2 . LEU   A 75  ? 0.2330 0.3402 0.4247 0.0179  -0.0037 0.1614  81  LEU   A CD2 
596  N N   . ILE   A 76  ? 0.1792 0.2463 0.3245 0.0205  0.0053  0.1061  82  ILE   A N   
597  C CA  . ILE   A 76  ? 0.1886 0.2496 0.3413 0.0243  0.0105  0.1015  82  ILE   A CA  
598  C C   . ILE   A 76  ? 0.1988 0.2453 0.3665 0.0299  0.0189  0.0975  82  ILE   A C   
599  O O   . ILE   A 76  ? 0.1859 0.2210 0.3474 0.0297  0.0208  0.0897  82  ILE   A O   
600  C CB  . ILE   A 76  ? 0.2115 0.2658 0.3427 0.0214  0.0095  0.0878  82  ILE   A CB  
601  C CG1 . ILE   A 76  ? 0.2423 0.3099 0.3591 0.0151  0.0025  0.0905  82  ILE   A CG1 
602  C CG2 . ILE   A 76  ? 0.2253 0.2721 0.3617 0.0245  0.0152  0.0813  82  ILE   A CG2 
603  C CD1 . ILE   A 76  ? 0.2514 0.3139 0.3499 0.0121  0.0016  0.0793  82  ILE   A CD1 
604  N N   . PHE   A 77  ? 0.1974 0.2438 0.3850 0.0343  0.0247  0.1018  83  PHE   A N   
605  C CA  . PHE   A 77  ? 0.2090 0.2410 0.4112 0.0386  0.0345  0.0960  83  PHE   A CA  
606  C C   . PHE   A 77  ? 0.2417 0.2610 0.4279 0.0368  0.0379  0.0787  83  PHE   A C   
607  O O   . PHE   A 77  ? 0.2726 0.2947 0.4514 0.0356  0.0370  0.0749  83  PHE   A O   
608  C CB  . PHE   A 77  ? 0.2123 0.2488 0.4426 0.0437  0.0406  0.1058  83  PHE   A CB  
609  C CG  . PHE   A 77  ? 0.2387 0.2607 0.4879 0.0477  0.0518  0.1014  83  PHE   A CG  
610  C CD1 . PHE   A 77  ? 0.2507 0.2696 0.5118 0.0494  0.0535  0.1078  83  PHE   A CD1 
611  C CD2 . PHE   A 77  ? 0.2813 0.2922 0.5346 0.0488  0.0611  0.0895  83  PHE   A CD2 
612  C CE1 . PHE   A 77  ? 0.2798 0.2845 0.5586 0.0525  0.0649  0.1029  83  PHE   A CE1 
613  C CE2 . PHE   A 77  ? 0.2861 0.2836 0.5570 0.0513  0.0726  0.0842  83  PHE   A CE2 
614  C CZ  . PHE   A 77  ? 0.2868 0.2808 0.5707 0.0532  0.0748  0.0907  83  PHE   A CZ  
615  N N   . VAL   A 78  ? 0.2189 0.2252 0.3991 0.0359  0.0416  0.0684  84  VAL   A N   
616  C CA  . VAL   A 78  ? 0.2142 0.2096 0.3786 0.0331  0.0444  0.0526  84  VAL   A CA  
617  C C   . VAL   A 78  ? 0.1994 0.1828 0.3789 0.0347  0.0560  0.0455  84  VAL   A C   
618  O O   . VAL   A 78  ? 0.2148 0.1936 0.4069 0.0363  0.0600  0.0482  84  VAL   A O   
619  C CB  . VAL   A 78  ? 0.2048 0.1968 0.3481 0.0293  0.0387  0.0462  84  VAL   A CB  
620  C CG1 . VAL   A 78  ? 0.2192 0.2018 0.3473 0.0260  0.0410  0.0316  84  VAL   A CG1 
621  C CG2 . VAL   A 78  ? 0.2071 0.2103 0.3373 0.0272  0.0290  0.0522  84  VAL   A CG2 
622  N N   . GLU   A 79  ? 0.2136 0.1919 0.3892 0.0330  0.0612  0.0353  85  GLU   A N   
623  C CA  . GLU   A 79  ? 0.2265 0.1938 0.4151 0.0329  0.0734  0.0264  85  GLU   A CA  
624  C C   . GLU   A 79  ? 0.2466 0.2041 0.4248 0.0288  0.0756  0.0157  85  GLU   A C   
625  O O   . GLU   A 79  ? 0.2565 0.2154 0.4148 0.0258  0.0676  0.0133  85  GLU   A O   
626  C CB  . GLU   A 79  ? 0.2561 0.2219 0.4397 0.0306  0.0778  0.0173  85  GLU   A CB  
627  C CG  . GLU   A 79  ? 0.3163 0.2911 0.5148 0.0348  0.0783  0.0268  85  GLU   A CG  
628  C CD  . GLU   A 79  ? 0.4129 0.3885 0.6430 0.0407  0.0856  0.0372  85  GLU   A CD  
629  O OE1 . GLU   A 79  ? 0.4310 0.3960 0.6758 0.0411  0.0966  0.0313  85  GLU   A OE1 
630  O OE2 . GLU   A 79  ? 0.4784 0.4660 0.7194 0.0445  0.0804  0.0518  85  GLU   A OE2 
631  N N   . ALA   A 80  ? 0.2515 0.1992 0.4439 0.0282  0.0872  0.0089  86  ALA   A N   
632  C CA  . ALA   A 80  ? 0.2675 0.2062 0.4524 0.0234  0.0910  -0.0018 86  ALA   A CA  
633  C C   . ALA   A 80  ? 0.2937 0.2316 0.4533 0.0165  0.0878  -0.0142 86  ALA   A C   
634  O O   . ALA   A 80  ? 0.3253 0.2658 0.4765 0.0146  0.0875  -0.0184 86  ALA   A O   
635  C CB  . ALA   A 80  ? 0.2819 0.2100 0.4880 0.0231  0.1060  -0.0083 86  ALA   A CB  
636  N N   . SER   A 81  ? 0.2712 0.2064 0.4182 0.0125  0.0849  -0.0193 87  SER   A N   
637  C CA  A SER   A 81  ? 0.2711 0.2064 0.3955 0.0053  0.0820  -0.0303 87  SER   A CA  
638  C CA  B SER   A 81  ? 0.2923 0.2276 0.4166 0.0053  0.0819  -0.0302 87  SER   A CA  
639  C C   . SER   A 81  ? 0.3001 0.2284 0.4246 -0.0001 0.0881  -0.0394 87  SER   A C   
640  O O   . SER   A 81  ? 0.3111 0.2337 0.4534 0.0026  0.0947  -0.0370 87  SER   A O   
641  C CB  A SER   A 81  ? 0.2490 0.1919 0.3553 0.0059  0.0687  -0.0245 87  SER   A CB  
642  C CB  B SER   A 81  ? 0.3294 0.2724 0.4359 0.0061  0.0685  -0.0242 87  SER   A CB  
643  O OG  A SER   A 81  ? 0.1879 0.1308 0.2940 0.0071  0.0644  -0.0202 87  SER   A OG  
644  O OG  B SER   A 81  ? 0.3771 0.3221 0.4636 0.0001  0.0649  -0.0320 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.3176 0.2470 0.4227 -0.0079 0.0858  -0.0491 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.3172 0.2414 0.4225 -0.0135 0.0913  -0.0572 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.2892 0.2146 0.3948 -0.0097 0.0838  -0.0488 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.2945 0.2151 0.4045 -0.0127 0.0886  -0.0532 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.3711 0.2979 0.4572 -0.0240 0.0913  -0.0692 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.4074 0.3433 0.4741 -0.0243 0.0777  -0.0643 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.5235 0.4647 0.5721 -0.0345 0.0758  -0.0732 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.5683 0.5091 0.6144 -0.0396 0.0771  -0.0779 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.5349 0.4817 0.5718 -0.0377 0.0726  -0.0746 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.2783 0.2100 0.3810 -0.0034 0.0734  -0.0370 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.2604 0.1941 0.3619 -0.0009 0.0668  -0.0302 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.2375 0.1703 0.3574 0.0060  0.0678  -0.0187 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.2379 0.1702 0.3610 0.0068  0.0660  -0.0147 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.2828 0.2247 0.3664 -0.0008 0.0548  -0.0266 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3160 0.2600 0.3827 -0.0079 0.0527  -0.0357 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3670 0.3102 0.4294 -0.0126 0.0531  -0.0408 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3623 0.3096 0.4187 -0.0106 0.0512  -0.0391 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.4051 0.3526 0.4527 -0.0197 0.0504  -0.0476 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3895 0.3407 0.4310 -0.0175 0.0486  -0.0456 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.4319 0.3836 0.4695 -0.0223 0.0484  -0.0498 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.5012 0.4589 0.5248 -0.0299 0.0454  -0.0551 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.2363 0.1700 0.3693 0.0106  0.0708  -0.0127 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.2307 0.1660 0.3824 0.0167  0.0713  0.0000  90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.2336 0.1654 0.4055 0.0198  0.0810  0.0013  90  TYR   A C   
669  O O   . TYR   A 84  ? 0.2353 0.1681 0.4025 0.0186  0.0826  -0.0039 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2187 0.1650 0.3637 0.0202  0.0603  0.0115  90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.1954 0.1461 0.3224 0.0180  0.0507  0.0117  90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.1880 0.1388 0.3183 0.0182  0.0490  0.0162  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.1964 0.1512 0.3045 0.0156  0.0442  0.0075  90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.1767 0.1319 0.2921 0.0163  0.0410  0.0164  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2015 0.1599 0.2958 0.0140  0.0366  0.0076  90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.1794 0.1379 0.2774 0.0143  0.0353  0.0117  90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.1808 0.1430 0.2666 0.0126  0.0287  0.0114  90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.2517 0.1808 0.4469 0.0242  0.0867  0.0098  91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.2544 0.1824 0.4723 0.0285  0.0950  0.0144  91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.2575 0.1980 0.4737 0.0325  0.0861  0.0262  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.2487 0.1978 0.4483 0.0319  0.0744  0.0314  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.2668 0.1902 0.5100 0.0324  0.1015  0.0232  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.2758 0.2044 0.5082 0.0320  0.0914  0.0303  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.2443 0.1732 0.4471 0.0259  0.0848  0.0180  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.2660 0.2085 0.4999 0.0364  0.0915  0.0310  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.2545 0.2104 0.4891 0.0398  0.0834  0.0432  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.2444 0.2091 0.4875 0.0429  0.0765  0.0599  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.2738 0.2337 0.5358 0.0453  0.0822  0.0652  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.2562 0.2121 0.5132 0.0436  0.0922  0.0460  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.2363 0.2129 0.4628 0.0415  0.0644  0.0664  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.2173 0.2033 0.4475 0.0424  0.0574  0.0805  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2113 0.2121 0.4254 0.0402  0.0460  0.0867  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.2347 0.2360 0.4334 0.0381  0.0437  0.0787  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.2421 0.2206 0.4602 0.0392  0.0562  0.0737  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.2783 0.2578 0.4664 0.0344  0.0483  0.0635  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.2728 0.2429 0.4482 0.0310  0.0493  0.0520  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.2426 0.2174 0.3957 0.0275  0.0403  0.0493  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.2524 0.2295 0.3872 0.0251  0.0354  0.0430  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.2458 0.2230 0.3799 0.0256  0.0373  0.0397  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2216 0.2014 0.3400 0.0223  0.0289  0.0406  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2008 0.2136 0.4176 0.0397  0.0393  0.1003  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2108 0.2374 0.4103 0.0358  0.0292  0.1045  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.1977 0.2197 0.3731 0.0313  0.0246  0.0942  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2151 0.2324 0.3909 0.0307  0.0252  0.0938  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2108 0.2540 0.4229 0.0357  0.0241  0.1235  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.2078 0.2608 0.4411 0.0394  0.0260  0.1354  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.2150 0.2789 0.4404 0.0373  0.0216  0.1364  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.2172 0.2671 0.4796 0.0452  0.0334  0.1445  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.2233 0.2966 0.4685 0.0407  0.0235  0.1470  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.2188 0.2776 0.5029 0.0491  0.0359  0.1554  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.2244 0.2955 0.4994 0.0468  0.0305  0.1569  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.2492 0.3306 0.5444 0.0502  0.0323  0.1674  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.1728 0.1961 0.3283 0.0281  0.0205  0.0860  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1694 0.1898 0.3032 0.0239  0.0161  0.0770  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1607 0.1958 0.2850 0.0197  0.0086  0.0841  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1665 0.2113 0.2910 0.0187  0.0063  0.0887  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1720 0.1825 0.2921 0.0232  0.0179  0.0628  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.1868 0.1946 0.2873 0.0196  0.0136  0.0547  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.1680 0.1651 0.2582 0.0191  0.0159  0.0419  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.1954 0.1840 0.2920 0.0205  0.0218  0.0366  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.1651 0.1627 0.2392 0.0163  0.0117  0.0367  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1515 0.1893 0.2676 0.0163  0.0051  0.0847  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1409 0.1925 0.2475 0.0108  -0.0010 0.0900  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1472 0.1956 0.2332 0.0069  -0.0031 0.0784  96  SER   A C   
725  O O   . SER   A 90  ? 0.1555 0.1913 0.2347 0.0086  -0.0009 0.0674  96  SER   A O   
726  C CB  . SER   A 90  ? 0.1636 0.2215 0.2746 0.0086  -0.0029 0.0985  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2033 0.2497 0.3066 0.0086  -0.0014 0.0888  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1457 0.2066 0.2229 0.0011  -0.0072 0.0813  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1489 0.2085 0.2086 -0.0034 -0.0086 0.0716  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1403 0.1888 0.1950 -0.0003 -0.0063 0.0620  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1567 0.1971 0.2001 -0.0012 -0.0059 0.0522  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1760 0.2303 0.2284 -0.0053 -0.0086 0.0659  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.1809 0.2465 0.2360 -0.0096 -0.0109 0.0746  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.1965 0.2734 0.2413 -0.0176 -0.0132 0.0748  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2087 0.2764 0.2761 -0.0074 -0.0107 0.0836  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2120 0.2981 0.2618 -0.0204 -0.0149 0.0839  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2233 0.3044 0.2874 -0.0141 -0.0137 0.0902  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1308 0.1798 0.1938 0.0030  -0.0049 0.0651  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1353 0.1748 0.1948 0.0057  -0.0024 0.0570  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1373 0.1848 0.1906 0.0022  -0.0042 0.0576  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1404 0.2012 0.1995 -0.0001 -0.0062 0.0667  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1437 0.1777 0.2182 0.0113  0.0019  0.0592  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.1659 0.1901 0.2369 0.0133  0.0052  0.0503  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.1729 0.1862 0.2331 0.0129  0.0058  0.0402  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2038 0.2242 0.2916 0.0178  0.0109  0.0524  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1364 0.1765 0.1789 0.0015  -0.0035 0.0485  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1301 0.1756 0.1658 -0.0020 -0.0044 0.0474  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1362 0.1735 0.1729 0.0017  -0.0017 0.0427  99  MET   A C   
749  O O   . MET   A 93  ? 0.1523 0.1781 0.1858 0.0042  0.0001  0.0360  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1478 0.1907 0.1696 -0.0066 -0.0052 0.0403  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1620 0.2129 0.1816 -0.0112 -0.0070 0.0432  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.1890 0.2354 0.1953 -0.0165 -0.0059 0.0338  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2352 0.2655 0.2424 -0.0098 -0.0044 0.0276  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1289 0.1727 0.1689 0.0011  -0.0015 0.0459  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1427 0.1795 0.1835 0.0039  0.0015  0.0414  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1347 0.1716 0.1641 0.0003  0.0007  0.0368  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1420 0.1884 0.1672 -0.0045 -0.0015 0.0394  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1568 0.1997 0.2135 0.0070  0.0037  0.0484  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.1975 0.2391 0.2693 0.0113  0.0061  0.0534  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2131 0.2587 0.3028 0.0151  0.0099  0.0594  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2354 0.2630 0.3045 0.0136  0.0092  0.0452  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1373 0.1647 0.1621 0.0018  0.0029  0.0302  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1308 0.1571 0.1461 -0.0012 0.0028  0.0263  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1289 0.1498 0.1461 0.0011  0.0058  0.0231  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1371 0.1529 0.1602 0.0043  0.0083  0.0216  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1535 0.1720 0.1574 -0.0031 0.0019  0.0204  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1296 0.1515 0.1412 -0.0014 0.0061  0.0212  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1311 0.1480 0.1418 -0.0005 0.0090  0.0174  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1583 0.1655 0.1579 -0.0015 0.0084  0.0117  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.1898 0.1956 0.1815 -0.0040 0.0067  0.0107  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1362 0.1597 0.1463 -0.0030 0.0094  0.0188  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1528 0.1711 0.1602 -0.0030 0.0125  0.0141  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1279 0.1631 0.1507 -0.0021 0.0095  0.0260  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1646 0.1661 0.1649 0.0001  0.0102  0.0085  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.1837 0.1781 0.1748 -0.0011 0.0091  0.0047  103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.1858 0.1766 0.1784 -0.0007 0.0116  0.0011  103 GLY   A C   
777  O O   . GLY   A 97  ? 0.1865 0.1782 0.1881 0.0012  0.0143  0.0011  103 GLY   A O   
778  N N   . HIS   A 98  ? 0.1934 0.1805 0.1773 -0.0031 0.0109  -0.0018 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2018 0.1868 0.1853 -0.0046 0.0133  -0.0061 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.1964 0.1794 0.1821 -0.0033 0.0121  -0.0063 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.1921 0.1744 0.1748 -0.0024 0.0082  -0.0038 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2119 0.1959 0.1848 -0.0087 0.0122  -0.0079 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2188 0.2025 0.1899 -0.0121 0.0149  -0.0129 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.2113 0.1954 0.1867 -0.0138 0.0210  -0.0178 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2226 0.2062 0.1890 -0.0146 0.0129  -0.0140 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.2234 0.2071 0.1960 -0.0177 0.0230  -0.0226 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.2289 0.2131 0.1952 -0.0186 0.0177  -0.0202 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2054 0.1874 0.1964 -0.0035 0.0159  -0.0096 105 SER   A N   
789  C CA  . SER   A 99  ? 0.1892 0.1692 0.1815 -0.0034 0.0155  -0.0111 105 SER   A CA  
790  C C   . SER   A 99  ? 0.1951 0.1733 0.1899 -0.0064 0.0211  -0.0174 105 SER   A C   
