data_7I33
# 
_entry.id   7I33 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I33         pdb_00007i33 10.2210/pdb7i33/pdb 
WWPDB D_1001408254 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I33 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                           15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '2-methyl-N-[2-(1,3-oxazol-4-yl)ethyl]-2H-1,2,3-triazole-4-carboxamide' 221.216   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                              65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                    78.133    3   ?         ? ? ? 
5 water       nat water                                                                   18.015    367 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '2-methyl-N-[2-(1,3-oxazol-4-yl)ethyl]-2H-1,2,3-triazole-4-carboxamide' A1B05 
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 
A1B05 non-polymer         . '2-methyl-N-[2-(1,3-oxazol-4-yl)ethyl]-2H-1,2,3-triazole-4-carboxamide' ? 'C9 H11 N5 O2'   221.216 
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        A1B05 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B05 
_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 A1B05 1   201 201 A1B05 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 4 DMS   1   203 6   DMS   DMS C . 
I 5 HOH   1   301 321 HOH   HOH A . 
I 5 HOH   2   302 98  HOH   HOH A . 
I 5 HOH   3   303 159 HOH   HOH A . 
I 5 HOH   4   304 261 HOH   HOH A . 
I 5 HOH   5   305 61  HOH   HOH A . 
I 5 HOH   6   306 242 HOH   HOH A . 
I 5 HOH   7   307 234 HOH   HOH A . 
I 5 HOH   8   308 221 HOH   HOH A . 
I 5 HOH   9   309 165 HOH   HOH A . 
I 5 HOH   10  310 327 HOH   HOH A . 
I 5 HOH   11  311 230 HOH   HOH A . 
I 5 HOH   12  312 122 HOH   HOH A . 
I 5 HOH   13  313 310 HOH   HOH A . 
I 5 HOH   14  314 91  HOH   HOH A . 
I 5 HOH   15  315 147 HOH   HOH A . 
I 5 HOH   16  316 201 HOH   HOH A . 
I 5 HOH   17  317 97  HOH   HOH A . 
I 5 HOH   18  318 274 HOH   HOH A . 
I 5 HOH   19  319 141 HOH   HOH A . 
I 5 HOH   20  320 276 HOH   HOH A . 
I 5 HOH   21  321 186 HOH   HOH A . 
I 5 HOH   22  322 96  HOH   HOH A . 
I 5 HOH   23  323 254 HOH   HOH A . 
I 5 HOH   24  324 207 HOH   HOH A . 
I 5 HOH   25  325 120 HOH   HOH A . 
I 5 HOH   26  326 238 HOH   HOH A . 
I 5 HOH   27  327 13  HOH   HOH A . 
I 5 HOH   28  328 101 HOH   HOH A . 
I 5 HOH   29  329 257 HOH   HOH A . 
I 5 HOH   30  330 89  HOH   HOH A . 
I 5 HOH   31  331 275 HOH   HOH A . 
I 5 HOH   32  332 143 HOH   HOH A . 
I 5 HOH   33  333 10  HOH   HOH A . 
I 5 HOH   34  334 42  HOH   HOH A . 
I 5 HOH   35  335 303 HOH   HOH A . 
I 5 HOH   36  336 351 HOH   HOH A . 
I 5 HOH   37  337 15  HOH   HOH A . 
I 5 HOH   38  338 88  HOH   HOH A . 
I 5 HOH   39  339 291 HOH   HOH A . 
I 5 HOH   40  340 125 HOH   HOH A . 
I 5 HOH   41  341 127 HOH   HOH A . 
I 5 HOH   42  342 45  HOH   HOH A . 
I 5 HOH   43  343 8   HOH   HOH A . 
I 5 HOH   44  344 302 HOH   HOH A . 
I 5 HOH   45  345 344 HOH   HOH A . 
I 5 HOH   46  346 7   HOH   HOH A . 
I 5 HOH   47  347 116 HOH   HOH A . 
I 5 HOH   48  348 51  HOH   HOH A . 
I 5 HOH   49  349 328 HOH   HOH A . 
I 5 HOH   50  350 70  HOH   HOH A . 
I 5 HOH   51  351 168 HOH   HOH A . 
I 5 HOH   52  352 18  HOH   HOH A . 
I 5 HOH   53  353 1   HOH   HOH A . 
I 5 HOH   54  354 192 HOH   HOH A . 
I 5 HOH   55  355 329 HOH   HOH A . 
I 5 HOH   56  356 132 HOH   HOH A . 
I 5 HOH   57  357 258 HOH   HOH A . 
I 5 HOH   58  358 48  HOH   HOH A . 
I 5 HOH   59  359 320 HOH   HOH A . 
I 5 HOH   60  360 324 HOH   HOH A . 
I 5 HOH   61  361 208 HOH   HOH A . 
I 5 HOH   62  362 164 HOH   HOH A . 
I 5 HOH   63  363 76  HOH   HOH A . 
I 5 HOH   64  364 273 HOH   HOH A . 
I 5 HOH   65  365 266 HOH   HOH A . 
I 5 HOH   66  366 79  HOH   HOH A . 
I 5 HOH   67  367 228 HOH   HOH A . 
I 5 HOH   68  368 224 HOH   HOH A . 
I 5 HOH   69  369 58  HOH   HOH A . 
I 5 HOH   70  370 179 HOH   HOH A . 
I 5 HOH   71  371 205 HOH   HOH A . 
I 5 HOH   72  372 28  HOH   HOH A . 
I 5 HOH   73  373 30  HOH   HOH A . 
I 5 HOH   74  374 140 HOH   HOH A . 
I 5 HOH   75  375 171 HOH   HOH A . 
I 5 HOH   76  376 12  HOH   HOH A . 
I 5 HOH   77  377 86  HOH   HOH A . 
I 5 HOH   78  378 367 HOH   HOH A . 
I 5 HOH   79  379 156 HOH   HOH A . 
I 5 HOH   80  380 63  HOH   HOH A . 
I 5 HOH   81  381 260 HOH   HOH A . 
I 5 HOH   82  382 54  HOH   HOH A . 
I 5 HOH   83  383 211 HOH   HOH A . 
I 5 HOH   84  384 368 HOH   HOH A . 
I 5 HOH   85  385 191 HOH   HOH A . 
I 5 HOH   86  386 33  HOH   HOH A . 
I 5 HOH   87  387 21  HOH   HOH A . 
I 5 HOH   88  388 280 HOH   HOH A . 
I 5 HOH   89  389 35  HOH   HOH A . 
I 5 HOH   90  390 129 HOH   HOH A . 
I 5 HOH   91  391 78  HOH   HOH A . 
I 5 HOH   92  392 292 HOH   HOH A . 
I 5 HOH   93  393 148 HOH   HOH A . 
I 5 HOH   94  394 289 HOH   HOH A . 
I 5 HOH   95  395 210 HOH   HOH A . 
I 5 HOH   96  396 182 HOH   HOH A . 
I 5 HOH   97  397 145 HOH   HOH A . 
I 5 HOH   98  398 162 HOH   HOH A . 
I 5 HOH   99  399 259 HOH   HOH A . 
I 5 HOH   100 400 39  HOH   HOH A . 
I 5 HOH   101 401 241 HOH   HOH A . 
I 5 HOH   102 402 111 HOH   HOH A . 
I 5 HOH   103 403 157 HOH   HOH A . 
I 5 HOH   104 404 37  HOH   HOH A . 
I 5 HOH   105 405 235 HOH   HOH A . 
I 5 HOH   106 406 49  HOH   HOH A . 
I 5 HOH   107 407 215 HOH   HOH A . 
I 5 HOH   108 408 307 HOH   HOH A . 
I 5 HOH   109 409 189 HOH   HOH A . 
I 5 HOH   110 410 263 HOH   HOH A . 
I 5 HOH   111 411 99  HOH   HOH A . 
I 5 HOH   112 412 316 HOH   HOH A . 
I 5 HOH   113 413 322 HOH   HOH A . 
I 5 HOH   114 414 345 HOH   HOH A . 
I 5 HOH   115 415 144 HOH   HOH A . 
I 5 HOH   116 416 17  HOH   HOH A . 
I 5 HOH   117 417 306 HOH   HOH A . 
I 5 HOH   118 418 138 HOH   HOH A . 
I 5 HOH   119 419 347 HOH   HOH A . 
I 5 HOH   120 420 336 HOH   HOH A . 
I 5 HOH   121 421 233 HOH   HOH A . 
I 5 HOH   122 422 249 HOH   HOH A . 
I 5 HOH   123 423 23  HOH   HOH A . 
I 5 HOH   124 424 115 HOH   HOH A . 
I 5 HOH   125 425 3   HOH   HOH A . 
I 5 HOH   126 426 106 HOH   HOH A . 
I 5 HOH   127 427 69  HOH   HOH A . 
I 5 HOH   128 428 64  HOH   HOH A . 
I 5 HOH   129 429 265 HOH   HOH A . 
I 5 HOH   130 430 68  HOH   HOH A . 
I 5 HOH   131 431 46  HOH   HOH A . 
I 5 HOH   132 432 172 HOH   HOH A . 
I 5 HOH   133 433 175 HOH   HOH A . 
I 5 HOH   134 434 4   HOH   HOH A . 
I 5 HOH   135 435 330 HOH   HOH A . 
I 5 HOH   136 436 314 HOH   HOH A . 
I 5 HOH   137 437 83  HOH   HOH A . 
I 5 HOH   138 438 277 HOH   HOH A . 
I 5 HOH   139 439 124 HOH   HOH A . 
I 5 HOH   140 440 158 HOH   HOH A . 
I 5 HOH   141 441 311 HOH   HOH A . 
I 5 HOH   142 442 297 HOH   HOH A . 
I 5 HOH   143 443 285 HOH   HOH A . 
I 5 HOH   144 444 181 HOH   HOH A . 
I 5 HOH   145 445 117 HOH   HOH A . 
I 5 HOH   146 446 308 HOH   HOH A . 
I 5 HOH   147 447 290 HOH   HOH A . 
I 5 HOH   148 448 342 HOH   HOH A . 
I 5 HOH   149 449 346 HOH   HOH A . 
I 5 HOH   150 450 216 HOH   HOH A . 
I 5 HOH   151 451 279 HOH   HOH A . 
I 5 HOH   152 452 301 HOH   HOH A . 
I 5 HOH   153 453 268 HOH   HOH A . 
I 5 HOH   154 454 200 HOH   HOH A . 
I 5 HOH   155 455 180 HOH   HOH A . 
I 5 HOH   156 456 340 HOH   HOH A . 
I 5 HOH   157 457 313 HOH   HOH A . 
I 5 HOH   158 458 318 HOH   HOH A . 
I 5 HOH   159 459 369 HOH   HOH A . 
I 5 HOH   160 460 209 HOH   HOH A . 
I 5 HOH   161 461 286 HOH   HOH A . 
I 5 HOH   162 462 264 HOH   HOH A . 
I 5 HOH   163 463 218 HOH   HOH A . 
I 5 HOH   164 464 196 HOH   HOH A . 
I 5 HOH   165 465 112 HOH   HOH A . 
I 5 HOH   166 466 139 HOH   HOH A . 
I 5 HOH   167 467 338 HOH   HOH A . 
I 5 HOH   168 468 359 HOH   HOH A . 
I 5 HOH   169 469 337 HOH   HOH A . 
I 5 HOH   170 470 269 HOH   HOH A . 
I 5 HOH   171 471 312 HOH   HOH A . 
I 5 HOH   172 472 323 HOH   HOH A . 
I 5 HOH   173 473 305 HOH   HOH A . 
I 5 HOH   174 474 288 HOH   HOH A . 
J 5 HOH   1   301 319 HOH   HOH C . 
J 5 HOH   2   302 237 HOH   HOH C . 
J 5 HOH   3   303 113 HOH   HOH C . 
J 5 HOH   4   304 82  HOH   HOH C . 
J 5 HOH   5   305 135 HOH   HOH C . 
J 5 HOH   6   306 283 HOH   HOH C . 
J 5 HOH   7   307 104 HOH   HOH C . 
J 5 HOH   8   308 178 HOH   HOH C . 
J 5 HOH   9   309 134 HOH   HOH C . 
J 5 HOH   10  310 296 HOH   HOH C . 
J 5 HOH   11  311 59  HOH   HOH C . 
J 5 HOH   12  312 251 HOH   HOH C . 
J 5 HOH   13  313 204 HOH   HOH C . 
J 5 HOH   14  314 187 HOH   HOH C . 
J 5 HOH   15  315 81  HOH   HOH C . 
J 5 HOH   16  316 5   HOH   HOH C . 
J 5 HOH   17  317 334 HOH   HOH C . 
J 5 HOH   18  318 36  HOH   HOH C . 
J 5 HOH   19  319 161 HOH   HOH C . 
J 5 HOH   20  320 100 HOH   HOH C . 
J 5 HOH   21  321 123 HOH   HOH C . 
J 5 HOH   22  322 154 HOH   HOH C . 
J 5 HOH   23  323 149 HOH   HOH C . 
J 5 HOH   24  324 41  HOH   HOH C . 
J 5 HOH   25  325 331 HOH   HOH C . 
J 5 HOH   26  326 110 HOH   HOH C . 
J 5 HOH   27  327 55  HOH   HOH C . 
J 5 HOH   28  328 53  HOH   HOH C . 
J 5 HOH   29  329 332 HOH   HOH C . 
J 5 HOH   30  330 350 HOH   HOH C . 
J 5 HOH   31  331 198 HOH   HOH C . 
J 5 HOH   32  332 93  HOH   HOH C . 
J 5 HOH   33  333 341 HOH   HOH C . 
J 5 HOH   34  334 225 HOH   HOH C . 
J 5 HOH   35  335 2   HOH   HOH C . 
J 5 HOH   36  336 56  HOH   HOH C . 
J 5 HOH   37  337 356 HOH   HOH C . 
J 5 HOH   38  338 24  HOH   HOH C . 
J 5 HOH   39  339 16  HOH   HOH C . 
J 5 HOH   40  340 152 HOH   HOH C . 
J 5 HOH   41  341 213 HOH   HOH C . 
J 5 HOH   42  342 118 HOH   HOH C . 
J 5 HOH   43  343 85  HOH   HOH C . 
J 5 HOH   44  344 105 HOH   HOH C . 
J 5 HOH   45  345 102 HOH   HOH C . 
J 5 HOH   46  346 62  HOH   HOH C . 
J 5 HOH   47  347 160 HOH   HOH C . 
J 5 HOH   48  348 44  HOH   HOH C . 
J 5 HOH   49  349 294 HOH   HOH C . 
J 5 HOH   50  350 163 HOH   HOH C . 
J 5 HOH   51  351 25  HOH   HOH C . 
J 5 HOH   52  352 6   HOH   HOH C . 
J 5 HOH   53  353 103 HOH   HOH C . 
J 5 HOH   54  354 194 HOH   HOH C . 
J 5 HOH   55  355 325 HOH   HOH C . 
J 5 HOH   56  356 142 HOH   HOH C . 
J 5 HOH   57  357 94  HOH   HOH C . 
J 5 HOH   58  358 77  HOH   HOH C . 
J 5 HOH   59  359 348 HOH   HOH C . 
J 5 HOH   60  360 304 HOH   HOH C . 
J 5 HOH   61  361 226 HOH   HOH C . 
J 5 HOH   62  362 223 HOH   HOH C . 
J 5 HOH   63  363 247 HOH   HOH C . 
J 5 HOH   64  364 92  HOH   HOH C . 
J 5 HOH   65  365 355 HOH   HOH C . 
J 5 HOH   66  366 203 HOH   HOH C . 
J 5 HOH   67  367 137 HOH   HOH C . 
J 5 HOH   68  368 271 HOH   HOH C . 
J 5 HOH   69  369 60  HOH   HOH C . 
J 5 HOH   70  370 40  HOH   HOH C . 
J 5 HOH   71  371 173 HOH   HOH C . 
J 5 HOH   72  372 193 HOH   HOH C . 
J 5 HOH   73  373 38  HOH   HOH C . 
J 5 HOH   74  374 339 HOH   HOH C . 
J 5 HOH   75  375 107 HOH   HOH C . 
J 5 HOH   76  376 47  HOH   HOH C . 
J 5 HOH   77  377 214 HOH   HOH C . 
J 5 HOH   78  378 130 HOH   HOH C . 
J 5 HOH   79  379 150 HOH   HOH C . 
J 5 HOH   80  380 121 HOH   HOH C . 
J 5 HOH   81  381 287 HOH   HOH C . 
J 5 HOH   82  382 177 HOH   HOH C . 
J 5 HOH   83  383 9   HOH   HOH C . 
J 5 HOH   84  384 174 HOH   HOH C . 
J 5 HOH   85  385 90  HOH   HOH C . 
J 5 HOH   86  386 72  HOH   HOH C . 
J 5 HOH   87  387 66  HOH   HOH C . 
J 5 HOH   88  388 109 HOH   HOH C . 
J 5 HOH   89  389 282 HOH   HOH C . 
J 5 HOH   90  390 19  HOH   HOH C . 
J 5 HOH   91  391 14  HOH   HOH C . 
J 5 HOH   92  392 190 HOH   HOH C . 
J 5 HOH   93  393 239 HOH   HOH C . 
J 5 HOH   94  394 75  HOH   HOH C . 
J 5 HOH   95  395 114 HOH   HOH C . 
J 5 HOH   96  396 29  HOH   HOH C . 
J 5 HOH   97  397 80  HOH   HOH C . 
J 5 HOH   98  398 20  HOH   HOH C . 
J 5 HOH   99  399 231 HOH   HOH C . 
J 5 HOH   100 400 126 HOH   HOH C . 
J 5 HOH   101 401 255 HOH   HOH C . 
J 5 HOH   102 402 31  HOH   HOH C . 
J 5 HOH   103 403 357 HOH   HOH C . 
J 5 HOH   104 404 298 HOH   HOH C . 
J 5 HOH   105 405 219 HOH   HOH C . 
J 5 HOH   106 406 153 HOH   HOH C . 
J 5 HOH   107 407 50  HOH   HOH C . 
J 5 HOH   108 408 71  HOH   HOH C . 
J 5 HOH   109 409 300 HOH   HOH C . 
J 5 HOH   110 410 256 HOH   HOH C . 
J 5 HOH   111 411 52  HOH   HOH C . 
J 5 HOH   112 412 128 HOH   HOH C . 
J 5 HOH   113 413 84  HOH   HOH C . 
J 5 HOH   114 414 95  HOH   HOH C . 
J 5 HOH   115 415 34  HOH   HOH C . 
J 5 HOH   116 416 32  HOH   HOH C . 
J 5 HOH   117 417 184 HOH   HOH C . 
J 5 HOH   118 418 57  HOH   HOH C . 
J 5 HOH   119 419 246 HOH   HOH C . 
J 5 HOH   120 420 136 HOH   HOH C . 
J 5 HOH   121 421 22  HOH   HOH C . 
J 5 HOH   122 422 281 HOH   HOH C . 
J 5 HOH   123 423 27  HOH   HOH C . 
J 5 HOH   124 424 65  HOH   HOH C . 
J 5 HOH   125 425 229 HOH   HOH C . 
J 5 HOH   126 426 262 HOH   HOH C . 
J 5 HOH   127 427 185 HOH   HOH C . 
J 5 HOH   128 428 119 HOH   HOH C . 
J 5 HOH   129 429 227 HOH   HOH C . 
J 5 HOH   130 430 349 HOH   HOH C . 
J 5 HOH   131 431 199 HOH   HOH C . 
J 5 HOH   132 432 245 HOH   HOH C . 
J 5 HOH   133 433 166 HOH   HOH C . 
J 5 HOH   134 434 26  HOH   HOH C . 
J 5 HOH   135 435 43  HOH   HOH C . 
J 5 HOH   136 436 87  HOH   HOH C . 
J 5 HOH   137 437 267 HOH   HOH C . 
J 5 HOH   138 438 11  HOH   HOH C . 
J 5 HOH   139 439 146 HOH   HOH C . 
J 5 HOH   140 440 250 HOH   HOH C . 
J 5 HOH   141 441 222 HOH   HOH C . 
J 5 HOH   142 442 167 HOH   HOH C . 
J 5 HOH   143 443 151 HOH   HOH C . 
J 5 HOH   144 444 183 HOH   HOH C . 
J 5 HOH   145 445 170 HOH   HOH C . 
J 5 HOH   146 446 74  HOH   HOH C . 
J 5 HOH   147 447 212 HOH   HOH C . 
J 5 HOH   148 448 195 HOH   HOH C . 
J 5 HOH   149 449 220 HOH   HOH C . 
J 5 HOH   150 450 326 HOH   HOH C . 
J 5 HOH   151 451 240 HOH   HOH C . 
J 5 HOH   152 452 333 HOH   HOH C . 
J 5 HOH   153 453 131 HOH   HOH C . 
J 5 HOH   154 454 343 HOH   HOH C . 
J 5 HOH   155 455 243 HOH   HOH C . 
J 5 HOH   156 456 362 HOH   HOH C . 
J 5 HOH   157 457 361 HOH   HOH C . 
J 5 HOH   158 458 108 HOH   HOH C . 
J 5 HOH   159 459 309 HOH   HOH C . 
J 5 HOH   160 460 73  HOH   HOH C . 
J 5 HOH   161 461 354 HOH   HOH C . 
J 5 HOH   162 462 366 HOH   HOH C . 
J 5 HOH   163 463 236 HOH   HOH C . 
J 5 HOH   164 464 188 HOH   HOH C . 
J 5 HOH   165 465 364 HOH   HOH C . 
J 5 HOH   166 466 217 HOH   HOH C . 
J 5 HOH   167 467 272 HOH   HOH C . 
J 5 HOH   168 468 353 HOH   HOH C . 
J 5 HOH   169 469 176 HOH   HOH C . 
J 5 HOH   170 470 206 HOH   HOH C . 
J 5 HOH   171 471 252 HOH   HOH C . 
J 5 HOH   172 472 315 HOH   HOH C . 
J 5 HOH   173 473 248 HOH   HOH C . 
J 5 HOH   174 474 253 HOH   HOH C . 
J 5 HOH   175 475 299 HOH   HOH C . 
J 5 HOH   176 476 293 HOH   HOH C . 
J 5 HOH   177 477 133 HOH   HOH C . 
J 5 HOH   178 478 202 HOH   HOH C . 
J 5 HOH   179 479 352 HOH   HOH C . 
J 5 HOH   180 480 363 HOH   HOH C . 
J 5 HOH   181 481 244 HOH   HOH C . 
J 5 HOH   182 482 197 HOH   HOH C . 
J 5 HOH   183 483 278 HOH   HOH C . 
J 5 HOH   184 484 169 HOH   HOH C . 
J 5 HOH   185 485 270 HOH   HOH C . 
J 5 HOH   186 486 232 HOH   HOH C . 
J 5 HOH   187 487 358 HOH   HOH C . 
J 5 HOH   188 488 360 HOH   HOH C . 
J 5 HOH   189 489 317 HOH   HOH C . 
J 5 HOH   190 490 335 HOH   HOH C . 
J 5 HOH   191 491 365 HOH   HOH C . 
J 5 HOH   192 492 284 HOH   HOH C . 
J 5 HOH   193 493 295 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           7I33 
_cell.length_a           86.555 
_cell.length_b           56.955 
_cell.length_c           64.899 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.69 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I33 
_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          7I33 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   50.96 
_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   2024-11-13 
_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   0.92202 
_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        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I33 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             39.15 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   84455 
_reflns.percent_possible_obs         75.7 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_netI_over_sigmaI        26.1 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.044 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     449543 
_reflns.pdbx_chi_squared             1.25 
_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                  1.15 
_reflns_shell.d_res_low                   1.17 
_reflns_shell.number_measured_all         302 
_reflns_shell.number_unique_obs           299 
_reflns_shell.Rmerge_I_obs                0.508 
_reflns_shell.pdbx_chi_squared            0.43 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        5.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             0.718 
_reflns_shell.pdbx_Rpim_I_all             0.508 
_reflns_shell.pdbx_CC_half                0.630 
_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                                 7I33 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     84415 
_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                             16.51 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    75.8 
_refine.ls_R_factor_obs                          0.1755 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1749 
_refine.ls_R_factor_R_free                       0.1881 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.010 
_refine.ls_number_reflns_R_free                  4227 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.965 
_refine.B_iso_mean                               18.39 
_refine.aniso_B[1][1]                            -0.95090 
_refine.aniso_B[2][2]                            0.55340 
_refine.aniso_B[3][3]                            0.39750 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.55650 
_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             0.041 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.041 
_refine.pdbx_overall_SU_R_Blow_DPI               0.044 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.044 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I33 
_refine_analyze.Luzzati_coordinate_error_obs    0.14 
_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         30 
_refine_hist.number_atoms_solvent             367 
_refine_hist.number_atoms_total               2563 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        16.51 
# 
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  2280 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.13  ? 2.00  3108 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  760  '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  412  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2280 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.35  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.00 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  281  '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  2099 '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                       1.15 
_refine_ls_shell.d_res_low                        1.20 
_refine_ls_shell.number_reflns_R_work             1594 
_refine_ls_shell.R_factor_R_work                  0.2767 
_refine_ls_shell.percent_reflns_obs               12.12 
_refine_ls_shell.R_factor_R_free                  0.2939 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.62 
_refine_ls_shell.number_reflns_R_free             95 
_refine_ls_shell.number_reflns_all                1689 
_refine_ls_shell.R_factor_all                     0.2776 
# 
_struct.entry_id                  7I33 
_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-0032179-001 (A71EV2A-x3436)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I33 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J 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 7I33 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I33 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,I 
2 1 B,F,G,H,J 
# 
_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 ? ? ? ? ? ? ? 2.314 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
# 
_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_555 112.2 ? 
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_555 107.4 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.5 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 104.8 ? 
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_555 101.1 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.3 ? 
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_555 109.4 ? 
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_555 107.3 ? 
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_555 106.1 ? 
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_555 100.7 ? 
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_555 114.6 ? 
# 
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                   7I33 
_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 303 ? ? O A HOH 310 ? ? 1.92 
2 1 O C HOH 337 ? ? O C HOH 420 ? ? 2.10 
3 1 O A HOH 349 ? ? O A HOH 407 ? ? 2.15 
4 1 O C HOH 388 ? ? O C HOH 447 ? ? 2.15 
# 
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 ? ? -133.68 -32.22 
2 1 SER C 125 ? ? -134.49 -31.03 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.9457 8.2083   14.4728 -0.0183 -0.0141 -0.0024 0.0066 -0.0023 0.0048 1.3147 0.8321 0.5052 0.8765 
-0.5272 -0.3084 -0.0074 0.0463 0.1010 0.0221 0.0436 0.0222 -0.0111 -0.0441 -0.0361 
'X-RAY DIFFRACTION' 2 ? refined 25.8271 -20.1340 17.7844 -0.0206 -0.0127 0.0097  0.0081 -0.0017 0.0149 0.7203 0.8917 0.1680 
-0.3200 -0.1640 -0.0440 -0.0044 0.0044 0.1133 0.0317 0.0391 0.0038 0.0284  0.0125  -0.0347 
# 
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 
A1B05 N1   N  Y N 1   
A1B05 N3   N  Y N 2   
A1B05 C4   C  N N 3   
A1B05 C5   C  N N 4   
A1B05 C6   C  Y N 5   
A1B05 C7   C  Y N 6   
A1B05 C8   C  Y N 7   
A1B05 O    O  N N 8   
A1B05 C3   C  N N 9   
A1B05 C2   C  Y N 10  
A1B05 C1   C  Y N 11  
A1B05 N4   N  Y N 12  
A1B05 N    N  Y N 13  
A1B05 C    C  N N 14  
A1B05 N2   N  N N 15  
A1B05 O1   O  Y N 16  
A1B05 H6   H  N N 17  
A1B05 H5   H  N N 18  
A1B05 H7   H  N N 19  
A1B05 H8   H  N N 20  
A1B05 H9   H  N N 21  
A1B05 H10  H  N N 22  
A1B05 H3   H  N N 23  
A1B05 H1   H  N N 24  
A1B05 H2   H  N N 25  
A1B05 H    H  N N 26  
A1B05 H4   H  N N 27  
ALA   N    N  N N 28  
ALA   CA   C  N S 29  
ALA   C    C  N N 30  
ALA   O    O  N N 31  
ALA   CB   C  N N 32  
ALA   OXT  O  N N 33  
ALA   H    H  N N 34  
ALA   H2   H  N N 35  
ALA   HA   H  N N 36  
ALA   HB1  H  N N 37  
ALA   HB2  H  N N 38  
ALA   HB3  H  N N 39  
ALA   HXT  H  N N 40  
ARG   N    N  N N 41  
ARG   CA   C  N S 42  
ARG   C    C  N N 43  
ARG   O    O  N N 44  
ARG   CB   C  N N 45  
ARG   CG   C  N N 46  
ARG   CD   C  N N 47  
ARG   NE   N  N N 48  
ARG   CZ   C  N N 49  
ARG   NH1  N  N N 50  
ARG   NH2  N  N N 51  
ARG   OXT  O  N N 52  
ARG   H    H  N N 53  
ARG   H2   H  N N 54  
ARG   HA   H  N N 55  
ARG   HB2  H  N N 56  
ARG   HB3  H  N N 57  
ARG   HG2  H  N N 58  
ARG   HG3  H  N N 59  
ARG   HD2  H  N N 60  
ARG   HD3  H  N N 61  
ARG   HE   H  N N 62  
ARG   HH11 H  N N 63  
ARG   HH12 H  N N 64  
ARG   HH21 H  N N 65  
ARG   HH22 H  N N 66  
ARG   HXT  H  N N 67  
ASN   N    N  N N 68  
ASN   CA   C  N S 69  
ASN   C    C  N N 70  
ASN   O    O  N N 71  
ASN   CB   C  N N 72  
ASN   CG   C  N N 73  
ASN   OD1  O  N N 74  
ASN   ND2  N  N N 75  
ASN   OXT  O  N N 76  
ASN   H    H  N N 77  
ASN   H2   H  N N 78  
ASN   HA   H  N N 79  
ASN   HB2  H  N N 80  
ASN   HB3  H  N N 81  
ASN   HD21 H  N N 82  
ASN   HD22 H  N N 83  
ASN   HXT  H  N N 84  
ASP   N    N  N N 85  
ASP   CA   C  N S 86  
ASP   C    C  N N 87  
ASP   O    O  N N 88  
ASP   CB   C  N N 89  
ASP   CG   C  N N 90  
ASP   OD1  O  N N 91  
ASP   OD2  O  N N 92  
ASP   OXT  O  N N 93  
ASP   H    H  N N 94  
ASP   H2   H  N N 95  
ASP   HA   H  N N 96  
ASP   HB2  H  N N 97  
ASP   HB3  H  N N 98  
ASP   HD2  H  N N 99  
ASP   HXT  H  N N 100 
CYS   N    N  N N 101 
CYS   CA   C  N R 102 
CYS   C    C  N N 103 
CYS   O    O  N N 104 
CYS   CB   C  N N 105 
CYS   SG   S  N N 106 
CYS   OXT  O  N N 107 
CYS   H    H  N N 108 
CYS   H2   H  N N 109 
CYS   HA   H  N N 110 
CYS   HB2  H  N N 111 
CYS   HB3  H  N N 112 
CYS   HG   H  N N 113 
CYS   HXT  H  N N 114 
DMS   S    S  N N 115 
DMS   O    O  N N 116 
DMS   C1   C  N N 117 
DMS   C2   C  N N 118 
DMS   H11  H  N N 119 
DMS   H12  H  N N 120 
DMS   H13  H  N N 121 
DMS   H21  H  N N 122 
DMS   H22  H  N N 123 
DMS   H23  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
HIS   N    N  N N 174 
HIS   CA   C  N S 175 
HIS   C    C  N N 176 
HIS   O    O  N N 177 
HIS   CB   C  N N 178 
HIS   CG   C  Y N 179 
HIS   ND1  N  Y N 180 
HIS   CD2  C  Y N 181 
HIS   CE1  C  Y N 182 
HIS   NE2  N  Y N 183 
HIS   OXT  O  N N 184 
HIS   H    H  N N 185 
HIS   H2   H  N N 186 
HIS   HA   H  N N 187 
HIS   HB2  H  N N 188 
HIS   HB3  H  N N 189 
HIS   HD1  H  N N 190 
HIS   HD2  H  N N 191 
HIS   HE1  H  N N 192 
HIS   HE2  H  N N 193 
HIS   HXT  H  N N 194 
HOH   O    O  N N 195 
HOH   H1   H  N N 196 
HOH   H2   H  N N 197 
ILE   N    N  N N 198 
ILE   CA   C  N S 199 
ILE   C    C  N N 200 
ILE   O    O  N N 201 
ILE   CB   C  N S 202 
ILE   CG1  C  N N 203 
ILE   CG2  C  N N 204 
ILE   CD1  C  N N 205 
ILE   OXT  O  N N 206 
ILE   H    H  N N 207 
ILE   H2   H  N N 208 
ILE   HA   H  N N 209 
ILE   HB   H  N N 210 
ILE   HG12 H  N N 211 
ILE   HG13 H  N N 212 
ILE   HG21 H  N N 213 
ILE   HG22 H  N N 214 
ILE   HG23 H  N N 215 
ILE   HD11 H  N N 216 
ILE   HD12 H  N N 217 
ILE   HD13 H  N N 218 
ILE   HXT  H  N N 219 
LEU   N    N  N N 220 
LEU   CA   C  N S 221 
LEU   C    C  N N 222 
LEU   O    O  N N 223 
LEU   CB   C  N N 224 
LEU   CG   C  N N 225 
LEU   CD1  C  N N 226 
LEU   CD2  C  N N 227 
LEU   OXT  O  N N 228 
LEU   H    H  N N 229 
LEU   H2   H  N N 230 
LEU   HA   H  N N 231 
LEU   HB2  H  N N 232 
LEU   HB3  H  N N 233 
LEU   HG   H  N N 234 
LEU   HD11 H  N N 235 
LEU   HD12 H  N N 236 
LEU   HD13 H  N N 237 
LEU   HD21 H  N N 238 
LEU   HD22 H  N N 239 
LEU   HD23 H  N N 240 
LEU   HXT  H  N N 241 
LYS   N    N  N N 242 
LYS   CA   C  N S 243 
LYS   C    C  N N 244 
LYS   O    O  N N 245 
LYS   CB   C  N N 246 
LYS   CG   C  N N 247 
LYS   CD   C  N N 248 
LYS   CE   C  N N 249 
LYS   NZ   N  N N 250 
LYS   OXT  O  N N 251 
LYS   H    H  N N 252 
LYS   H2   H  N N 253 
LYS   HA   H  N N 254 
LYS   HB2  H  N N 255 
LYS   HB3  H  N N 256 
LYS   HG2  H  N N 257 
LYS   HG3  H  N N 258 
LYS   HD2  H  N N 259 
LYS   HD3  H  N N 260 
LYS   HE2  H  N N 261 
LYS   HE3  H  N N 262 
LYS   HZ1  H  N N 263 
LYS   HZ2  H  N N 264 
LYS   HZ3  H  N N 265 
LYS   HXT  H  N N 266 
MET   N    N  N N 267 
MET   CA   C  N S 268 
MET   C    C  N N 269 
MET   O    O  N N 270 
MET   CB   C  N N 271 
MET   CG   C  N N 272 
MET   SD   S  N N 273 
MET   CE   C  N N 274 
MET   OXT  O  N N 275 
MET   H    H  N N 276 
MET   H2   H  N N 277 
MET   HA   H  N N 278 
MET   HB2  H  N N 279 
MET   HB3  H  N N 280 
MET   HG2  H  N N 281 
MET   HG3  H  N N 282 
MET   HE1  H  N N 283 
MET   HE2  H  N N 284 
MET   HE3  H  N N 285 
MET   HXT  H  N N 286 
PHE   N    N  N N 287 
PHE   CA   C  N S 288 
PHE   C    C  N N 289 
PHE   O    O  N N 290 
PHE   CB   C  N N 291 
PHE   CG   C  Y N 292 
PHE   CD1  C  Y N 293 
PHE   CD2  C  Y N 294 
PHE   CE1  C  Y N 295 
PHE   CE2  C  Y N 296 
PHE   CZ   C  Y N 297 
PHE   OXT  O  N N 298 
PHE   H    H  N N 299 
PHE   H2   H  N N 300 
PHE   HA   H  N N 301 
PHE   HB2  H  N N 302 
PHE   HB3  H  N N 303 
PHE   HD1  H  N N 304 
PHE   HD2  H  N N 305 
PHE   HE1  H  N N 306 
PHE   HE2  H  N N 307 
PHE   HZ   H  N N 308 
PHE   HXT  H  N N 309 
PRO   N    N  N N 310 
PRO   CA   C  N S 311 
PRO   C    C  N N 312 
PRO   O    O  N N 313 
PRO   CB   C  N N 314 
PRO   CG   C  N N 315 
PRO   CD   C  N N 316 
PRO   OXT  O  N N 317 
PRO   H    H  N N 318 
PRO   HA   H  N N 319 
PRO   HB2  H  N N 320 
PRO   HB3  H  N N 321 
PRO   HG2  H  N N 322 
PRO   HG3  H  N N 323 
PRO   HD2  H  N N 324 
PRO   HD3  H  N N 325 
PRO   HXT  H  N N 326 
SER   N    N  N N 327 
SER   CA   C  N S 328 
SER   C    C  N N 329 
SER   O    O  N N 330 
SER   CB   C  N N 331 
SER   OG   O  N N 332 
SER   OXT  O  N N 333 
SER   H    H  N N 334 
SER   H2   H  N N 335 
SER   HA   H  N N 336 
SER   HB2  H  N N 337 
SER   HB3  H  N N 338 
SER   HG   H  N N 339 
SER   HXT  H  N N 340 
THR   N    N  N N 341 
THR   CA   C  N S 342 
THR   C    C  N N 343 
THR   O    O  N N 344 
THR   CB   C  N R 345 
THR   OG1  O  N N 346 
THR   CG2  C  N N 347 
THR   OXT  O  N N 348 
THR   H    H  N N 349 
THR   H2   H  N N 350 
THR   HA   H  N N 351 
THR   HB   H  N N 352 
THR   HG1  H  N N 353 
THR   HG21 H  N N 354 
THR   HG22 H  N N 355 
THR   HG23 H  N N 356 
THR   HXT  H  N N 357 
TRP   N    N  N N 358 
TRP   CA   C  N S 359 
TRP   C    C  N N 360 
TRP   O    O  N N 361 
TRP   CB   C  N N 362 
TRP   CG   C  Y N 363 
TRP   CD1  C  Y N 364 
TRP   CD2  C  Y N 365 
TRP   NE1  N  Y N 366 
TRP   CE2  C  Y N 367 
TRP   CE3  C  Y N 368 
TRP   CZ2  C  Y N 369 
TRP   CZ3  C  Y N 370 
TRP   CH2  C  Y N 371 
TRP   OXT  O  N N 372 
TRP   H    H  N N 373 
TRP   H2   H  N N 374 
TRP   HA   H  N N 375 
TRP   HB2  H  N N 376 
TRP   HB3  H  N N 377 
TRP   HD1  H  N N 378 
TRP   HE1  H  N N 379 
TRP   HE3  H  N N 380 
TRP   HZ2  H  N N 381 
TRP   HZ3  H  N N 382 
TRP   HH2  H  N N 383 
TRP   HXT  H  N N 384 
TYR   N    N  N N 385 
TYR   CA   C  N S 386 
TYR   C    C  N N 387 
TYR   O    O  N N 388 
TYR   CB   C  N N 389 
TYR   CG   C  Y N 390 
TYR   CD1  C  Y N 391 
TYR   CD2  C  Y N 392 
TYR   CE1  C  Y N 393 
TYR   CE2  C  Y N 394 
TYR   CZ   C  Y N 395 
TYR   OH   O  N N 396 
TYR   OXT  O  N N 397 
TYR   H    H  N N 398 
TYR   H2   H  N N 399 
TYR   HA   H  N N 400 
TYR   HB2  H  N N 401 
TYR   HB3  H  N N 402 
TYR   HD1  H  N N 403 
TYR   HD2  H  N N 404 
TYR   HE1  H  N N 405 
TYR   HE2  H  N N 406 
TYR   HH   H  N N 407 
TYR   HXT  H  N N 408 
VAL   N    N  N N 409 
VAL   CA   C  N S 410 
VAL   C    C  N N 411 
VAL   O    O  N N 412 
VAL   CB   C  N N 413 
VAL   CG1  C  N N 414 
VAL   CG2  C  N N 415 
VAL   OXT  O  N N 416 
VAL   H    H  N N 417 
VAL   H2   H  N N 418 
VAL   HA   H  N N 419 
VAL   HB   H  N N 420 
VAL   HG11 H  N N 421 
VAL   HG12 H  N N 422 
VAL   HG13 H  N N 423 
VAL   HG21 H  N N 424 
VAL   HG22 H  N N 425 
VAL   HG23 H  N N 426 
VAL   HXT  H  N N 427 
ZN    ZN   ZN N N 428 
# 
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 
A1B05 C   N    sing N N 1   
A1B05 N   N1   sing Y N 2   
A1B05 N1  C1   doub Y N 3   
A1B05 C1  C2   sing Y N 4   
A1B05 C2  C3   sing N N 5   
A1B05 C3  O    doub N N 6   
A1B05 N2  C3   sing N N 7   
A1B05 C4  N2   sing N N 8   
A1B05 C5  C4   sing N N 9   
A1B05 C6  C5   sing N N 10  
A1B05 C6  C7   doub Y N 11  
A1B05 C7  O1   sing Y N 12  
A1B05 O1  C8   sing Y N 13  
A1B05 C8  N3   doub Y N 14  
A1B05 N3  C6   sing Y N 15  
A1B05 N4  C2   doub Y N 16  
A1B05 N   N4   sing Y N 17  
A1B05 C4  H6   sing N N 18  
A1B05 C4  H5   sing N N 19  
A1B05 C5  H7   sing N N 20  
A1B05 C5  H8   sing N N 21  
A1B05 C7  H9   sing N N 22  
A1B05 C8  H10  sing N N 23  
A1B05 C1  H3   sing N N 24  
A1B05 C   H1   sing N N 25  
A1B05 C   H2   sing N N 26  