791  O O   . SER   A 99  ? 0.2213 0.1994 0.2219 -0.0067 0.0266  -0.0200 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2066 0.1869 0.2065 0.0006  0.0140  -0.0069 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.2042 0.1856 0.2158 0.0032  0.0179  -0.0054 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.1889 0.1661 0.1810 -0.0087 0.0204  -0.0200 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.1917 0.1672 0.1856 -0.0128 0.0260  -0.0271 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.2025 0.1762 0.2007 -0.0112 0.0251  -0.0265 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.1867 0.1613 0.1839 -0.0079 0.0193  -0.0210 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.2073 0.1860 0.1885 -0.0201 0.0250  -0.0312 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.2310 0.2116 0.2078 -0.0220 0.0262  -0.0315 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.2651 0.2504 0.2288 -0.0297 0.0246  -0.0339 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.3312 0.3190 0.2904 -0.0357 0.0257  -0.0384 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.2460 0.2335 0.2040 -0.0303 0.0221  -0.0308 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.2014 0.1722 0.2053 -0.0136 0.0312  -0.0323 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.2010 0.1697 0.2106 -0.0116 0.0307  -0.0312 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.1995 0.1714 0.2004 -0.0125 0.0233  -0.0285 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.1937 0.1652 0.1984 -0.0084 0.0199  -0.0237 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.2257 0.1907 0.2406 -0.0162 0.0396  -0.0398 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.2482 0.2120 0.2676 -0.0169 0.0460  -0.0431 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.2204 0.1891 0.2280 -0.0179 0.0401  -0.0402 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2016 0.1776 0.1914 -0.0181 0.0206  -0.0307 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.1953 0.1755 0.1787 -0.0191 0.0138  -0.0273 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.1783 0.1595 0.1606 -0.0139 0.0075  -0.0196 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.1838 0.1679 0.1638 -0.0136 0.0025  -0.0161 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.1563 0.1354 0.1413 -0.0102 0.0083  -0.0172 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.1513 0.1307 0.1360 -0.0060 0.0038  -0.0111 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.1552 0.1332 0.1469 -0.0019 0.0031  -0.0085 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1471 0.1256 0.1385 0.0005  0.0000  -0.0047 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1542 0.1330 0.1391 -0.0045 0.0053  -0.0098 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.1599 0.1408 0.1368 -0.0085 0.0047  -0.0109 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.1629 0.1463 0.1343 -0.0107 0.0009  -0.0090 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.1712 0.1518 0.1481 -0.0094 0.0081  -0.0128 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1470 0.1232 0.1451 -0.0016 0.0065  -0.0108 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1497 0.1255 0.1537 0.0016  0.0054  -0.0076 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1485 0.1260 0.1491 0.0015  0.0011  -0.0062 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.1541 0.1332 0.1504 -0.0014 -0.0004 -0.0080 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.1657 0.1390 0.1775 0.0015  0.0099  -0.0100 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.1727 0.1440 0.1948 0.0036  0.0158  -0.0091 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1385 0.1166 0.1410 0.0041  -0.0009 -0.0026 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1451 0.1245 0.1465 0.0045  -0.0040 -0.0011 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1433 0.1231 0.1416 0.0051  -0.0059 0.0011  111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1488 0.1290 0.1485 0.0060  -0.0073 0.0025  111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1413 0.1206 0.1361 0.0045  -0.0053 0.0011  112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1396 0.1184 0.1322 0.0049  -0.0063 0.0031  112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1264 0.1053 0.1214 0.0058  -0.0053 0.0039  112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1320 0.1124 0.1287 0.0058  -0.0040 0.0041  112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1340 0.1118 0.1296 0.0060  -0.0054 0.0046  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1352 0.1136 0.1321 0.0052  -0.0035 0.0041  113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1286 0.1076 0.1224 0.0035  -0.0021 0.0039  113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1295 0.1062 0.1210 0.0034  -0.0019 0.0043  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1407 0.1171 0.1411 0.0056  -0.0027 0.0037  113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1548 0.1326 0.1590 0.0067  -0.0038 0.0036  113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1591 0.1353 0.1599 0.0033  0.0008  0.0017  113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.1864 0.1630 0.1963 0.0077  -0.0029 0.0038  113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1230 0.1060 0.1169 0.0017  -0.0011 0.0040  114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1204 0.1061 0.1116 -0.0014 0.0005  0.0036  114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1242 0.1100 0.1154 -0.0045 0.0031  0.0010  114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1359 0.1242 0.1291 -0.0051 0.0031  0.0008  114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1274 0.1200 0.1194 -0.0025 -0.0002 0.0064  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1295 0.1283 0.1187 -0.0070 0.0009  0.0069  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1463 0.1427 0.1325 -0.0072 0.0016  0.0060  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1611 0.1692 0.1537 -0.0079 -0.0005 0.0118  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1328 0.1159 0.1224 -0.0067 0.0058  -0.0013 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1359 0.1182 0.1264 -0.0104 0.0100  -0.0053 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1517 0.1363 0.1381 -0.0160 0.0132  -0.0079 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1568 0.1408 0.1405 -0.0159 0.0125  -0.0067 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1552 0.1295 0.1515 -0.0072 0.0119  -0.0062 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1558 0.1247 0.1525 -0.0056 0.0124  -0.0049 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.1750 0.1379 0.1798 -0.0021 0.0137  -0.0036 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.1827 0.1470 0.1894 0.0020  0.0089  0.0004  115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.1811 0.1453 0.1944 0.0043  0.0087  0.0012  115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.1926 0.1554 0.2108 0.0028  0.0133  -0.0024 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.1968 0.1631 0.2109 0.0071  0.0041  0.0048  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.1810 0.1684 0.1665 -0.0217 0.0172  -0.0122 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2132 0.2037 0.1941 -0.0290 0.0213  -0.0161 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.2337 0.2174 0.2181 -0.0319 0.0284  -0.0226 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2213 0.1980 0.2128 -0.0273 0.0297  -0.0229 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.1985 0.2020 0.1742 -0.0354 0.0197  -0.0149 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.1973 0.2057 0.1733 -0.0401 0.0220  -0.0180 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.2500 0.2358 0.2304 -0.0401 0.0339  -0.0282 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.2747 0.2537 0.2597 -0.0440 0.0426  -0.0359 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.2937 0.2740 0.2822 -0.0453 0.0452  -0.0390 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.3234 0.2954 0.3199 -0.0449 0.0520  -0.0439 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.3289 0.3113 0.3078 -0.0547 0.0489  -0.0427 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.3844 0.3821 0.3542 -0.0643 0.0476  -0.0442 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.4644 0.4668 0.4277 -0.0760 0.0539  -0.0514 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.4940 0.5042 0.4511 -0.0791 0.0504  -0.0483 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.4768 0.4750 0.4419 -0.0833 0.0638  -0.0614 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.2539 0.2441 0.2381 -0.0464 0.0401  -0.0358 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.2473 0.2403 0.2335 -0.0487 0.0424  -0.0388 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2453 0.2331 0.2390 -0.0392 0.0384  -0.0342 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.2685 0.2573 0.2655 -0.0402 0.0406  -0.0366 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2566 0.2647 0.2338 -0.0563 0.0390  -0.0370 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.2860 0.3021 0.2550 -0.0673 0.0425  -0.0412 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.2640 0.2888 0.2274 -0.0687 0.0370  -0.0354 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3185 0.3361 0.2844 -0.0780 0.0512  -0.0509 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.3116 0.3432 0.2683 -0.0798 0.0418  -0.0412 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3406 0.3681 0.2981 -0.0862 0.0506  -0.0511 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2219 0.2063 0.2174 -0.0310 0.0321  -0.0274 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2057 0.1871 0.2071 -0.0233 0.0281  -0.0231 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.1740 0.1587 0.1719 -0.0189 0.0203  -0.0162 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.1783 0.1652 0.1716 -0.0196 0.0183  -0.0141 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1613 0.1464 0.1625 -0.0144 0.0166  -0.0130 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1514 0.1386 0.1508 -0.0104 0.0107  -0.0076 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1391 0.1352 0.1341 -0.0142 0.0088  -0.0052 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1492 0.1508 0.1437 -0.0180 0.0098  -0.0060 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1501 0.1349 0.1546 -0.0055 0.0082  -0.0058 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.1652 0.1519 0.1684 -0.0027 0.0036  -0.0016 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.1659 0.1441 0.1759 -0.0017 0.0091  -0.0059 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1332 0.1314 0.1263 -0.0128 0.0060  -0.0015 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1396 0.1472 0.1311 -0.0156 0.0039  0.0027  121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1365 0.1445 0.1325 -0.0110 0.0007  0.0076  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1462 0.1613 0.1440 -0.0127 -0.0006 0.0118  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1560 0.1662 0.1444 -0.0173 0.0038  0.0038  121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.1750 0.1958 0.1645 -0.0189 0.0010  0.0103  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.1733 0.1836 0.1572 -0.0232 0.0078  -0.0014 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1349 0.1356 0.1330 -0.0057 -0.0003 0.0073  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1408 0.1411 0.1435 -0.0022 -0.0020 0.0105  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1315 0.1247 0.1344 0.0016  -0.0024 0.0086  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1341 0.1232 0.1343 0.0018  -0.0020 0.0060  122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1370 0.1290 0.1437 0.0040  -0.0027 0.0101  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1275 0.1143 0.1335 0.0059  -0.0027 0.0076  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1269 0.1138 0.1357 0.0068  -0.0014 0.0087  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1370 0.1272 0.1517 0.0073  -0.0004 0.0121  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1380 0.1223 0.1459 0.0067  -0.0032 0.0060  123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1577 0.1438 0.1714 0.0070  -0.0023 0.0080  123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1527 0.1364 0.1589 0.0063  -0.0042 0.0047  123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1556 0.1390 0.1712 0.0073  -0.0023 0.0057  123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1307 0.1146 0.1364 0.0069  -0.0009 0.0062  124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1292 0.1126 0.1381 0.0074  0.0016  0.0058  124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1276 0.1095 0.1439 0.0083  0.0040  0.0055  124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1365 0.1161 0.1517 0.0077  0.0036  0.0029  124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1343 0.1150 0.1373 0.0060  0.0019  0.0022  124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1372 0.1169 0.1437 0.0058  0.0057  0.0002  124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1410 0.1223 0.1380 0.0052  0.0001  0.0030  124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1331 0.1164 0.1578 0.0097  0.0068  0.0082  125 SER   A N   
926  C CA  . SER   A 119 ? 0.1469 0.1280 0.1813 0.0108  0.0103  0.0086  125 SER   A CA  
927  C C   . SER   A 119 ? 0.1506 0.1298 0.1931 0.0117  0.0156  0.0075  125 SER   A C   
928  O O   . SER   A 119 ? 0.1713 0.1460 0.2205 0.0115  0.0203  0.0042  125 SER   A O   
929  C CB  . SER   A 119 ? 0.1561 0.1417 0.1967 0.0120  0.0088  0.0151  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.1778 0.1614 0.2302 0.0135  0.0125  0.0172  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1525 0.1352 0.1961 0.0123  0.0158  0.0100  126 THR   A N   
932  C CA  . THR   A 120 ? 0.1554 0.1370 0.2095 0.0136  0.0216  0.0095  126 THR   A CA  
933  C C   . THR   A 120 ? 0.1754 0.1581 0.2225 0.0121  0.0216  0.0067  126 THR   A C   
934  O O   . THR   A 120 ? 0.1611 0.1458 0.1966 0.0106  0.0167  0.0068  126 THR   A O   
935  C CB  . THR   A 120 ? 0.1612 0.1486 0.2302 0.0168  0.0224  0.0190  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.1662 0.1619 0.2313 0.0164  0.0180  0.0244  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.1647 0.1525 0.2409 0.0180  0.0218  0.0237  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.1873 0.1688 0.2418 0.0124  0.0272  0.0046  127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2078 0.1913 0.2566 0.0110  0.0272  0.0029  127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.2107 0.1915 0.2680 0.0106  0.0350  -0.0016 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.2264 0.2032 0.2953 0.0116  0.0411  -0.0036 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.2230 0.2056 0.2739 0.0087  0.0351  -0.0040 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.2337 0.2144 0.2900 0.0072  0.0426  -0.0095 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.2346 0.2212 0.2927 0.0082  0.0418  -0.0056 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.2387 0.2316 0.3007 0.0109  0.0374  0.0027  128 GLY   A O   
946  N N   . ASN   A 123 ? 0.2152 0.2007 0.2714 0.0053  0.0467  -0.0116 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.2207 0.2117 0.2801 0.0059  0.0474  -0.0089 129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.2226 0.2193 0.2723 0.0059  0.0392  -0.0029 129 ASN   A C   
949  O O   . ASN   A 123 ? 0.2276 0.2313 0.2847 0.0078  0.0385  0.0030  129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.2410 0.2351 0.3232 0.0105  0.0534  -0.0040 129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.2947 0.2819 0.3880 0.0098  0.0637  -0.0115 129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.3248 0.3090 0.4125 0.0053  0.0690  -0.0206 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.2976 0.2826 0.4069 0.0136  0.0671  -0.0081 129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.2002 0.1944 0.2337 0.0032  0.0337  -0.0048 130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.1934 0.1913 0.2176 0.0025  0.0274  -0.0007 130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.1645 0.1662 0.1921 0.0049  0.0229  0.0059  130 GLY   A C   
957  O O   . GLY   A 124 ? 0.1884 0.1937 0.2094 0.0035  0.0187  0.0087  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1734 0.1741 0.2102 0.0075  0.0240  0.0079  131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1749 0.1794 0.2131 0.0088  0.0194  0.0139  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.1895 0.1874 0.2205 0.0083  0.0176  0.0104  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2213 0.2131 0.2511 0.0077  0.0206  0.0046  131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1820 0.1917 0.2375 0.0122  0.0216  0.0206  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.1901 0.2089 0.2555 0.0130  0.0228  0.0264  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.2224 0.2446 0.3093 0.0172  0.0271  0.0328  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.1894 0.2177 0.2473 0.0101  0.0167  0.0316  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1410 0.1413 0.1675 0.0079  0.0130  0.0136  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1527 0.1482 0.1749 0.0079  0.0112  0.0114  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1469 0.1481 0.1747 0.0088  0.0088  0.0177  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1469 0.1553 0.1740 0.0074  0.0066  0.0220  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1604 0.1523 0.1694 0.0056  0.0083  0.0077  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1695 0.1653 0.1732 0.0038  0.0058  0.0100  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1706 0.1589 0.1769 0.0058  0.0064  0.0063  132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1431 0.1418 0.1758 0.0103  0.0094  0.0181  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1424 0.1465 0.1800 0.0106  0.0072  0.0241  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1329 0.1334 0.1630 0.0095  0.0049  0.0212  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1480 0.1415 0.1750 0.0098  0.0059  0.0159  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1213 0.1276 0.1485 0.0074  0.0019  0.0245  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1334 0.1372 0.1544 0.0061  0.0001  0.0217  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1348 0.1437 0.1610 0.0055  -0.0008 0.0266  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1352 0.1533 0.1654 0.0039  -0.0018 0.0331  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1373 0.1429 0.1490 0.0027  -0.0014 0.0195  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1262 0.1280 0.1328 0.0027  -0.0007 0.0161  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1303 0.1246 0.1323 0.0036  -0.0006 0.0115  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1425 0.1495 0.1490 0.0012  -0.0004 0.0182  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1331 0.1246 0.1303 0.0031  -0.0001 0.0094  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1492 0.1526 0.1508 0.0008  0.0004  0.0151  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1407 0.1363 0.1376 0.0017  0.0005  0.0109  