A1B05 C   H    sing N N 27  
A1B05 N2  H4   sing N N 28  
ALA   N   CA   sing N N 29  
ALA   N   H    sing N N 30  
ALA   N   H2   sing N N 31  
ALA   CA  C    sing N N 32  
ALA   CA  CB   sing N N 33  
ALA   CA  HA   sing N N 34  
ALA   C   O    doub N N 35  
ALA   C   OXT  sing N N 36  
ALA   CB  HB1  sing N N 37  
ALA   CB  HB2  sing N N 38  
ALA   CB  HB3  sing N N 39  
ALA   OXT HXT  sing N N 40  
ARG   N   CA   sing N N 41  
ARG   N   H    sing N N 42  
ARG   N   H2   sing N N 43  
ARG   CA  C    sing N N 44  
ARG   CA  CB   sing N N 45  
ARG   CA  HA   sing N N 46  
ARG   C   O    doub N N 47  
ARG   C   OXT  sing N N 48  
ARG   CB  CG   sing N N 49  
ARG   CB  HB2  sing N N 50  
ARG   CB  HB3  sing N N 51  
ARG   CG  CD   sing N N 52  
ARG   CG  HG2  sing N N 53  
ARG   CG  HG3  sing N N 54  
ARG   CD  NE   sing N N 55  
ARG   CD  HD2  sing N N 56  
ARG   CD  HD3  sing N N 57  
ARG   NE  CZ   sing N N 58  
ARG   NE  HE   sing N N 59  
ARG   CZ  NH1  sing N N 60  
ARG   CZ  NH2  doub N N 61  
ARG   NH1 HH11 sing N N 62  
ARG   NH1 HH12 sing N N 63  
ARG   NH2 HH21 sing N N 64  
ARG   NH2 HH22 sing N N 65  
ARG   OXT HXT  sing N N 66  
ASN   N   CA   sing N N 67  
ASN   N   H    sing N N 68  
ASN   N   H2   sing N N 69  
ASN   CA  C    sing N N 70  
ASN   CA  CB   sing N N 71  
ASN   CA  HA   sing N N 72  
ASN   C   O    doub N N 73  
ASN   C   OXT  sing N N 74  
ASN   CB  CG   sing N N 75  
ASN   CB  HB2  sing N N 76  
ASN   CB  HB3  sing N N 77  
ASN   CG  OD1  doub N N 78  
ASN   CG  ND2  sing N N 79  
ASN   ND2 HD21 sing N N 80  
ASN   ND2 HD22 sing N N 81  
ASN   OXT HXT  sing N N 82  
ASP   N   CA   sing N N 83  
ASP   N   H    sing N N 84  
ASP   N   H2   sing N N 85  
ASP   CA  C    sing N N 86  
ASP   CA  CB   sing N N 87  
ASP   CA  HA   sing N N 88  
ASP   C   O    doub N N 89  
ASP   C   OXT  sing N N 90  
ASP   CB  CG   sing N N 91  
ASP   CB  HB2  sing N N 92  
ASP   CB  HB3  sing N N 93  
ASP   CG  OD1  doub N N 94  
ASP   CG  OD2  sing N N 95  
ASP   OD2 HD2  sing N N 96  
ASP   OXT HXT  sing N N 97  
CYS   N   CA   sing N N 98  
CYS   N   H    sing N N 99  
CYS   N   H2   sing N N 100 
CYS   CA  C    sing N N 101 
CYS   CA  CB   sing N N 102 
CYS   CA  HA   sing N N 103 
CYS   C   O    doub N N 104 
CYS   C   OXT  sing N N 105 
CYS   CB  SG   sing N N 106 
CYS   CB  HB2  sing N N 107 
CYS   CB  HB3  sing N N 108 
CYS   SG  HG   sing N N 109 
CYS   OXT HXT  sing N N 110 
DMS   S   O    doub N N 111 
DMS   S   C1   sing N N 112 
DMS   S   C2   sing N N 113 
DMS   C1  H11  sing N N 114 
DMS   C1  H12  sing N N 115 
DMS   C1  H13  sing N N 116 
DMS   C2  H21  sing N N 117 
DMS   C2  H22  sing N N 118 
DMS   C2  H23  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TRP   N   CA   sing N N 343 
TRP   N   H    sing N N 344 
TRP   N   H2   sing N N 345 
TRP   CA  C    sing N N 346 
TRP   CA  CB   sing N N 347 
TRP   CA  HA   sing N N 348 
TRP   C   O    doub N N 349 
TRP   C   OXT  sing N N 350 
TRP   CB  CG   sing N N 351 
TRP   CB  HB2  sing N N 352 
TRP   CB  HB3  sing N N 353 
TRP   CG  CD1  doub Y N 354 
TRP   CG  CD2  sing Y N 355 
TRP   CD1 NE1  sing Y N 356 
TRP   CD1 HD1  sing N N 357 
TRP   CD2 CE2  doub Y N 358 
TRP   CD2 CE3  sing Y N 359 
TRP   NE1 CE2  sing Y N 360 
TRP   NE1 HE1  sing N N 361 
TRP   CE2 CZ2  sing Y N 362 
TRP   CE3 CZ3  doub Y N 363 
TRP   CE3 HE3  sing N N 364 
TRP   CZ2 CH2  doub Y N 365 
TRP   CZ2 HZ2  sing N N 366 
TRP   CZ3 CH2  sing Y N 367 
TRP   CZ3 HZ3  sing N N 368 
TRP   CH2 HH2  sing N N 369 
TRP   OXT HXT  sing N N 370 
TYR   N   CA   sing N N 371 
TYR   N   H    sing N N 372 
TYR   N   H2   sing N N 373 
TYR   CA  C    sing N N 374 
TYR   CA  CB   sing N N 375 
TYR   CA  HA   sing N N 376 
TYR   C   O    doub N N 377 
TYR   C   OXT  sing N N 378 
TYR   CB  CG   sing N N 379 
TYR   CB  HB2  sing N N 380 
TYR   CB  HB3  sing N N 381 
TYR   CG  CD1  doub Y N 382 
TYR   CG  CD2  sing Y N 383 
TYR   CD1 CE1  sing Y N 384 
TYR   CD1 HD1  sing N N 385 
TYR   CD2 CE2  doub Y N 386 
TYR   CD2 HD2  sing N N 387 
TYR   CE1 CZ   doub Y N 388 
TYR   CE1 HE1  sing N N 389 
TYR   CE2 CZ   sing Y N 390 
TYR   CE2 HE2  sing N N 391 
TYR   CZ  OH   sing N N 392 
TYR   OH  HH   sing N N 393 
TYR   OXT HXT  sing N N 394 
VAL   N   CA   sing N N 395 
VAL   N   H    sing N N 396 
VAL   N   H2   sing N N 397 
VAL   CA  C    sing N N 398 
VAL   CA  CB   sing N N 399 
VAL   CA  HA   sing N N 400 
VAL   C   O    doub N N 401 
VAL   C   OXT  sing N N 402 
VAL   CB  CG1  sing N N 403 
VAL   CB  CG2  sing N N 404 
VAL   CB  HB   sing N N 405 
VAL   CG1 HG11 sing N N 406 
VAL   CG1 HG12 sing N N 407 
VAL   CG1 HG13 sing N N 408 
VAL   CG2 HG21 sing N N 409 
VAL   CG2 HG22 sing N N 410 
VAL   CG2 HG23 sing N N 411 
VAL   OXT HXT  sing N N 412 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I33 
_atom_sites.fract_transf_matrix[1][1]   0.011553 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000948 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017558 
_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]   0.015460 
_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   ? 17.751 8.032   24.876 1.00 14.61  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.019 8.118   24.095 1.00 13.94  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.145 6.918   23.158 1.00 14.18  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.417 5.924   23.339 1.00 15.28  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.213 8.170   25.053 1.00 16.50  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.266 6.969   25.794 1.00 19.99  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.052 6.997   22.180 1.00 12.75  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.303 5.898   21.257 1.00 12.69  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.721 6.365   19.882 1.00 11.01  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.414 7.487   19.494 1.00 12.63  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.382 5.524   19.154 1.00 10.58  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.854 5.868   17.812 1.00 11.02  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.812 4.648   16.907 1.00 10.55  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.740 3.498   17.390 1.00 11.38  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.308 6.382   17.929 1.00 13.06  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.900 4.896   15.603 1.00 10.04  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.117 3.857   14.580 1.00 9.97   ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.581 3.936   14.173 1.00 10.69  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.063 5.046   13.883 1.00 11.05  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.241 4.071   13.341 1.00 9.93   ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.755 4.220   13.699 1.00 11.80  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.432 2.917   12.355 1.00 11.60  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.916 4.791   12.508 1.00 12.74  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.279 2.802   14.130 1.00 10.90  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.689 2.774   13.720 1.00 11.61  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.780 1.959   12.447 1.00 12.29  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.739 0.717   12.499 1.00 13.20  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.567 2.179   14.844 1.00 12.82  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.622 3.069   16.060 1.00 12.25  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.510 4.145   16.128 1.00 13.67  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.791 2.850   17.146 1.00 14.44  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.508 5.022   17.218 1.00 14.46  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.817 3.692   18.264 1.00 15.12  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.663 4.790   18.278 1.00 14.91  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.665 5.668   19.360 1.00 17.31  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.832 2.610   11.288 1.00 12.55  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.887 1.978   9.977  1.00 13.06  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.127 2.468   9.260  1.00 13.67  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.376 3.675   9.179  1.00 12.92  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.589 2.238   9.163  1.00 14.80  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.272 3.729   9.039  1.00 15.16  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.706 1.613   7.779  1.00 16.83  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.966 1.552   8.757  1.00 14.67  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.230 1.956   8.117  1.00 16.44  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.068 2.834   9.040  1.00 14.68  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.185 2.546   10.237 1.00 14.80  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.535 3.998   8.522  1.00 14.12  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.240 4.979   9.364  1.00 13.68  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.350 6.163   9.686  1.00 13.02  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.847 7.295   9.818  1.00 12.96  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.589 5.434   8.781  1.00 15.69  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.649 4.351   8.874  1.00 19.02  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.395 4.268   9.868  1.00 22.03  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.701 3.491   7.903  1.00 18.38  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.068 5.893   9.925  1.00 11.55  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.093 6.924   10.298 1.00 11.40  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.442 6.594   11.638 1.00 11.09  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.148 5.416   11.953 1.00 12.26  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.983 7.025   9.233  1.00 11.82  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.478 7.435   7.862  1.00 12.98  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.152 8.640   7.669  1.00 14.02  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.280 6.617   6.759  1.00 15.67  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.610 9.020   6.412  1.00 15.28  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.705 7.013   5.489  1.00 16.50  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.353 8.214   5.327  1.00 16.56  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.802 8.643   4.084  1.00 21.07  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.103 7.649   12.384 1.00 10.41  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.312 7.584   13.608 1.00 10.22  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.092 8.453   13.377 1.00 10.33  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.235 9.662   13.090 1.00 10.63  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.145 8.095   14.799 1.00 12.16  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.357 8.429   16.060 1.00 12.52  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.313 8.817   17.232 1.00 13.48  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.771 9.884   18.095 1.00 13.31  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.106 9.694   19.236 1.00 15.16  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.822 8.451   19.656 1.00 16.44  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.681 10.739  19.944 1.00 15.57  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.894 7.871   13.446 1.00 10.09  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.621 8.595   13.237 1.00 9.55   ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.954 8.803   14.578 1.00 10.41  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.679 7.806   15.285 1.00 10.58  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.681 7.821   12.296 1.00 10.16  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.464 8.664   11.963 1.00 11.18  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.374 7.300   11.037 1.00 11.90  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.719 10.063  14.957 1.00 9.43   ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.113 10.381  16.264 0.50 9.31   ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.168 10.370  16.283 0.50 10.94  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 20.023 11.387  16.094 1.00 9.42   ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.877 12.030  15.012 1.00 10.88  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.156 10.979  17.255 0.50 9.18   ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.347 10.980  17.147 0.50 14.26  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.082 9.905   17.752 0.50 11.19  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.973 11.232  18.597 0.50 14.72  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.877 12.222  16.661 0.50 6.23   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.581 10.117  17.092 0.50 17.52  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.184 11.558  17.126 1.00 9.73   ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.196 12.655  17.097 1.00 9.78   ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 19.004 13.975  17.119 1.00 10.25  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.954 14.141  17.912 1.00 10.35  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.333 12.657  18.369 1.00 10.42  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.454 11.429  18.474 1.00 10.32  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.850 10.399  19.062 1.00 11.18  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.267 11.488  17.869 1.00 11.65  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.631 14.905  16.236 1.00 10.90  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.381 16.183  16.177 1.00 10.84  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.370 16.874  17.547 1.00 12.00  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.405 17.412  17.967 1.00 12.71  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.772 17.071  15.130 1.00 12.25  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.563 18.396  14.879 1.00 12.27  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.790 19.266  13.904 1.00 13.87  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.510 20.468  13.442 1.00 14.55  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.503 21.623  14.076 1.00 15.91  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.974 21.721  15.290 1.00 16.08  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.072 22.696  13.518 1.00 16.94  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.226 16.773  18.284 1.00 11.54  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.146 17.462  19.576 1.00 12.96  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 19.015 16.852  20.671 1.00 13.39  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.183 17.469  21.746 1.00 15.79  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.689 17.625  20.070 1.00 14.02  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 16.006 16.369  20.563 1.00 13.34  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.394 15.487  19.685 1.00 13.35  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.850 15.887  21.829 1.00 14.27  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.863 14.510  20.447 1.00 13.89  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.105 14.722  21.733 1.00 14.22  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.535 15.624  20.461 1.00 13.39  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.408 14.908  21.404 1.00 13.03  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.866 14.850  20.929 1.00 14.23  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.698 14.255  21.589 1.00 14.81  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.880 13.510  21.745 1.00 12.52  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.488 13.509  22.350 1.00 13.33  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 18.029 12.055  22.612 1.00 14.18  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.469 14.313  23.694 1.00 15.30  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.193 15.513  19.806 1.00 13.08  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.568 15.473  19.271 1.00 13.59  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.547 16.114  20.241 1.00 13.98  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.225 17.141  20.864 1.00 14.90  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.618 16.204  17.921 1.00 13.30  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.719 15.500  20.366 1.00 13.60  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.765 16.018  21.273 1.00 12.96  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.699 17.022  20.544 1.00 13.60  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.651 17.158  19.302 1.00 12.83  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.622 14.860  21.778 1.00 15.50  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.339 14.328  20.654 1.00 15.41  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.808 13.763  22.473 1.00 16.30  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.636 17.691  21.273 1.00 13.85  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.603 18.554  20.627 1.00 14.12  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.450 17.731  19.662 1.00 13.60  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.731 18.198  18.553 1.00 14.12  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.521 19.243  21.672 1.00 15.41  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.801 19.833  21.049 1.00 21.08  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.799 21.009  20.279 1.00 24.67  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.048 19.277  20.953 1.00 24.87  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 33.052 21.214  19.903 1.00 25.60  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.839 20.161  20.215 1.00 26.71  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.829 16.472  20.029 1.00 13.76  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.615 15.659  19.110 1.00 13.75  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.843 15.379  17.808 1.00 12.17  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.421 15.414  16.716 1.00 12.94  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.054 14.330  19.727 1.00 15.99  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 33.029 13.622  18.809 1.00 21.75  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.215 14.060  18.651 1.00 25.46  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.579 12.533  18.160 1.00 24.25  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.510 15.146  17.923 1.00 12.35  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.709 14.982  16.702 1.00 11.85  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.763 16.229  15.795 1.00 11.34  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.970 16.127  14.577 1.00 12.16  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.249 14.694  17.054 1.00 11.66  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.995 13.337  17.642 1.00 13.00  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.625 12.358  17.177 1.00 13.66  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.154 13.252  18.581 1.00 12.99  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.560 17.413  16.396 1.00 10.96  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.575 18.660  15.614 1.00 11.70  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.983 18.928  15.022 1.00 11.35  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.049 19.504  13.923 1.00 12.34  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.141 19.841  16.515 1.00 12.41  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.643 19.915  16.650 1.00 11.78  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.905 19.600  17.757 1.00 13.19  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.699 20.369  15.658 1.00 12.15  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.565 19.820  17.514 1.00 13.08  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.411 20.302  16.229 1.00 12.56  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.826 20.875  14.353 1.00 13.25  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.248 20.672  15.513 1.00 14.24  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.679 21.142  13.631 1.00 14.47  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.434 21.160  14.237 1.00 14.69  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.057 18.520  15.731 1.00 11.65  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.411 18.742  15.232 1.00 12.16  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.832 17.737  14.155 1.00 13.28  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.868 17.900  13.512 1.00 14.84  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.388 18.682  16.394 1.00 14.29  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.053 16.663  13.955 1.00 12.90  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.324 15.619  12.939 1.00 12.74  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.046 15.451  12.083 1.00 12.26  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.645 14.314  11.732 1.00 12.84  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.712 14.285  13.635 1.00 14.17  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.054 14.476  14.292 1.00 15.12  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.090 14.403  13.614 1.00 18.68  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.074 14.778  15.581 1.00 16.30  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.399 16.540  11.749 1.00 12.15  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.090 16.515  11.105 1.00 11.22  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.131 16.079  9.671  1.00 12.68  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.959 16.548  8.881  1.00 14.48  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.527 17.937  11.178 1.00 11.80  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.103 18.093  10.596 1.00 12.53  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.074 17.317  11.438 1.00 12.76  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.688 19.585  10.565 1.00 14.68  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.202 15.193  9.276  1.00 11.32  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.020 14.792  7.869  1.00 11.77  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.763 15.503  7.309  1.00 12.10  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.786 16.042  6.205  1.00 13.93  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.893 13.258  7.760  1.00 11.84  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.501 12.852  6.319  1.00 14.37  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.196 12.582  8.221  1.00 14.33  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.636 15.494  8.057  1.00 12.24  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.361 16.025  7.556  1.00 12.10  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.417 16.239  8.715  1.00 11.99  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.452 15.455  9.691  1.00 11.91  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.741 14.998  6.530  1.00 12.97  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.318 15.277  6.105  1.00 14.23  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.901 16.151  5.132  1.00 16.28  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.127 14.689  6.649  1.00 13.49  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.526 16.114  5.025  1.00 17.30  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.029 15.192  5.909  1.00 15.41  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.886 13.739  7.647  1.00 14.52  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.704 14.759  6.140  1.00 16.99  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.586 13.306  7.848  1.00 15.61  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.507 13.861  7.150  1.00 16.78  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.593 17.274  8.671  1.00 12.16  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.601 17.475  9.720  1.00 12.86  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.363 18.115  9.112  1.00 13.40  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.458 18.912  8.148  1.00 13.80  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.157 18.300  10.885 1.00 14.66  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.716 19.677  10.507 1.00 15.53  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.738 20.841  10.306 1.00 15.41  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.077 21.806  9.565  1.00 17.42  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.653 20.852  10.933 1.00 15.41  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.207 17.828  9.681  1.00 13.27  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.944 18.400  9.213  1.00 13.28  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.975 18.586  10.380 1.00 12.80  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.469 17.596  10.950 1.00 13.32  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.330 17.498  8.115  1.00 15.37  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.049 17.988  7.482  1.00 18.24  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.215 18.517  8.200  1.00 19.56  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.847 17.735  6.286  1.00 22.21  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.759 19.835  10.795 1.00 13.34  ? 36  SER   A N   1 
ATOM   245  C  CA  . SER   A 1 30  ? 15.930 20.164  11.931 1.00 13.84  ? 36  SER   A CA  1 
ATOM   246  C  C   . SER   A 1 30  ? 14.468 19.757  11.701 1.00 14.53  ? 36  SER   A C   1 
ATOM   247  O  O   . SER   A 1 30  ? 13.840 19.244  12.641 1.00 15.36  ? 36  SER   A O   1 
ATOM   248  C  CB  . SER   A 1 30  ? 16.060 21.655  12.241 1.00 16.10  ? 36  SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 30  ? 15.153 22.027  13.275 1.00 19.81  ? 36  SER   A OG  1 
ATOM   250  N  N   . SER   A 1 31  ? 13.966 19.857  10.473 1.00 15.11  ? 37  SER   A N   1 
ATOM   251  C  CA  . SER   A 1 31  ? 12.580 19.458  10.205 1.00 14.85  ? 37  SER   A CA  1 
ATOM   252  C  C   . SER   A 1 31  ? 12.342 17.966  10.396 1.00 14.36  ? 37  SER   A C   1 
ATOM   253  O  O   . SER   A 1 31  ? 11.193 17.562  10.636 1.00 16.32  ? 37  SER   A O   1 
ATOM   254  C  CB  . SER   A 1 31  ? 12.141 19.873  8.806  1.00 17.86  ? 37  SER   A CB  1 
ATOM   255  O  OG  . SER   A 1 31  ? 12.644 19.062  7.771  1.00 21.96  ? 37  SER   A OG  1 
ATOM   256  N  N   . ARG   A 1 32  ? 13.398 17.146  10.315 1.00 12.81  ? 38  ARG   A N   1 
ATOM   257  C  CA  . ARG   A 1 32  ? 13.309 15.703  10.518 1.00 12.72  ? 38  ARG   A CA  1 
ATOM   258  C  C   . ARG   A 1 32  ? 13.782 15.255  11.902 1.00 12.67  ? 38  ARG   A C   1 
ATOM   259  O  O   . ARG   A 1 32  ? 13.666 14.050  12.211 1.00 12.30  ? 38  ARG   A O   1 
ATOM   260  C  CB  . ARG   A 1 32  ? 14.155 14.967  9.445  1.00 13.06  ? 38  ARG   A CB  1 
ATOM   261  C  CG  . ARG   A 1 32  ? 13.638 15.167  8.016  1.00 15.40  ? 38  ARG   A CG  1 
ATOM   262  C  CD  . ARG   A 1 32  ? 14.507 14.500  6.969  1.00 14.84  ? 38  ARG   A CD  1 
ATOM   263  N  NE  . ARG   A 1 32  ? 14.402 13.028  7.093  1.00 12.77  ? 38  ARG   A NE  1 
ATOM   264  C  CZ  . ARG   A 1 32  ? 14.581 12.187  6.076  1.00 12.94  ? 38  ARG   A CZ  1 
ATOM   265  N  NH1 . ARG   A 1 32  ? 14.850 12.653  4.851  1.00 15.39  ? 38  ARG   A NH1 1 
ATOM   266  N  NH2 . ARG   A 1 32  ? 14.432 10.872  6.252  1.00 13.53  ? 38  ARG   A NH2 1 
ATOM   267  N  N   . ASP   A 1 33  ? 14.377 16.146  12.703 1.00 12.06  ? 39  ASP   A N   1 
ATOM   268  C  CA  . ASP   A 1 33  ? 15.006 15.804  13.955 1.00 11.16  ? 39  ASP   A CA  1 
ATOM   269  C  C   . ASP   A 1 33  ? 16.128 14.775  13.783 1.00 11.05  ? 39  ASP   A C   1 
ATOM   270  O  O   . ASP   A 1 33  ? 16.343 13.937  14.663 1.00 11.42  ? 39  ASP   A O   1 
ATOM   271  C  CB  . ASP   A 1 33  ? 13.998 15.337  15.034 1.00 12.46  ? 39  ASP   A CB  1 
ATOM   272  C  CG  . ASP   A 1 33  ? 14.642 15.095  16.393 1.00 11.84  ? 39  ASP   A CG  1 
ATOM   273  O  OD1 . ASP   A 1 33  ? 15.513 15.917  16.830 1.00 12.51  ? 39  ASP   A OD1 1 
ATOM   274  O  OD2 . ASP   A 1 33  ? 14.234 14.124  17.111 1.00 13.16  ? 39  ASP   A OD2 1 
ATOM   275  N  N   . LEU   A 1 34  ? 16.920 14.901  12.696 1.00 10.80  ? 40  LEU   A N   1 
ATOM   276  C  CA  . LEU   A 1 34  ? 18.009 13.952  12.472 1.00 10.97  ? 40  LEU   A CA  1 
ATOM   277  C  C   . LEU   A 1 34  ? 19.365 14.643  12.325 1.00 10.30  ? 40  LEU   A C   1 
ATOM   278  O  O   . LEU   A 1 34  ? 19.449 15.756  11.745 1.00 11.42  ? 40  LEU   A O   1 
ATOM   279  C  CB  . LEU   A 1 34  ? 17.777 13.141  11.202 1.00 11.92  ? 40  LEU   A CB  1 
ATOM   280  C  CG  . LEU   A 1 34  ? 16.692 12.041  11.258 1.00 12.58  ? 40  LEU   A CG  1 
ATOM   281  C  CD1 . LEU   A 1 34  ? 16.606 11.336  9.905  1.00 13.64  ? 40  LEU   A CD1 1 
ATOM   282  C  CD2 . LEU   A 1 34  ? 16.966 11.014  12.375 1.00 12.83  ? 40  LEU   A CD2 1 
ATOM   283  N  N   . LEU   A 1 35  ? 20.414 13.973  12.778 1.00 10.00  ? 41  LEU   A N   1 
ATOM   284  C  CA  . LEU   A 1 35  ? 21.787 14.411  12.543 1.00 9.84   ? 41  LEU   A CA  1 
ATOM   285  C  C   . LEU   A 1 35  ? 22.616 13.183  12.375 1.00 9.66   ? 41  LEU   A C   1 
ATOM   286  O  O   . LEU   A 1 35  ? 22.429 12.165  13.082 1.00 10.23  ? 41  LEU   A O   1 
ATOM   287  C  CB  . LEU   A 1 35  ? 22.252 15.286  13.737 1.00 10.79  ? 41  LEU   A CB  1 
ATOM   288  C  CG  . LEU   A 1 35  ? 23.676 15.853  13.635 1.00 10.76  ? 41  LEU   A CG  1 
ATOM   289  C  CD1 . LEU   A 1 35  ? 23.780 17.189  14.331 1.00 12.63  ? 41  LEU   A CD1 1 
ATOM   290  C  CD2 . LEU   A 1 35  ? 24.721 14.906  14.269 1.00 11.27  ? 41  LEU   A CD2 1 
ATOM   291  N  N   . VAL   A 1 36  ? 23.588 13.278  11.453 1.00 10.04  ? 42  VAL   A N   1 
ATOM   292  C  CA  . VAL   A 1 36  ? 24.523 12.179  11.171 1.00 9.94   ? 42  VAL   A CA  1 
ATOM   293  C  C   . VAL   A 1 36  ? 25.933 12.682  11.326 1.00 10.04  ? 42  VAL   A C   1 
ATOM   294  O  O   . VAL   A 1 36  ? 26.271 13.726  10.728 1.00 11.07  ? 42  VAL   A O   1 
ATOM   295  C  CB  . VAL   A 1 36  ? 24.285 11.605  9.750  1.00 10.08  ? 42  VAL   A CB  1 
ATOM   296  C  CG1 . VAL   A 1 36  ? 25.304 10.499  9.442  1.00 11.59  ? 42  VAL   A CG1 1 
ATOM   297  C  CG2 . VAL   A 1 36  ? 22.839 11.077  9.628  1.00 11.40  ? 42  VAL   A CG2 1 
ATOM   298  N  N   . SER   A 1 37  ? 26.757 11.986  12.078 1.00 9.60   ? 43  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 37  ? 28.177 12.323  12.263 1.00 10.55  ? 43  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 37  ? 29.039 11.146  11.807 1.00 10.86  ? 43  SER   A C   1 
ATOM   301  O  O   . SER   A 1 37  ? 28.569 9.999   11.571 1.00 11.41  ? 43  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 37  ? 28.460 12.686  13.714 1.00 11.83  ? 43  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 37  ? 28.152 11.609  14.590 1.00 12.16  ? 43  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 38  ? 30.320 11.420  11.587 1.00 12.00  ? 44  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 38  ? 31.247 10.374  11.143 1.00 13.44  ? 44  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 38  ? 31.881 9.648   12.332 1.00 15.02  ? 44  SER   A C   1 
ATOM   307  O  O   . SER   A 1 38  ? 32.064 10.245  13.427 1.00 17.48  ? 44  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 38  ? 32.331 10.982  10.248 1.00 15.28  ? 44  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 38  ? 33.039 11.952  11.001 1.00 18.48  ? 44  SER   A OG  1 
ATOM   310  N  N   . THR   A 1 39  ? 32.222 8.341   12.148 1.00 15.03  ? 45  THR   A N   1 
ATOM   311  C  CA  . THR   A 1 39  ? 32.828 7.547   13.207 1.00 17.25  ? 45  THR   A CA  1 
ATOM   312  C  C   . THR   A 1 39  ? 34.162 6.981   12.743 1.00 19.20  ? 45  THR   A C   1 
ATOM   313  O  O   . THR   A 1 39  ? 34.365 6.728   11.552 1.00 18.65  ? 45  THR   A O   1 
ATOM   314  C  CB  . THR   A 1 39  ? 31.899 6.363   13.596 1.00 17.81  ? 45  THR   A CB  1 
ATOM   315  O  OG1 . THR   A 1 39  ? 31.739 5.479   12.502 1.00 18.55  ? 45  THR   A OG1 1 
ATOM   316  C  CG2 . THR   A 1 39  ? 30.513 6.813   14.036 1.00 17.76  ? 45  THR   A CG2 1 
ATOM   317  N  N   . THR   A 1 40  ? 35.012 6.681   13.714 1.00 20.05  ? 46  THR   A N   1 
ATOM   318  C  CA  . THR   A 1 40  ? 36.291 6.051   13.414 1.00 21.82  ? 46  THR   A CA  1 
ATOM   319  C  C   . THR   A 1 40  ? 36.079 4.540   13.210 1.00 21.89  ? 46  THR   A C   1 
ATOM   320  O  O   . THR   A 1 40  ? 36.608 3.971   12.249 1.00 24.58  ? 46  THR   A O   1 
ATOM   321  C  CB  . THR   A 1 40  ? 37.314 6.394   14.521 1.00 25.88  ? 46  THR   A CB  1 
ATOM   322  O  OG1 . THR   A 1 40  ? 36.801 5.976   15.776 1.00 30.38  ? 46  THR   A OG1 1 
ATOM   323  C  CG2 . THR   A 1 40  ? 37.571 7.858   14.608 1.00 26.58  ? 46  THR   A CG2 1 
ATOM   324  N  N   . ALA   A 1 41  ? 35.240 3.910   14.048 1.00 22.05  ? 47  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 41  ? 34.974 2.469   13.910 1.00 23.29  ? 47  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 41  ? 33.749 2.169   13.009 1.00 21.45  ? 47  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 41  ? 32.785 2.946   13.008 1.00 21.12  ? 47  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 41  ? 34.704 1.866   15.275 1.00 26.30  ? 47  ALA   A CB  1 
ATOM   329  N  N   . GLN   A 1 42  ? 33.725 1.026   12.333 1.00 20.07  ? 48  GLN   A N   1 
ATOM   330  C  CA  . GLN   A 1 42  ? 32.573 0.627   11.504 1.00 20.45  ? 48  GLN   A CA  1 
ATOM   331  C  C   . GLN   A 1 42  ? 31.477 0.026   12.364 1.00 20.17  ? 48  GLN   A C   1 