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1288 0.1327 0.1553 0.0064  -0.0006 0.0242  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1286 0.1369 0.1591 0.0055  -0.0015 0.0285  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1269 0.1395 0.1491 0.0013  -0.0033 0.0270  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1332 0.1405 0.1494 0.0010  -0.0032 0.0212  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1346 0.1358 0.1678 0.0075  -0.0002 0.0253  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1324 0.1552 0.1548 -0.0024 -0.0046 0.0323  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1386 0.1664 0.1531 -0.0080 -0.0051 0.0300  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1397 0.1651 0.1537 -0.0086 -0.0049 0.0278  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1406 0.1663 0.1612 -0.0066 -0.0053 0.0318  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1578 0.1998 0.1729 -0.0132 -0.0068 0.0371  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2112 0.2595 0.2175 -0.0207 -0.0063 0.0338  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2057 0.2488 0.2054 -0.0223 -0.0043 0.0264  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.2524 0.3104 0.2588 -0.0255 -0.0074 0.0381  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1352 0.1588 0.1427 -0.0116 -0.0036 0.0216  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1374 0.1606 0.1444 -0.0134 -0.0028 0.0192  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1476 0.1784 0.1487 -0.0210 -0.0012 0.0169  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1432 0.1744 0.1437 -0.0233 0.0002  0.0143  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1434 0.1561 0.1509 -0.0093 -0.0017 0.0132  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1619 0.1684 0.1741 -0.0036 -0.0028 0.0146  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1566 0.1649 0.1602 -0.0098 0.0002  0.0077  137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1465 0.1841 0.1432 -0.0258 -0.0010 0.0176  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1511 0.1956 0.1412 -0.0345 0.0018  0.0133  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.1637 0.2202 0.1527 -0.0408 0.0008  0.0177  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.1770 0.2381 0.1604 -0.0486 0.0041  0.0123  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1590 0.2089 0.1443 -0.0391 0.0023  0.0128  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1523 0.1901 0.1376 -0.0341 0.0042  0.0075  138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.1756 0.2189 0.1562 -0.0389 0.0048  0.0071  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1675 0.2179 0.1517 -0.0365 0.0005  0.0160  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.1885 0.2446 0.1708 -0.0389 -0.0003 0.0181  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.2015 0.2586 0.1772 -0.0452 0.0030  0.0119  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.2043 0.2658 0.1925 -0.0353 -0.0037 0.0263  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1633 0.2254 0.1582 -0.0382 -0.0032 0.0275  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.1685 0.2426 0.1630 -0.0443 -0.0046 0.0332  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.1636 0.2317 0.1602 -0.0425 -0.0032 0.0303  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.1842 0.2619 0.1796 -0.0482 -0.0038 0.0340  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.1883 0.2711 0.1908 -0.0422 -0.0089 0.0463  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2406 0.3120 0.2533 -0.0319 -0.0095 0.0490  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2190 0.2776 0.2320 -0.0259 -0.0079 0.0425  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2583 0.3337 0.2791 -0.0303 -0.0112 0.0579  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1495 0.2033 0.1495 -0.0348 -0.0018 0.0247  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1598 0.2080 0.1628 -0.0325 -0.0009 0.0224  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.1656 0.2129 0.1636 -0.0375 0.0034  0.0132  140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.1622 0.1995 0.1617 -0.0336 0.0059  0.0063  140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1485 0.1841 0.1574 -0.0233 -0.0015 0.0209  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1741 0.2090 0.1893 -0.0184 -0.0040 0.0284  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.1864 0.2093 0.2054 -0.0114 -0.0036 0.0248  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.2104 0.2520 0.2314 -0.0195 -0.0056 0.0370  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.1605 0.2194 0.1533 -0.0468 0.0046  0.0135  141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.1776 0.2364 0.1658 -0.0531 0.0103  0.0036  141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.1770 0.2279 0.1697 -0.0498 0.0129  -0.0016 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.1926 0.2376 0.1862 -0.0504 0.0182  -0.0105 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.1930 0.2678 0.1732 -0.0660 0.0116  0.0044  141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2049 0.2912 0.1809 -0.0706 0.0082  0.0113  141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2433 0.3465 0.2101 -0.0852 0.0101  0.0104  141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2127 0.2918 0.1875 -0.0679 0.0099  0.0063  141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.1618 0.2121 0.1591 -0.0456 0.0095  0.0043  142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.1639 0.2082 0.1659 -0.0425 0.0113  0.0005  142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.1753 0.2074 0.1828 -0.0345 0.0123  -0.0044 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.1848 0.2127 0.1967 -0.0326 0.0147  -0.0088 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.1717 0.2187 0.1774 -0.0407 0.0075  0.0084  142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.1602 0.2033 0.1702 -0.0339 0.0033  0.0154  142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.1693 0.2193 0.1798 -0.0350 0.0002  0.0244  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.1600 0.1922 0.1756 -0.0255 0.0022  0.0143  142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.1800 0.2226 0.1967 -0.0274 -0.0018 0.0279  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.1669 0.1987 0.1857 -0.0222 -0.0006 0.0213  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.1707 0.1946 0.1892 -0.0212 0.0035  0.0083  142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.1866 0.2093 0.2103 -0.0153 -0.0014 0.0209  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.1951 0.2115 0.2176 -0.0148 0.0017  0.0090  142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.1954 0.2110 0.2199 -0.0124 -0.0004 0.0146  142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.1640 0.1910 0.1717 -0.0297 0.0104  -0.0031 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.1771 0.1941 0.1896 -0.0232 0.0111  -0.0068 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.1996 0.2140 0.2140 -0.0255 0.0170  -0.0145 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2140 0.2218 0.2351 -0.0203 0.0180  -0.0167 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.1732 0.1865 0.1844 -0.0193 0.0087  -0.0044 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.1651 0.1778 0.1777 -0.0152 0.0042  0.0019  143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.1849 0.1956 0.1956 -0.0130 0.0027  0.0037  143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.1756 0.1824 0.1935 -0.0099 0.0028  0.0015  143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2238 0.2441 0.2333 -0.0336 0.0213  -0.0185 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.2636 0.2808 0.2758 -0.0369 0.0289  -0.0271 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3187 0.3372 0.3355 -0.0394 0.0333  -0.0317 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3399 0.3556 0.3610 -0.0422 0.0408  -0.0393 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.2723 0.2954 0.2766 -0.0464 0.0330  -0.0311 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.3127 0.3351 0.3128 -0.0453 0.0302  -0.0281 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.3301 0.3454 0.3342 -0.0368 0.0264  -0.0243 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.3899 0.4201 0.3823 -0.0536 0.0318  -0.0296 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3379 0.3602 0.3549 -0.0386 0.0296  -0.0275 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.3893 0.4133 0.4107 -0.0413 0.0339  -0.0321 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.4138 0.4373 0.4394 -0.0362 0.0293  -0.0273 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.4100 0.4311 0.4355 -0.0305 0.0232  -0.0210 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.4541 0.4884 0.4671 -0.0528 0.0375  -0.0352 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5713 0.6142 0.5766 -0.0555 0.0308  -0.0263 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.7144 0.7674 0.7097 -0.0654 0.0317  -0.0261 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.7638 0.8281 0.7530 -0.0742 0.0318  -0.0244 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.7609 0.8115 0.7541 -0.0650 0.0321  -0.0273 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.4349 0.4609 0.4643 -0.0389 0.0329  -0.0309 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.4642 0.4913 0.4972 -0.0362 0.0297  -0.0276 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.4818 0.5022 0.5218 -0.0269 0.0253  -0.0242 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.4843 0.5048 0.5243 -0.0242 0.0205  -0.0194 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.4996 0.5340 0.5248 -0.0408 0.0257  -0.0214 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.6010 0.6348 0.6290 -0.0371 0.0210  -0.0158 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.7315 0.7673 0.7641 -0.0387 0.0234  -0.0185 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.7560 0.7935 0.7885 -0.0387 0.0203  -0.0136 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.7706 0.8060 0.8078 -0.0400 0.0289  -0.0255 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2060 0.2203 0.2209 -0.0003 -0.0183 0.0434  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.1988 0.2138 0.2222 -0.0012 -0.0186 0.0440  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.1957 0.2072 0.2171 -0.0017 -0.0182 0.0398  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2179 0.2268 0.2316 -0.0017 -0.0186 0.0367  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2345 0.2524 0.2601 -0.0025 -0.0225 0.0474  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.3031 0.3195 0.3206 -0.0038 -0.0258 0.0451  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.1966 0.2078 0.2251 -0.0020 -0.0170 0.0398  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.1870 0.1950 0.2139 -0.0023 -0.0164 0.0367  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1688 0.1761 0.2020 -0.0016 -0.0131 0.0362  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.1744 0.1828 0.2118 -0.0006 -0.0110 0.0369  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1538 0.1590 0.1878 -0.0020 -0.0125 0.0351  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1577 0.1616 0.1963 -0.0011 -0.0090 0.0345  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1496 0.1497 0.1833 -0.0006 -0.0078 0.0319  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1663 0.1650 0.1953 -0.0014 -0.0098 0.0310  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.1813 0.1873 0.2293 -0.0019 -0.0086 0.0378  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1446 0.1429 0.1793 0.0006  -0.0045 0.0306  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1488 0.1436 0.1796 0.0014  -0.0026 0.0291  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1421 0.1368 0.1799 0.0011  -0.0002 0.0312  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1521 0.1483 0.1962 0.0013  0.0017  0.0323  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1457 0.1386 0.1718 0.0033  -0.0007 0.0261  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.1634 0.1571 0.1852 0.0037  -0.0027 0.0243  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.1743 0.1637 0.1950 0.0043  0.0009  0.0251  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.1776 0.1702 0.1969 0.0054  -0.0014 0.0214  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1463 0.1394 0.1841 0.0005  0.0001  0.0320  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1556 0.1484 0.2009 0.0003  0.0029  0.0343  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1623 0.1510 0.2027 0.0019  0.0067  0.0332  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.1866 0.1734 0.2236 0.0016  0.0060  0.0331  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1654 0.1601 0.2171 -0.0020 0.0001  0.0369  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1629 0.1619 0.2192 -0.0034 -0.0036 0.0385  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1623 0.1641 0.2280 -0.0035 -0.0024 0.0413  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.1801 0.1801 0.2308 -0.0043 -0.0079 0.0375  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.1750 0.1808 0.2446 -0.0044 -0.0058 0.0435  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.2046 0.2085 0.2582 -0.0052 -0.0111 0.0394  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.1931 0.1999 0.2561 -0.0052 -0.0102 0.0426  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2191 0.2299 0.2847 -0.0058 -0.0133 0.0450  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.1743 0.1615 0.2137 0.0037  0.0107  0.0324  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.1866 0.1698 0.2198 0.0057  0.0145  0.0315  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.1890 0.1713 0.2280 0.0065  0.0197  0.0331  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.1736 0.1573 0.2172 0.0066  0.0210  0.0328  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2059 0.1876 0.2291 0.0075  0.0140  0.0279  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2089 0.1923 0.2344 0.0077  0.0141  0.0261  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2299 0.2076 0.2459 0.0098  0.0177  0.0273  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2026 0.1826 0.2429 0.0070  0.0232  0.0353  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2020 0.1809 0.2483 0.0079  0.0289  0.0371  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.1984 0.1812 0.2576 0.0062  0.0281  0.0394  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2070 0.1929 0.2722 0.0039  0.0237  0.0411  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.1948 0.1776 0.2580 0.0072  0.0318  0.0391  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.1937 0.1804 0.2697 0.0058  0.0310  0.0416  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.1804 0.1691 0.2552 0.0056  0.0281  0.0394  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.1819 0.1722 0.2650 0.0057  0.0297  0.0405  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2228 0.2086 0.3083 0.0068  0.0375  0.0440  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.2951 0.2806 0.3869 0.0061  0.0393  0.0476  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3105 0.2997 0.4141 0.0041  0.0368  0.0510  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3393 0.3207 0.4234 0.0077  0.0432  0.0470  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.1598 0.1485 0.2253 0.0054  0.0238  0.0368  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1424 0.1330 0.2067 0.0052  0.0209  0.0349  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1427 0.1365 0.2063 0.0034  0.0149  0.0359  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1546 0.1477 0.2131 0.0028  0.0125  0.0358  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.1644 0.1518 0.2176 0.0069  0.0218  0.0302  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.1831 0.1669 0.2343 0.0089  0.0275  0.0283  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2064 0.1904 0.2657 0.0093  0.0310  0.0284  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2251 0.2050 0.2660 0.0106  0.0295  0.0263  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.2407 0.2208 0.2972 0.0112  0.0366  0.0261  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.2636 0.2399 0.3008 0.0126  0.0348  0.0243  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.2869 0.2631 0.3316 0.0129  0.0383  0.0238  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.3598 0.3319 0.4004 0.0149  0.0439  0.0214  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1363 0.1331 0.2045 0.0028  0.0129  0.0367  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1348 0.1344 0.2010 0.0015  0.0077  0.0374  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1391 0.1387 0.2017 0.0024  0.0075  0.0348  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1400 0.1401 0.2086 0.0030  0.0099  0.0349  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1426 0.1466 0.2189 0.0000  0.0054  0.0419  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.1530 0.1602 0.2275 -0.0008 0.0007  0.0430  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1455 0.1571 0.2292 -0.0022 -0.0020 0.0477  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.1567 0.1713 0.2421 -0.0021 -0.0040 0.0498  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.1676 0.1842 0.2475 -0.0028 -0.0082 0.0506  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.1958 0.2112 0.2675 -0.0037 -0.0112 0.0486  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.1856 0.2049 0.2677 -0.0023 -0.0091 0.0531  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1340 0.1329 0.1880 0.0025  0.0050  0.0324  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1222 0.1212 0.1734 0.0033  0.0047  0.0299  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1288 0.1307 0.1804 0.0024  0.0013  0.0318  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1433 0.1454 0.1895 0.0017  -0.0015 0.0321  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1304 0.1263 0.1718 0.0045  0.0046  0.0259  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.1592 0.1553 0.1998 0.0052  0.0044  0.0231  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.1603 0.1529 0.1989 0.0055  0.0078  0.0245  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1249 0.1291 0.1824 0.0025  0.0018  0.0332  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1259 0.1329 0.1834 0.0019  -0.0009 0.0356  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1473 0.1544 0.2049 0.0019  -0.0009 0.0357  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1377 0.1452 0.1971 0.0027  0.0002  0.0344  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1397 0.1457 0.2023 0.0035  0.0028  0.0319  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1231 0.1336 0.1884 0.0011  -0.0019 0.0406  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.1889 0.1992 0.2550 0.0011  -0.0016 0.0406  