ATOM   332  O  O   . GLN   A 1 42  ? 31.756 -0.756  13.276 1.00 21.40  ? 48  GLN   A O   1 
ATOM   333  C  CB  . GLN   A 1 42  ? 32.971 -0.369  10.414 1.00 23.09  ? 48  GLN   A CB  1 
ATOM   334  C  CG  . GLN   A 1 42  ? 33.797 0.257   9.279  1.00 28.60  ? 48  GLN   A CG  1 
ATOM   335  C  CD  . GLN   A 1 42  ? 34.180 -0.802  8.287  1.00 35.24  ? 48  GLN   A CD  1 
ATOM   336  O  OE1 . GLN   A 1 42  ? 35.069 -1.634  8.545  1.00 34.48  ? 48  GLN   A OE1 1 
ATOM   337  N  NE2 . GLN   A 1 42  ? 33.491 -0.815  7.153  1.00 37.01  ? 48  GLN   A NE2 1 
ATOM   338  N  N   . GLY   A 1 43  ? 30.227 0.380   12.054 1.00 17.24  ? 49  GLY   A N   1 
ATOM   339  C  CA  . GLY   A 1 43  ? 29.055 -0.098  12.785 1.00 17.85  ? 49  GLY   A CA  1 
ATOM   340  C  C   . GLY   A 1 43  ? 28.467 -1.377  12.235 1.00 16.66  ? 49  GLY   A C   1 
ATOM   341  O  O   . GLY   A 1 43  ? 28.747 -1.741  11.095 1.00 17.02  ? 49  GLY   A O   1 
ATOM   342  N  N   . CYS   A 1 44  ? 27.498 -1.956  12.991 1.00 14.89  ? 50  CYS   A N   1 
ATOM   343  C  CA  . CYS   A 1 44  ? 26.892 -3.247  12.641 1.00 15.53  ? 50  CYS   A CA  1 
ATOM   344  C  C   . CYS   A 1 44  ? 25.439 -3.193  12.197 1.00 15.71  ? 50  CYS   A C   1 
ATOM   345  O  O   . CYS   A 1 44  ? 24.887 -4.236  11.799 1.00 16.24  ? 50  CYS   A O   1 
ATOM   346  C  CB  . CYS   A 1 44  ? 27.053 -4.233  13.798 1.00 17.23  ? 50  CYS   A CB  1 
ATOM   347  S  SG  . CYS   A 1 44  ? 28.760 -4.671  14.166 1.00 20.78  ? 50  CYS   A SG  1 
ATOM   348  N  N   . ASP   A 1 45  ? 24.791 -2.039  12.339 1.00 14.13  ? 51  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 45  ? 23.408 -1.932  11.930 1.00 13.40  ? 51  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 45  ? 23.317 -1.876  10.412 1.00 14.30  ? 51  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 45  ? 24.195 -1.304  9.742  1.00 16.47  ? 51  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 45  ? 22.779 -0.670  12.536 1.00 12.34  ? 51  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 45  ? 22.677 -0.729  14.046 1.00 13.44  ? 51  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 45  ? 22.303 -1.834  14.578 1.00 14.15  ? 51  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 45  ? 22.905 0.312   14.708 1.00 13.54  ? 51  ASP   A OD2 1 
ATOM   356  N  N   . THR   A 1 46  ? 22.290 -2.425  9.851  1.00 15.01  ? 52  THR   A N   1 
ATOM   357  C  CA  . THR   A 1 46  ? 21.966 -2.379  8.410  1.00 16.86  ? 52  THR   A CA  1 
ATOM   358  C  C   . THR   A 1 46  ? 20.644 -1.591  8.245  1.00 15.35  ? 52  THR   A C   1 
ATOM   359  O  O   . THR   A 1 46  ? 19.737 -1.725  9.085  1.00 15.81  ? 52  THR   A O   1 
ATOM   360  C  CB  . THR   A 1 46  ? 21.766 -3.804  7.877  1.00 23.14  ? 52  THR   A CB  1 
ATOM   361  O  OG1 . THR   A 1 46  ? 23.050 -4.471  7.892  1.00 28.18  ? 52  THR   A OG1 1 
ATOM   362  C  CG2 . THR   A 1 46  ? 21.131 -3.854  6.489  1.00 26.33  ? 52  THR   A CG2 1 
ATOM   363  N  N   . ILE   A 1 47  ? 20.526 -0.749  7.224  1.00 14.63  ? 53  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 47  ? 19.312 0.013   6.997  1.00 13.43  ? 53  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 47  ? 18.322 -0.735  6.110  1.00 13.45  ? 53  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 47  ? 18.676 -1.254  5.040  1.00 14.66  ? 53  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 47  ? 19.636 1.394   6.377  1.00 13.35  ? 53  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 47  ? 20.739 2.137   7.149  1.00 14.23  ? 53  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 47  ? 18.381 2.274   6.250  1.00 13.18  ? 53  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 47  ? 20.386 2.423   8.659  1.00 14.62  ? 53  ILE   A CD1 1 
ATOM   371  N  N   . ALA   A 1 48  ? 17.068 -0.777  6.499  1.00 12.20  ? 54  ALA   A N   1 
ATOM   372  C  CA  . ALA   A 1 48  ? 15.984 -1.328  5.686  1.00 12.78  ? 54  ALA   A CA  1 
ATOM   373  C  C   . ALA   A 1 48  ? 15.730 -0.463  4.436  1.00 12.67  ? 54  ALA   A C   1 
ATOM   374  O  O   . ALA   A 1 48  ? 15.707 0.772   4.503  1.00 13.39  ? 54  ALA   A O   1 
ATOM   375  C  CB  . ALA   A 1 48  ? 14.697 -1.377  6.513  1.00 12.37  ? 54  ALA   A CB  1 
ATOM   376  N  N   . ARG   A 1 49  ? 15.448 -1.130  3.301  1.00 14.72  ? 55  ARG   A N   1 
ATOM   377  C  CA  . ARG   A 1 49  ? 15.100 -0.424  2.061  1.00 16.29  ? 55  ARG   A CA  1 
ATOM   378  C  C   . ARG   A 1 49  ? 13.784 -1.056  1.591  1.00 17.85  ? 55  ARG   A C   1 
ATOM   379  O  O   . ARG   A 1 49  ? 13.800 -2.028  0.822  1.00 19.48  ? 55  ARG   A O   1 
ATOM   380  C  CB  . ARG   A 1 49  ? 16.244 -0.546  1.023  1.00 17.58  ? 55  ARG   A CB  1 
ATOM   381  C  CG  . ARG   A 1 49  ? 17.589 -0.020  1.543  1.00 17.57  ? 55  ARG   A CG  1 
ATOM   382  C  CD  . ARG   A 1 49  ? 17.670 1.490   1.847  1.00 16.24  ? 55  ARG   A CD  1 
ATOM   383  N  NE  . ARG   A 1 49  ? 19.006 1.919   2.316  1.00 15.61  ? 55  ARG   A NE  1 
ATOM   384  C  CZ  . ARG   A 1 49  ? 19.234 3.071   2.944  1.00 15.33  ? 55  ARG   A CZ  1 
ATOM   385  N  NH1 . ARG   A 1 49  ? 18.251 3.943   3.133  1.00 15.75  ? 55  ARG   A NH1 1 
ATOM   386  N  NH2 . ARG   A 1 49  ? 20.448 3.347   3.431  1.00 18.01  ? 55  ARG   A NH2 1 
ATOM   387  N  N   . CYS   A 1 50  ? 12.644 -0.462  2.006  1.00 17.45  ? 56  CYS   A N   1 
ATOM   388  C  CA  . CYS   A 1 50  ? 11.288 -1.082  1.910  1.00 16.75  ? 56  CYS   A CA  1 
ATOM   389  C  C   . CYS   A 1 50  ? 10.196 -0.074  2.250  1.00 17.17  ? 56  CYS   A C   1 
ATOM   390  O  O   . CYS   A 1 50  ? 10.425 1.063   2.658  1.00 19.11  ? 56  CYS   A O   1 
ATOM   391  C  CB  . CYS   A 1 50  ? 11.265 -2.246  2.890  1.00 15.99  ? 56  CYS   A CB  1 
ATOM   392  S  SG  . CYS   A 1 50  ? 11.227 -1.696  4.617  1.00 16.79  ? 56  CYS   A SG  1 
ATOM   393  N  N   . ASP   A 1 51  ? 8.886  -0.574  2.171  1.00 19.61  ? 57  ASP   A N   1 
ATOM   394  C  CA  . ASP   A 1 51  ? 7.726  0.216   2.581  1.00 21.74  ? 57  ASP   A CA  1 
ATOM   395  C  C   . ASP   A 1 51  ? 6.985  -0.529  3.685  1.00 21.12  ? 57  ASP   A C   1 
ATOM   396  O  O   . ASP   A 1 51  ? 5.758  -0.378  3.795  1.00 21.89  ? 57  ASP   A O   1 
ATOM   397  C  CB  . ASP   A 1 51  ? 6.781  0.568   1.405  1.00 27.32  ? 57  ASP   A CB  1 
ATOM   398  C  CG  . ASP   A 1 51  ? 6.155  -0.617  0.735  1.00 34.15  ? 57  ASP   A CG  1 
ATOM   399  O  OD1 . ASP   A 1 51  ? 6.473  -1.774  1.134  1.00 35.41  ? 57  ASP   A OD1 1 
ATOM   400  O  OD2 . ASP   A 1 51  ? 5.327  -0.407  -0.204 1.00 38.56  ? 57  ASP   A OD2 1 
ATOM   401  N  N   . CYS   A 1 52  ? 7.688  -1.326  4.545  1.00 17.43  ? 58  CYS   A N   1 
ATOM   402  C  CA  . CYS   A 1 52  ? 7.006  -2.008  5.677  1.00 15.98  ? 58  CYS   A CA  1 
ATOM   403  C  C   . CYS   A 1 52  ? 6.262  -0.978  6.542  1.00 16.71  ? 58  CYS   A C   1 
ATOM   404  O  O   . CYS   A 1 52  ? 6.731  0.159   6.746  1.00 16.17  ? 58  CYS   A O   1 
ATOM   405  C  CB  . CYS   A 1 52  ? 8.027  -2.744  6.545  1.00 17.17  ? 58  CYS   A CB  1 
ATOM   406  S  SG  . CYS   A 1 52  ? 8.702  -4.272  5.827  1.00 18.33  ? 58  CYS   A SG  1 
ATOM   407  N  N   . GLN   A 1 53  ? 5.152  -1.409  7.083  1.00 15.36  ? 59  GLN   A N   1 
ATOM   408  C  CA  . GLN   A 1 53  ? 4.375  -0.687  8.068  1.00 14.59  ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.178  -1.511  9.320  1.00 12.90  ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.341  -1.159  10.107 1.00 13.64  ? 59  GLN   A O   1 
ATOM   411  C  CB  . GLN   A 1 53  ? 3.013  -0.210  7.515  1.00 16.46  ? 59  GLN   A CB  1 
ATOM   412  C  CG  . GLN   A 1 53  ? 3.153  0.936   6.499  1.00 17.70  ? 59  GLN   A CG  1 
ATOM   413  C  CD  . GLN   A 1 53  ? 1.757  1.433   6.110  1.00 23.80  ? 59  GLN   A CD  1 
ATOM   414  O  OE1 . GLN   A 1 53  ? 1.253  1.222   4.975  1.00 26.96  ? 59  GLN   A OE1 1 
ATOM   415  N  NE2 . GLN   A 1 53  ? 1.065  2.103   7.016  1.00 20.89  ? 59  GLN   A NE2 1 
ATOM   416  N  N   . THR   A 1 54  ? 4.929  -2.620  9.497  1.00 12.42  ? 60  THR   A N   1 
ATOM   417  C  CA  . THR   A 1 54  ? 4.952  -3.355  10.761 1.00 12.74  ? 60  THR   A CA  1 
ATOM   418  C  C   . THR   A 1 54  ? 6.414  -3.605  11.143 1.00 11.26  ? 60  THR   A C   1 
ATOM   419  O  O   . THR   A 1 54  ? 7.268  -3.801  10.277 1.00 13.16  ? 60  THR   A O   1 
ATOM   420  C  CB  . THR   A 1 54  ? 4.212  -4.648  10.686 1.00 16.15  ? 60  THR   A CB  1 
ATOM   421  O  OG1 . THR   A 1 54  ? 4.821  -5.533  9.815  1.00 23.29  ? 60  THR   A OG1 1 
ATOM   422  C  CG2 . THR   A 1 54  ? 2.772  -4.511  10.273 1.00 15.36  ? 60  THR   A CG2 1 
ATOM   423  N  N   . GLY   A 1 55  ? 6.689  -3.551  12.432 1.00 10.82  ? 61  GLY   A N   1 
ATOM   424  C  CA  . GLY   A 1 55  ? 8.051  -3.733  12.912 1.00 11.19  ? 61  GLY   A CA  1 
ATOM   425  C  C   . GLY   A 1 55  ? 8.051  -3.774  14.420 1.00 9.78   ? 61  GLY   A C   1 
ATOM   426  O  O   . GLY   A 1 55  ? 7.021  -4.024  15.037 1.00 10.41  ? 61  GLY   A O   1 
ATOM   427  N  N   . VAL   A 1 56  ? 9.220  -3.556  15.024 1.00 9.28   ? 62  VAL   A N   1 
ATOM   428  C  CA  . VAL   A 1 56  ? 9.416  -3.627  16.467 1.00 9.03   ? 62  VAL   A CA  1 
ATOM   429  C  C   . VAL   A 1 56  ? 10.265 -2.458  16.892 1.00 8.87   ? 62  VAL   A C   1 
ATOM   430  O  O   . VAL   A 1 56  ? 11.260 -2.162  16.222 1.00 9.61   ? 62  VAL   A O   1 
ATOM   431  C  CB  . VAL   A 1 56  ? 10.127 -4.979  16.792 1.00 10.47  ? 62  VAL   A CB  1 
ATOM   432  C  CG1 . VAL   A 1 56  ? 10.525 -5.082  18.252 1.00 13.09  ? 62  VAL   A CG1 1 
ATOM   433  C  CG2 . VAL   A 1 56  ? 9.254  -6.183  16.406 1.00 10.91  ? 62  VAL   A CG2 1 
ATOM   434  N  N   . TYR   A 1 57  ? 9.915  -1.804  17.984 1.00 8.87   ? 63  TYR   A N   1 
ATOM   435  C  CA  . TYR   A 1 57  ? 10.764 -0.709  18.497 1.00 8.85   ? 63  TYR   A CA  1 
ATOM   436  C  C   . TYR   A 1 57  ? 11.209 -0.919  19.932 1.00 9.03   ? 63  TYR   A C   1 
ATOM   437  O  O   . TYR   A 1 57  ? 10.513 -1.598  20.717 1.00 9.77   ? 63  TYR   A O   1 
ATOM   438  C  CB  . TYR   A 1 57  ? 10.085 0.714   18.366 1.00 9.54   ? 63  TYR   A CB  1 
ATOM   439  C  CG  . TYR   A 1 57  ? 9.096  1.076   19.465 1.00 9.00   ? 63  TYR   A CG  1 
ATOM   440  C  CD1 . TYR   A 1 57  ? 7.813  0.543   19.477 1.00 10.04  ? 63  TYR   A CD1 1 
ATOM   441  C  CD2 . TYR   A 1 57  ? 9.443  1.960   20.489 1.00 10.05  ? 63  TYR   A CD2 1 
ATOM   442  C  CE1 . TYR   A 1 57  ? 6.908  0.862   20.488 1.00 11.63  ? 63  TYR   A CE1 1 
ATOM   443  C  CE2 . TYR   A 1 57  ? 8.515  2.326   21.470 1.00 11.01  ? 63  TYR   A CE2 1 
ATOM   444  C  CZ  . TYR   A 1 57  ? 7.260  1.779   21.456 1.00 12.11  ? 63  TYR   A CZ  1 
ATOM   445  O  OH  . TYR   A 1 57  ? 6.313  2.064   22.444 1.00 14.37  ? 63  TYR   A OH  1 
ATOM   446  N  N   . TYR   A 1 58  ? 12.346 -0.334  20.308 1.00 8.80   ? 64  TYR   A N   1 
ATOM   447  C  CA  . TYR   A 1 58  ? 12.819 -0.400  21.681 1.00 9.04   ? 64  TYR   A CA  1 
ATOM   448  C  C   . TYR   A 1 58  ? 12.357 0.811   22.490 1.00 9.39   ? 64  TYR   A C   1 
ATOM   449  O  O   . TYR   A 1 58  ? 12.593 1.967   22.093 1.00 9.69   ? 64  TYR   A O   1 
ATOM   450  C  CB  . TYR   A 1 58  ? 14.370 -0.462  21.720 1.00 10.13  ? 64  TYR   A CB  1 
ATOM   451  C  CG  . TYR   A 1 58  ? 14.860 -0.623  23.143 1.00 10.71  ? 64  TYR   A CG  1 
ATOM   452  C  CD1 . TYR   A 1 58  ? 14.522 -1.736  23.894 1.00 10.84  ? 64  TYR   A CD1 1 
ATOM   453  C  CD2 . TYR   A 1 58  ? 15.613 0.383   23.765 1.00 11.02  ? 64  TYR   A CD2 1 
ATOM   454  C  CE1 . TYR   A 1 58  ? 14.915 -1.847  25.229 1.00 12.31  ? 64  TYR   A CE1 1 
ATOM   455  C  CE2 . TYR   A 1 58  ? 16.025 0.263   25.092 1.00 11.80  ? 64  TYR   A CE2 1 
ATOM   456  C  CZ  . TYR   A 1 58  ? 15.678 -0.859  25.805 1.00 12.83  ? 64  TYR   A CZ  1 
ATOM   457  O  OH  . TYR   A 1 58  ? 16.024 -0.997  27.145 1.00 15.75  ? 64  TYR   A OH  1 
ATOM   458  N  N   . CYS   A 1 59  ? 11.752 0.507   23.639 1.00 9.36   ? 65  CYS   A N   1 
ATOM   459  C  CA  . CYS   A 1 59  ? 11.237 1.491   24.597 1.00 10.14  ? 65  CYS   A CA  1 
ATOM   460  C  C   . CYS   A 1 59  ? 12.065 1.471   25.884 1.00 10.36  ? 65  CYS   A C   1 
ATOM   461  O  O   . CYS   A 1 59  ? 11.863 0.557   26.728 1.00 10.83  ? 65  CYS   A O   1 
ATOM   462  C  CB  . CYS   A 1 59  ? 9.770  1.205   24.870 1.00 10.64  ? 65  CYS   A CB  1 
ATOM   463  S  SG  . CYS   A 1 59  ? 9.034  2.318   26.110 1.00 11.65  ? 65  CYS   A SG  1 
ATOM   464  N  N   . SER   A 1 60  ? 12.974 2.423   26.051 1.00 10.43  ? 66  SER   A N   1 
ATOM   465  C  CA  . SER   A 1 60  ? 13.856 2.392   27.238 1.00 11.77  ? 66  SER   A CA  1 
ATOM   466  C  C   . SER   A 1 60  ? 13.113 2.574   28.555 1.00 11.26  ? 66  SER   A C   1 
ATOM   467  O  O   . SER   A 1 60  ? 13.528 2.003   29.572 1.00 13.18  ? 66  SER   A O   1 
ATOM   468  C  CB  . SER   A 1 60  ? 14.988 3.407   27.090 1.00 13.82  ? 66  SER   A CB  1 
ATOM   469  O  OG  . SER   A 1 60  ? 14.584 4.748   27.248 1.00 15.92  ? 66  SER   A OG  1 
ATOM   470  N  N   . SER   A 1 61  ? 11.989 3.327   28.533 1.00 10.68  ? 67  SER   A N   1 
ATOM   471  C  CA  . SER   A 1 61  ? 11.206 3.541   29.735 1.00 11.53  ? 67  SER   A CA  1 
ATOM   472  C  C   . SER   A 1 61  ? 10.393 2.328   30.179 1.00 11.56  ? 67  SER   A C   1 
ATOM   473  O  O   . SER   A 1 61  ? 9.759  2.361   31.232 1.00 12.26  ? 67  SER   A O   1 
ATOM   474  C  CB  . SER   A 1 61  ? 10.325 4.779   29.602 1.00 12.57  ? 67  SER   A CB  1 
ATOM   475  O  OG  . SER   A 1 61  ? 9.325  4.584   28.630 1.00 12.50  ? 67  SER   A OG  1 
ATOM   476  N  N   . ARG   A 1 62  ? 10.462 1.227   29.418 1.00 11.59  ? 68  ARG   A N   1 
ATOM   477  C  CA  . ARG   A 1 62  ? 9.883  -0.057  29.790 1.00 12.12  ? 68  ARG   A CA  1 
ATOM   478  C  C   . ARG   A 1 62  ? 10.910 -1.187  29.729 1.00 12.86  ? 68  ARG   A C   1 
ATOM   479  O  O   . ARG   A 1 62  ? 10.542 -2.344  29.992 1.00 13.40  ? 68  ARG   A O   1 
ATOM   480  C  CB  . ARG   A 1 62  ? 8.691  -0.350  28.864 1.00 12.49  ? 68  ARG   A CB  1 
ATOM   481  C  CG  . ARG   A 1 62  ? 7.522  0.608   28.995 1.00 13.04  ? 68  ARG   A CG  1 
ATOM   482  C  CD  . ARG   A 1 62  ? 6.759  0.303   30.281 1.00 13.60  ? 68  ARG   A CD  1 
ATOM   483  N  NE  . ARG   A 1 62  ? 5.608  1.204   30.455 1.00 15.46  ? 68  ARG   A NE  1 
ATOM   484  C  CZ  . ARG   A 1 62  ? 5.660  2.359   31.105 1.00 13.57  ? 68  ARG   A CZ  1 
ATOM   485  N  NH1 . ARG   A 1 62  ? 6.814  2.792   31.631 1.00 15.37  ? 68  ARG   A NH1 1 
ATOM   486  N  NH2 . ARG   A 1 62  ? 4.551  3.096   31.261 1.00 16.35  ? 68  ARG   A NH2 1 
ATOM   487  N  N   . ARG   A 1 63  ? 12.144 -0.936  29.307 1.00 13.31  ? 69  ARG   A N   1 
ATOM   488  C  CA  . ARG   A 1 63  ? 13.137 -2.001  28.990 1.00 13.96  ? 69  ARG   A CA  1 
ATOM   489  C  C   . ARG   A 1 63  ? 12.506 -3.118  28.118 1.00 16.06  ? 69  ARG   A C   1 
ATOM   490  O  O   . ARG   A 1 63  ? 12.673 -4.328  28.397 1.00 18.87  ? 69  ARG   A O   1 
ATOM   491  C  CB  . ARG   A 1 63  ? 13.730 -2.634  30.263 1.00 17.35  ? 69  ARG   A CB  1 
ATOM   492  C  CG  . ARG   A 1 63  ? 14.683 -1.714  30.872 1.00 19.28  ? 69  ARG   A CG  1 
ATOM   493  C  CD  . ARG   A 1 63  ? 15.470 -2.553  31.881 1.00 20.82  ? 69  ARG   A CD  1 
ATOM   494  N  NE  . ARG   A 1 63  ? 16.262 -1.642  32.681 1.00 21.35  ? 69  ARG   A NE  1 
ATOM   495  C  CZ  . ARG   A 1 63  ? 15.925 -1.211  33.896 1.00 17.99  ? 69  ARG   A CZ  1 
ATOM   496  N  NH1 . ARG   A 1 63  ? 14.842 -1.692  34.506 1.00 18.76  ? 69  ARG   A NH1 1 
ATOM   497  N  NH2 . ARG   A 1 63  ? 16.698 -0.340  34.534 1.00 19.90  ? 69  ARG   A NH2 1 
ATOM   498  N  N   . LYS   A 1 64  ? 11.780 -2.725  27.096 1.00 13.07  ? 70  LYS   A N   1 
ATOM   499  C  CA  . LYS   A 1 64  ? 11.074 -3.725  26.285 1.00 14.06  ? 70  LYS   A CA  1 
ATOM   500  C  C   . LYS   A 1 64  ? 11.057 -3.313  24.845 1.00 12.67  ? 70  LYS   A C   1 
ATOM   501  O  O   . LYS   A 1 64  ? 10.973 -2.110  24.515 1.00 12.52  ? 70  LYS   A O   1 
ATOM   502  C  CB  . LYS   A 1 64  ? 9.604  -3.819  26.787 1.00 17.05  ? 70  LYS   A CB  1 
ATOM   503  C  CG  . LYS   A 1 64  ? 8.833  -5.096  26.383 1.00 27.21  ? 70  LYS   A CG  1 
ATOM   504  C  CD  . LYS   A 1 64  ? 7.972  -5.550  27.556 1.00 35.97  ? 70  LYS   A CD  1 
ATOM   505  C  CE  . LYS   A 1 64  ? 7.096  -6.716  27.155 1.00 40.91  ? 70  LYS   A CE  1 
ATOM   506  N  NZ  . LYS   A 1 64  ? 7.870  -7.781  26.454 1.00 41.93  ? 70  LYS   A NZ  1 
ATOM   507  N  N   . HIS   A 1 65  ? 11.013 -4.330  23.970 1.00 11.61  ? 71  HIS   A N   1 
ATOM   508  C  CA  . HIS   A 1 65  ? 10.778 -4.170  22.548 1.00 11.15  ? 71  HIS   A CA  1 
ATOM   509  C  C   . HIS   A 1 65  ? 9.320  -4.497  22.277 1.00 12.32  ? 71  HIS   A C   1 
ATOM   510  O  O   . HIS   A 1 65  ? 8.813  -5.576  22.692 1.00 15.51  ? 71  HIS   A O   1 
ATOM   511  C  CB  . HIS   A 1 65  ? 11.670 -5.118  21.730 1.00 10.94  ? 71  HIS   A CB  1 
ATOM   512  C  CG  . HIS   A 1 65  ? 13.144 -4.797  21.829 1.00 11.60  ? 71  HIS   A CG  1 
ATOM   513  N  ND1 . HIS   A 1 65  ? 13.849 -4.108  20.865 1.00 14.77  ? 71  HIS   A ND1 1 
ATOM   514  C  CD2 . HIS   A 1 65  ? 14.003 -5.104  22.837 1.00 11.64  ? 71  HIS   A CD2 1 