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1366 0.1474 0.2000 -0.0001 -0.0044 0.0419  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.1912 0.2048 0.2567 0.0006  -0.0046 0.0439  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.0749 0.0859 0.1508 0.0016  0.0014  0.0421  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2276 0.2375 0.2943 0.0001  -0.0025 0.0416  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1215 0.1310 0.1791 0.0026  -0.0015 0.0361  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1251 0.1355 0.1868 0.0033  -0.0001 0.0359  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1273 0.1393 0.2002 0.0033  0.0021  0.0390  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1222 0.1365 0.1984 0.0028  0.0011  0.0433  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1320 0.1444 0.1905 0.0034  -0.0016 0.0383  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1252 0.1360 0.1738 0.0035  -0.0033 0.0355  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1446 0.1550 0.1870 0.0029  -0.0054 0.0359  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1437 0.1533 0.1912 0.0043  -0.0023 0.0324  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1184 0.1293 0.1972 0.0039  0.0047  0.0368  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1206 0.1326 0.2109 0.0041  0.0073  0.0395  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1349 0.1505 0.2299 0.0041  0.0065  0.0456  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1365 0.1540 0.2388 0.0040  0.0070  0.0498  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1172 0.1271 0.2127 0.0046  0.0101  0.0355  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1275 0.1375 0.2355 0.0048  0.0134  0.0373  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1376 0.1452 0.2507 0.0051  0.0158  0.0327  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1402 0.1468 0.2650 0.0053  0.0197  0.0330  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1366 0.1451 0.2728 0.0055  0.0215  0.0374  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1460 0.1579 0.2830 0.0055  0.0199  0.0426  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1372 0.1440 0.2841 0.0058  0.0253  0.0369  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1348 0.1516 0.2255 0.0043  0.0053  0.0464  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1403 0.1604 0.2342 0.0046  0.0049  0.0525  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1552 0.1776 0.2444 0.0040  0.0015  0.0566  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.1816 0.2071 0.2738 0.0044  0.0008  0.0622  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1499 0.1704 0.2411 0.0052  0.0054  0.0526  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1321 0.1520 0.2109 0.0051  0.0029  0.0509  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1379 0.1551 0.2107 0.0049  0.0025  0.0451  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1451 0.1666 0.2166 0.0052  0.0009  0.0541  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1629 0.1801 0.2260 0.0050  0.0006  0.0451  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1520 0.1715 0.2135 0.0051  -0.0004 0.0501  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1385 0.1596 0.2210 0.0032  -0.0007 0.0539  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1505 0.1735 0.2295 0.0023  -0.0044 0.0569  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1515 0.1747 0.2375 0.0017  -0.0041 0.0576  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.1666 0.1914 0.2511 0.0007  -0.0074 0.0596  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1558 0.1771 0.2225 0.0017  -0.0070 0.0535  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1675 0.1887 0.2270 0.0024  -0.0071 0.0533  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.1762 0.1952 0.2243 0.0019  -0.0092 0.0495  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1799 0.2045 0.2402 0.0029  -0.0081 0.0590  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1527 0.1742 0.2465 0.0022  -0.0003 0.0559  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1507 0.1721 0.2514 0.0019  0.0008  0.0566  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.1538 0.1793 0.2633 0.0017  -0.0007 0.0631  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.1586 0.1866 0.2730 0.0023  -0.0005 0.0670  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1646 0.1830 0.2714 0.0027  0.0057  0.0533  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.1538 0.1802 0.2662 0.0008  -0.0022 0.0644  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.1641 0.1950 0.2859 0.0005  -0.0043 0.0707  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1510 0.1818 0.2868 0.0014  0.0002  0.0725  24  THR   C C   
1231 O O   . THR   B 18  ? 0.1509 0.1778 0.2883 0.0020  0.0049  0.0684  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.1763 0.2085 0.2952 -0.0010 -0.0087 0.0712  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.1803 0.2095 0.3017 -0.0012 -0.0057 0.0681  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.2093 0.2408 0.3141 -0.0019 -0.0130 0.0687  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.1570 0.1921 0.3038 0.0014  -0.0012 0.0789  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.1566 0.1917 0.3180 0.0022  0.0032  0.0810  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.1398 0.1721 0.3014 0.0017  0.0054  0.0774  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.1588 0.1878 0.3257 0.0026  0.0111  0.0750  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.1720 0.2130 0.3448 0.0022  0.0001  0.0888  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.1898 0.2311 0.3785 0.0029  0.0043  0.0914  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2156 0.2550 0.4138 0.0044  0.0103  0.0916  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.2113 0.2538 0.4072 0.0022  0.0041  0.0927  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.2126 0.2526 0.4240 0.0048  0.0132  0.0940  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.2036 0.2455 0.4142 0.0035  0.0098  0.0947  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.1499 0.1830 0.3056 0.0003  0.0013  0.0769  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.1566 0.1868 0.3129 -0.0001 0.0040  0.0739  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.1508 0.1751 0.2980 0.0007  0.0084  0.0673  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1461 0.1673 0.2966 0.0015  0.0135  0.0652  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.1803 0.2121 0.3322 -0.0019 -0.0012 0.0743  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2648 0.2940 0.4202 -0.0021 0.0022  0.0726  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.2945 0.3253 0.4633 -0.0018 0.0048  0.0759  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.2956 0.3207 0.4399 -0.0024 0.0030  0.0676  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1398 0.1627 0.2754 0.0008  0.0068  0.0640  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1465 0.1643 0.2739 0.0016  0.0103  0.0579  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1394 0.1552 0.2747 0.0030  0.0160  0.0567  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1578 0.1695 0.2915 0.0038  0.0203  0.0528  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1575 0.1748 0.2736 0.0015  0.0075  0.0552  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1534 0.1710 0.2594 0.0004  0.0030  0.0543  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1734 0.1892 0.2774 -0.0001 0.0033  0.0530  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1574 0.1767 0.2578 0.0000  -0.0006 0.0551  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1380 0.1563 0.2817 0.0034  0.0162  0.0601  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1415 0.1576 0.2939 0.0047  0.0216  0.0589  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1355 0.1508 0.2985 0.0053  0.0260  0.0605  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1485 0.1598 0.3141 0.0063  0.0315  0.0568  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1387 0.1577 0.2985 0.0050  0.0209  0.0629  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1336 0.1517 0.2852 0.0050  0.0195  0.0598  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.1534 0.1741 0.2980 0.0044  0.0150  0.0618  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1232 0.1372 0.2727 0.0055  0.0227  0.0539  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.1510 0.1699 0.2909 0.0047  0.0156  0.0583  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1436 0.1585 0.2870 0.0053  0.0200  0.0534  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.1515 0.1612 0.3050 0.0063  0.0277  0.0492  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.1416 0.1538 0.2837 0.0056  0.0217  0.0485  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.1701 0.1769 0.3211 0.0065  0.0290  0.0439  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.1694 0.1777 0.3153 0.0060  0.0259  0.0437  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1343 0.1534 0.3032 0.0046  0.0236  0.0656  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1523 0.1711 0.3326 0.0051  0.0278  0.0678  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.1702 0.1846 0.3437 0.0053  0.0312  0.0632  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.1824 0.1955 0.3643 0.0061  0.0361  0.0641  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1623 0.1870 0.3518 0.0041  0.0234  0.0748  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.1632 0.1753 0.3217 0.0048  0.0286  0.0589  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.1601 0.1680 0.3105 0.0051  0.0314  0.0550  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.1645 0.1682 0.3013 0.0058  0.0320  0.0485  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1666 0.1682 0.2920 0.0056  0.0307  0.0456  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.1865 0.1967 0.3336 0.0036  0.0269  0.0572  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.1970 0.2113 0.3586 0.0030  0.0265  0.0631  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.2301 0.2427 0.3986 0.0037  0.0316  0.0639  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.1958 0.2153 0.3622 0.0017  0.0207  0.0675  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.1703 0.1728 0.3089 0.0065  0.0337  0.0463  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.1673 0.1668 0.2948 0.0069  0.0331  0.0404  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.1913 0.1854 0.3100 0.0081  0.0372  0.0350  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.2081 0.1995 0.3317 0.0092  0.0428  0.0344  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.1680 0.1677 0.3026 0.0072  0.0344  0.0397  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.1775 0.1747 0.3031 0.0074  0.0333  0.0339  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.1713 0.1712 0.2886 0.0064  0.0274  0.0347  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.2107 0.2075 0.3456 0.0077  0.0356  0.0331  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.1750 0.1673 0.2803 0.0081  0.0345  0.0311  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.1844 0.1718 0.2794 0.0094  0.0375  0.0257  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.1915 0.1770 0.2815 0.0097  0.0364  0.0201  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2082 0.1898 0.2965 0.0109  0.0402  0.0156  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.1897 0.1763 0.2735 0.0094  0.0352  0.0256  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2188 0.2005 0.2901 0.0110  0.0374  0.0201  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.1907 0.1787 0.2804 0.0089  0.0365  0.0306  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.1673 0.1556 0.2554 0.0087  0.0315  0.0204  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.1774 0.1644 0.2617 0.0089  0.0300  0.0154  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.1711 0.1622 0.2584 0.0077  0.0255  0.0179  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1688 0.1627 0.2542 0.0070  0.0225  0.0218  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.1943 0.1782 0.2641 0.0097  0.0287  0.0105  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.2025 0.1859 0.2676 0.0097  0.0256  0.0057  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2262 0.2071 0.2919 0.0101  0.0269  0.0001  33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.1862 0.1721 0.2467 0.0091  0.0207  0.0060  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2366 0.2184 0.2984 0.0097  0.0226  -0.0030 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.2036 0.1885 0.2624 0.0092  0.0191  0.0008  33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.1859 0.1746 0.2438 0.0084  0.0175  0.0099  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.2030 0.1897 0.2576 0.0089  0.0147  -0.0002 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.2010 0.1910 0.2539 0.0082  0.0136  0.0086  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.2023 0.1915 0.2544 0.0084  0.0123  0.0040  33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1555 0.1468 0.2475 0.0075  0.0253  0.0158  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.1680 0.1628 0.2626 0.0067  0.0219  0.0181  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1683 0.1620 0.2632 0.0067  0.0212  0.0133  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.1767 0.1673 0.2748 0.0071  0.0239  0.0090  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.1783 0.1766 0.2843 0.0062  0.0224  0.0244  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.1908 0.1881 0.3091 0.0066  0.0268  0.0247  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.2141 0.2108 0.3391 0.0065  0.0276  0.0221  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2307 0.2246 0.3630 0.0069  0.0315  0.0195  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.1885 0.1874 0.3125 0.0060  0.0248  0.0229  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1524 0.1483 0.2446 0.0062  0.0177  0.0138  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1517 0.1471 0.2459 0.0061  0.0167  0.0096  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1487 0.1478 0.2468 0.0056  0.0148  0.0135  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1497 0.1503 0.2404 0.0055  0.0120  0.0150  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.1732 0.1662 0.2560 0.0066  0.0146  0.0038  35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2211 0.2137 0.3056 0.0064  0.0128  -0.0012 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2241 0.2192 0.3158 0.0058  0.0119  0.0008  35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.2778 0.2676 0.3556 0.0069  0.0119  -0.0069 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1463 0.1466 0.2563 0.0053  0.0166  0.0154  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1387 0.1424 0.2531 0.0050  0.0157  0.0197  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1491 0.1528 0.2629 0.0051  0.0156  0.0198  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1481 0.1520 0.2580 0.0050  0.0131  0.0163  36  SER   C C   
1338 O O   . SER   B 30  ? 0.1368 0.1431 0.2431 0.0051  0.0114  0.0195  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.1338 0.1382 0.2627 0.0049  0.0188  0.0220  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.1799 0.1847 0.3078 0.0050  0.0186  0.0232  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.1291 0.1361 0.2623 0.0049  0.0184  0.0253  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.2248 0.2270 0.3597 0.0048  0.0203  0.0179  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1507 0.1522 0.2604 0.0049  0.0126  0.0097  37  SER   C N   
1344 C CA  . SER   B 31  ? 0.1632 0.1654 0.2701 0.0048  0.0097  0.0066  37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1522 0.1549 0.2462 0.0053  0.0068  0.0070  37  SER   C C   
1346 O O   . SER   B 31  ? 0.1606 0.1648 0.2532 0.0054  0.0049  0.0069  37  SER   C O   
1347 C CB  . SER   B 31  ? 0.1969 0.1966 0.3053 0.0046  0.0089  -0.0007 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.2575 0.2545 0.3549 0.0051  0.0076  -0.0049 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1379 0.1392 0.2236 0.0056  0.0068  0.0078  38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1420 0.1434 0.2162 0.0061  0.0044  0.0084  38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1305 0.1340 0.2033 0.0058  0.0045  0.0144  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1294 0.1329 0.1937 0.0060  0.0027  0.0152  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.1576 0.1560 0.2236 0.0066  0.0044  0.0055  38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.1792 0.1754 0.2433 0.0070  0.0035  -0.0008 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.1546 0.1476 0.2095 0.0078  0.0041  -0.0032 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.1547 0.1476 0.1992 0.0085  0.0021  -0.0018 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.1548 0.1453 0.1896 0.0096  0.0013  -0.0044 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.1810 0.1688 0.2134 0.0102  0.0023  -0.0089 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.1608 0.1514 0.1877 0.0102  -0.0004 -0.0027 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1193 0.1244 0.2001 0.0055  0.0065  0.0187  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1176 0.1247 0.1968 0.0052  0.0062  0.0242  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1213 0.1271 0.1935 0.0051  0.0054  0.0243  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1265 0.1333 0.1932 0.0048  0.0037  0.0269  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1195 0.1286 0.1947 0.0054  0.0046  0.0265  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1349 0.1461 0.2083 0.0051  0.0040  0.0321  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1412 0.1538 0.2213 0.0049  0.0052  0.0357  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1323 0.1438 0.1979 0.0051  0.0022  0.0328  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1174 0.1208 0.1904 0.0053  0.0071  0.0216  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1269 0.1290 0.1945 0.0053  0.0070  0.0221  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1267 0.1285 0.2018 0.0052  0.0099  0.0241  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1357 0.1367 0.2181 0.0055  0.0124  0.0225  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1393 0.1381 0.1983 0.0060  0.0067  0.0172  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1421 0.1408 0.1924 0.0063  0.0038  0.0157  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.1670 0.1627 0.2095 0.0073  0.0036  0.0114  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1582 0.1583 0.2046 0.0057  0.0021  0.0193  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1210 0.1234 0.1951 0.0048  0.0096  0.0271  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1284 0.1304 0.2096 0.0049  0.0125  0.0290  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1340 0.1347 0.2094 0.0047  0.0122  0.0294  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1447 0.1466 0.2148 0.0041  0.0091  0.0309  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1368 0.1425 0.2279 0.0043  0.0123  0.0348  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1369 0.1428 0.2376 0.0044  0.0153  0.0375  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1646 0.1732 0.2771 0.0045  0.0164  0.0414  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1403 0.1479 0.2401 0.0037  0.0134  0.0409  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1424 0.1407 0.2196 0.0054  0.0158  0.0282  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1405 0.1374 0.2143 0.0055  0.0167  0.0290  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1320 0.1297 0.2164 0.0054  0.0198  0.0325  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1524 0.1490 0.2434 0.0061  0.0235  0.0317  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1522 0.1447 0.2167 0.0068  0.0187  0.0243  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.1670 0.1578 0.2285 0.0070  0.0204  0.0257  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1612 0.1532 0.2162 0.0070  0.0153  0.0211  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1359 0.1356 0.2230 0.0044  0.0182  0.0365  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1362 0.1374 0.2345 0.0042  0.0207  0.0404  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1481 0.1473 0.2440 0.0043  0.0224  0.0407  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1576 0.1551 0.2437 0.0042  0.0207  0.0388  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1572 0.1634 0.2634 0.0029  0.0167  0.0456  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.1555 0.1635 0.2557 0.0016  0.0116  0.0466  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1532 0.1525 0.2588 0.0046  0.0262  0.0434  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1663 0.1638 0.2719 0.0047  0.0285  0.0444  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.1837 0.1852 0.2958 0.0027  0.0243  0.0489  44  SER   C C   
1400 O O   . SER   B 38  ? 0.1966 0.2025 0.3169 0.0016  0.0209  0.0522  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.1895 0.1848 0.3024 0.0062  0.0357  0.0448  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2353 0.2342 0.3626 0.0057  0.0359  0.0489  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.1808 0.1808 0.2896 0.0023  0.0244  0.0490  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.1941 0.1974 0.3087 0.0002  0.0200  0.0523  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2214 0.2237 0.3448 0.0003  0.0243  0.0550  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2331 0.2313 0.3532 0.0021  0.0303  0.0535  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2098 0.2119 0.3127 -0.0007 0.0155  0.0499  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2230 0.2204 0.3183 0.0006  0.0194  0.0476  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2115 0.2140 0.3051 -0.0006 0.0118  0.0472  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2456 0.2519 0.3798 -0.0016 0.0209  0.0588  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2684 0.2743 0.4128 -0.0019 0.0244  0.0618  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.2717 0.2746 0.4086 -0.0024 0.0240  0.0601  46  THR   C C   
1413 O O   . THR   B 40  ? 0.2971 0.2964 0.4341 -0.0011 0.0299  0.0604  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3170 0.3289 0.4773 -0.0038 0.0204  0.0666  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3570 0.3719 0.5134 -0.0061 0.0120  0.0662  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.3135 0.3282 0.4817 -0.0029 0.0214  0.0686  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.2373 0.2412 0.3671 -0.0042 0.0173  0.0585  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.2503 0.2512 0.3735 -0.0047 0.0166  0.0569  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.2290 0.2252 0.3361 -0.0028 0.0187  0.0528  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2274 0.2238 0.3272 -0.0019 0.0174  0.0505  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.2809 0.2848 0.4048 -0.0076 0.0086  0.0568  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.2213 0.2136 0.3234 -0.0020 0.0215  0.0521  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.2343 0.2224 0.3215 -0.0001 0.0229  0.0487  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2367 0.2256 0.3163 -0.0015 0.0164  0.0463  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.2589 0.2493 0.3430 -0.0038 0.0122  0.0470  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3017 0.2855 0.3867 0.0014  0.0283  0.0497  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4056 0.3874 0.4936 0.0036  0.0360  0.0513  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.5487 0.5258 0.6311 0.0056  0.0414  0.0521  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6081 0.5846 0.6985 0.0047  0.0432  0.0552  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.5820 0.5556 0.6507 0.0082  0.0438  0.0496  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2151 0.2027 0.2836 -0.0001 0.0156  0.0431  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2130 0.2008 0.2734 -0.0008 0.0106  0.0406  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2119 0.1954 0.2635 0.0004  0.0120  0.0391  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2414 0.2219 0.2910 0.0023  0.0170  0.0398  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.1918 0.1750 0.2377 -0.0004 0.0080  0.0372  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2001 0.1796 0.2394 0.0006  0.0089  0.0363  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2154 0.1938 0.2440 0.0020  0.0073  0.0334  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.2473 0.2228 0.2707 0.0029  0.0075  0.0328  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.2023 0.1815 0.2466 -0.0018 0.0062  0.0369  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.2846 0.2650 0.3433 -0.0036 0.0081  0.0407  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.1810 0.1617 0.2071 0.0023  0.0056  0.0317  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.1771 0.1571 0.1946 0.0037  0.0041  0.0291  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.1976 0.1752 0.2094 0.0064  0.0076  0.0285  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2191 0.1963 0.2332 0.0072  0.0111  0.0295  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.1942 0.1776 0.2123 0.0032  0.0016  0.0278  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2270 0.2128 0.2481 0.0009  -0.0022 0.0282  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.2493 0.2337 0.2689 0.0000  -0.0040 0.0279  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.1975 0.1864 0.2222 0.0002  -0.0035 0.0289  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.1783 0.1541 0.1824 0.0079  0.0068  0.0270  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.1884 0.1623 0.1854 0.0106  0.0089  0.0260  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.1866 0.1624 0.1800 0.0112  0.0063  0.0230  52  THR   C C   
1452 O O   . THR   B 46  ? 0.1936 0.1706 0.1865 0.0105  0.0032  0.0220  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2181 0.1889 0.2098 0.0121  0.0096  0.0270  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.2401 0.2089 0.2362 0.0115  0.0125  0.0300  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.2460 0.2151 0.2289 0.0151  0.0107  0.0260  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.1835 0.1594 0.1747 0.0125  0.0076  0.0215  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.1798 0.1574 0.1687 0.0130  0.0052  0.0184  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.1736 0.1496 0.1542 0.0152  0.0039  0.0172  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.1897 0.1631 0.1646 0.0171  0.0060  0.0179  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.1940 0.1720 0.1844 0.0134  0.0070  0.0167  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.2075 0.1870 0.2069 0.0116  0.0088  0.0187  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.1969 0.1768 0.1866 0.0137  0.0043  0.0134  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2165 0.1993 0.2217 0.0095  0.0056  0.0195  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.1646 0.1422 0.1445 0.0152  0.0007  0.0157  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.1613 0.1381 0.1347 0.0173  -0.0011 0.0146  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.1685 0.1452 0.1375 0.0189  -0.0012 0.0120  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.1697 0.1479 0.1424 0.0180  -0.0013 0.0099  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.1696 0.1486 0.1453 0.0168  -0.0043 0.0135  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.1730 0.1477 0.1340 0.0213  -0.0013 0.0122  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.1797 0.1541 0.1348 0.0229  -0.0021 0.0093  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.1795 0.1547 0.1300 0.0246  -0.0060 0.0089  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.1946 0.1678 0.1389 0.0266  -0.0056 0.0112  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.1862 0.1572 0.1350 0.0244  0.0020  0.0104  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.1775 0.1480 0.1328 0.0227  0.0061  0.0114  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2021 0.1745 0.1631 0.0212  0.0056  0.0081  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2043 0.1763 0.1720 0.0198  0.0097  0.0098  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.1948 0.1687 0.1707 0.0181  0.0099  0.0087  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.1931 0.1691 0.1713 0.0175  0.0068  0.0057  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2142 0.1880 0.1969 0.0170  0.0133  0.0111  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.1709 0.1491 0.1256 0.0239  -0.0097 0.0062  56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.1719 0.1518 0.1257 0.0252  -0.0137 0.0061  56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.1746 0.1580 0.1350 0.0240  -0.0169 0.0029  56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.1750 0.1592 0.1405 0.0223  -0.0159 0.0010  56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.1743 0.1537 0.1311 0.0248  -0.0126 0.0096  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.1692 0.1505 0.1360 0.0217  -0.0119 0.0094  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.1807 0.1660 0.1416 0.0252  -0.0206 0.0027  57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.1851 0.1739 0.1539 0.0242  -0.0234 0.0003  57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.1839 0.1739 0.1579 0.0241  -0.0236 0.0026  57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.1909 0.1838 0.1702 0.0243  -0.0263 0.0016  57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2110 0.2016 0.1776 0.0256  -0.0281 -0.0029 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.2742 0.2647 0.2349 0.0281  -0.0308 -0.0010 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.2586 0.2474 0.2171 0.0290  -0.0287 0.0027  57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.3463 0.3388 0.3056 0.0293  -0.0355 -0.0034 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.1690 0.1569 0.1424 0.0235  -0.0204 0.0056  58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.1615 0.1500 0.1395 0.0233  -0.0200 0.0072  58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.1598 0.1513 0.1459 0.0218  -0.0204 0.0057  58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.1632 0.1555 0.1521 0.0202  -0.0196 0.0044  58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.1762 0.1619 0.1529 0.0223  -0.0166 0.0096  58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.1772 0.1591 0.1467 0.0241  -0.0154 0.0125  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1470 0.1397 0.1369 0.0224  -0.0210 0.0064  59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.1574 0.1525 0.1550 0.0214  -0.0204 0.0059  59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1516 0.1452 0.1497 0.0213  -0.0180 0.0078  59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1498 0.1451 0.1535 0.0210  -0.0170 0.0078  59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.1602 0.1587 0.1638 0.0223  -0.0235 0.0043  59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.1940 0.1940 0.1987 0.0218  -0.0259 0.0014  59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2305 0.2342 0.2431 0.0223  -0.0292 -0.0004 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.2573 0.2621 0.2680 0.0235  -0.0332 -0.0020 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.1964 0.2023 0.2182 0.0213  -0.0276 -0.0002 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1531 0.1435 0.1457 0.0214  -0.0165 0.0093  60  THR   C N   
1510 C CA  . THR   B 54  ? 0.1655 0.1539 0.1580 0.0209  -0.0141 0.0104  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1642 0.1499 0.1526 0.0193  -0.0125 0.0111  60  THR   C C   
1512 O O   . THR   B 54  ? 0.1704 0.1548 0.1553 0.0195  -0.0128 0.0116  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.1931 0.1798 0.1851 0.0228  -0.0140 0.0114  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2610 0.2455 0.2482 0.0238  -0.0146 0.0125  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.1930 0.1827 0.1902 0.0245  -0.0159 0.0110  60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1459 0.1310 0.1348 0.0178  -0.0108 0.0113  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1504 0.1335 0.1367 0.0160  -0.0099 0.0119  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1371 0.1197 0.1233 0.0147  -0.0087 0.0118  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1562 0.1388 0.1433 0.0155  -0.0079 0.0113  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1414 0.1234 0.1265 0.0128  -0.0085 0.0123  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1354 0.1167 0.1191 0.0114  -0.0080 0.0120  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1345 0.1182 0.1197 0.0097  -0.0086 0.0130  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1488 0.1328 0.1353 0.0090  -0.0091 0.0138  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1464 0.1238 0.1271 0.0106  -0.0079 0.0116  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1664 0.1430 0.1447 0.0088  -0.0082 0.0109  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1578 0.1324 0.1376 0.0125  -0.0070 0.0110  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1325 0.1179 0.1178 0.0092  -0.0083 0.0133  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1247 0.1126 0.1120 0.0077  -0.0089 0.0149  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1344 0.1217 0.1180 0.0063  -0.0095 0.0152  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1464 0.1319 0.1259 0.0068  -0.0088 0.0139  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1357 0.1270 0.1277 0.0083  -0.0081 0.0158  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1335 0.1259 0.1249 0.0088  -0.0068 0.0163  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1466 0.1381 0.1376 0.0104  -0.0054 0.0152  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1329 0.1273 0.1247 0.0080  -0.0066 0.0184  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1510 0.1434 0.1417 0.0110  -0.0034 0.0159  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1493 0.1447 0.1403 0.0088  -0.0047 0.0194  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1529 0.1471 0.1433 0.0103  -0.0029 0.0180  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.1857 0.1806 0.1756 0.0112  -0.0004 0.0192  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1358 0.1247 0.1208 0.0048  -0.0109 0.0168  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1461 0.1351 0.1275 0.0034  -0.0123 0.0173  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1493 0.1415 0.1311 0.0038  -0.0116 0.0193  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1443 0.1394 0.1317 0.0038  -0.0114 0.0215  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1584 0.1478 0.1418 0.0014  -0.0146 0.0183  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1772 0.1668 0.1564 -0.0001 -0.0170 0.0184  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1871 0.1734 0.1597 -0.0004 -0.0174 0.0156  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1767 0.1696 0.1579 -0.0011 -0.0188 0.0211  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.1975 0.1836 0.1647 -0.0017 -0.0199 0.0151  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.1913 0.1846 0.1676 -0.0024 -0.0217 0.0212  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.1984 0.1883 0.1673 -0.0027 -0.0223 0.0180  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2489 0.2388 0.2116 -0.0040 -0.0254 0.0175  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1457 0.1369 0.1215 0.0040  -0.0112 0.0188  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1508 0.1444 0.1254 0.0047  -0.0101 0.0211  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1631 0.1569 0.1318 0.0033  -0.0127 0.0220  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.1747 0.1658 0.1357 0.0031  -0.0130 0.0198  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1513 0.1435 0.1233 0.0065  -0.0069 0.0200  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.1771 0.1717 0.1471 0.0076  -0.0046 0.0232  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.1762 0.1733 0.1488 0.0023  -0.0146 0.0250  66  SER   C N   
1558 C CA  A SER   B 60  ? 0.1994 0.1972 0.1668 0.0009  -0.0180 0.0260  66  SER   C CA  
1559 C CA  B SER   B 60  ? 0.1890 0.1870 0.1567 0.0009  -0.0180 0.0261  66  SER   C CA  
1560 C C   . SER   B 60  ? 0.2063 0.2041 0.1653 0.0019  -0.0171 0.0268  66  SER   C C   
1561 O O   . SER   B 60  ? 0.2306 0.2269 0.1815 0.0010  -0.0197 0.0253  66  SER   C O   
1562 C CB  A SER   B 60  ? 0.2371 0.2386 0.2116 -0.0002 -0.0203 0.0294  66  SER   C CB  
1563 C CB  B SER   B 60  ? 0.1964 0.1983 0.1711 0.0000  -0.0200 0.0300  66  SER   C CB  
1564 O OG  A SER   B 60  ? 0.2798 0.2843 0.2596 0.0011  -0.0179 0.0329  66  SER   C OG  
1565 O OG  B SER   B 60  ? 0.1849 0.1879 0.1550 -0.0014 -0.0240 0.0310  66  SER   C OG  
1566 N N   . SER   B 61  ? 0.1904 0.1895 0.1510 0.0038  -0.0133 0.0290  67  SER   C N   
1567 C CA  . SER   B 61  ? 0.1914 0.1904 0.1439 0.0052  -0.0115 0.0304  67  SER   C CA  
1568 C C   . SER   B 61  ? 0.2134 0.2080 0.1573 0.0059  -0.0096 0.0262  67  SER   C C   
1569 O O   . SER   B 61  ? 0.2403 0.2340 0.1758 0.0071  -0.0078 0.0268  67  SER   C O   
1570 C CB  . SER   B 61  ? 0.2029 0.2047 0.1614 0.0070  -0.0075 0.0342  67  SER   C CB  
1571 O OG  . SER   B 61  ? 0.2074 0.2078 0.1712 0.0081  -0.0041 0.0322  67  SER   C OG  