ATOM   515  C  CE1 . HIS   A 1 65  ? 15.129 -4.049  21.295 1.00 13.01  ? 71  HIS   A CE1 1 
ATOM   516  N  NE2 . HIS   A 1 65  ? 15.237 -4.646  22.458 1.00 15.17  ? 71  HIS   A NE2 1 
ATOM   517  N  N   . TYR   A 1 66  ? 8.619  -3.630  21.548 1.00 10.30  ? 72  TYR   A N   1 
ATOM   518  C  CA  . TYR   A 1 66  ? 7.200  -3.808  21.265 1.00 10.26  ? 72  TYR   A CA  1 
ATOM   519  C  C   . TYR   A 1 66  ? 6.957  -3.935  19.788 1.00 10.22  ? 72  TYR   A C   1 
ATOM   520  O  O   . TYR   A 1 66  ? 7.450  -3.084  19.017 1.00 10.24  ? 72  TYR   A O   1 
ATOM   521  C  CB  . TYR   A 1 66  ? 6.379  -2.585  21.751 1.00 11.14  ? 72  TYR   A CB  1 
ATOM   522  C  CG  . TYR   A 1 66  ? 6.310  -2.413  23.255 1.00 11.84  ? 72  TYR   A CG  1 
ATOM   523  C  CD1 . TYR   A 1 66  ? 5.464  -3.212  24.027 1.00 14.01  ? 72  TYR   A CD1 1 
ATOM   524  C  CD2 . TYR   A 1 66  ? 7.060  -1.441  23.897 1.00 12.13  ? 72  TYR   A CD2 1 
ATOM   525  C  CE1 . TYR   A 1 66  ? 5.358  -3.041  25.403 1.00 14.61  ? 72  TYR   A CE1 1 
ATOM   526  C  CE2 . TYR   A 1 66  ? 6.973  -1.267  25.284 1.00 13.89  ? 72  TYR   A CE2 1 
ATOM   527  C  CZ  . TYR   A 1 66  ? 6.109  -2.061  26.026 1.00 14.33  ? 72  TYR   A CZ  1 
ATOM   528  O  OH  . TYR   A 1 66  ? 6.016  -1.875  27.406 1.00 16.92  ? 72  TYR   A OH  1 
ATOM   529  N  N   . PRO   A 1 67  ? 6.135  -4.902  19.370 1.00 10.02  ? 73  PRO   A N   1 
ATOM   530  C  CA  . PRO   A 1 67  ? 5.704  -4.940  17.963 1.00 10.42  ? 73  PRO   A CA  1 
ATOM   531  C  C   . PRO   A 1 67  ? 4.659  -3.862  17.674 1.00 11.06  ? 73  PRO   A C   1 
ATOM   532  O  O   . PRO   A 1 67  ? 3.715  -3.705  18.494 1.00 13.26  ? 73  PRO   A O   1 
ATOM   533  C  CB  . PRO   A 1 67  ? 5.113  -6.360  17.782 1.00 12.60  ? 73  PRO   A CB  1 
ATOM   534  C  CG  . PRO   A 1 67  ? 4.692  -6.753  19.177 1.00 14.66  ? 73  PRO   A CG  1 
ATOM   535  C  CD  . PRO   A 1 67  ? 5.575  -6.005  20.182 1.00 11.06  ? 73  PRO   A CD  1 
ATOM   536  N  N   . VAL   A 1 68  ? 4.784  -3.183  16.570 1.00 9.45   ? 74  VAL   A N   1 
ATOM   537  C  CA  . VAL   A 1 68  ? 3.850  -2.088  16.218 1.00 11.05  ? 74  VAL   A CA  1 
ATOM   538  C  C   . VAL   A 1 68  ? 3.550  -2.074  14.742 1.00 10.82  ? 74  VAL   A C   1 
ATOM   539  O  O   . VAL   A 1 68  ? 4.350  -2.433  13.899 1.00 11.53  ? 74  VAL   A O   1 
ATOM   540  C  CB  . VAL   A 1 68  ? 4.434  -0.695  16.602 1.00 14.16  ? 74  VAL   A CB  1 
ATOM   541  C  CG1 . VAL   A 1 68  ? 4.420  -0.497  18.115 1.00 15.84  ? 74  VAL   A CG1 1 
ATOM   542  C  CG2 . VAL   A 1 68  ? 5.825  -0.487  16.034 1.00 13.99  ? 74  VAL   A CG2 1 
ATOM   543  N  N   . SER   A 1 69  ? 2.356  -1.505  14.421 1.00 11.18  ? 75  SER   A N   1 
ATOM   544  C  CA  A SER   A 1 69  ? 1.983  -1.048  13.077 0.50 11.03  ? 75  SER   A CA  1 
ATOM   545  C  CA  B SER   A 1 69  ? 1.908  -1.067  13.112 0.50 11.34  ? 75  SER   A CA  1 
ATOM   546  C  C   . SER   A 1 69  ? 2.197  0.453   13.046 1.00 10.83  ? 75  SER   A C   1 
ATOM   547  O  O   . SER   A 1 69  ? 1.904  1.140   14.034 1.00 12.10  ? 75  SER   A O   1 
ATOM   548  C  CB  A SER   A 1 69  ? 0.520  -1.298  12.774 0.50 12.27  ? 75  SER   A CB  1 
ATOM   549  C  CB  B SER   A 1 69  ? 0.404  -1.276  13.013 0.50 13.48  ? 75  SER   A CB  1 
ATOM   550  O  OG  A SER   A 1 69  ? 0.236  -2.674  12.894 0.50 15.56  ? 75  SER   A OG  1 
ATOM   551  O  OG  B SER   A 1 69  ? -0.071 -0.801  11.767 0.50 16.71  ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.781  0.964   11.974 1.00 11.88  ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.102  2.385   11.906 1.00 11.91  ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.727  2.973   10.573 1.00 12.28  ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.644  2.268   9.564  1.00 13.45  ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.616  2.628   12.276 1.00 12.08  ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.612  1.833   11.460 1.00 10.99  ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.025  0.564   11.860 1.00 11.07  ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.185  2.370   10.319 1.00 11.55  ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.958  -0.141  11.120 1.00 12.00  ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.142  1.652   9.585  1.00 13.15  ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.487  0.397   9.982  1.00 12.12  ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.466  4.280   10.565 1.00 12.36  ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 2.058  4.961   9.331  1.00 13.35  ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.231  5.193   8.363  1.00 13.37  ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.402  5.050   8.752  1.00 13.88  ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.359  6.282   9.684  1.00 14.81  ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.226  7.177   10.362 1.00 16.44  ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.953  5.532   7.128  1.00 14.19  ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 4.010  5.850   6.167  1.00 14.42  ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.622  7.208   6.516  1.00 14.93  ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.943  8.077   7.099  1.00 16.18  ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.435  5.882   4.754  1.00 16.24  ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.949  4.528   4.308  1.00 18.38  ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.536  4.567   2.829  1.00 25.24  ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.135  3.175   2.432  1.00 31.66  ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.286  2.952   0.972  1.00 36.86  ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.884  7.472   6.161  1.00 14.04  ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.515  8.755   6.520  1.00 14.44  ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.719  9.929   5.955  1.00 15.95  ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.360  9.936   4.774  1.00 17.91  ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.934  8.646   5.924  1.00 16.35  ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.169  7.212   5.724  1.00 19.50  ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.831  6.544   5.496  1.00 15.96  ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.429  10.889  6.815  1.00 15.75  ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.506  11.998  6.481  1.00 17.43  ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.956  13.291  7.175  1.00 15.87  ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.801  13.281  8.085  1.00 14.87  ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.052  11.692  6.942  1.00 21.58  ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.689  10.322  6.928  1.00 28.43  ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.243  14.407  6.825  1.00 17.17  ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.444  15.707  7.415  1.00 18.54  ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.345  15.839  8.483  1.00 19.44  ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.145  15.893  8.134  1.00 21.56  ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.257  16.770  6.313  1.00 19.94  ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.576  18.180  6.751  1.00 23.67  ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.055  18.350  7.052  1.00 24.08  ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.198  19.198  5.641  1.00 25.79  ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.710  15.822  9.757  1.00 18.37  ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.780  15.825  10.894 1.00 19.50  ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.037  17.000  11.804 1.00 20.53  ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.206  17.292  12.128 1.00 19.48  ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.010  14.509  11.675 1.00 21.15  ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.868  13.274  10.726 1.00 23.28  ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.161  14.420  12.982 1.00 22.60  ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 2.812  12.037  11.254 1.00 21.95  ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.973  17.640  12.312 1.00 21.08  ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.111  18.706  13.288 1.00 22.51  ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.346  18.088  14.634 1.00 23.93  ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.566  17.251  15.090 1.00 27.46  ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.816  19.553  13.362 1.00 23.61  ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.060  20.839  14.099 1.00 26.43  ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.810  21.849  13.526 1.00 28.82  ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.625  20.991  15.408 1.00 29.85  ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 2.063  23.020  14.223 1.00 30.97  ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.859  22.158  16.100 1.00 30.72  ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.562  23.178  15.502 1.00 31.01  ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.478  18.445  15.255 1.00 21.40  ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 3.907  17.918  16.535 1.00 20.30  ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 3.891  19.050  17.555 1.00 19.69  ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.410  20.141  17.287 1.00 20.51  ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.353  17.315  16.421 1.00 18.91  ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 5.838  16.765  17.773 1.00 19.21  ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.395  16.210  15.356 1.00 19.81  ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.347  18.753  18.751 1.00 19.56  ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.272  19.756  19.804 1.00 20.51  ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.635  20.131  20.334 1.00 20.23  ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.622  19.417  20.142 1.00 20.53  ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.375  19.267  20.951 1.00 24.18  ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 0.898  19.169  20.556 1.00 30.05  ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 0.289  20.435  19.981 1.00 37.63  ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 0.550  21.541  20.513 1.00 38.80  ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.464 20.318  18.990 1.00 42.47  ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.703  21.292  20.983 1.00 20.76  ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.942  21.792  21.556 1.00 21.48  ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.523  20.839  22.577 1.00 22.60  ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.809  20.129  23.300 1.00 23.90  ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.661  23.125  22.259 1.00 22.92  ? 86  ALA   A CB  1 
ATOM   639  N  N   A SER   A 1 81  ? 7.853  20.811  22.652 0.50 20.79  ? 87  SER   A N   1 
ATOM   640  N  N   B SER   A 1 81  ? 7.843  20.845  22.652 0.50 23.08  ? 87  SER   A N   1 
ATOM   641  C  CA  A SER   A 1 81  ? 8.575  20.038  23.661 0.50 20.32  ? 87  SER   A CA  1 
ATOM   642  C  CA  B SER   A 1 81  ? 8.599  20.061  23.613 0.50 24.68  ? 87  SER   A CA  1 
ATOM   643  C  C   A SER   A 1 81  ? 9.648  20.993  24.249 0.50 22.18  ? 87  SER   A C   1 
ATOM   644  C  C   B SER   A 1 81  ? 9.701  20.991  24.176 0.50 24.52  ? 87  SER   A C   1 
ATOM   645  O  O   A SER   A 1 81  ? 9.644  22.177  23.917 0.50 22.17  ? 87  SER   A O   1 
ATOM   646  O  O   B SER   A 1 81  ? 9.755  22.165  23.784 0.50 24.95  ? 87  SER   A O   1 
ATOM   647  C  CB  A SER   A 1 81  ? 9.245  18.822  23.020 0.50 18.37  ? 87  SER   A CB  1 
ATOM   648  C  CB  B SER   A 1 81  ? 9.225  18.865  22.902 0.50 28.47  ? 87  SER   A CB  1 
ATOM   649  O  OG  A SER   A 1 81  ? 10.333 19.226  22.197 0.50 13.26  ? 87  SER   A OG  1 
ATOM   650  O  OG  B SER   A 1 81  ? 9.061  17.691  23.670 0.50 33.72  ? 87  SER   A OG  1 
ATOM   651  N  N   . GLU   A 1 82  ? 10.603 20.482  25.054 1.00 24.15  ? 88  GLU   A N   1 
ATOM   652  C  CA  . GLU   A 1 82  ? 11.687 21.351  25.525 1.00 24.76  ? 88  GLU   A CA  1 
ATOM   653  C  C   . GLU   A 1 82  ? 12.725 21.599  24.385 1.00 21.42  ? 88  GLU   A C   1 
ATOM   654  O  O   . GLU   A 1 82  ? 13.517 22.532  24.480 1.00 22.31  ? 88  GLU   A O   1 
ATOM   655  C  CB  . GLU   A 1 82  ? 12.325 20.926  26.851 1.00 32.04  ? 88  GLU   A CB  1 
ATOM   656  C  CG  . GLU   A 1 82  ? 13.333 19.828  26.736 1.00 38.91  ? 88  GLU   A CG  1 
ATOM   657  C  CD  . GLU   A 1 82  ? 14.126 19.556  27.999 1.00 47.07  ? 88  GLU   A CD  1 
ATOM   658  O  OE1 . GLU   A 1 82  ? 15.229 20.135  28.147 1.00 49.13  ? 88  GLU   A OE1 1 
ATOM   659  O  OE2 . GLU   A 1 82  ? 13.648 18.754  28.834 1.00 46.92  ? 88  GLU   A OE2 1 
ATOM   660  N  N   . TYR   A 1 83  ? 12.645 20.831  23.255 1.00 19.75  ? 89  TYR   A N   1 
ATOM   661  C  CA  . TYR   A 1 83  ? 13.618 20.947  22.169 1.00 18.26  ? 89  TYR   A CA  1 
ATOM   662  C  C   . TYR   A 1 83  ? 13.127 21.652  20.912 1.00 17.66  ? 89  TYR   A C   1 
ATOM   663  O  O   . TYR   A 1 83  ? 13.953 22.152  20.143 1.00 18.24  ? 89  TYR   A O   1 
ATOM   664  C  CB  . TYR   A 1 83  ? 14.142 19.549  21.818 1.00 18.24  ? 89  TYR   A CB  1 
ATOM   665  C  CG  . TYR   A 1 83  ? 14.810 18.890  23.004 1.00 18.67  ? 89  TYR   A CG  1 
ATOM   666  C  CD1 . TYR   A 1 83  ? 16.118 19.202  23.353 1.00 21.10  ? 89  TYR   A CD1 1 
ATOM   667  C  CD2 . TYR   A 1 83  ? 14.116 18.006  23.811 1.00 19.97  ? 89  TYR   A CD2 1 
ATOM   668  C  CE1 . TYR   A 1 83  ? 16.758 18.555  24.409 1.00 23.14  ? 89  TYR   A CE1 1 
ATOM   669  C  CE2 . TYR   A 1 83  ? 14.736 17.369  24.880 1.00 22.51  ? 89  TYR   A CE2 1 
ATOM   670  C  CZ  . TYR   A 1 83  ? 16.039 17.680  25.205 1.00 25.58  ? 89  TYR   A CZ  1 
ATOM   671  O  OH  . TYR   A 1 83  ? 16.636 17.019  26.256 1.00 29.72  ? 89  TYR   A OH  1 
ATOM   672  N  N   . TYR   A 1 84  ? 11.828 21.664  20.668 1.00 19.02  ? 90  TYR   A N   1 
ATOM   673  C  CA  . TYR   A 1 84  ? 11.285 22.327  19.483 1.00 18.21  ? 90  TYR   A CA  1 
ATOM   674  C  C   . TYR   A 1 84  ? 9.962  22.987  19.855 1.00 19.13  ? 90  TYR   A C   1 
ATOM   675  O  O   . TYR   A 1 84  ? 9.191  22.401  20.637 1.00 19.41  ? 90  TYR   A O   1 
ATOM   676  C  CB  . TYR   A 1 84  ? 10.965 21.286  18.373 1.00 17.22  ? 90  TYR   A CB  1 
ATOM   677  C  CG  . TYR   A 1 84  ? 12.167 20.533  17.821 1.00 15.65  ? 90  TYR   A CG  1 
ATOM   678  C  CD1 . TYR   A 1 84  ? 13.031 21.130  16.920 1.00 16.19  ? 90  TYR   A CD1 1 
ATOM   679  C  CD2 . TYR   A 1 84  ? 12.397 19.201  18.162 1.00 15.48  ? 90  TYR   A CD2 1 
ATOM   680  C  CE1 . TYR   A 1 84  ? 14.122 20.439  16.402 1.00 15.38  ? 90  TYR   A CE1 1 
ATOM   681  C  CE2 . TYR   A 1 84  ? 13.488 18.502  17.658 1.00 15.43  ? 90  TYR   A CE2 1 
ATOM   682  C  CZ  . TYR   A 1 84  ? 14.333 19.121  16.764 1.00 14.13  ? 90  TYR   A CZ  1 
ATOM   683  O  OH  . TYR   A 1 84  ? 15.428 18.465  16.283 1.00 14.28  ? 90  TYR   A OH  1 
ATOM   684  N  N   . PRO   A 1 85  ? 9.641  24.109  19.203 1.00 20.53  ? 91  PRO   A N   1 
ATOM   685  C  CA  . PRO   A 1 85  ? 8.280  24.649  19.343 1.00 21.41  ? 91  PRO   A CA  1 
ATOM   686  C  C   . PRO   A 1 85  ? 7.298  23.737  18.602 1.00 22.26  ? 91  PRO   A C   1 
ATOM   687  O  O   . PRO   A 1 85  ? 7.736  22.823  17.842 1.00 21.45  ? 91  PRO   A O   1 
ATOM   688  C  CB  . PRO   A 1 85  ? 8.396  26.007  18.619 1.00 22.82  ? 91  PRO   A CB  1 
ATOM   689  C  CG  . PRO   A 1 85  ? 9.427  25.775  17.540 1.00 23.93  ? 91  PRO   A CG  1 
ATOM   690  C  CD  . PRO   A 1 85  ? 10.435 24.850  18.189 1.00 21.55  ? 91  PRO   A CD  1 
ATOM   691  N  N   . ALA   A 1 86  ? 5.988  23.954  18.733 1.00 23.17  ? 92  ALA   A N   1 
ATOM   692  C  CA  . ALA   A 1 86  ? 4.998  23.189  17.969 1.00 23.51  ? 92  ALA   A CA  1 
ATOM   693  C  C   . ALA   A 1 86  ? 5.250  23.531  16.480 1.00 24.04  ? 92  ALA   A C   1 
ATOM   694  O  O   . ALA   A 1 86  ? 5.501  24.699  16.138 1.00 25.97  ? 92  ALA   A O   1 
ATOM   695  C  CB  . ALA   A 1 86  ? 3.594  23.624  18.383 1.00 24.37  ? 92  ALA   A CB  1 
ATOM   696  N  N   . ARG   A 1 87  ? 5.361  22.503  15.639 1.00 23.82  ? 93  ARG   A N   1 
ATOM   697  C  CA  . ARG   A 1 87  ? 5.738  22.708  14.248 1.00 23.02  ? 93  ARG   A CA  1 
ATOM   698  C  C   . ARG   A 1 87  ? 5.405  21.448  13.464 1.00 22.46  ? 93  ARG   A C   1 
ATOM   699  O  O   . ARG   A 1 87  ? 5.081  20.398  14.041 1.00 22.85  ? 93  ARG   A O   1 
ATOM   700  C  CB  . ARG   A 1 87  ? 7.257  22.944  14.171 1.00 23.23  ? 93  ARG   A CB  1 
ATOM   701  C  CG  . ARG   A 1 87  ? 8.034  21.613  14.443 1.00 25.00  ? 93  ARG   A CG  1 
ATOM   702  C  CD  . ARG   A 1 87  ? 9.445  21.793  14.746 1.00 23.84  ? 93  ARG   A CD  1 
ATOM   703  N  NE  . ARG   A 1 87  ? 10.345 20.695  14.377 1.00 21.80  ? 93  ARG   A NE  1 
ATOM   704  C  CZ  . ARG   A 1 87  ? 10.414 19.452  14.812 1.00 24.47  ? 93  ARG   A CZ  1 