1572 N N   . ARG   B 62  ? 0.1931 0.1846 0.1382 0.0053  -0.0099 0.0221  68  ARG   C N   
1573 C CA  . ARG   B 62  ? 0.2089 0.1957 0.1466 0.0058  -0.0084 0.0179  68  ARG   C CA  
1574 C C   . ARG   B 62  ? 0.2253 0.2091 0.1605 0.0037  -0.0122 0.0142  68  ARG   C C   
1575 O O   . ARG   B 62  ? 0.2421 0.2216 0.1721 0.0039  -0.0111 0.0103  68  ARG   C O   
1576 C CB  . ARG   B 62  ? 0.2136 0.1990 0.1563 0.0076  -0.0042 0.0168  68  ARG   C CB  
1577 C CG  . ARG   B 62  ? 0.2401 0.2282 0.1868 0.0097  -0.0002 0.0201  68  ARG   C CG  
1578 C CD  . ARG   B 62  ? 0.2569 0.2430 0.1943 0.0111  0.0029  0.0199  68  ARG   C CD  
1579 N NE  . ARG   B 62  ? 0.2606 0.2491 0.2024 0.0132  0.0076  0.0234  68  ARG   C NE  
1580 C CZ  . ARG   B 62  ? 0.2842 0.2760 0.2266 0.0136  0.0082  0.0279  68  ARG   C CZ  
1581 N NH1 . ARG   B 62  ? 0.3051 0.2984 0.2431 0.0122  0.0043  0.0296  68  ARG   C NH1 
1582 N NH2 . ARG   B 62  ? 0.3142 0.3076 0.2611 0.0156  0.0130  0.0309  68  ARG   C NH2 
1583 N N   . ARG   B 63  ? 0.2367 0.2227 0.1772 0.0018  -0.0160 0.0154  69  ARG   C N   
1584 C CA  . ARG   B 63  ? 0.2503 0.2339 0.1917 -0.0004 -0.0194 0.0125  69  ARG   C CA  
1585 C C   . ARG   B 63  ? 0.2595 0.2392 0.2028 0.0004  -0.0169 0.0093  69  ARG   C C   
1586 O O   . ARG   B 63  ? 0.2802 0.2558 0.2195 -0.0005 -0.0176 0.0056  69  ARG   C O   
1587 C CB  . ARG   B 63  ? 0.2795 0.2612 0.2115 -0.0019 -0.0229 0.0100  69  ARG   C CB  
1588 C CG  . ARG   B 63  ? 0.3042 0.2900 0.2341 -0.0028 -0.0265 0.0132  69  ARG   C CG  
1589 C CD  . ARG   B 63  ? 0.3688 0.3580 0.3084 -0.0046 -0.0299 0.0157  69  ARG   C CD  
1590 N NE  . ARG   B 63  ? 0.3974 0.3897 0.3342 -0.0059 -0.0347 0.0179  69  ARG   C NE  
1591 C CZ  . ARG   B 63  ? 0.3955 0.3924 0.3339 -0.0051 -0.0350 0.0228  69  ARG   C CZ  
1592 N NH1 . ARG   B 63  ? 0.3535 0.3520 0.2965 -0.0030 -0.0305 0.0259  69  ARG   C NH1 
1593 N NH2 . ARG   B 63  ? 0.4045 0.4043 0.3404 -0.0063 -0.0399 0.0249  69  ARG   C NH2 
1594 N N   . LYS   B 64  ? 0.2183 0.1992 0.1677 0.0021  -0.0138 0.0107  70  LYS   C N   
1595 C CA  . LYS   B 64  ? 0.2162 0.1937 0.1672 0.0033  -0.0114 0.0083  70  LYS   C CA  
1596 C C   . LYS   B 64  ? 0.1937 0.1732 0.1532 0.0039  -0.0108 0.0101  70  LYS   C C   
1597 O O   . LYS   B 64  ? 0.1927 0.1760 0.1565 0.0043  -0.0106 0.0128  70  LYS   C O   
1598 C CB  . LYS   B 64  ? 0.2652 0.2415 0.2127 0.0055  -0.0074 0.0076  70  LYS   C CB  
1599 C CG  . LYS   B 64  ? 0.4224 0.3944 0.3605 0.0054  -0.0068 0.0043  70  LYS   C CG  
1600 C CD  . LYS   B 64  ? 0.5363 0.5063 0.4720 0.0079  -0.0020 0.0033  70  LYS   C CD  
1601 C CE  . LYS   B 64  ? 0.6075 0.5728 0.5331 0.0078  -0.0011 -0.0003 70  LYS   C CE  
1602 N NZ  . LYS   B 64  ? 0.6615 0.6281 0.5789 0.0066  -0.0035 0.0003  70  LYS   C NZ  
1603 N N   . HIS   B 65  ? 0.1904 0.1670 0.1519 0.0042  -0.0104 0.0084  71  HIS   C N   
1604 C CA  . HIS   B 65  ? 0.1792 0.1569 0.1468 0.0053  -0.0095 0.0095  71  HIS   C CA  
1605 C C   . HIS   B 65  ? 0.2010 0.1777 0.1688 0.0076  -0.0067 0.0087  71  HIS   C C   
1606 O O   . HIS   B 65  ? 0.2446 0.2177 0.2093 0.0082  -0.0055 0.0065  71  HIS   C O   
1607 C CB  . HIS   B 65  ? 0.1750 0.1503 0.1448 0.0044  -0.0106 0.0089  71  HIS   C CB  
1608 C CG  . HIS   B 65  ? 0.1595 0.1361 0.1311 0.0022  -0.0132 0.0100  71  HIS   C CG  
1609 N ND1 . HIS   B 65  ? 0.2008 0.1799 0.1777 0.0019  -0.0135 0.0122  71  HIS   C ND1 
1610 C CD2 . HIS   B 65  ? 0.1715 0.1472 0.1406 0.0001  -0.0155 0.0091  71  HIS   C CD2 
1611 C CE1 . HIS   B 65  ? 0.1721 0.1518 0.1505 -0.0002 -0.0158 0.0129  71  HIS   C CE1 
1612 N NE2 . HIS   B 65  ? 0.2169 0.1948 0.1910 -0.0014 -0.0174 0.0110  71  HIS   C NE2 
1613 N N   . TYR   B 66  ? 0.1658 0.1455 0.1382 0.0090  -0.0057 0.0102  72  TYR   C N   
1614 C CA  . TYR   B 66  ? 0.1596 0.1390 0.1337 0.0112  -0.0034 0.0097  72  TYR   C CA  
1615 C C   . TYR   B 66  ? 0.1500 0.1302 0.1289 0.0123  -0.0040 0.0100  72  TYR   C C   
1616 O O   . TYR   B 66  ? 0.1450 0.1277 0.1272 0.0119  -0.0053 0.0111  72  TYR   C O   
1617 C CB  . TYR   B 66  ? 0.1650 0.1479 0.1416 0.0119  -0.0019 0.0113  72  TYR   C CB  
1618 C CG  . TYR   B 66  ? 0.1836 0.1660 0.1547 0.0115  -0.0005 0.0115  72  TYR   C CG  
1619 C CD1 . TYR   B 66  ? 0.2015 0.1812 0.1686 0.0127  0.0022  0.0099  72  TYR   C CD1 
1620 C CD2 . TYR   B 66  ? 0.1911 0.1759 0.1611 0.0103  -0.0017 0.0134  72  TYR   C CD2 
1621 C CE1 . TYR   B 66  ? 0.2265 0.2055 0.1872 0.0127  0.0037  0.0101  72  TYR   C CE1 
1622 C CE2 . TYR   B 66  ? 0.2081 0.1927 0.1721 0.0102  -0.0006 0.0140  72  TYR   C CE2 
1623 C CZ  . TYR   B 66  ? 0.2228 0.2043 0.1814 0.0114  0.0021  0.0121  72  TYR   C CZ  
1624 O OH  . TYR   B 66  ? 0.2537 0.2348 0.2050 0.0115  0.0034  0.0128  72  TYR   C OH  
1625 N N   . PRO   B 67  ? 0.1543 0.1323 0.1337 0.0139  -0.0030 0.0091  73  PRO   C N   
1626 C CA  . PRO   B 67  ? 0.1533 0.1324 0.1368 0.0154  -0.0038 0.0097  73  PRO   C CA  
1627 C C   . PRO   B 67  ? 0.1598 0.1427 0.1485 0.0166  -0.0035 0.0103  73  PRO   C C   
1628 O O   . PRO   B 67  ? 0.1802 0.1635 0.1700 0.0173  -0.0014 0.0102  73  PRO   C O   
1629 C CB  . PRO   B 67  ? 0.1792 0.1548 0.1619 0.0169  -0.0028 0.0089  73  PRO   C CB  
1630 C CG  . PRO   B 67  ? 0.2146 0.1880 0.1944 0.0167  -0.0004 0.0075  73  PRO   C CG  
1631 C CD  . PRO   B 67  ? 0.1733 0.1475 0.1494 0.0145  -0.0010 0.0074  73  PRO   C CD  
1632 N N   . VAL   B 68  ? 0.1405 0.1261 0.1326 0.0167  -0.0053 0.0107  74  VAL   C N   
1633 C CA  . VAL   B 68  ? 0.1479 0.1372 0.1461 0.0174  -0.0054 0.0110  74  VAL   C CA  
1634 C C   . VAL   B 68  ? 0.1465 0.1372 0.1476 0.0185  -0.0078 0.0105  74  VAL   C C   
1635 O O   . VAL   B 68  ? 0.1489 0.1383 0.1467 0.0184  -0.0093 0.0105  74  VAL   C O   
1636 C CB  . VAL   B 68  ? 0.1709 0.1626 0.1708 0.0158  -0.0053 0.0117  74  VAL   C CB  
1637 C CG1 . VAL   B 68  ? 0.2064 0.1976 0.2039 0.0151  -0.0030 0.0126  74  VAL   C CG1 
1638 C CG2 . VAL   B 68  ? 0.1783 0.1696 0.1761 0.0145  -0.0070 0.0118  74  VAL   C CG2 
1639 N N   . SER   B 69  ? 0.1411 0.1347 0.1485 0.0196  -0.0082 0.0103  75  SER   C N   
1640 C CA  . SER   B 69  ? 0.1435 0.1395 0.1547 0.0202  -0.0112 0.0094  75  SER   C CA  
1641 C C   . SER   B 69  ? 0.1303 0.1288 0.1454 0.0188  -0.0114 0.0090  75  SER   C C   
1642 O O   . SER   B 69  ? 0.1334 0.1330 0.1518 0.0181  -0.0091 0.0098  75  SER   C O   
1643 C CB  . SER   B 69  ? 0.1564 0.1545 0.1741 0.0220  -0.0119 0.0093  75  SER   C CB  
1644 O OG  . SER   B 69  ? 0.2309 0.2267 0.2458 0.0235  -0.0116 0.0100  75  SER   C OG  
1645 N N   . PHE   B 70  ? 0.1259 0.1251 0.1406 0.0184  -0.0137 0.0078  76  PHE   C N   
1646 C CA  . PHE   B 70  ? 0.1244 0.1254 0.1433 0.0170  -0.0135 0.0071  76  PHE   C CA  
1647 C C   . PHE   B 70  ? 0.1313 0.1341 0.1537 0.0174  -0.0167 0.0047  76  PHE   C C   
1648 O O   . PHE   B 70  ? 0.1365 0.1386 0.1548 0.0186  -0.0191 0.0037  76  PHE   C O   
1649 C CB  . PHE   B 70  ? 0.1321 0.1314 0.1464 0.0155  -0.0123 0.0080  76  PHE   C CB  
1650 C CG  . PHE   B 70  ? 0.1202 0.1169 0.1275 0.0158  -0.0133 0.0076  76  PHE   C CG  
1651 C CD1 . PHE   B 70  ? 0.1329 0.1269 0.1345 0.0161  -0.0126 0.0088  76  PHE   C CD1 
1652 C CD2 . PHE   B 70  ? 0.1400 0.1368 0.1466 0.0157  -0.0146 0.0061  76  PHE   C CD2 
1653 C CE1 . PHE   B 70  ? 0.1328 0.1245 0.1290 0.0165  -0.0131 0.0090  76  PHE   C CE1 
1654 C CE2 . PHE   B 70  ? 0.1416 0.1358 0.1414 0.0162  -0.0148 0.0062  76  PHE   C CE2 
1655 C CZ  . PHE   B 70  ? 0.1433 0.1351 0.1384 0.0166  -0.0140 0.0079  76  PHE   C CZ  
1656 N N   . SER   B 71  ? 0.1223 0.1273 0.1519 0.0164  -0.0166 0.0037  77  SER   C N   
1657 C CA  . SER   B 71  ? 0.1322 0.1390 0.1662 0.0165  -0.0197 0.0008  77  SER   C CA  
1658 C C   . SER   B 71  ? 0.1471 0.1522 0.1753 0.0162  -0.0210 -0.0013 77  SER   C C   
1659 O O   . SER   B 71  ? 0.1563 0.1590 0.1785 0.0157  -0.0191 0.0000  77  SER   C O   
1660 C CB  . SER   B 71  ? 0.1346 0.1443 0.1800 0.0156  -0.0189 0.0003  77  SER   C CB  
1661 O OG  . SER   B 71  ? 0.1566 0.1658 0.2036 0.0142  -0.0160 0.0014  77  SER   C OG  
1662 N N   . LYS   B 72  ? 0.1610 0.1672 0.1915 0.0163  -0.0242 -0.0046 78  LYS   C N   
1663 C CA  . LYS   B 72  ? 0.1650 0.1693 0.1896 0.0161  -0.0251 -0.0070 78  LYS   C CA  
1664 C C   . LYS   B 72  ? 0.1623 0.1664 0.1923 0.0144  -0.0226 -0.0078 78  LYS   C C   
1665 O O   . LYS   B 72  ? 0.1843 0.1907 0.2244 0.0134  -0.0218 -0.0077 78  LYS   C O   
1666 C CB  . LYS   B 72  ? 0.2007 0.2062 0.2254 0.0170  -0.0299 -0.0108 78  LYS   C CB  
1667 C CG  . LYS   B 72  ? 0.2458 0.2517 0.2658 0.0189  -0.0327 -0.0097 78  LYS   C CG  
1668 C CD  . LYS   B 72  ? 0.3973 0.4038 0.4126 0.0202  -0.0378 -0.0130 78  LYS   C CD  
1669 C CE  . LYS   B 72  ? 0.5138 0.5186 0.5189 0.0224  -0.0388 -0.0104 78  LYS   C CE  
1670 N NZ  . LYS   B 72  ? 0.5848 0.5888 0.5808 0.0239  -0.0426 -0.0129 78  LYS   C NZ  
1671 N N   . PRO   B 73  ? 0.1551 0.1567 0.1797 0.0140  -0.0208 -0.0081 79  PRO   C N   
1672 C CA  . PRO   B 73  ? 0.1636 0.1649 0.1942 0.0125  -0.0180 -0.0081 79  PRO   C CA  
1673 C C   . PRO   B 73  ? 0.1708 0.1736 0.2100 0.0118  -0.0196 -0.0120 79  PRO   C C   
1674 O O   . PRO   B 73  ? 0.1928 0.1952 0.2295 0.0123  -0.0229 -0.0162 79  PRO   C O   
1675 C CB  . PRO   B 73  ? 0.1897 0.1880 0.2127 0.0127  -0.0165 -0.0087 79  PRO   C CB  
1676 C CG  . PRO   B 73  ? 0.2242 0.2209 0.2371 0.0141  -0.0174 -0.0072 79  PRO   C CG  
1677 C CD  . PRO   B 73  ? 0.1683 0.1670 0.1817 0.0152  -0.0209 -0.0078 79  PRO   C CD  
1678 N N   . SER   B 74  ? 0.1569 0.1616 0.2068 0.0106  -0.0177 -0.0107 80  SER   C N   
1679 C CA  . SER   B 74  ? 0.1679 0.1742 0.2286 0.0097  -0.0190 -0.0140 80  SER   C CA  
1680 C C   . SER   B 74  ? 0.1569 0.1638 0.2279 0.0084  -0.0152 -0.0120 80  SER   C C   
1681 O O   . SER   B 74  ? 0.1551 0.1615 0.2244 0.0083  -0.0120 -0.0078 80  SER   C O   
1682 C CB  . SER   B 74  ? 0.2023 0.2116 0.2685 0.0102  -0.0215 -0.0139 80  SER   C CB  
1683 O OG  . SER   B 74  ? 0.3242 0.3332 0.3814 0.0116  -0.0250 -0.0151 80  SER   C OG  
1684 N N   . LEU   B 75  ? 0.1650 0.1729 0.2469 0.0075  -0.0158 -0.0150 81  LEU   C N   
1685 C CA  . LEU   B 75  ? 0.1721 0.1806 0.2658 0.0063  -0.0122 -0.0131 81  LEU   C CA  
1686 C C   . LEU   B 75  ? 0.1776 0.1893 0.2798 0.0064  -0.0112 -0.0095 81  LEU   C C   
1687 O O   . LEU   B 75  ? 0.2044 0.2180 0.3129 0.0064  -0.0139 -0.0119 81  LEU   C O   
1688 C CB  . LEU   B 75  ? 0.1994 0.2070 0.3010 0.0053  -0.0135 -0.0188 81  LEU   C CB  
1689 C CG  . LEU   B 75  ? 0.2217 0.2293 0.3365 0.0041  -0.0096 -0.0175 81  LEU   C CG  
1690 C CD1 . LEU   B 75  ? 0.2126 0.2182 0.3235 0.0042  -0.0058 -0.0144 81  LEU   C CD1 
1691 C CD2 . LEU   B 75  ? 0.2556 0.2621 0.3791 0.0029  -0.0115 -0.0242 81  LEU   C CD2 
1692 N N   . ILE   B 76  ? 0.1821 0.1944 0.2840 0.0067  -0.0076 -0.0038 82  ILE   C N   
1693 C CA  . ILE   B 76  ? 0.1966 0.2113 0.3036 0.0071  -0.0057 0.0004  82  ILE   C CA  
1694 C C   . ILE   B 76  ? 0.1886 0.2042 0.3052 0.0066  -0.0014 0.0047  82  ILE   C C   
1695 O O   . ILE   B 76  ? 0.1706 0.1850 0.2843 0.0064  0.0006  0.0070  82  ILE   C O   
1696 C CB  . ILE   B 76  ? 0.2389 0.2531 0.3338 0.0082  -0.0056 0.0035  82  ILE   C CB  
1697 C CG1 . ILE   B 76  ? 0.2742 0.2876 0.3604 0.0090  -0.0097 -0.0001 82  ILE   C CG1 
1698 C CG2 . ILE   B 76  ? 0.2659 0.2821 0.3641 0.0089  -0.0028 0.0080  82  ILE   C CG2 
1699 C CD1 . ILE   B 76  ? 0.2791 0.2917 0.3553 0.0100  -0.0097 0.0021  82  ILE   C CD1 
1700 N N   . PHE   B 77  ? 0.1888 0.2067 0.3168 0.0066  0.0004  0.0064  83  PHE   C N   
1701 C CA  . PHE   B 77  ? 0.1909 0.2097 0.3275 0.0065  0.0050  0.0115  83  PHE   C CA  
1702 C C   . PHE   B 77  ? 0.2008 0.2199 0.3277 0.0077  0.0073  0.0172  83  PHE   C C   
1703 O O   . PHE   B 77  ? 0.2259 0.2458 0.3488 0.0086  0.0071  0.0179  83  PHE   C O   
1704 C CB  . PHE   B 77  ? 0.1835 0.2045 0.3359 0.0063  0.0067  0.0119  83  PHE   C CB  
1705 C CG  . PHE   B 77  ? 0.1881 0.2097 0.3504 0.0061  0.0117  0.0171  83  PHE   C CG  
1706 C CD1 . PHE   B 77  ? 0.1967 0.2169 0.3657 0.0051  0.0125  0.0160  83  PHE   C CD1 
1707 C CD2 . PHE   B 77  ? 0.2101 0.2333 0.3740 0.0073  0.0158  0.0235  83  PHE   C CD2 
1708 C CE1 . PHE   B 77  ? 0.2127 0.2335 0.3915 0.0052  0.0172  0.0214  83  PHE   C CE1 
1709 C CE2 . PHE   B 77  ? 0.2145 0.2383 0.3871 0.0075  0.0205  0.0289  83  PHE   C CE2 
1710 C CZ  . PHE   B 77  ? 0.2096 0.2323 0.3900 0.0064  0.0210  0.0280  83  PHE   C CZ  
1711 N N   . VAL   B 78  ? 0.1706 0.1891 0.2944 0.0077  0.0095  0.0212  84  VAL   C N   
1712 C CA  . VAL   B 78  ? 0.1640 0.1827 0.2783 0.0086  0.0112  0.0263  84  VAL   C CA  
1713 C C   . VAL   B 78  ? 0.1578 0.1782 0.2803 0.0091  0.0157  0.0323  84  VAL   C C   
1714 O O   . VAL   B 78  ? 0.1583 0.1787 0.2895 0.0085  0.0171  0.0335  84  VAL   C O   
1715 C CB  . VAL   B 78  ? 0.1649 0.1819 0.2689 0.0082  0.0094  0.0261  84  VAL   C CB  
1716 C CG1 . VAL   B 78  ? 0.1725 0.1898 0.2666 0.0089  0.0104  0.0309  84  VAL   C CG1 
1717 C CG2 . VAL   B 78  ? 0.1738 0.1891 0.2706 0.0079  0.0056  0.0204  84  VAL   C CG2 
1718 N N   . GLU   B 79  ? 0.1423 0.1636 0.2610 0.0103  0.0181  0.0365  85  GLU   C N   
1719 C CA  . GLU   B 79  ? 0.1451 0.1678 0.2695 0.0111  0.0227  0.0430  85  GLU   C CA  
1720 C C   . GLU   B 79  ? 0.1439 0.1665 0.2626 0.0111  0.0227  0.0470  85  GLU   C C   
1721 O O   . GLU   B 79  ? 0.1467 0.1681 0.2555 0.0105  0.0194  0.0450  85  GLU   C O   
1722 C CB  . GLU   B 79  ? 0.1713 0.1947 0.2912 0.0127  0.0255  0.0462  85  GLU   C CB  
1723 C CG  . GLU   B 79  ? 0.2121 0.2362 0.3407 0.0130  0.0263  0.0435  85  GLU   C CG  
1724 C CD  . GLU   B 79  ? 0.2695 0.2951 0.4165 0.0124  0.0288  0.0442  85  GLU   C CD  
1725 O OE1 . GLU   B 79  ? 0.2985 0.3247 0.4515 0.0127  0.0324  0.0494  85  GLU   C OE1 
1726 O OE2 . GLU   B 79  ? 0.2870 0.3130 0.4431 0.0116  0.0268  0.0395  85  GLU   C OE2 
1727 N N   . ALA   B 80  ? 0.1548 0.1787 0.2803 0.0117  0.0264  0.0530  86  ALA   C N   
1728 C CA  . ALA   B 80  ? 0.1671 0.1915 0.2887 0.0118  0.0263  0.0576  86  ALA   C CA  
1729 C C   . ALA   B 80  ? 0.1802 0.2042 0.2852 0.0123  0.0242  0.0590  86  ALA   C C   
1730 O O   . ALA   B 80  ? 0.2018 0.2257 0.2995 0.0133  0.0252  0.0593  86  ALA   C O   
1731 C CB  . ALA   B 80  ? 0.1754 0.2014 0.3064 0.0129  0.0309  0.0647  86  ALA   C CB  
1732 N N   . SER   B 81  ? 0.1630 0.1869 0.2628 0.0116  0.0214  0.0593  87  SER   C N   
1733 C CA  . SER   B 81  ? 0.1798 0.2036 0.2654 0.0118  0.0190  0.0607  87  SER   C CA  
1734 C C   . SER   B 81  ? 0.1878 0.2135 0.2743 0.0121  0.0191  0.0671  87  SER   C C   
1735 O O   . SER   B 81  ? 0.1939 0.2208 0.2925 0.0123  0.0214  0.0704  87  SER   C O   
1736 C CB  . SER   B 81  ? 0.1735 0.1955 0.2522 0.0105  0.0148  0.0551  87  SER   C CB  
1737 O OG  . SER   B 81  ? 0.1756 0.1977 0.2610 0.0096  0.0138  0.0547  87  SER   C OG  
1738 N N   . GLU   B 82  ? 0.2086 0.2345 0.2830 0.0121  0.0162  0.0687  88  GLU   C N   
1739 C CA  . GLU   B 82  ? 0.2210 0.2492 0.2964 0.0124  0.0155  0.0748  88  GLU   C CA  
1740 C C   . GLU   B 82  ? 0.2211 0.2497 0.3060 0.0112  0.0141  0.0741  88  GLU   C C   
1741 O O   . GLU   B 82  ? 0.2379 0.2686 0.3288 0.0116  0.0145  0.0796  88  GLU   C O   
1742 C CB  . GLU   B 82  ? 0.2853 0.3139 0.3457 0.0126  0.0123  0.0767  88  GLU   C CB  
1743 C CG  . GLU   B 82  ? 0.4003 0.4278 0.4533 0.0110  0.0075  0.0721  88  GLU   C CG  
1744 C CD  . GLU   B 82  ? 0.4621 0.4903 0.5019 0.0110  0.0042  0.0743  88  GLU   C CD  
1745 O OE1 . GLU   B 82  ? 0.4564 0.4845 0.4882 0.0124  0.0058  0.0765  88  GLU   C OE1 
1746 O OE2 . GLU   B 82  ? 0.4774 0.5062 0.5151 0.0097  0.0000  0.0737  88  GLU   C OE2 
1747 N N   . TYR   B 83  ? 0.1861 0.2126 0.2728 0.0100  0.0129  0.0676  89  TYR   C N   
1748 C CA  . TYR   B 83  ? 0.1709 0.1972 0.2648 0.0090  0.0119  0.0663  89  TYR   C CA  
1749 C C   . TYR   B 83  ? 0.1748 0.1994 0.2805 0.0087  0.0144  0.0622  89  TYR   C C   
1750 O O   . TYR   B 83  ? 0.1787 0.2029 0.2915 0.0081  0.0146  0.0616  89  TYR   C O   
1751 C CB  . TYR   B 83  ? 0.1669 0.1921 0.2515 0.0079  0.0079  0.0627  89  TYR   C CB  
1752 C CG  . TYR   B 83  ? 0.1664 0.1891 0.2418 0.0076  0.0068  0.0569  89  TYR   C CG  
1753 C CD1 . TYR   B 83  ? 0.1635 0.1860 0.2275 0.0080  0.0055  0.0573  89  TYR   C CD1 
1754 C CD2 . TYR   B 83  ? 0.1672 0.1876 0.2451 0.0071  0.0069  0.0510  89  TYR   C CD2 
1755 C CE1 . TYR   B 83  ? 0.1611 0.1814 0.2180 0.0079  0.0048  0.0523  89  TYR   C CE1 
1756 C CE2 . TYR   B 83  ? 0.1698 0.1883 0.2401 0.0070  0.0058  0.0463  89  TYR   C CE2 
1757 C CZ  . TYR   B 83  ? 0.1642 0.1827 0.2246 0.0075  0.0048  0.0471  89  TYR   C CZ  
1758 O OH  . TYR   B 83  ? 0.1756 0.1921 0.2295 0.0076  0.0040  0.0428  89  TYR   C OH  
1759 N N   . TYR   B 84  ? 0.1488 0.1725 0.2574 0.0089  0.0162  0.0594  90  TYR   C N   
1760 C CA  . TYR   B 84  ? 0.1518 0.1742 0.2724 0.0084  0.0183  0.0556  90  TYR   C CA  
1761 C C   . TYR   B 84  ? 0.1508 0.1741 0.2789 0.0092  0.0215  0.0574  90  TYR   C C   
1762 O O   . TYR   B 84  ? 0.1520 0.1759 0.2733 0.0100  0.0218  0.0587  90  TYR   C O   
1763 C CB  . TYR   B 84  ? 0.1409 0.1608 0.2569 0.0076  0.0159  0.0475  90  TYR   C CB  
1764 C CG  . TYR   B 84  ? 0.1242 0.1426 0.2357 0.0068  0.0137  0.0448  90  TYR   C CG  
1765 C CD1 . TYR   B 84  ? 0.1229 0.1408 0.2431 0.0065  0.0151  0.0452  90  TYR   C CD1 
1766 C CD2 . TYR   B 84  ? 0.1272 0.1445 0.2268 0.0065  0.0108  0.0419  90  TYR   C CD2 
1767 C CE1 . TYR   B 84  ? 0.1337 0.1502 0.2503 0.0060  0.0138  0.0429  90  TYR   C CE1 
1768 C CE2 . TYR   B 84  ? 0.1336 0.1494 0.2296 0.0060  0.0093  0.0397  90  TYR   C CE2 
1769 C CZ  . TYR   B 84  ? 0.1324 0.1478 0.2368 0.0057  0.0109  0.0402  90  TYR   C CZ  
1770 O OH  . TYR   B 84  ? 0.1357 0.1496 0.2370 0.0053  0.0102  0.0382  90  TYR   C OH  
1771 N N   . PRO   B 85  ? 0.1541 0.1770 0.2966 0.0089  0.0242  0.0567  91  PRO   C N   
1772 C CA  . PRO   B 85  ? 0.1448 0.1682 0.2960 0.0094  0.0271  0.0572  91  PRO   C CA  
1773 C C   . PRO   B 85  ? 0.1467 0.1689 0.2943 0.0088  0.0249  0.0501  91  PRO   C C   
1774 O O   . PRO   B 85  ? 0.1468 0.1674 0.2860 0.0080  0.0214  0.0447  91  PRO   C O   
1775 C CB  . PRO   B 85  ? 0.1447 0.1675 0.3127 0.0089  0.0299  0.0573  91  PRO   C CB  
1776 C CG  . PRO   B 85  ? 0.1659 0.1868 0.3321 0.0078  0.0274  0.0521  91  PRO   C CG  
1777 C CD  . PRO   B 85  ? 0.1569 0.1784 0.3086 0.0081  0.0246  0.0543  91  PRO   C CD  
1778 N N   . ALA   B 86  ? 0.1428 0.1657 0.2977 0.0091  0.0270  0.0500  92  ALA   C N   
1779 C CA  . ALA   B 86  ? 0.1563 0.1785 0.3111 0.0085  0.0249  0.0436  92  ALA   C CA  
1780 C C   . ALA   B 86  ? 0.1646 0.1849 0.3261 0.0070  0.0227  0.0369  92  ALA   C C   
1781 O O   . ALA   B 86  ? 0.1807 0.2007 0.3543 0.0065  0.0250  0.0378  92  ALA   C O   
1782 C CB  . ALA   B 86  ? 0.1515 0.1752 0.3165 0.0091  0.0281  0.0456  92  ALA   C CB  
1783 N N   . ARG   B 87  ? 0.1614 0.1803 0.3143 0.0065  0.0187  0.0307  93  ARG   C N   
1784 C CA  . ARG   B 87  ? 0.1561 0.1730 0.3122 0.0053  0.0166  0.0244  93  ARG   C CA  
1785 C C   . ARG   B 87  ? 0.1616 0.1774 0.3077 0.0051  0.0122  0.0182  93  ARG   C C   
1786 O O   . ARG   B 87  ? 0.1568 0.1733 0.2929 0.0059  0.0109  0.0194  93  ARG   C O   
1787 C CB  . ARG   B 87  ? 0.1723 0.1878 0.3251 0.0052  0.0172  0.0259  93  ARG   C CB  
1788 C CG  . ARG   B 87  ? 0.1501 0.1651 0.2867 0.0056  0.0148  0.0264  93  ARG   C CG  
1789 C CD  . ARG   B 87  ? 0.1618 0.1763 0.2967 0.0056  0.0157  0.0293  93  ARG   C CD  
1790 N NE  . ARG   B 87  ? 0.1570 0.1706 0.2780 0.0057  0.0129  0.0279  93  ARG   C NE  
1791 C CZ  . ARG   B 87  ? 0.1647 0.1764 0.2817 0.0054  0.0121  0.0258  93  ARG   C CZ  
1792 N NH1 . ARG   B 87  ? 0.1791 0.1896 0.3047 0.0050  0.0142  0.0249  93  ARG   C NH1 
1793 N NH2 . ARG   B 87  ? 0.1743 0.1852 0.2794 0.0055  0.0097  0.0245  93  ARG   C NH2 
1794 N N   . TYR   B 88  ? 0.1721 0.1860 0.3202 0.0042  0.0100  0.0117  94  TYR   C N   
1795 C CA  . TYR   B 88  ? 0.1959 0.2086 0.3329 0.0043  0.0058  0.0064  94  TYR   C CA  
1796 C C   . TYR   B 88  ? 0.1698 0.1806 0.2946 0.0046  0.0054  0.0069  94  TYR   C C   
1797 O O   . TYR   B 88  ? 0.1790 0.1884 0.3065 0.0043  0.0074  0.0076  94  TYR   C O   
1798 C CB  . TYR   B 88  ? 0.2301 0.2413 0.3727 0.0034  0.0033  -0.0011 94  TYR   C CB  
1799 C CG  . TYR   B 88  ? 0.2467 0.2599 0.4003 0.0029  0.0023  -0.0027 94  TYR   C CG  
1800 C CD1 . TYR   B 88  ? 0.2624 0.2772 0.4115 0.0034  -0.0010 -0.0043 94  TYR   C CD1 
1801 C CD2 . TYR   B 88  ? 0.2494 0.2633 0.4194 0.0021  0.0051  -0.0019 94  TYR   C CD2 
1802 C CE1 . TYR   B 88  ? 0.2690 0.2861 0.4298 0.0031  -0.0017 -0.0053 94  TYR   C CE1 
1803 C CE2 . TYR   B 88  ? 0.2576 0.2737 0.4394 0.0016  0.0046  -0.0029 94  TYR   C CE2 
1804 C CZ  . TYR   B 88  ? 0.2666 0.2844 0.4439 0.0021  0.0010  -0.0047 94  TYR   C CZ  
1805 O OH  . TYR   B 88  ? 0.3006 0.3208 0.4915 0.0016  0.0007  -0.0053 94  TYR   C OH  
1806 N N   . GLN   B 89  ? 0.1618 0.1726 0.2743 0.0053  0.0032  0.0070  95  GLN   C N   
1807 C CA  . GLN   B 89  ? 0.1453 0.1542 0.2464 0.0056  0.0025  0.0071  95  GLN   C CA  
1808 C C   . GLN   B 89  ? 0.1484 0.1556 0.2413 0.0059  -0.0010 0.0014  95  GLN   C C   
1809 O O   . GLN   B 89  ? 0.1596 0.1678 0.2509 0.0063  -0.0034 -0.0003 95  GLN   C O   
1810 C CB  . GLN   B 89  ? 0.1587 0.1688 0.2525 0.0062  0.0030  0.0125  95  GLN   C CB  
1811 C CG  . GLN   B 89  ? 0.1709 0.1793 0.2544 0.0063  0.0023  0.0129  95  GLN   C CG  
1812 C CD  . GLN   B 89  ? 0.1479 0.1575 0.2271 0.0064  0.0031  0.0185  95  GLN   C CD  
1813 O OE1 . GLN   B 89  ? 0.1571 0.1685 0.2416 0.0064  0.0050  0.0230  95  GLN   C OE1 
1814 N NE2 . GLN   B 89  ? 0.1460 0.1544 0.2152 0.0065  0.0015  0.0182  95  GLN   C NE2 
1815 N N   . SER   B 90  ? 0.1378 0.1424 0.2256 0.0059  -0.0011 -0.0012 96  SER   C N   
1816 C CA  . SER   B 90  ? 0.1423 0.1451 0.2214 0.0064  -0.0040 -0.0062 96  SER   C CA  
1817 C C   . SER   B 90  ? 0.1401 0.1419 0.2064 0.0073  -0.0049 -0.0042 96  SER   C C   
1818 O O   . SER   B 90  ? 0.1366 0.1387 0.2010 0.0072  -0.0030 0.0003  96  SER   C O   
1819 C CB  . SER   B 90  ? 0.1652 0.1651 0.2455 0.0061  -0.0033 -0.0109 96  SER   C CB  
1820 O OG  . SER   B 90  ? 0.1746 0.1730 0.2524 0.0062  -0.0003 -0.0081 96  SER   C OG  
1821 N N   . HIS   B 91  ? 0.1444 0.1451 0.2025 0.0081  -0.0078 -0.0077 97  HIS   C N   
1822 C CA  . HIS   B 91  ? 0.1447 0.1441 0.1912 0.0091  -0.0086 -0.0064 97  HIS   C CA  
1823 C C   . HIS   B 91  ? 0.1436 0.1448 0.1891 0.0091  -0.0082 -0.0015 97  HIS   C C   
1824 O O   . HIS   B 91  ? 0.1541 0.1541 0.1933 0.0092  -0.0072 0.0011  97  HIS   C O   
1825 C CB  . HIS   B 91  ? 0.1601 0.1569 0.2019 0.0091  -0.0062 -0.0060 97  HIS   C CB  
1826 C CG  . HIS   B 91  ? 0.1697 0.1640 0.2103 0.0094  -0.0061 -0.0111 97  HIS   C CG  
1827 N ND1 . HIS   B 91  ? 0.2041 0.1962 0.2342 0.0106  -0.0077 -0.0139 97  HIS   C ND1 
1828 C CD2 . HIS   B 91  ? 0.1779 0.1716 0.2265 0.0086  -0.0047 -0.0138 97  HIS   C CD2 
1829 C CE1 . HIS   B 91  ? 0.2103 0.2003 0.2410 0.0106  -0.0072 -0.0185 97  HIS   C CE1 
1830 N NE2 . HIS   B 91  ? 0.2061 0.1969 0.2482 0.0094  -0.0053 -0.0188 97  HIS   C NE2 
1831 N N   . LEU   B 92  ? 0.1267 0.1302 0.1781 0.0090  -0.0088 -0.0008 98  LEU   C N   
1832 C CA  . LEU   B 92  ? 0.1287 0.1336 0.1794 0.0091  -0.0079 0.0033  98  LEU   C CA  
1833 C C   . LEU   B 92  ? 0.1286 0.1339 0.1751 0.0101  -0.0102 0.0023  98  LEU   C C   
1834 O O   . LEU   B 92  ? 0.1290 0.1351 0.1785 0.0105  -0.0125 -0.0009 98  LEU   C O   
1835 C CB  . LEU   B 92  ? 0.1419 0.1492 0.2032 0.0085  -0.0057 0.0057  98  LEU   C CB  
1836 C CG  . LEU   B 92  ? 0.1501 0.1586 0.2098 0.0087  -0.0042 0.0102  98  LEU   C CG  
1837 C CD1 . LEU   B 92  ? 0.1507 0.1582 0.2048 0.0083  -0.0032 0.0133  98  LEU   C CD1 
1838 C CD2 . LEU   B 92  ? 0.1771 0.1879 0.2473 0.0085  -0.0019 0.0126  98  LEU   C CD2 
1839 N N   . MET   B 93  ? 0.1226 0.1273 0.1628 0.0106  -0.0098 0.0049  99  MET   C N   
1840 C CA  . MET   B 93  ? 0.1127 0.1175 0.1493 0.0118  -0.0114 0.0045  99  MET   C CA  
1841 C C   . MET   B 93  ? 0.1274 0.1333 0.1656 0.0118  -0.0094 0.0077  99  MET   C C   
1842 O O   . MET   B 93  ? 0.1408 0.1460 0.1766 0.0112  -0.0075 0.0104  99  MET   C O   
1843 C CB  . MET   B 93  ? 0.1412 0.1434 0.1677 0.0124  -0.0123 0.0046  99  MET   C CB  
1844 C CG  . MET   B 93  ? 0.1564 0.1571 0.1796 0.0126  -0.0137 0.0019  99  MET   C CG  
1845 S SD  . MET   B 93  ? 0.1724 0.1699 0.1848 0.0134  -0.0136 0.0028  99  MET   C SD  
1846 C CE  . MET   B 93  ? 0.1809 0.1777 0.1938 0.0119  -0.0106 0.0061  99  MET   C CE  
1847 N N   . LEU   B 94  ? 0.1234 0.1307 0.1653 0.0127  -0.0096 0.0075  100 LEU   C N   
1848 C CA  . LEU   B 94  ? 0.1298 0.1377 0.1727 0.0130  -0.0070 0.0104  100 LEU   C CA  
1849 C C   . LEU   B 94  ? 0.1250 0.1314 0.1617 0.0142  -0.0073 0.0105  100 LEU   C C   
1850 O O   . LEU   B 94  ? 0.1367 0.1429 0.1724 0.0152  -0.0097 0.0086  100 LEU   C O   
1851 C CB  . LEU   B 94  ? 0.1334 0.1441 0.1875 0.0133  -0.0058 0.0107  100 LEU   C CB  
1852 C CG  . LEU   B 94  ? 0.1468 0.1591 0.2096 0.0122  -0.0048 0.0109  100 LEU   C CG  
1853 C CD1 . LEU   B 94  ? 0.1885 0.2034 0.2631 0.0125  -0.0033 0.0115  100 LEU   C CD1 
1854 C CD2 . LEU   B 94  ? 0.1761 0.1876 0.2360 0.0114  -0.0024 0.0140  100 LEU   C CD2 
1855 N N   . ALA   B 95  ? 0.1283 0.1338 0.1614 0.0143  -0.0048 0.0128  101 ALA   C N   
1856 C CA  . ALA   B 95  ? 0.1321 0.1359 0.1605 0.0155  -0.0041 0.0129  101 ALA   C CA  
1857 C C   . ALA   B 95  ? 0.1327 0.1371 0.1627 0.0159  -0.0005 0.0152  101 ALA   C C   
1858 O O   . ALA   B 95  ? 0.1283 0.1338 0.1602 0.0152  0.0012  0.0171  101 ALA   C O   
1859 C CB  . ALA   B 95  ? 0.1473 0.1479 0.1659 0.0151  -0.0049 0.0128  101 ALA   C CB  
1860 N N   . VAL   B 96  ? 0.1337 0.1371 0.1627 0.0173  0.0010  0.0151  102 VAL   C N   
1861 C CA  . VAL   B 96  ? 0.1497 0.1527 0.1777 0.0180  0.0051  0.0171  102 VAL   C CA  
1862 C C   . VAL   B 96  ? 0.1594 0.1593 0.1763 0.0173  0.0057  0.0175  102 VAL   C C   
1863 O O   . VAL   B 96  ? 0.1846 0.1817 0.1954 0.0174  0.0044  0.0158  102 VAL   C O   
1864 C CB  . VAL   B 96  ? 0.1618 0.1647 0.1938 0.0199  0.0067  0.0166  102 VAL   C CB  
1865 C CG1 . VAL   B 96  ? 0.1918 0.1938 0.2220 0.0209  0.0117  0.0185  102 VAL   C CG1 
1866 C CG2 . VAL   B 96  ? 0.1705 0.1770 0.2145 0.0203  0.0052  0.0161  102 VAL   C CG2 
1867 N N   . GLY   B 97  ? 0.1690 0.1695 0.1838 0.0165  0.0071  0.0196  103 GLY   C N   
1868 C CA  . GLY   B 97  ? 0.1827 0.1807 0.1872 0.0157  0.0068  0.0198  103 GLY   C CA  
1869 C C   . GLY   B 97  ? 0.1819 0.1814 0.1852 0.0149  0.0076  0.0226  103 GLY   C C   
1870 O O   . GLY   B 97  ? 0.2025 0.2049 0.2136 0.0149  0.0087  0.0247  103 GLY   C O   
1871 N N   . HIS   B 98  ? 0.1845 0.1822 0.1787 0.0142  0.0071  0.0230  104 HIS   C N   
1872 C CA  . HIS   B 98  ? 0.1855 0.1848 0.1773 0.0136  0.0075  0.0261  104 HIS   C CA  
1873 C C   . HIS   B 98  ? 0.1701 0.1711 0.1646 0.0119  0.0043  0.0272  104 HIS   C C   
1874 O O   . HIS   B 98  ? 0.1750 0.1747 0.1673 0.0108  0.0013  0.0251  104 HIS   C O   
1875 C CB  . HIS   B 98  ? 0.2273 0.2239 0.2075 0.0136  0.0079  0.0257  104 HIS   C CB  
1876 C CG  . HIS   B 98  ? 0.2491 0.2474 0.2258 0.0134  0.0083  0.0293  104 HIS   C CG  
1877 N ND1 . HIS   B 98  ? 0.2712 0.2715 0.2514 0.0149  0.0122  0.0328  104 HIS   C ND1 
1878 C CD2 . HIS   B 98  ? 0.2768 0.2754 0.2479 0.0120  0.0051  0.0303  104 HIS   C CD2 
1879 C CE1 . HIS   B 98  ? 0.2950 0.2967 0.2711 0.0144  0.0112  0.0361  104 HIS   C CE1 
1880 N NE2 . HIS   B 98  ? 0.3037 0.3046 0.2740 0.0127  0.0068  0.0346  104 HIS   C NE2 
1881 N N   . SER   B 99  ? 0.1705 0.1743 0.1699 0.0118  0.0052  0.0307  105 SER   C N   
1882 C CA  . SER   B 99  ? 0.1786 0.1843 0.1814 0.0104  0.0027  0.0322  105 SER   C CA  
1883 C C   . SER   B 99  ? 0.1924 0.2007 0.1974 0.0107  0.0043  0.0370  105 SER   C C   
1884 O O   . SER   B 99  ? 0.2232 0.2330 0.2351 0.0118  0.0074  0.0389  105 SER   C O   
1885 C CB  . SER   B 99  ? 0.1884 0.1950 0.2008 0.0102  0.0023  0.0306  105 SER   C CB  
1886 O OG  . SER   B 99  ? 0.1973 0.2054 0.2139 0.0091  0.0008  0.0321  105 SER   C OG  
1887 N N   . GLU   B 100 ? 0.1828 0.1916 0.1825 0.0099  0.0022  0.0391  106 GLU   C N   
1888 C CA  . GLU   B 100 ? 0.1986 0.2101 0.2001 0.0102  0.0029  0.0443  106 GLU   C CA  
1889 C C   . GLU   B 100 ? 0.1765 0.1899 0.1848 0.0088  0.0004  0.0455  106 GLU   C C   
1890 O O   . GLU   B 100 ? 0.1755 0.1877 0.1844 0.0077  -0.0020 0.0423  106 GLU   C O   
1891 C CB  . GLU   B 100 ? 0.2567 0.2676 0.2461 0.0102  0.0014  0.0457  106 GLU   C CB  
1892 C CG  . GLU   B 100 ? 0.3762 0.3851 0.3581 0.0118  0.0047  0.0449  106 GLU   C CG  
1893 C CD  . GLU   B 100 ? 0.4214 0.4288 0.3896 0.0117  0.0029  0.0450  106 GLU   C CD  
1894 O OE1 . GLU   B 100 ? 0.4717 0.4810 0.4371 0.0109  -0.0003 0.0478  106 GLU   C OE1 
1895 O OE2 . GLU   B 100 ? 0.4310 0.4353 0.3915 0.0125  0.0046  0.0421  106 GLU   C OE2 
1896 N N   . PRO   B 101 ? 0.1853 0.2016 0.1992 0.0091  0.0012  0.0504  107 PRO   C N   
1897 C CA  . PRO   B 101 ? 0.1734 0.1912 0.1951 0.0080  -0.0007 0.0516  107 PRO   C CA  
1898 C C   . PRO   B 101 ? 0.1841 0.2013 0.2007 0.0064  -0.0050 0.0501  107 PRO   C C   
1899 O O   . PRO   B 101 ? 0.1833 0.2001 0.2055 0.0055  -0.0059 0.0482  107 PRO   C O   
1900 C CB  . PRO   B 101 ? 0.2058 0.2268 0.2324 0.0088  0.0008  0.0580  107 PRO   C CB  
1901 C CG  . PRO   B 101 ? 0.2521 0.2728 0.2788 0.0104  0.0049  0.0592  107 PRO   C CG  
1902 C CD  . PRO   B 101 ? 0.2206 0.2386 0.2362 0.0107  0.0047  0.0553  107 PRO   C CD  
1903 N N   . GLY   B 102 ? 0.1805 0.1972 0.1867 0.0061  -0.0073 0.0505  108 GLY   C N   
1904 C CA  . GLY   B 102 ? 0.1942 0.2105 0.1966 0.0044  -0.0117 0.0491  108 GLY   C CA  
1905 C C   . GLY   B 102 ? 0.1812 0.1943 0.1820 0.0036  -0.0123 0.0436  108 GLY   C C   
1906 O O   . GLY   B 102 ? 0.1904 0.2029 0.1905 0.0021  -0.0154 0.0423  108 GLY   C O   
1907 N N   . ASP   B 103 ? 0.1627 0.1737 0.1633 0.0046  -0.0095 0.0406  109 ASP   C N   
1908 C CA  . ASP   B 103 ? 0.1539 0.1618 0.1531 0.0041  -0.0099 0.0359  109 ASP   C CA  
1909 C C   . ASP   B 103 ? 0.1530 0.1612 0.1606 0.0038  -0.0095 0.0351  109 ASP   C C   
1910 O O   . ASP   B 103 ? 0.1518 0.1578 0.1585 0.0035  -0.0101 0.0320  109 ASP   C O   
1911 C CB  . ASP   B 103 ? 0.1672 0.1732 0.1634 0.0056  -0.0073 0.0335  109 ASP   C CB  
1912 C CG  . ASP   B 103 ? 0.1888 0.1934 0.1751 0.0059  -0.0074 0.0332  109 ASP   C CG  
1913 O OD1 . ASP   B 103 ? 0.1943 0.1977 0.1745 0.0047  -0.0103 0.0324  109 ASP   C OD1 
1914 O OD2 . ASP   B 103 ? 0.1954 0.1996 0.1800 0.0074  -0.0043 0.0336  109 ASP   C OD2 
1915 N N   . CYS   B 104 ? 0.1364 0.1472 0.1525 0.0041  -0.0082 0.0379  110 CYS   C N   
1916 C CA  . CYS   B 104 ? 0.1334 0.1440 0.1570 0.0038  -0.0075 0.0367  110 CYS   C CA  
1917 C C   . CYS   B 104 ? 0.1373 0.1470 0.1599 0.0026  -0.0097 0.0360  110 CYS   C C   
1918 O O   . CYS   B 104 ? 0.1577 0.1686 0.1788 0.0016  -0.0120 0.0383  110 CYS   C O   
1919 C CB  . CYS   B 104 ? 0.1306 0.1439 0.1636 0.0041  -0.0059 0.0401  110 CYS   C CB  
1920 S SG  . CYS   B 104 ? 0.1562 0.1701 0.1942 0.0055  -0.0025 0.0402  110 CYS   C SG  
1921 N N   . GLY   B 105 ? 0.1253 0.1329 0.1489 0.0027  -0.0090 0.0330  111 GLY   C N   
1922 C CA  . GLY   B 105 ? 0.1394 0.1457 0.1629 0.0017  -0.0101 0.0324  111 GLY   C CA  
1923 C C   . GLY   B 105 ? 0.1385 0.1419 0.1545 0.0014  -0.0114 0.0297  111 GLY   C C   
1924 O O   . GLY   B 105 ? 0.1519 0.1538 0.1682 0.0009  -0.0117 0.0288  111 GLY   C O   
1925 N N   . GLY   B 106 ? 0.1429 0.1455 0.1529 0.0020  -0.0116 0.0284  112 GLY   C N   
1926 C CA  . GLY   B 106 ? 0.1533 0.1528 0.1570 0.0020  -0.0123 0.0257  112 GLY   C CA  
1927 C C   . GLY   B 106 ? 0.1409 0.1383 0.1452 0.0030  -0.0109 0.0233  112 GLY   C C   
1928 O O   . GLY   B 106 ? 0.1370 0.1350 0.1442 0.0041  -0.0094 0.0227  112 GLY   C O   
1929 N N   . ILE   B 107 ? 0.1398 0.1345 0.1415 0.0026  -0.0114 0.0221  113 ILE   C N   
1930 C CA  . ILE   B 107 ? 0.1383 0.1310 0.1398 0.0037  -0.0101 0.0205  113 ILE   C CA  
1931 C C   . ILE   B 107 ? 0.1334 0.1245 0.1307 0.0052  -0.0098 0.0184  113 ILE   C C   
1932 O O   . ILE   B 107 ? 0.1343 0.1242 0.1278 0.0051  -0.0103 0.0177  113 ILE   C O   
1933 C CB  . ILE   B 107 ? 0.1737 0.1642 0.1749 0.0029  -0.0104 0.0208  113 ILE   C CB  
1934 C CG1 . ILE   B 107 ? 0.2142 0.2064 0.2216 0.0022  -0.0096 0.0228  113 ILE   C CG1 
1935 C CG2 . ILE   B 107 ? 0.1786 0.1661 0.1767 0.0043  -0.0091 0.0192  113 ILE   C CG2 
1936 C CD1 . ILE   B 107 ? 0.2612 0.2522 0.2712 0.0011  -0.0094 0.0240  113 ILE   C CD1 
1937 N N   . LEU   B 108 ? 0.1236 0.1148 0.1221 0.0066  -0.0089 0.0172  114 LEU   C N   
1938 C CA  . LEU   B 108 ? 0.1244 0.1142 0.1200 0.0083  -0.0089 0.0155  114 LEU   C CA  
1939 C C   . LEU   B 108 ? 0.1251 0.1124 0.1183 0.0089  -0.0086 0.0152  114 LEU   C C   
1940 O O   . LEU   B 108 ? 0.1340 0.1214 0.1286 0.0090  -0.0079 0.0154  114 LEU   C O   
1941 C CB  . LEU   B 108 ? 0.1225 0.1145 0.1214 0.0093  -0.0088 0.0144  114 LEU   C CB  
1942 C CG  . LEU   B 108 ? 0.1300 0.1212 0.1272 0.0111  -0.0093 0.0127  114 LEU   C CG  
1943 C CD1 . LEU   B 108 ? 0.1479 0.1383 0.1432 0.0117  -0.0092 0.0126  114 LEU   C CD1 
1944 C CD2 . LEU   B 108 ? 0.1416 0.1352 0.1433 0.0117  -0.0098 0.0114  114 LEU   C CD2 
1945 N N   . ARG   B 109 ? 0.1328 0.1176 0.1224 0.0095  -0.0087 0.0148  115 ARG   C N   
1946 C CA  . ARG   B 109 ? 0.1382 0.1204 0.1255 0.0104  -0.0080 0.0152  115 ARG   C CA  
1947 C C   . ARG   B 109 ? 0.1492 0.1299 0.1335 0.0124  -0.0083 0.0145  115 ARG   C C   
1948 O O   . ARG   B 109 ? 0.1580 0.1386 0.1420 0.0127  -0.0088 0.0138  115 ARG   C O   
1949 C CB  . ARG   B 109 ? 0.1863 0.1664 0.1737 0.0088  -0.0077 0.0164  115 ARG   C CB  
1950 C CG  . ARG   B 109 ? 0.2300 0.2085 0.2156 0.0083  -0.0083 0.0156  115 ARG   C CG  
1951 C CD  . ARG   B 109 ? 0.2901 0.2665 0.2766 0.0064  -0.0085 0.0161  115 ARG   C CD  
1952 N NE  . ARG   B 109 ? 0.3803 0.3590 0.3693 0.0043  -0.0098 0.0167  115 ARG   C NE  
1953 C CZ  . ARG   B 109 ? 0.4896 0.4688 0.4824 0.0030  -0.0098 0.0182  115 ARG   C CZ  
1954 N NH1 . ARG   B 109 ? 0.5244 0.5017 0.5185 0.0036  -0.0081 0.0193  115 ARG   C NH1 
1955 N NH2 . ARG   B 109 ? 0.5184 0.5001 0.5140 0.0012  -0.0113 0.0190  115 ARG   C NH2 
1956 N N   . CYS   B 110 ? 0.1454 0.1248 0.1273 0.0139  -0.0079 0.0150  116 CYS   C N   
1957 C CA  . CYS   B 110 ? 0.1579 0.1360 0.1369 0.0161  -0.0084 0.0150  116 CYS   C CA  
1958 C C   . CYS   B 110 ? 0.1806 0.1553 0.1571 0.0166  -0.0068 0.0169  116 CYS   C C   
1959 O O   . CYS   B 110 ? 0.1783 0.1518 0.1562 0.0150  -0.0054 0.0179  116 CYS   C O   
1960 C CB  . CYS   B 110 ? 0.1547 0.1347 0.1326 0.0177  -0.0098 0.0139  116 CYS   C CB  
1961 S SG  . CYS   B 110 ? 0.1613 0.1405 0.1361 0.0182  -0.0087 0.0142  116 CYS   C SG  
1962 N N   . GLN   B 111 ? 0.1933 0.1664 0.1668 0.0189  -0.0069 0.0179  117 GLN   C N   
1963 C CA  . GLN   B 111 ? 0.2174 0.1871 0.1890 0.0196  -0.0049 0.0203  117 GLN   C CA  
1964 C C   . GLN   B 111 ? 0.2155 0.1847 0.1852 0.0197  -0.0032 0.0214  117 GLN   C C   
1965 O O   . GLN   B 111 ? 0.2390 0.2055 0.2089 0.0196  -0.0008 0.0236  117 GLN   C O   
1966 C CB  . GLN   B 111 ? 0.2479 0.2162 0.2164 0.0225  -0.0053 0.0218  117 GLN   C CB  
1967 C CG  . GLN   B 111 ? 0.2811 0.2515 0.2456 0.0247  -0.0072 0.0213  117 GLN   C CG  
1968 C CD  . GLN   B 111 ? 0.4157 0.3854 0.3775 0.0276  -0.0082 0.0231  117 GLN   C CD  
1969 O OE1 . GLN   B 111 ? 0.4633 0.4348 0.4270 0.0285  -0.0105 0.0222  117 GLN   C OE1 
1970 N NE2 . GLN   B 111 ? 0.4133 0.3803 0.3709 0.0293  -0.0065 0.0261  117 GLN   C NE2 
1971 N N   . HIS   B 112 ? 0.1837 0.1554 0.1525 0.0197  -0.0040 0.0198  118 HIS   C N   
1972 C CA  . HIS   B 112 ? 0.1851 0.1560 0.1518 0.0201  -0.0019 0.0205  118 HIS   C CA  
1973 C C   . HIS   B 112 ? 0.1960 0.1676 0.1678 0.0176  -0.0003 0.0206  118 HIS   C C   
1974 O O   . HIS   B 112 ? 0.2105 0.1813 0.1819 0.0178  0.0021  0.0214  118 HIS   C O   
1975 C CB  . HIS   B 112 ? 0.2019 0.1744 0.1643 0.0217  -0.0034 0.0185  118 HIS   C CB  
1976 C CG  . HIS   B 112 ? 0.1964 0.1687 0.1539 0.0243  -0.0056 0.0187  118 HIS   C CG  
1977 N ND1 . HIS   B 112 ? 0.1729 0.1480 0.1323 0.0245  -0.0089 0.0167  118 HIS   C ND1 
1978 C CD2 . HIS   B 112 ? 0.2250 0.1951 0.1765 0.0268  -0.0047 0.0210  118 HIS   C CD2 
1979 C CE1 . HIS   B 112 ? 0.1944 0.1690 0.1495 0.0271  -0.0105 0.0178  118 HIS   C CE1 
1980 N NE2 . HIS   B 112 ? 0.2274 0.1990 0.1772 0.0285  -0.0081 0.0205  118 HIS   C NE2 
1981 N N   . GLY   B 113 ? 0.1832 0.1567 0.1598 0.0155  -0.0019 0.0196  119 GLY   C N   
1982 C CA  . GLY   B 113 ? 0.1737 0.1486 0.1557 0.0132  -0.0012 0.0199  119 GLY   C CA  
1983 C C   . GLY   B 113 ? 0.1626 0.1406 0.1475 0.0121  -0.0032 0.0181  119 GLY   C C   
1984 O O   . GLY   B 113 ? 0.1563 0.1353 0.1403 0.0124  -0.0050 0.0168  119 GLY   C O   
1985 N N   . VAL   B 114 ? 0.1490 0.1287 0.1383 0.0107  -0.0024 0.0185  120 VAL   C N   
1986 C CA  . VAL   B 114 ? 0.1455 0.1284 0.1387 0.0096  -0.0038 0.0176  120 VAL   C CA  
1987 C C   . VAL   B 114 ? 0.1515 0.1355 0.1436 0.0109  -0.0042 0.0154  120 VAL   C C   
1988 O O   . VAL   B 114 ? 0.1571 0.1404 0.1482 0.0118  -0.0027 0.0147  120 VAL   C O   
1989 C CB  . VAL   B 114 ? 0.1570 0.1412 0.1560 0.0078  -0.0029 0.0193  120 VAL   C CB  
1990 C CG1 . VAL   B 114 ? 0.1729 0.1603 0.1760 0.0070  -0.0040 0.0189  120 VAL   C CG1 
1991 C CG2 . VAL   B 114 ? 0.1769 0.1603 0.1777 0.0062  -0.0034 0.0210  120 VAL   C CG2 
1992 N N   . VAL   B 115 ? 0.1324 0.1182 0.1251 0.0110  -0.0060 0.0142  121 VAL   C N   
1993 C CA  . VAL   B 115 ? 0.1423 0.1296 0.1358 0.0120  -0.0069 0.0119  121 VAL   C CA  