ATOM   705  N  NH1 . ARG   A 1 87  ? 9.426  18.936  15.574 1.00 23.22  ? 93  ARG   A NH1 1 
ATOM   706  N  NH2 . ARG   A 1 87  ? 11.410 18.667  14.407 1.00 19.87  ? 93  ARG   A NH2 1 
ATOM   707  N  N   . TYR   A 1 88  ? 5.563  21.536  12.142 1.00 22.68  ? 94  TYR   A N   1 
ATOM   708  C  CA  . TYR   A 1 88  ? 5.444  20.380  11.285 1.00 22.85  ? 94  TYR   A CA  1 
ATOM   709  C  C   . TYR   A 1 88  ? 6.788  19.668  11.224 1.00 20.16  ? 94  TYR   A C   1 
ATOM   710  O  O   . TYR   A 1 88  ? 7.806  20.291  10.926 1.00 21.37  ? 94  TYR   A O   1 
ATOM   711  C  CB  . TYR   A 1 88  ? 5.039  20.809  9.883  1.00 23.99  ? 94  TYR   A CB  1 
ATOM   712  C  CG  . TYR   A 1 88  ? 3.559  21.126  9.806  1.00 25.45  ? 94  TYR   A CG  1 
ATOM   713  C  CD1 . TYR   A 1 88  ? 2.617  20.114  9.713  1.00 26.82  ? 94  TYR   A CD1 1 
ATOM   714  C  CD2 . TYR   A 1 88  ? 3.095  22.431  9.916  1.00 26.96  ? 94  TYR   A CD2 1 
ATOM   715  C  CE1 . TYR   A 1 88  ? 1.260  20.383  9.686  1.00 28.88  ? 94  TYR   A CE1 1 
ATOM   716  C  CE2 . TYR   A 1 88  ? 1.730  22.712  9.899  1.00 28.35  ? 94  TYR   A CE2 1 
ATOM   717  C  CZ  . TYR   A 1 88  ? 0.818  21.680  9.783  1.00 29.66  ? 94  TYR   A CZ  1 
ATOM   718  O  OH  . TYR   A 1 88  ? -0.539 21.876  9.763  1.00 33.44  ? 94  TYR   A OH  1 
ATOM   719  N  N   . GLN   A 1 89  ? 6.782  18.336  11.513 1.00 17.60  ? 95  GLN   A N   1 
ATOM   720  C  CA  . GLN   A 1 89  ? 7.983  17.494  11.412 1.00 15.75  ? 95  GLN   A CA  1 
ATOM   721  C  C   . GLN   A 1 89  ? 7.775  16.617  10.180 1.00 15.83  ? 95  GLN   A C   1 
ATOM   722  O  O   . GLN   A 1 89  ? 6.694  16.038  9.970  1.00 16.57  ? 95  GLN   A O   1 
ATOM   723  C  CB  . GLN   A 1 89  ? 8.190  16.671  12.688 1.00 16.10  ? 95  GLN   A CB  1 
ATOM   724  C  CG  . GLN   A 1 89  ? 9.446  15.819  12.608 1.00 16.43  ? 95  GLN   A CG  1 
ATOM   725  C  CD  . GLN   A 1 89  ? 9.976  15.365  13.967 1.00 14.82  ? 95  GLN   A CD  1 
ATOM   726  O  OE1 . GLN   A 1 89  ? 9.949  16.085  14.985 1.00 16.07  ? 95  GLN   A OE1 1 
ATOM   727  N  NE2 . GLN   A 1 89  ? 10.545 14.167  14.005 1.00 13.82  ? 95  GLN   A NE2 1 
ATOM   728  N  N   . SER   A 1 90  ? 8.808  16.542  9.330  1.00 14.73  ? 96  SER   A N   1 
ATOM   729  C  CA  . SER   A 1 90  ? 8.714  15.779  8.112  1.00 14.77  ? 96  SER   A CA  1 
ATOM   730  C  C   . SER   A 1 90  ? 9.294  14.354  8.300  1.00 13.82  ? 96  SER   A C   1 
ATOM   731  O  O   . SER   A 1 90  ? 10.055 14.096  9.230  1.00 13.38  ? 96  SER   A O   1 
ATOM   732  C  CB  . SER   A 1 90  ? 9.429  16.525  6.987  1.00 16.90  ? 96  SER   A CB  1 
ATOM   733  O  OG  . SER   A 1 90  ? 10.806 16.608  7.288  1.00 19.30  ? 96  SER   A OG  1 
ATOM   734  N  N   . HIS   A 1 91  ? 8.908  13.466  7.375  1.00 13.46  ? 97  HIS   A N   1 
ATOM   735  C  CA  . HIS   A 1 91  ? 9.398  12.088  7.323  1.00 13.14  ? 97  HIS   A CA  1 
ATOM   736  C  C   . HIS   A 1 91  ? 9.126  11.356  8.661  1.00 12.21  ? 97  HIS   A C   1 
ATOM   737  O  O   . HIS   A 1 91  ? 9.968  10.534  9.097  1.00 13.30  ? 97  HIS   A O   1 
ATOM   738  C  CB  . HIS   A 1 91  ? 10.921 12.058  6.952  1.00 14.53  ? 97  HIS   A CB  1 
ATOM   739  C  CG  . HIS   A 1 91  ? 11.219 12.646  5.593  1.00 15.72  ? 97  HIS   A CG  1 
ATOM   740  N  ND1 . HIS   A 1 91  ? 11.349 11.842  4.479  1.00 17.69  ? 97  HIS   A ND1 1 
ATOM   741  C  CD2 . HIS   A 1 91  ? 11.345 13.939  5.219  1.00 18.17  ? 97  HIS   A CD2 1 
ATOM   742  C  CE1 . HIS   A 1 91  ? 11.575 12.673  3.449  1.00 18.59  ? 97  HIS   A CE1 1 
ATOM   743  N  NE2 . HIS   A 1 91  ? 11.577 13.940  3.849  1.00 19.41  ? 97  HIS   A NE2 1 
ATOM   744  N  N   . LEU   A 1 92  ? 7.996  11.606  9.275  1.00 12.02  ? 98  LEU   A N   1 
ATOM   745  C  CA  . LEU   A 1 92  ? 7.656  11.074  10.598 1.00 12.08  ? 98  LEU   A CA  1 
ATOM   746  C  C   . LEU   A 1 92  ? 6.597  9.991   10.412 1.00 12.32  ? 98  LEU   A C   1 
ATOM   747  O  O   . LEU   A 1 92  ? 5.648  10.153  9.617  1.00 13.04  ? 98  LEU   A O   1 
ATOM   748  C  CB  . LEU   A 1 92  ? 7.094  12.220  11.490 1.00 13.76  ? 98  LEU   A CB  1 
ATOM   749  C  CG  . LEU   A 1 92  ? 6.790  11.811  12.973 1.00 15.08  ? 98  LEU   A CG  1 
ATOM   750  C  CD1 . LEU   A 1 92  ? 8.055  11.504  13.726 1.00 14.68  ? 98  LEU   A CD1 1 
ATOM   751  C  CD2 . LEU   A 1 92  ? 6.066  12.958  13.735 1.00 17.78  ? 98  LEU   A CD2 1 
ATOM   752  N  N   . MET   A 1 93  ? 6.718  8.912   11.206 1.00 11.97  ? 99  MET   A N   1 
ATOM   753  C  CA  . MET   A 1 93  ? 5.757  7.787   11.180 1.00 12.39  ? 99  MET   A CA  1 
ATOM   754  C  C   . MET   A 1 93  ? 5.179  7.631   12.578 1.00 12.11  ? 99  MET   A C   1 
ATOM   755  O  O   . MET   A 1 93  ? 5.944  7.672   13.549 1.00 12.30  ? 99  MET   A O   1 
ATOM   756  C  CB  . MET   A 1 93  ? 6.505  6.504   10.826 1.00 12.41  ? 99  MET   A CB  1 
ATOM   757  C  CG  . MET   A 1 93  ? 7.155  6.608   9.453  1.00 14.02  ? 99  MET   A CG  1 
ATOM   758  S  SD  . MET   A 1 93  ? 8.271  5.239   9.010  1.00 16.09  ? 99  MET   A SD  1 
ATOM   759  C  CE  . MET   A 1 93  ? 9.565  5.484   10.242 1.00 19.07  ? 99  MET   A CE  1 
ATOM   760  N  N   . LEU   A 1 94  ? 3.868  7.413   12.738 1.00 12.04  ? 100 LEU   A N   1 
ATOM   761  C  CA  . LEU   A 1 94  ? 3.264  7.271   14.047 1.00 12.31  ? 100 LEU   A CA  1 
ATOM   762  C  C   . LEU   A 1 94  ? 2.782  5.853   14.309 1.00 12.08  ? 100 LEU   A C   1 
ATOM   763  O  O   . LEU   A 1 94  ? 2.353  5.144   13.370 1.00 12.99  ? 100 LEU   A O   1 
ATOM   764  C  CB  . LEU   A 1 94  ? 2.033  8.212   14.203 1.00 14.31  ? 100 LEU   A CB  1 
ATOM   765  C  CG  . LEU   A 1 94  ? 2.288  9.696   14.146 1.00 18.39  ? 100 LEU   A CG  1 
ATOM   766  C  CD1 . LEU   A 1 94  ? 0.995  10.520  14.509 1.00 21.18  ? 100 LEU   A CD1 1 
ATOM   767  C  CD2 . LEU   A 1 94  ? 3.357  10.137  15.127 1.00 20.25  ? 100 LEU   A CD2 1 
ATOM   768  N  N   . ALA   A 1 95  ? 2.821  5.459   15.555 1.00 11.86  ? 101 ALA   A N   1 
ATOM   769  C  CA  . ALA   A 1 95  ? 2.277  4.157   16.011 1.00 11.27  ? 101 ALA   A CA  1 
ATOM   770  C  C   . ALA   A 1 95  ? 1.658  4.360   17.394 1.00 11.00  ? 101 ALA   A C   1 
ATOM   771  O  O   . ALA   A 1 95  ? 1.951  5.360   18.096 1.00 11.61  ? 101 ALA   A O   1 
ATOM   772  C  CB  . ALA   A 1 95  ? 3.385  3.081   16.126 1.00 11.67  ? 101 ALA   A CB  1 
ATOM   773  N  N   . VAL   A 1 96  ? 0.868  3.383   17.823 1.00 10.83  ? 102 VAL   A N   1 
ATOM   774  C  CA  . VAL   A 1 96  ? 0.344  3.368   19.154 1.00 10.74  ? 102 VAL   A CA  1 
ATOM   775  C  C   . VAL   A 1 96  ? 1.369  2.618   20.040 1.00 12.09  ? 102 VAL   A C   1 
ATOM   776  O  O   . VAL   A 1 96  ? 1.672  1.451   19.810 1.00 14.00  ? 102 VAL   A O   1 
ATOM   777  C  CB  . VAL   A 1 96  ? -1.031 2.680   19.188 1.00 11.23  ? 102 VAL   A CB  1 
ATOM   778  C  CG1 . VAL   A 1 96  ? -1.543 2.495   20.630 1.00 13.00  ? 102 VAL   A CG1 1 
ATOM   779  C  CG2 . VAL   A 1 96  ? -2.020 3.441   18.307 1.00 12.02  ? 102 VAL   A CG2 1 
ATOM   780  N  N   . GLY   A 1 97  ? 1.852  3.336   21.039 1.00 12.94  ? 103 GLY   A N   1 
ATOM   781  C  CA  . GLY   A 1 97  ? 2.817  2.745   21.963 1.00 14.09  ? 103 GLY   A CA  1 
ATOM   782  C  C   . GLY   A 1 97  ? 3.277  3.757   22.966 1.00 15.24  ? 103 GLY   A C   1 
ATOM   783  O  O   . GLY   A 1 97  ? 3.059  4.942   22.848 1.00 16.35  ? 103 GLY   A O   1 
ATOM   784  N  N   . HIS   A 1 98  ? 3.871  3.206   24.056 1.00 17.11  ? 104 HIS   A N   1 
ATOM   785  C  CA  . HIS   A 1 98  ? 4.372  4.035   25.115 1.00 18.97  ? 104 HIS   A CA  1 
ATOM   786  C  C   . HIS   A 1 98  ? 5.672  4.693   24.729 1.00 18.27  ? 104 HIS   A C   1 
ATOM   787  O  O   . HIS   A 1 98  ? 6.596  4.058   24.150 1.00 17.88  ? 104 HIS   A O   1 
ATOM   788  C  CB  . HIS   A 1 98  ? 4.575  3.197   26.405 1.00 18.90  ? 104 HIS   A CB  1 
ATOM   789  C  CG  . HIS   A 1 98  ? 5.016  4.064   27.532 1.00 19.48  ? 104 HIS   A CG  1 
ATOM   790  N  ND1 . HIS   A 1 98  ? 4.143  4.952   28.131 1.00 19.10  ? 104 HIS   A ND1 1 
ATOM   791  C  CD2 . HIS   A 1 98  ? 6.240  4.219   28.091 1.00 20.44  ? 104 HIS   A CD2 1 
ATOM   792  C  CE1 . HIS   A 1 98  ? 4.874  5.622   29.023 1.00 20.15  ? 104 HIS   A CE1 1 
ATOM   793  N  NE2 . HIS   A 1 98  ? 6.132  5.193   29.038 1.00 20.96  ? 104 HIS   A NE2 1 
ATOM   794  N  N   . SER   A 1 99  ? 5.783  5.931   25.033 1.00 19.76  ? 105 SER   A N   1 
ATOM   795  C  CA  . SER   A 1 99  ? 6.976  6.623   24.968 1.00 19.26  ? 105 SER   A CA  1 
ATOM   796  C  C   . SER   A 1 99  ? 6.991  7.764   25.955 1.00 18.93  ? 105 SER   A C   1 
ATOM   797  O  O   . SER   A 1 99  ? 5.911  8.231   26.367 1.00 22.02  ? 105 SER   A O   1 
ATOM   798  C  CB  . SER   A 1 99  ? 7.320  7.002   23.546 1.00 21.28  ? 105 SER   A CB  1 
ATOM   799  O  OG  . SER   A 1 99  ? 6.375  7.908   23.028 1.00 23.23  ? 105 SER   A OG  1 
ATOM   800  N  N   . GLU   A 1 100 ? 8.228  8.216   26.281 1.00 15.12  ? 106 GLU   A N   1 
ATOM   801  C  CA  . GLU   A 1 100 ? 8.595  9.371   27.138 1.00 15.74  ? 106 GLU   A CA  1 
ATOM   802  C  C   . GLU   A 1 100 ? 9.770  10.068  26.490 1.00 16.70  ? 106 GLU   A C   1 
ATOM   803  O  O   . GLU   A 1 100 ? 10.441 9.500   25.596 1.00 15.33  ? 106 GLU   A O   1 
ATOM   804  C  CB  . GLU   A 1 100 ? 9.003  8.863   28.540 1.00 16.68  ? 106 GLU   A CB  1 
ATOM   805  C  CG  . GLU   A 1 100 ? 7.813  8.204   29.220 1.00 20.21  ? 106 GLU   A CG  1 
ATOM   806  C  CD  . GLU   A 1 100 ? 8.096  7.569   30.574 1.00 20.99  ? 106 GLU   A CD  1 
ATOM   807  O  OE1 . GLU   A 1 100 ? 9.032  8.021   31.274 1.00 25.61  ? 106 GLU   A OE1 1 
ATOM   808  O  OE2 . GLU   A 1 100 ? 7.388  6.602   30.924 1.00 20.51  ? 106 GLU   A OE2 1 
ATOM   809  N  N   . PRO   A 1 101 ? 10.072 11.320  26.865 1.00 16.82  ? 107 PRO   A N   1 
ATOM   810  C  CA  . PRO   A 1 101 ? 11.121 12.063  26.128 1.00 16.27  ? 107 PRO   A CA  1 
ATOM   811  C  C   . PRO   A 1 101 ? 12.453 11.350  25.990 1.00 15.33  ? 107 PRO   A C   1 
ATOM   812  O  O   . PRO   A 1 101 ? 13.021 11.293  24.885 1.00 15.48  ? 107 PRO   A O   1 
ATOM   813  C  CB  . PRO   A 1 101 ? 11.228 13.392  26.911 1.00 18.47  ? 107 PRO   A CB  1 
ATOM   814  C  CG  . PRO   A 1 101 ? 9.845  13.590  27.416 1.00 20.49  ? 107 PRO   A CG  1 
ATOM   815  C  CD  . PRO   A 1 101 ? 9.341  12.208  27.803 1.00 17.75  ? 107 PRO   A CD  1 
ATOM   816  N  N   . GLY   A 1 102 ? 12.943 10.728  27.053 1.00 15.03  ? 108 GLY   A N   1 
ATOM   817  C  CA  . GLY   A 1 102 ? 14.190 9.983   27.059 1.00 14.45  ? 108 GLY   A CA  1 
ATOM   818  C  C   . GLY   A 1 102 ? 14.174 8.680   26.262 1.00 12.70  ? 108 GLY   A C   1 
ATOM   819  O  O   . GLY   A 1 102 ? 15.230 8.072   26.084 1.00 13.25  ? 108 GLY   A O   1 
ATOM   820  N  N   . ASP   A 1 103 ? 13.017 8.272   25.709 1.00 11.44  ? 109 ASP   A N   1 
ATOM   821  C  CA  . ASP   A 1 103 ? 12.958 7.114   24.795 1.00 11.09  ? 109 ASP   A CA  1 
ATOM   822  C  C   . ASP   A 1 103 ? 13.494 7.486   23.403 1.00 11.12  ? 109 ASP   A C   1 
ATOM   823  O  O   . ASP   A 1 103 ? 13.738 6.573   22.577 1.00 10.54  ? 109 ASP   A O   1 
ATOM   824  C  CB  . ASP   A 1 103 ? 11.502 6.576   24.670 1.00 10.85  ? 109 ASP   A CB  1 
ATOM   825  C  CG  . ASP   A 1 103 ? 11.109 5.835   25.932 1.00 11.95  ? 109 ASP   A CG  1 
ATOM   826  O  OD1 . ASP   A 1 103 ? 11.992 5.166   26.519 1.00 12.45  ? 109 ASP   A OD1 1 
ATOM   827  O  OD2 . ASP   A 1 103 ? 9.910  5.950   26.365 1.00 12.46  ? 109 ASP   A OD2 1 
ATOM   828  N  N   . CYS   A 1 104 ? 13.665 8.792   23.091 1.00 10.77  ? 110 CYS   A N   1 
ATOM   829  C  CA  . CYS   A 1 104 ? 14.236 9.162   21.782 1.00 11.03  ? 110 CYS   A CA  1 
ATOM   830  C  C   . CYS   A 1 104 ? 15.559 8.463   21.540 1.00 10.64  ? 110 CYS   A C   1 
ATOM   831  O  O   . CYS   A 1 104 ? 16.393 8.344   22.423 1.00 11.25  ? 110 CYS   A O   1 
ATOM   832  C  CB  . CYS   A 1 104 ? 14.409 10.672  21.702 1.00 10.85  ? 110 CYS   A CB  1 
ATOM   833  S  SG  . CYS   A 1 104 ? 12.819 11.544  21.452 1.00 13.01  ? 110 CYS   A SG  1 
ATOM   834  N  N   . GLY   A 1 105 ? 15.720 7.941   20.325 1.00 9.62   ? 111 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 105 ? 16.917 7.231   19.929 1.00 10.56  ? 111 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 105 ? 16.723 5.719   19.851 1.00 10.00  ? 111 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 105 ? 17.577 5.016   19.284 1.00 10.68  ? 111 GLY   A O   1 
ATOM   838  N  N   . GLY   A 1 106 ? 15.649 5.199   20.474 1.00 9.72   ? 112 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 106 ? 15.357 3.784   20.350 1.00 9.70   ? 112 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 106 ? 15.099 3.387   18.903 1.00 8.58   ? 112 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 106 ? 14.411 4.123   18.163 1.00 9.25   ? 112 GLY   A O   1 
ATOM   842  N  N   . ILE   A 1 107 ? 15.572 2.232   18.500 1.00 8.67   ? 113 ILE   A N   1 
ATOM   843  C  CA  . ILE   A 1 107 ? 15.429 1.815   17.098 1.00 8.84   ? 113 ILE   A CA  1 
ATOM   844  C  C   . ILE   A 1 107 ? 14.087 1.166   16.825 1.00 8.47   ? 113 ILE   A C   1 
ATOM   845  O  O   . ILE   A 1 107 ? 13.628 0.320   17.619 1.00 9.14   ? 113 ILE   A O   1 
ATOM   846  C  CB  . ILE   A 1 107 ? 16.589 0.846   16.740 1.00 9.50   ? 113 ILE   A CB  1 
ATOM   847  C  CG1 . ILE   A 1 107 ? 17.878 1.696   16.484 1.00 11.30  ? 113 ILE   A CG1 1 
ATOM   848  C  CG2 . ILE   A 1 107 ? 16.279 -0.040  15.514 1.00 10.48  ? 113 ILE   A CG2 1 
ATOM   849  C  CD1 . ILE   A 1 107 ? 19.145 0.866   16.296 1.00 14.25  ? 113 ILE   A CD1 1 
ATOM   850  N  N   . LEU   A 1 108 ? 13.511 1.497   15.677 1.00 8.39   ? 114 LEU   A N   1 
ATOM   851  C  CA  . LEU   A 1 108 ? 12.397 0.790   15.037 1.00 8.56   ? 114 LEU   A CA  1 
ATOM   852  C  C   . LEU   A 1 108 ? 13.014 -0.045  13.910 1.00 8.29   ? 114 LEU   A C   1 
ATOM   853  O  O   . LEU   A 1 108 ? 13.782 0.497   13.084 1.00 9.16   ? 114 LEU   A O   1 
ATOM   854  C  CB  . LEU   A 1 108 ? 11.403 1.810   14.433 1.00 8.99   ? 114 LEU   A CB  1 
ATOM   855  C  CG  . LEU   A 1 108 ? 10.283 1.198   13.553 1.00 8.88   ? 114 LEU   A CG  1 
ATOM   856  C  CD1 . LEU   A 1 108 ? 9.312  0.376   14.416 1.00 10.84  ? 114 LEU   A CD1 1 
ATOM   857  C  CD2 . LEU   A 1 108 ? 9.506  2.329   12.820 1.00 11.24  ? 114 LEU   A CD2 1 
ATOM   858  N  N   . ARG   A 1 109 ? 12.695 -1.335  13.860 1.00 8.92   ? 115 ARG   A N   1 
ATOM   859  C  CA  . ARG   A 1 109 ? 13.254 -2.234  12.804 1.00 9.42   ? 115 ARG   A CA  1 
ATOM   860  C  C   . ARG   A 1 109 ? 12.166 -3.111  12.264 1.00 9.88   ? 115 ARG   A C   1 
ATOM   861  O  O   . ARG   A 1 109 ? 11.170 -3.444  12.941 1.00 9.94   ? 115 ARG   A O   1 
ATOM   862  C  CB  . ARG   A 1 109 ? 14.422 -3.065  13.395 1.00 10.83  ? 115 ARG   A CB  1 
ATOM   863  C  CG  . ARG   A 1 109 ? 13.950 -4.060  14.483 1.00 11.31  ? 115 ARG   A CG  1 
ATOM   864  C  CD  . ARG   A 1 109 ? 15.163 -4.794  15.076 1.00 12.45  ? 115 ARG   A CD  1 
ATOM   865  N  NE  . ARG   A 1 109 ? 15.979 -3.914  15.907 1.00 13.42  ? 115 ARG   A NE  1 
ATOM   866  C  CZ  . ARG   A 1 109 ? 17.277 -3.707  15.797 1.00 12.73  ? 115 ARG   A CZ  1 
ATOM   867  N  NH1 . ARG   A 1 109 ? 17.954 -4.161  14.733 1.00 14.56  ? 115 ARG   A NH1 1 
ATOM   868  N  NH2 . ARG   A 1 109 ? 17.919 -2.996  16.718 1.00 14.54  ? 115 ARG   A NH2 1 
ATOM   869  N  N   . CYS   A 1 110 ? 12.368 -3.568  11.042 1.00 12.52  ? 116 CYS   A N   1 
ATOM   870  C  CA  . CYS   A 1 110 ? 11.421 -4.470  10.344 1.00 15.27  ? 116 CYS   A CA  1 
ATOM   871  C  C   . CYS   A 1 110 ? 12.250 -5.671  9.923  1.00 16.48  ? 116 CYS   A C   1 
ATOM   872  O  O   . CYS   A 1 110 ? 13.447 -5.834  10.266 1.00 15.53  ? 116 CYS   A O   1 
ATOM   873  C  CB  . CYS   A 1 110 ? 10.771 -3.771  9.142  1.00 13.29  ? 116 CYS   A CB  1 
ATOM   874  S  SG  . CYS   A 1 110 ? 11.948 -3.465  7.805  1.00 14.63  ? 116 CYS   A SG  1 
ATOM   875  N  N   . GLN   A 1 111 ? 11.590 -6.577  9.141  1.00 17.51  ? 117 GLN   A N   1 
ATOM   876  C  CA  . GLN   A 1 111 ? 12.289 -7.729  8.618  1.00 19.76  ? 117 GLN   A CA  1 
ATOM   877  C  C   . GLN   A 1 111 ? 13.536 -7.412  7.761  1.00 21.44  ? 117 GLN   A C   1 
ATOM   878  O  O   . GLN   A 1 111 ? 14.432 -8.258  7.666  1.00 23.68  ? 117 GLN   A O   1 
ATOM   879  C  CB  . GLN   A 1 111 ? 11.326 -8.662  7.828  1.00 22.69  ? 117 GLN   A CB  1 
ATOM   880  C  CG  . GLN   A 1 111 ? 10.862 -8.064  6.508  1.00 26.61  ? 117 GLN   A CG  1 
ATOM   881  C  CD  . GLN   A 1 111 ? 9.960  -9.026  5.770  1.00 33.01  ? 117 GLN   A CD  1 
ATOM   882  O  OE1 . GLN   A 1 111 ? 8.732  -8.931  5.848  1.00 36.10  ? 117 GLN   A OE1 1 
ATOM   883  N  NE2 . GLN   A 1 111 ? 10.562 -9.967  5.039  1.00 32.45  ? 117 GLN   A NE2 1 
ATOM   884  N  N   . HIS   A 1 112 ? 13.641 -6.221  7.179  1.00 17.60  ? 118 HIS   A N   1 
ATOM   885  C  CA  . HIS   A 1 112 ? 14.750 -5.830  6.273  1.00 17.71  ? 118 HIS   A CA  1 
ATOM   886  C  C   . HIS   A 1 112 ? 15.906 -5.097  6.985  1.00 18.29  ? 118 HIS   A C   1 
ATOM   887  O  O   . HIS   A 1 112 ? 16.961 -4.834  6.378  1.00 20.76  ? 118 HIS   A O   1 
ATOM   888  C  CB  . HIS   A 1 112 ? 14.160 -4.912  5.197  1.00 17.57  ? 118 HIS   A CB  1 