1994 C C   . VAL   B 115 ? 0.1538 0.1435 0.1536 0.0108  -0.0064 0.0117  121 VAL   C C   
1995 O O   . VAL   B 115 ? 0.1523 0.1424 0.1537 0.0113  -0.0062 0.0097  121 VAL   C O   
1996 C CB  . VAL   B 115 ? 0.1434 0.1315 0.1358 0.0128  -0.0088 0.0110  121 VAL   C CB  
1997 C CG1 . VAL   B 115 ? 0.1647 0.1549 0.1600 0.0134  -0.0101 0.0087  121 VAL   C CG1 
1998 C CG2 . VAL   B 115 ? 0.1550 0.1407 0.1420 0.0142  -0.0092 0.0114  121 VAL   C CG2 
1999 N N   . GLY   B 116 ? 0.1347 0.1258 0.1380 0.0093  -0.0063 0.0136  122 GLY   C N   
2000 C CA  . GLY   B 116 ? 0.1522 0.1457 0.1620 0.0084  -0.0058 0.0143  122 GLY   C CA  
2001 C C   . GLY   B 116 ? 0.1324 0.1274 0.1438 0.0071  -0.0063 0.0168  122 GLY   C C   
2002 O O   . GLY   B 116 ? 0.1369 0.1307 0.1445 0.0067  -0.0070 0.0177  122 GLY   C O   
2003 N N   . ILE   B 117 ? 0.1285 0.1260 0.1456 0.0065  -0.0058 0.0181  123 ILE   C N   
2004 C CA  . ILE   B 117 ? 0.1247 0.1239 0.1427 0.0055  -0.0064 0.0209  123 ILE   C CA  
2005 C C   . ILE   B 117 ? 0.1246 0.1259 0.1454 0.0058  -0.0061 0.0214  123 ILE   C C   
2006 O O   . ILE   B 117 ? 0.1289 0.1310 0.1545 0.0064  -0.0052 0.0202  123 ILE   C O   
2007 C CB  . ILE   B 117 ? 0.1384 0.1389 0.1614 0.0043  -0.0060 0.0237  123 ILE   C CB  
2008 C CG1 . ILE   B 117 ? 0.1529 0.1543 0.1829 0.0047  -0.0041 0.0234  123 ILE   C CG1 
2009 C CG2 . ILE   B 117 ? 0.1616 0.1602 0.1823 0.0037  -0.0064 0.0240  123 ILE   C CG2 
2010 C CD1 . ILE   B 117 ? 0.1580 0.1613 0.1949 0.0037  -0.0034 0.0270  123 ILE   C CD1 
2011 N N   . VAL   B 118 ? 0.1174 0.1193 0.1352 0.0055  -0.0067 0.0231  124 VAL   C N   
2012 C CA  . VAL   B 118 ? 0.1270 0.1309 0.1473 0.0060  -0.0057 0.0243  124 VAL   C CA  
2013 C C   . VAL   B 118 ? 0.1221 0.1283 0.1506 0.0058  -0.0045 0.0266  124 VAL   C C   
2014 O O   . VAL   B 118 ? 0.1239 0.1309 0.1544 0.0049  -0.0049 0.0289  124 VAL   C O   
2015 C CB  . VAL   B 118 ? 0.1252 0.1292 0.1398 0.0058  -0.0063 0.0261  124 VAL   C CB  
2016 C CG1 . VAL   B 118 ? 0.1324 0.1384 0.1493 0.0065  -0.0046 0.0282  124 VAL   C CG1 
2017 C CG2 . VAL   B 118 ? 0.1336 0.1349 0.1410 0.0061  -0.0071 0.0237  124 VAL   C CG2 
2018 N N   . SER   B 119 ? 0.1218 0.1291 0.1558 0.0065  -0.0030 0.0261  125 SER   C N   
2019 C CA  . SER   B 119 ? 0.1103 0.1196 0.1533 0.0063  -0.0014 0.0281  125 SER   C CA  
2020 C C   . SER   B 119 ? 0.1183 0.1294 0.1656 0.0070  0.0004  0.0303  125 SER   C C   
2021 O O   . SER   B 119 ? 0.1262 0.1391 0.1802 0.0069  0.0019  0.0336  125 SER   C O   
2022 C CB  . SER   B 119 ? 0.1233 0.1316 0.1712 0.0063  -0.0010 0.0248  125 SER   C CB  
2023 O OG  . SER   B 119 ? 0.1354 0.1450 0.1932 0.0062  0.0009  0.0262  125 SER   C OG  
2024 N N   . THR   B 120 ? 0.1246 0.1353 0.1697 0.0078  0.0007  0.0286  126 THR   C N   
2025 C CA  . THR   B 120 ? 0.1260 0.1385 0.1764 0.0085  0.0031  0.0308  126 THR   C CA  
2026 C C   . THR   B 120 ? 0.1202 0.1320 0.1631 0.0094  0.0036  0.0313  126 THR   C C   
2027 O O   . THR   B 120 ? 0.1291 0.1390 0.1640 0.0094  0.0019  0.0290  126 THR   C O   
2028 C CB  . THR   B 120 ? 0.1218 0.1346 0.1813 0.0088  0.0038  0.0279  126 THR   C CB  
2029 O OG1 . THR   B 120 ? 0.1329 0.1446 0.1887 0.0093  0.0023  0.0242  126 THR   C OG1 
2030 C CG2 . THR   B 120 ? 0.1405 0.1532 0.2068 0.0080  0.0034  0.0261  126 THR   C CG2 
2031 N N   . GLY   B 121 ? 0.1375 0.1508 0.1832 0.0102  0.0063  0.0344  127 GLY   C N   
2032 C CA  . GLY   B 121 ? 0.1553 0.1678 0.1946 0.0113  0.0078  0.0349  127 GLY   C CA  
2033 C C   . GLY   B 121 ? 0.1865 0.2008 0.2329 0.0124  0.0118  0.0379  127 GLY   C C   
2034 O O   . GLY   B 121 ? 0.2190 0.2350 0.2719 0.0124  0.0134  0.0414  127 GLY   C O   
2035 N N   . GLY   B 122 ? 0.2283 0.2420 0.2738 0.0136  0.0137  0.0371  128 GLY   C N   
2036 C CA  . GLY   B 122 ? 0.2478 0.2631 0.3006 0.0148  0.0181  0.0402  128 GLY   C CA  
2037 C C   . GLY   B 122 ? 0.2496 0.2646 0.3059 0.0158  0.0193  0.0377  128 GLY   C C   
2038 O O   . GLY   B 122 ? 0.2459 0.2604 0.3037 0.0154  0.0164  0.0336  128 GLY   C O   
2039 N N   . ASN   B 123 ? 0.2341 0.2495 0.2925 0.0174  0.0240  0.0406  129 ASN   C N   
2040 C CA  . ASN   B 123 ? 0.2361 0.2517 0.3003 0.0185  0.0259  0.0390  129 ASN   C CA  
2041 C C   . ASN   B 123 ? 0.2166 0.2298 0.2719 0.0187  0.0234  0.0350  129 ASN   C C   
2042 O O   . ASN   B 123 ? 0.2485 0.2621 0.3099 0.0192  0.0226  0.0325  129 ASN   C O   
2043 C CB  . ASN   B 123 ? 0.2805 0.2987 0.3612 0.0179  0.0251  0.0375  129 ASN   C CB  
2044 C CG  . ASN   B 123 ? 0.3524 0.3727 0.4457 0.0187  0.0300  0.0414  129 ASN   C CG  
2045 O OD1 . ASN   B 123 ? 0.3740 0.3941 0.4645 0.0202  0.0350  0.0456  129 ASN   C OD1 
2046 N ND2 . ASN   B 123 ? 0.3728 0.3952 0.4805 0.0176  0.0289  0.0402  129 ASN   C ND2 
2047 N N   . GLY   B 124 ? 0.2020 0.2127 0.2437 0.0185  0.0221  0.0347  130 GLY   C N   
2048 C CA  . GLY   B 124 ? 0.2023 0.2104 0.2363 0.0186  0.0200  0.0310  130 GLY   C CA  
2049 C C   . GLY   B 124 ? 0.1806 0.1885 0.2161 0.0174  0.0150  0.0274  130 GLY   C C   
2050 O O   . GLY   B 124 ? 0.1848 0.1909 0.2166 0.0179  0.0135  0.0246  130 GLY   C O   
2051 N N   . LEU   B 125 ? 0.1601 0.1697 0.2007 0.0161  0.0128  0.0275  131 LEU   C N   
2052 C CA  . LEU   B 125 ? 0.1560 0.1653 0.1972 0.0151  0.0085  0.0242  131 LEU   C CA  
2053 C C   . LEU   B 125 ? 0.1560 0.1645 0.1911 0.0137  0.0065  0.0248  131 LEU   C C   
2054 O O   . LEU   B 125 ? 0.1951 0.2046 0.2302 0.0133  0.0079  0.0279  131 LEU   C O   
2055 C CB  . LEU   B 125 ? 0.1730 0.1849 0.2267 0.0148  0.0076  0.0230  131 LEU   C CB  
2056 C CG  . LEU   B 125 ? 0.2014 0.2148 0.2637 0.0160  0.0089  0.0224  131 LEU   C CG  
2057 C CD1 . LEU   B 125 ? 0.2570 0.2732 0.3332 0.0156  0.0092  0.0224  131 LEU   C CD1 
2058 C CD2 . LEU   B 125 ? 0.2220 0.2342 0.2809 0.0168  0.0065  0.0196  131 LEU   C CD2 
2059 N N   . VAL   B 126 ? 0.1269 0.1338 0.1575 0.0131  0.0034  0.0221  132 VAL   C N   
2060 C CA  . VAL   B 126 ? 0.1229 0.1292 0.1497 0.0118  0.0015  0.0225  132 VAL   C CA  
2061 C C   . VAL   B 126 ? 0.1194 0.1261 0.1510 0.0113  -0.0007 0.0199  132 VAL   C C   
2062 O O   . VAL   B 126 ? 0.1286 0.1347 0.1605 0.0120  -0.0022 0.0172  132 VAL   C O   
2063 C CB  . VAL   B 126 ? 0.1349 0.1384 0.1513 0.0114  0.0001  0.0217  132 VAL   C CB  
2064 C CG1 . VAL   B 126 ? 0.1648 0.1663 0.1782 0.0123  -0.0008 0.0189  132 VAL   C CG1 
2065 C CG2 . VAL   B 126 ? 0.1425 0.1456 0.1566 0.0100  -0.0019 0.0221  132 VAL   C CG2 
2066 N N   . GLY   B 127 ? 0.1174 0.1248 0.1523 0.0103  -0.0009 0.0209  133 GLY   C N   
2067 C CA  . GLY   B 127 ? 0.1213 0.1287 0.1601 0.0099  -0.0025 0.0182  133 GLY   C CA  
2068 C C   . GLY   B 127 ? 0.1181 0.1239 0.1518 0.0091  -0.0037 0.0182  133 GLY   C C   
2069 O O   . GLY   B 127 ? 0.1275 0.1336 0.1597 0.0083  -0.0031 0.0210  133 GLY   C O   
2070 N N   . PHE   B 128 ? 0.1126 0.1168 0.1439 0.0093  -0.0053 0.0152  134 PHE   C N   
2071 C CA  . PHE   B 128 ? 0.1163 0.1187 0.1431 0.0087  -0.0059 0.0150  134 PHE   C CA  
2072 C C   . PHE   B 128 ? 0.1143 0.1166 0.1451 0.0086  -0.0058 0.0130  134 PHE   C C   
2073 O O   . PHE   B 128 ? 0.1191 0.1214 0.1518 0.0092  -0.0068 0.0100  134 PHE   C O   
2074 C CB  . PHE   B 128 ? 0.1236 0.1237 0.1427 0.0094  -0.0073 0.0136  134 PHE   C CB  
2075 C CG  . PHE   B 128 ? 0.1232 0.1229 0.1384 0.0097  -0.0072 0.0146  134 PHE   C CG  
2076 C CD1 . PHE   B 128 ? 0.1340 0.1329 0.1451 0.0089  -0.0070 0.0166  134 PHE   C CD1 
2077 C CD2 . PHE   B 128 ? 0.1317 0.1317 0.1474 0.0109  -0.0074 0.0134  134 PHE   C CD2 
2078 C CE1 . PHE   B 128 ? 0.1350 0.1329 0.1417 0.0092  -0.0068 0.0168  134 PHE   C CE1 
2079 C CE2 . PHE   B 128 ? 0.1393 0.1385 0.1514 0.0114  -0.0067 0.0142  134 PHE   C CE2 
2080 C CZ  . PHE   B 128 ? 0.1429 0.1408 0.1500 0.0105  -0.0063 0.0156  134 PHE   C CZ  
2081 N N   . ALA   B 129 ? 0.1243 0.1263 0.1567 0.0078  -0.0048 0.0144  135 ALA   C N   
2082 C CA  . ALA   B 129 ? 0.1162 0.1172 0.1514 0.0078  -0.0040 0.0123  135 ALA   C CA  
2083 C C   . ALA   B 129 ? 0.1247 0.1230 0.1520 0.0084  -0.0048 0.0104  135 ALA   C C   
2084 O O   . ALA   B 129 ? 0.1306 0.1279 0.1537 0.0082  -0.0046 0.0123  135 ALA   C O   
2085 C CB  . ALA   B 129 ? 0.1305 0.1323 0.1708 0.0069  -0.0022 0.0152  135 ALA   C CB  
2086 N N   . ASP   B 130 ? 0.1238 0.1212 0.1491 0.0093  -0.0059 0.0068  136 ASP   C N   
2087 C CA  . ASP   B 130 ? 0.1333 0.1281 0.1506 0.0104  -0.0064 0.0053  136 ASP   C CA  
2088 C C   . ASP   B 130 ? 0.1421 0.1351 0.1590 0.0102  -0.0040 0.0056  136 ASP   C C   
2089 O O   . ASP   B 130 ? 0.1434 0.1367 0.1663 0.0096  -0.0024 0.0050  136 ASP   C O   
2090 C CB  . ASP   B 130 ? 0.1465 0.1410 0.1620 0.0114  -0.0085 0.0012  136 ASP   C CB  
2091 C CG  . ASP   B 130 ? 0.1841 0.1762 0.1904 0.0129  -0.0093 0.0000  136 ASP   C CG  
2092 O OD1 . ASP   B 130 ? 0.1803 0.1715 0.1816 0.0134  -0.0095 0.0022  136 ASP   C OD1 
2093 O OD2 . ASP   B 130 ? 0.2234 0.2140 0.2270 0.0136  -0.0094 -0.0031 136 ASP   C OD2 
2094 N N   . VAL   B 131 ? 0.1403 0.1312 0.1508 0.0107  -0.0034 0.0066  137 VAL   C N   
2095 C CA  . VAL   B 131 ? 0.1444 0.1330 0.1538 0.0109  -0.0005 0.0069  137 VAL   C CA  
2096 C C   . VAL   B 131 ? 0.1645 0.1503 0.1650 0.0127  -0.0004 0.0051  137 VAL   C C   
2097 O O   . VAL   B 131 ? 0.1691 0.1526 0.1676 0.0132  0.0025  0.0053  137 VAL   C O   
2098 C CB  . VAL   B 131 ? 0.1546 0.1435 0.1668 0.0098  0.0011  0.0109  137 VAL   C CB  
2099 C CG1 . VAL   B 131 ? 0.1583 0.1502 0.1788 0.0083  0.0008  0.0131  137 VAL   C CG1 
2100 C CG2 . VAL   B 131 ? 0.1612 0.1493 0.1682 0.0099  -0.0002 0.0127  137 VAL   C CG2 
2101 N N   . ARG   B 132 ? 0.1529 0.1386 0.1480 0.0138  -0.0032 0.0036  138 ARG   C N   
2102 C CA  . ARG   B 132 ? 0.1667 0.1499 0.1525 0.0157  -0.0032 0.0028  138 ARG   C CA  
2103 C C   . ARG   B 132 ? 0.1636 0.1451 0.1457 0.0168  -0.0024 -0.0008 138 ARG   C C   
2104 O O   . ARG   B 132 ? 0.1931 0.1719 0.1669 0.0184  -0.0011 -0.0007 138 ARG   C O   
2105 C CB  . ARG   B 132 ? 0.1582 0.1422 0.1404 0.0166  -0.0067 0.0025  138 ARG   C CB  
2106 C CG  . ARG   B 132 ? 0.1602 0.1449 0.1443 0.0159  -0.0070 0.0057  138 ARG   C CG  
2107 C CD  . ARG   B 132 ? 0.1576 0.1432 0.1392 0.0171  -0.0100 0.0052  138 ARG   C CD  
2108 N NE  . ARG   B 132 ? 0.1486 0.1370 0.1357 0.0166  -0.0122 0.0029  138 ARG   C NE  
2109 C CZ  . ARG   B 132 ? 0.1559 0.1459 0.1438 0.0173  -0.0149 0.0023  138 ARG   C CZ  
2110 N NH1 . ARG   B 132 ? 0.1618 0.1507 0.1447 0.0188  -0.0158 0.0036  138 ARG   C NH1 
2111 N NH2 . ARG   B 132 ? 0.1558 0.1485 0.1504 0.0167  -0.0163 0.0006  138 ARG   C NH2 
2112 N N   . ASP   B 133 ? 0.1583 0.1408 0.1460 0.0159  -0.0028 -0.0037 139 ASP   C N   
2113 C CA  . ASP   B 133 ? 0.1787 0.1591 0.1629 0.0168  -0.0019 -0.0079 139 ASP   C CA  
2114 C C   . ASP   B 133 ? 0.1929 0.1710 0.1789 0.0166  0.0032  -0.0070 139 ASP   C C   
2115 O O   . ASP   B 133 ? 0.2097 0.1853 0.1915 0.0176  0.0048  -0.0105 139 ASP   C O   
2116 C CB  . ASP   B 133 ? 0.1980 0.1804 0.1889 0.0158  -0.0044 -0.0119 139 ASP   C CB  
2117 C CG  . ASP   B 133 ? 0.1916 0.1759 0.1944 0.0139  -0.0025 -0.0104 139 ASP   C CG  
2118 O OD1 . ASP   B 133 ? 0.1947 0.1806 0.2012 0.0131  -0.0019 -0.0060 139 ASP   C OD1 
2119 O OD2 . ASP   B 133 ? 0.2193 0.2032 0.2276 0.0133  -0.0016 -0.0135 139 ASP   C OD2 
2120 N N   . LEU   B 134 ? 0.1804 0.1595 0.1729 0.0154  0.0055  -0.0028 140 LEU   C N   
2121 C CA  . LEU   B 134 ? 0.1815 0.1591 0.1783 0.0151  0.0103  -0.0014 140 LEU   C CA  
2122 C C   . LEU   B 134 ? 0.1865 0.1613 0.1759 0.0166  0.0132  0.0007  140 LEU   C C   
2123 O O   . LEU   B 134 ? 0.1815 0.1567 0.1738 0.0160  0.0147  0.0050  140 LEU   C O   
2124 C CB  . LEU   B 134 ? 0.1750 0.1555 0.1826 0.0132  0.0107  0.0024  140 LEU   C CB  
2125 C CG  . LEU   B 134 ? 0.1767 0.1602 0.1922 0.0119  0.0083  0.0012  140 LEU   C CG  
2126 C CD1 . LEU   B 134 ? 0.1870 0.1734 0.2115 0.0103  0.0085  0.0058  140 LEU   C CD1 
2127 C CD2 . LEU   B 134 ? 0.2059 0.1880 0.2252 0.0120  0.0100  -0.0029 140 LEU   C CD2 
2128 N N   . LEU   B 135 ? 0.2018 0.1734 0.1813 0.0186  0.0142  -0.0023 141 LEU   C N   
2129 C CA  . LEU   B 135 ? 0.2083 0.1770 0.1794 0.0204  0.0170  0.0000  141 LEU   C CA  
2130 C C   . LEU   B 135 ? 0.2002 0.1673 0.1761 0.0202  0.0229  0.0032  141 LEU   C C   
2131 O O   . LEU   B 135 ? 0.2284 0.1942 0.2020 0.0209  0.0252  0.0069  141 LEU   C O   
2132 C CB  . LEU   B 135 ? 0.2197 0.1854 0.1778 0.0228  0.0167  -0.0037 141 LEU   C CB  
2133 C CG  . LEU   B 135 ? 0.2198 0.1874 0.1738 0.0230  0.0104  -0.0071 141 LEU   C CG  
2134 C CD1 . LEU   B 135 ? 0.2435 0.2083 0.1840 0.0255  0.0096  -0.0107 141 LEU   C CD1 
2135 C CD2 . LEU   B 135 ? 0.2318 0.2019 0.1868 0.0226  0.0068  -0.0036 141 LEU   C CD2 
2136 N N   . TRP   B 136 ? 0.1989 0.1662 0.1827 0.0194  0.0253  0.0018  142 TRP   C N   
2137 C CA  . TRP   B 136 ? 0.2159 0.1820 0.2063 0.0193  0.0311  0.0046  142 TRP   C CA  
2138 C C   . TRP   B 136 ? 0.2281 0.1971 0.2276 0.0175  0.0306  0.0101  142 TRP   C C   
2139 O O   . TRP   B 136 ? 0.2429 0.2111 0.2476 0.0176  0.0349  0.0134  142 TRP   C O   
2140 C CB  . TRP   B 136 ? 0.2178 0.1836 0.2157 0.0188  0.0334  0.0017  142 TRP   C CB  
2141 C CG  . TRP   B 136 ? 0.2080 0.1775 0.2146 0.0168  0.0292  0.0009  142 TRP   C CG  
2142 C CD1 . TRP   B 136 ? 0.2227 0.1927 0.2277 0.0165  0.0258  -0.0037 142 TRP   C CD1 
2143 C CD2 . TRP   B 136 ? 0.2028 0.1760 0.2218 0.0148  0.0286  0.0050  142 TRP   C CD2 
2144 N NE1 . TRP   B 136 ? 0.2159 0.1896 0.2316 0.0146  0.0233  -0.0024 142 TRP   C NE1 
2145 C CE2 . TRP   B 136 ? 0.2117 0.1874 0.2355 0.0136  0.0250  0.0030  142 TRP   C CE2 
2146 C CE3 . TRP   B 136 ? 0.1964 0.1712 0.2230 0.0139  0.0304  0.0102  142 TRP   C CE3 
2147 C CZ2 . TRP   B 136 ? 0.1998 0.1793 0.2345 0.0119  0.0236  0.0065  142 TRP   C CZ2 
2148 C CZ3 . TRP   B 136 ? 0.1968 0.1755 0.2344 0.0121  0.0284  0.0133  142 TRP   C CZ3 
2149 C CH2 . TRP   B 136 ? 0.2017 0.1827 0.2425 0.0112  0.0251  0.0116  142 TRP   C CH2 
2150 N N   . LEU   B 137 ? 0.2096 0.1818 0.2113 0.0160  0.0254  0.0111  143 LEU   C N   
2151 C CA  . LEU   B 137 ? 0.2075 0.1821 0.2162 0.0143  0.0245  0.0158  143 LEU   C CA  
2152 C C   . LEU   B 137 ? 0.2453 0.2175 0.2495 0.0153  0.0268  0.0187  143 LEU   C C   
2153 O O   . LEU   B 137 ? 0.2717 0.2451 0.2830 0.0140  0.0275  0.0225  143 LEU   C O   
2154 C CB  . LEU   B 137 ? 0.2001 0.1778 0.2098 0.0129  0.0189  0.0160  143 LEU   C CB  
2155 C CG  . LEU   B 137 ? 0.1898 0.1705 0.2066 0.0116  0.0169  0.0148  143 LEU   C CG  
2156 C CD1 . LEU   B 137 ? 0.2003 0.1833 0.2152 0.0108  0.0120  0.0143  143 LEU   C CD1 
2157 C CD2 . LEU   B 137 ? 0.2036 0.1865 0.2319 0.0101  0.0184  0.0183  143 LEU   C CD2 
2158 N N   . ASP   B 138 ? 0.2359 0.2050 0.2287 0.0175  0.0277  0.0170  144 ASP   C N   
2159 C CA  . ASP   B 138 ? 0.2540 0.2207 0.2419 0.0188  0.0300  0.0200  144 ASP   C CA  
2160 C C   . ASP   B 138 ? 0.2881 0.2519 0.2773 0.0200  0.0369  0.0221  144 ASP   C C   
2161 O O   . ASP   B 138 ? 0.3066 0.2681 0.2926 0.0212  0.0396  0.0251  144 ASP   C O   
2162 C CB  . ASP   B 138 ? 0.2567 0.2213 0.2314 0.0210  0.0282  0.0183  144 ASP   C CB  
2163 C CG  . ASP   B 138 ? 0.2664 0.2335 0.2400 0.0201  0.0220  0.0171  144 ASP   C CG  
2164 O OD1 . ASP   B 138 ? 0.2696 0.2395 0.2513 0.0178  0.0195  0.0181  144 ASP   C OD1 
2165 O OD2 . ASP   B 138 ? 0.3022 0.2684 0.2664 0.0218  0.0197  0.0151  144 ASP   C OD2 
2166 N N   . GLU   B 139 ? 0.2918 0.2555 0.2863 0.0200  0.0400  0.0207  145 GLU   C N   
2167 C CA  . GLU   B 139 ? 0.3489 0.3096 0.3450 0.0214  0.0473  0.0227  145 GLU   C CA  
2168 C C   . GLU   B 139 ? 0.4034 0.3655 0.4119 0.0203  0.0503  0.0231  145 GLU   C C   
2169 O O   . GLU   B 139 ? 0.4096 0.3751 0.4256 0.0184  0.0466  0.0222  145 GLU   C O   
2170 C CB  . GLU   B 139 ? 0.4094 0.3657 0.3911 0.0245  0.0502  0.0194  145 GLU   C CB  
2171 C CG  . GLU   B 139 ? 0.4871 0.4435 0.4656 0.0245  0.0480  0.0136  145 GLU   C CG  
2172 C CD  . GLU   B 139 ? 0.6409 0.5956 0.6046 0.0263  0.0446  0.0097  145 GLU   C CD  
2173 O OE1 . GLU   B 139 ? 0.6280 0.5793 0.5829 0.0284  0.0474  0.0060  145 GLU   C OE1 
2174 O OE2 . GLU   B 139 ? 0.7117 0.6685 0.6727 0.0258  0.0392  0.0103  145 GLU   C OE2 
2175 N N   . GLU   B 140 ? 0.4415 0.4006 0.4520 0.0219  0.0576  0.0245  146 GLU   C N   
2176 C CA  . GLU   B 140 ? 0.4694 0.4289 0.4912 0.0216  0.0621  0.0249  146 GLU   C CA  
2177 C C   . GLU   B 140 ? 0.4792 0.4436 0.5167 0.0188  0.0592  0.0285  146 GLU   C C   
2178 O O   . GLU   B 140 ? 0.4868 0.4532 0.5335 0.0179  0.0591  0.0280  146 GLU   C O   
2179 C CB  . GLU   B 140 ? 0.5109 0.4685 0.5277 0.0225  0.0625  0.0190  146 GLU   C CB  
2180 C CG  . GLU   B 140 ? 0.6240 0.5828 0.6536 0.0217  0.0649  0.0185  146 GLU   C CG  
2181 C CD  . GLU   B 140 ? 0.7296 0.6859 0.7662 0.0230  0.0735  0.0202  146 GLU   C CD  
2182 O OE1 . GLU   B 140 ? 0.7631 0.7188 0.8064 0.0231  0.0760  0.0181  146 GLU   C OE1 
2183 O OE2 . GLU   B 140 ? 0.7725 0.7272 0.8088 0.0241  0.0779  0.0240  146 GLU   C OE2 
2184 N N1  . A1BP1 C .   ? 0.2571 0.2199 0.3154 0.0067  0.0365  -0.0120 201 A1BP1 A N1  
2185 N N3  . A1BP1 C .   ? 0.2023 0.1747 0.2314 0.0038  0.0259  -0.0115 201 A1BP1 A N3  
2186 C C4  . A1BP1 C .   ? 0.2919 0.2601 0.3770 0.0161  0.0331  0.0098  201 A1BP1 A C4  
2187 C C5  . A1BP1 C .   ? 0.2830 0.2445 0.3938 0.0186  0.0461  0.0094  201 A1BP1 A C5  
2188 C C6  . A1BP1 C .   ? 0.2483 0.2101 0.3059 0.0047  0.0409  -0.0169 201 A1BP1 A C6  
2189 C C7  . A1BP1 C .   ? 0.2151 0.1813 0.2615 0.0041  0.0359  -0.0156 201 A1BP1 A C7  
2190 C C8  . A1BP1 C .   ? 0.1997 0.1750 0.2182 0.0037  0.0189  -0.0083 201 A1BP1 A C8  
2191 C C10 . A1BP1 C .   ? 0.2174 0.1902 0.2442 0.0002  0.0323  -0.0177 201 A1BP1 A C10 
2192 C C13 . A1BP1 C .   ? 0.2191 0.1833 0.2700 0.0003  0.0473  -0.0248 201 A1BP1 A C13 
2193 O O1  . A1BP1 C .   ? 0.2609 0.2182 0.3269 0.0029  0.0494  -0.0227 201 A1BP1 A O1  
2194 C C14 . A1BP1 C .   ? 0.2141 0.1810 0.2584 0.0023  0.0389  -0.0190 201 A1BP1 A C14 
2195 C C12 . A1BP1 C .   ? 0.2335 0.2002 0.2783 -0.0018 0.0478  -0.0270 201 A1BP1 A C12 
2196 C C11 . A1BP1 C .   ? 0.2218 0.1927 0.2542 -0.0019 0.0401  -0.0233 201 A1BP1 A C11 
2197 C C9  . A1BP1 C .   ? 0.2023 0.1734 0.2349 0.0022  0.0319  -0.0158 201 A1BP1 A C9  
2198 N N2  . A1BP1 C .   ? 0.2138 0.1837 0.2511 0.0050  0.0281  -0.0112 201 A1BP1 A N2  
2199 C C1  . A1BP1 C .   ? 0.2834 0.2416 0.3449 0.0047  0.0399  -0.0162 201 A1BP1 A C1  
2200 C C   . A1BP1 C .   ? 0.3066 0.2648 0.3536 -0.0012 0.0380  -0.0238 201 A1BP1 A C   
2201 C C2  . A1BP1 C .   ? 0.2746 0.2346 0.3411 0.0082  0.0359  -0.0084 201 A1BP1 A C2  
2202 C C3  . A1BP1 C .   ? 0.2810 0.2426 0.3634 0.0130  0.0382  0.0001  201 A1BP1 A C3  
2203 N N   . A1BP1 C .   ? 0.2739 0.2308 0.3725 0.0142  0.0471  -0.0010 201 A1BP1 A N   
2204 O O   . A1BP1 C .   ? 0.2922 0.2615 0.3951 0.0195  0.0375  0.0166  201 A1BP1 A O   
# 