ATOM   889  C  CG  . HIS   A 1 112 ? 13.022 -5.582  4.429  1.00 19.97  ? 118 HIS   A CG  1 
ATOM   890  N  ND1 . HIS   A 1 112 ? 11.691 -5.165  4.532  1.00 18.59  ? 118 HIS   A ND1 1 
ATOM   891  C  CD2 . HIS   A 1 112 ? 13.087 -6.524  3.443  1.00 22.76  ? 118 HIS   A CD2 1 
ATOM   892  C  CE1 . HIS   A 1 112 ? 10.989 -5.950  3.721  1.00 21.92  ? 118 HIS   A CE1 1 
ATOM   893  N  NE2 . HIS   A 1 112 ? 11.789 -6.793  3.061  1.00 24.84  ? 118 HIS   A NE2 1 
ATOM   894  N  N   . GLY   A 1 113 ? 15.692 -4.635  8.242  1.00 16.09  ? 119 GLY   A N   1 
ATOM   895  C  CA  . GLY   A 1 113 ? 16.737 -3.887  8.941  1.00 15.16  ? 119 GLY   A CA  1 
ATOM   896  C  C   . GLY   A 1 113 ? 16.182 -2.702  9.733  1.00 12.74  ? 119 GLY   A C   1 
ATOM   897  O  O   . GLY   A 1 113 ? 14.994 -2.674  10.059 1.00 12.73  ? 119 GLY   A O   1 
ATOM   898  N  N   . VAL   A 1 114 ? 17.056 -1.713  10.006 1.00 11.46  ? 120 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 114 ? 16.618 -0.515  10.766 1.00 11.70  ? 120 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 114 ? 15.779 0.407   9.913  1.00 9.88   ? 120 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 114 ? 16.175 0.753   8.777  1.00 11.15  ? 120 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 114 ? 17.854 0.226   11.328 1.00 11.78  ? 120 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 114 ? 17.454 1.548   11.996 1.00 12.67  ? 120 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 114 ? 18.621 -0.682  12.290 1.00 12.83  ? 120 VAL   A CG2 1 
ATOM   905  N  N   . VAL   A 1 115 ? 14.655 0.835   10.438 1.00 9.61   ? 121 VAL   A N   1 
ATOM   906  C  CA  . VAL   A 1 115 ? 13.700 1.706   9.773  1.00 9.71   ? 121 VAL   A CA  1 
ATOM   907  C  C   . VAL   A 1 115 ? 13.843 3.145   10.205 1.00 9.72   ? 121 VAL   A C   1 
ATOM   908  O  O   . VAL   A 1 115 ? 13.696 4.083   9.397  1.00 10.82  ? 121 VAL   A O   1 
ATOM   909  C  CB  . VAL   A 1 115 ? 12.240 1.215   10.034 1.00 10.96  ? 121 VAL   A CB  1 
ATOM   910  C  CG1 . VAL   A 1 115 ? 11.168 2.206   9.510  1.00 13.49  ? 121 VAL   A CG1 1 
ATOM   911  C  CG2 . VAL   A 1 115 ? 12.004 -0.186  9.479  1.00 12.78  ? 121 VAL   A CG2 1 
ATOM   912  N  N   . GLY   A 1 116 ? 14.065 3.376   11.505 1.00 9.59   ? 122 GLY   A N   1 
ATOM   913  C  CA  . GLY   A 1 116 ? 14.129 4.750   12.019 1.00 10.30  ? 122 GLY   A CA  1 
ATOM   914  C  C   . GLY   A 1 116 ? 14.390 4.756   13.512 1.00 9.26   ? 122 GLY   A C   1 
ATOM   915  O  O   . GLY   A 1 116 ? 14.687 3.689   14.085 1.00 9.57   ? 122 GLY   A O   1 
ATOM   916  N  N   . ILE   A 1 117 ? 14.275 5.941   14.131 1.00 9.11   ? 123 ILE   A N   1 
ATOM   917  C  CA  . ILE   A 1 117 ? 14.513 6.078   15.578 1.00 9.10   ? 123 ILE   A CA  1 
ATOM   918  C  C   . ILE   A 1 117 ? 13.380 6.849   16.213 1.00 9.07   ? 123 ILE   A C   1 
ATOM   919  O  O   . ILE   A 1 117 ? 12.793 7.767   15.584 1.00 9.74   ? 123 ILE   A O   1 
ATOM   920  C  CB  . ILE   A 1 117 ? 15.875 6.759   15.929 1.00 9.75   ? 123 ILE   A CB  1 
ATOM   921  C  CG1 . ILE   A 1 117 ? 16.035 8.086   15.191 1.00 11.99  ? 123 ILE   A CG1 1 
ATOM   922  C  CG2 . ILE   A 1 117 ? 17.013 5.775   15.705 1.00 11.71  ? 123 ILE   A CG2 1 
ATOM   923  C  CD1 . ILE   A 1 117 ? 17.316 8.866   15.713 1.00 11.73  ? 123 ILE   A CD1 1 
ATOM   924  N  N   . VAL   A 1 118 ? 13.077 6.550   17.471 1.00 8.97   ? 124 VAL   A N   1 
ATOM   925  C  CA  . VAL   A 1 118 ? 12.043 7.290   18.207 1.00 9.43   ? 124 VAL   A CA  1 
ATOM   926  C  C   . VAL   A 1 118 ? 12.409 8.790   18.235 1.00 9.79   ? 124 VAL   A C   1 
ATOM   927  O  O   . VAL   A 1 118 ? 13.589 9.134   18.538 1.00 9.67   ? 124 VAL   A O   1 
ATOM   928  C  CB  . VAL   A 1 118 ? 11.933 6.777   19.649 1.00 9.60   ? 124 VAL   A CB  1 
ATOM   929  C  CG1 . VAL   A 1 118 ? 10.969 7.643   20.489 1.00 10.45  ? 124 VAL   A CG1 1 
ATOM   930  C  CG2 . VAL   A 1 118 ? 11.458 5.311   19.706 1.00 10.37  ? 124 VAL   A CG2 1 
ATOM   931  N  N   . SER   A 1 119 ? 11.449 9.656   17.954 1.00 9.95   ? 125 SER   A N   1 
ATOM   932  C  CA  . SER   A 1 119 ? 11.636 11.115  17.929 1.00 11.08  ? 125 SER   A CA  1 
ATOM   933  C  C   . SER   A 1 119 ? 10.539 11.861  18.662 1.00 11.77  ? 125 SER   A C   1 
ATOM   934  O  O   . SER   A 1 119 ? 10.826 12.987  19.189 1.00 13.37  ? 125 SER   A O   1 
ATOM   935  C  CB  . SER   A 1 119 ? 11.765 11.559  16.485 1.00 10.74  ? 125 SER   A CB  1 
ATOM   936  O  OG  . SER   A 1 119 ? 11.846 12.978  16.339 1.00 13.54  ? 125 SER   A OG  1 
ATOM   937  N  N   . THR   A 1 120 ? 9.275  11.365  18.681 1.00 12.46  ? 126 THR   A N   1 
ATOM   938  C  CA  . THR   A 1 120 ? 8.174  12.136  19.294 1.00 13.76  ? 126 THR   A CA  1 
ATOM   939  C  C   . THR   A 1 120 ? 7.369  11.188  20.180 1.00 14.79  ? 126 THR   A C   1 
ATOM   940  O  O   . THR   A 1 120 ? 7.459  9.948   20.042 1.00 12.71  ? 126 THR   A O   1 
ATOM   941  C  CB  . THR   A 1 120 ? 7.274  12.813  18.219 1.00 14.50  ? 126 THR   A CB  1 
ATOM   942  O  OG1 . THR   A 1 120 ? 6.481  11.817  17.556 1.00 15.29  ? 126 THR   A OG1 1 
ATOM   943  C  CG2 . THR   A 1 120 ? 8.049  13.629  17.207 1.00 14.64  ? 126 THR   A CG2 1 
ATOM   944  N  N   . GLY   A 1 121 ? 6.575  11.737  21.082 1.00 16.88  ? 127 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 121 ? 5.722  10.924  21.923 1.00 19.21  ? 127 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 121 ? 4.680  11.711  22.688 1.00 21.65  ? 127 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 121 ? 4.789  12.928  22.798 1.00 24.17  ? 127 GLY   A O   1 
ATOM   948  N  N   . GLY   A 1 122 ? 3.750  10.947  23.270 1.00 23.87  ? 128 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 122 ? 2.680  11.438  24.146 1.00 24.39  ? 128 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 122 ? 1.383  10.676  23.940 1.00 26.66  ? 128 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 122 ? 1.074  10.258  22.815 1.00 28.49  ? 128 GLY   A O   1 
ATOM   952  N  N   . ASN   A 1 123 ? 0.596  10.538  25.034 1.00 25.36  ? 129 ASN   A N   1 
ATOM   953  C  CA  . ASN   A 1 123 ? -0.755 9.975   25.042 1.00 25.36  ? 129 ASN   A CA  1 
ATOM   954  C  C   . ASN   A 1 123 ? -0.954 8.662   24.291 1.00 22.99  ? 129 ASN   A C   1 
ATOM   955  O  O   . ASN   A 1 123 ? -2.016 8.446   23.677 1.00 22.64  ? 129 ASN   A O   1 
ATOM   956  C  CB  . ASN   A 1 123 ? -1.713 11.036  24.507 1.00 28.18  ? 129 ASN   A CB  1 
ATOM   957  C  CG  . ASN   A 1 123 ? -1.772 12.273  25.367 1.00 31.93  ? 129 ASN   A CG  1 
ATOM   958  O  OD1 . ASN   A 1 123 ? -2.102 12.188  26.556 1.00 35.10  ? 129 ASN   A OD1 1 
ATOM   959  N  ND2 . ASN   A 1 123 ? -1.486 13.446  24.764 1.00 31.45  ? 129 ASN   A ND2 1 
ATOM   960  N  N   . GLY   A 1 124 ? -0.066 7.711   24.512 1.00 19.70  ? 130 GLY   A N   1 
ATOM   961  C  CA  . GLY   A 1 124 ? -0.179 6.404   23.928 1.00 18.00  ? 130 GLY   A CA  1 
ATOM   962  C  C   . GLY   A 1 124 ? 0.238  6.418   22.473 1.00 14.05  ? 130 GLY   A C   1 
ATOM   963  O  O   . GLY   A 1 124 ? 0.063  5.381   21.885 1.00 16.18  ? 130 GLY   A O   1 
ATOM   964  N  N   . LEU   A 1 125 ? 0.878  7.531   21.943 1.00 14.68  ? 131 LEU   A N   1 
ATOM   965  C  CA  . LEU   A 1 125 ? 1.470  7.524   20.572 1.00 14.60  ? 131 LEU   A CA  1 
ATOM   966  C  C   . LEU   A 1 125 ? 3.001  7.626   20.643 1.00 15.63  ? 131 LEU   A C   1 
ATOM   967  O  O   . LEU   A 1 125 ? 3.560  8.303   21.561 1.00 18.12  ? 131 LEU   A O   1 
ATOM   968  C  CB  . LEU   A 1 125 ? 0.953  8.693   19.757 1.00 15.24  ? 131 LEU   A CB  1 
ATOM   969  C  CG  . LEU   A 1 125 ? -0.560 8.620   19.507 1.00 15.93  ? 131 LEU   A CG  1 
ATOM   970  C  CD1 . LEU   A 1 125 ? -1.145 10.006  19.176 1.00 19.42  ? 131 LEU   A CD1 1 
ATOM   971  C  CD2 . LEU   A 1 125 ? -0.914 7.521   18.476 1.00 16.82  ? 131 LEU   A CD2 1 
ATOM   972  N  N   . VAL   A 1 126 ? 3.676  7.004   19.680 1.00 11.93  ? 132 VAL   A N   1 
ATOM   973  C  CA  . VAL   A 1 126 ? 5.135  7.136   19.529 1.00 11.33  ? 132 VAL   A CA  1 
ATOM   974  C  C   . VAL   A 1 126 ? 5.365  7.508   18.068 1.00 11.66  ? 132 VAL   A C   1 
ATOM   975  O  O   . VAL   A 1 126 ? 4.754  6.920   17.171 1.00 11.99  ? 132 VAL   A O   1 
ATOM   976  C  CB  . VAL   A 1 126 ? 5.845  5.848   19.997 1.00 12.12  ? 132 VAL   A CB  1 
ATOM   977  C  CG1 . VAL   A 1 126 ? 5.310  4.574   19.336 1.00 13.38  ? 132 VAL   A CG1 1 
ATOM   978  C  CG2 . VAL   A 1 126 ? 7.374  5.958   19.826 1.00 12.21  ? 132 VAL   A CG2 1 
ATOM   979  N  N   . GLY   A 1 127 ? 6.275  8.436   17.815 1.00 11.27  ? 133 GLY   A N   1 
ATOM   980  C  CA  . GLY   A 1 127 ? 6.632  8.819   16.461 1.00 11.36  ? 133 GLY   A CA  1 
ATOM   981  C  C   . GLY   A 1 127 ? 8.093  8.535   16.169 1.00 10.69  ? 133 GLY   A C   1 
ATOM   982  O  O   . GLY   A 1 127 ? 8.966  8.699   17.056 1.00 11.85  ? 133 GLY   A O   1 
ATOM   983  N  N   . PHE   A 1 128 ? 8.340  8.057   14.968 1.00 10.12  ? 134 PHE   A N   1 
ATOM   984  C  CA  . PHE   A 1 128 ? 9.690  7.659   14.518 1.00 9.77   ? 134 PHE   A CA  1 
ATOM   985  C  C   . PHE   A 1 128 ? 10.141 8.459   13.326 1.00 9.89   ? 134 PHE   A C   1 
ATOM   986  O  O   . PHE   A 1 128 ? 9.370  8.628   12.359 1.00 10.55  ? 134 PHE   A O   1 
ATOM   987  C  CB  . PHE   A 1 128 ? 9.666  6.156   14.103 1.00 10.21  ? 134 PHE   A CB  1 
ATOM   988  C  CG  . PHE   A 1 128 ? 9.042  5.234   15.127 1.00 10.09  ? 134 PHE   A CG  1 
ATOM   989  C  CD1 . PHE   A 1 128 ? 9.791  4.740   16.186 1.00 9.13   ? 134 PHE   A CD1 1 
ATOM   990  C  CD2 . PHE   A 1 128 ? 7.714  4.840   15.012 1.00 11.25  ? 134 PHE   A CD2 1 
ATOM   991  C  CE1 . PHE   A 1 128 ? 9.214  3.859   17.115 1.00 9.64   ? 134 PHE   A CE1 1 
ATOM   992  C  CE2 . PHE   A 1 128 ? 7.152  3.962   15.939 1.00 11.50  ? 134 PHE   A CE2 1 
ATOM   993  C  CZ  . PHE   A 1 128 ? 7.918  3.468   16.971 1.00 10.66  ? 134 PHE   A CZ  1 
ATOM   994  N  N   . ALA   A 1 129 ? 11.391 8.941   13.402 1.00 9.65   ? 135 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? 12.028 9.624   12.264 1.00 10.77  ? 135 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? 12.502 8.530   11.286 1.00 9.74   ? 135 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? 13.378 7.724   11.654 1.00 10.49  ? 135 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? 13.187 10.454  12.777 1.00 10.99  ? 135 ALA   A CB  1 
ATOM   999  N  N   . ASP   A 1 130 ? 11.957 8.488   10.074 1.00 10.34  ? 136 ASP   A N   1 
ATOM   1000 C  CA  . ASP   A 1 130 ? 12.373 7.498   9.076  1.00 10.74  ? 136 ASP   A CA  1 
ATOM   1001 C  C   . ASP   A 1 130 ? 13.779 7.782   8.586  1.00 10.61  ? 136 ASP   A C   1 
ATOM   1002 O  O   . ASP   A 1 130 ? 14.182 8.964   8.438  1.00 12.16  ? 136 ASP   A O   1 
ATOM   1003 C  CB  . ASP   A 1 130 ? 11.408 7.587   7.857  1.00 13.41  ? 136 ASP   A CB  1 
ATOM   1004 C  CG  . ASP   A 1 130 ? 11.659 6.571   6.792  1.00 14.88  ? 136 ASP   A CG  1 
ATOM   1005 O  OD1 . ASP   A 1 130 ? 11.728 5.377   7.115  1.00 16.79  ? 136 ASP   A OD1 1 
ATOM   1006 O  OD2 . ASP   A 1 130 ? 11.930 7.001   5.629  1.00 20.14  ? 136 ASP   A OD2 1 
ATOM   1007 N  N   . VAL   A 1 131 ? 14.522 6.713   8.262  1.00 10.05  ? 137 VAL   A N   1 
ATOM   1008 C  CA  . VAL   A 1 131 ? 15.857 6.830   7.629  1.00 10.72  ? 137 VAL   A CA  1 
ATOM   1009 C  C   . VAL   A 1 131 ? 15.941 6.023   6.336  1.00 11.24  ? 137 VAL   A C   1 
ATOM   1010 O  O   . VAL   A 1 131 ? 17.011 6.015   5.699  1.00 10.95  ? 137 VAL   A O   1 
ATOM   1011 C  CB  . VAL   A 1 131 ? 17.034 6.449   8.568  1.00 10.49  ? 137 VAL   A CB  1 
ATOM   1012 C  CG1 . VAL   A 1 131 ? 17.045 7.358   9.803  1.00 11.43  ? 137 VAL   A CG1 1 
ATOM   1013 C  CG2 . VAL   A 1 131 ? 17.010 5.001   8.988  1.00 11.55  ? 137 VAL   A CG2 1 
ATOM   1014 N  N   . ARG   A 1 132 ? 14.865 5.348   5.910  1.00 11.07  ? 138 ARG   A N   1 
ATOM   1015 C  CA  . ARG   A 1 132 ? 14.938 4.433   4.777  1.00 11.43  ? 138 ARG   A CA  1 
ATOM   1016 C  C   . ARG   A 1 132 ? 15.205 5.130   3.455  1.00 12.59  ? 138 ARG   A C   1 
ATOM   1017 O  O   . ARG   A 1 132 ? 15.655 4.467   2.487  1.00 14.02  ? 138 ARG   A O   1 
ATOM   1018 C  CB  . ARG   A 1 132 ? 13.662 3.597   4.675  1.00 12.03  ? 138 ARG   A CB  1 
ATOM   1019 C  CG  . ARG   A 1 132 ? 13.519 2.628   5.870  1.00 11.31  ? 138 ARG   A CG  1 
ATOM   1020 C  CD  . ARG   A 1 132 ? 12.211 1.863   5.730  1.00 13.40  ? 138 ARG   A CD  1 
ATOM   1021 N  NE  . ARG   A 1 132 ? 11.089 2.778   5.981  1.00 13.17  ? 138 ARG   A NE  1 
ATOM   1022 C  CZ  . ARG   A 1 132 ? 9.805  2.410   6.096  1.00 14.69  ? 138 ARG   A CZ  1 
ATOM   1023 N  NH1 . ARG   A 1 132 ? 9.440  1.175   5.811  1.00 15.70  ? 138 ARG   A NH1 1 
ATOM   1024 N  NH2 . ARG   A 1 132 ? 8.883  3.305   6.428  1.00 15.50  ? 138 ARG   A NH2 1 
ATOM   1025 N  N   . ASP   A 1 133 ? 14.875 6.440   3.323  1.00 12.51  ? 139 ASP   A N   1 
ATOM   1026 C  CA  . ASP   A 1 133 ? 15.155 7.161   2.090  1.00 13.87  ? 139 ASP   A CA  1 
ATOM   1027 C  C   . ASP   A 1 133 ? 16.591 7.655   1.986  1.00 13.53  ? 139 ASP   A C   1 
ATOM   1028 O  O   . ASP   A 1 133 ? 16.987 8.182   0.930  1.00 15.74  ? 139 ASP   A O   1 
ATOM   1029 C  CB  . ASP   A 1 133 ? 14.182 8.365   1.996  1.00 16.60  ? 139 ASP   A CB  1 
ATOM   1030 C  CG  . ASP   A 1 133 ? 14.413 9.398   3.089  1.00 18.04  ? 139 ASP   A CG  1 
ATOM   1031 O  OD1 . ASP   A 1 133 ? 14.587 9.007   4.258  1.00 17.02  ? 139 ASP   A OD1 1 
ATOM   1032 O  OD2 . ASP   A 1 133 ? 14.399 10.614  2.779  1.00 20.40  ? 139 ASP   A OD2 1 
ATOM   1033 N  N   . LEU   A 1 134 ? 17.395 7.569   3.059  1.00 12.16  ? 140 LEU   A N   1 
ATOM   1034 C  CA  . LEU   A 1 134 ? 18.773 8.110   3.101  1.00 12.33  ? 140 LEU   A CA  1 
ATOM   1035 C  C   . LEU   A 1 134 ? 19.711 7.065   2.525  1.00 12.76  ? 140 LEU   A C   1 
ATOM   1036 O  O   . LEU   A 1 134 ? 20.415 6.340   3.251  1.00 13.18  ? 140 LEU   A O   1 
ATOM   1037 C  CB  . LEU   A 1 134 ? 19.150 8.501   4.535  1.00 12.14  ? 140 LEU   A CB  1 
ATOM   1038 C  CG  . LEU   A 1 134 ? 18.209 9.541   5.220  1.00 13.56  ? 140 LEU   A CG  1 
ATOM   1039 C  CD1 . LEU   A 1 134 ? 18.617 9.760   6.659  1.00 14.42  ? 140 LEU   A CD1 1 
ATOM   1040 C  CD2 . LEU   A 1 134 ? 18.171 10.869  4.475  1.00 15.16  ? 140 LEU   A CD2 1 
ATOM   1041 N  N   . LEU   A 1 135 ? 19.693 6.929   1.187  1.00 12.58  ? 141 LEU   A N   1 
ATOM   1042 C  CA  . LEU   A 1 135 ? 20.424 5.824   0.537  1.00 13.36  ? 141 LEU   A CA  1 
ATOM   1043 C  C   . LEU   A 1 135 ? 21.916 5.920   0.709  1.00 13.97  ? 141 LEU   A C   1 
ATOM   1044 O  O   . LEU   A 1 135 ? 22.616 4.897   0.718  1.00 15.29  ? 141 LEU   A O   1 
ATOM   1045 C  CB  . LEU   A 1 135 ? 20.052 5.724   -0.978 1.00 14.65  ? 141 LEU   A CB  1 
ATOM   1046 C  CG  . LEU   A 1 135 ? 18.538 5.716   -1.259 1.00 15.43  ? 141 LEU   A CG  1 
ATOM   1047 C  CD1 . LEU   A 1 135 ? 18.322 5.358   -2.746 1.00 18.14  ? 141 LEU   A CD1 1 
ATOM   1048 C  CD2 . LEU   A 1 135 ? 17.746 4.702   -0.416 1.00 17.56  ? 141 LEU   A CD2 1 
ATOM   1049 N  N   . TRP   A 1 136 ? 22.417 7.148   0.859  1.00 12.67  ? 142 TRP   A N   1 
ATOM   1050 C  CA  . TRP   A 1 136 ? 23.848 7.403   1.018  1.00 13.50  ? 142 TRP   A CA  1 
ATOM   1051 C  C   . TRP   A 1 136 ? 24.403 6.809   2.310  1.00 13.88  ? 142 TRP   A C   1 
ATOM   1052 O  O   . TRP   A 1 136 ? 25.629 6.664   2.433  1.00 14.88  ? 142 TRP   A O   1 
ATOM   1053 C  CB  . TRP   A 1 136 ? 24.153 8.918   0.907  1.00 14.31  ? 142 TRP   A CB  1 
ATOM   1054 C  CG  . TRP   A 1 136 ? 23.341 9.744   1.857  1.00 13.32  ? 142 TRP   A CG  1 
ATOM   1055 C  CD1 . TRP   A 1 136 ? 22.198 10.421  1.573  1.00 14.07  ? 142 TRP   A CD1 1 
ATOM   1056 C  CD2 . TRP   A 1 136 ? 23.684 10.067  3.218  1.00 13.16  ? 142 TRP   A CD2 1 
ATOM   1057 N  NE1 . TRP   A 1 136 ? 21.764 11.110  2.699  1.00 15.37  ? 142 TRP   A NE1 1 
ATOM   1058 C  CE2 . TRP   A 1 136 ? 22.682 10.930  3.705  1.00 13.75  ? 142 TRP   A CE2 1 
ATOM   1059 C  CE3 . TRP   A 1 136 ? 24.770 9.750   4.051  1.00 14.40  ? 142 TRP   A CE3 1 
ATOM   1060 C  CZ2 . TRP   A 1 136 ? 22.710 11.438  5.017  1.00 14.97  ? 142 TRP   A CZ2 1 
ATOM   1061 C  CZ3 . TRP   A 1 136 ? 24.812 10.280  5.335  1.00 15.90  ? 142 TRP   A CZ3 1 
ATOM   1062 C  CH2 . TRP   A 1 136 ? 23.794 11.115  5.792  1.00 15.39  ? 142 TRP   A CH2 1 
ATOM   1063 N  N   . LEU   A 1 137 ? 23.547 6.472   3.318  1.00 12.83  ? 143 LEU   A N   1 
ATOM   1064 C  CA  . LEU   A 1 137 ? 24.083 5.812   4.533  1.00 13.95  ? 143 LEU   A CA  1 
ATOM   1065 C  C   . LEU   A 1 137 ? 24.781 4.491   4.197  1.00 16.28  ? 143 LEU   A C   1 
ATOM   1066 O  O   . LEU   A 1 137 ? 25.610 4.015   5.000  1.00 17.45  ? 143 LEU   A O   1 
ATOM   1067 C  CB  . LEU   A 1 137 ? 22.953 5.532   5.530  1.00 13.46  ? 143 LEU   A CB  1 
ATOM   1068 C  CG  . LEU   A 1 137 ? 22.415 6.776   6.223  1.00 12.64  ? 143 LEU   A CG  1 
ATOM   1069 C  CD1 . LEU   A 1 137 ? 21.162 6.422   7.007  1.00 14.72  ? 143 LEU   A CD1 1 
ATOM   1070 C  CD2 . LEU   A 1 137 ? 23.490 7.405   7.180  1.00 14.00  ? 143 LEU   A CD2 1 
ATOM   1071 N  N   . ASP   A 1 138 ? 24.446 3.870   3.021  1.00 17.78  ? 144 ASP   A N   1 
ATOM   1072 C  CA  . ASP   A 1 138 ? 24.983 2.552   2.629  1.00 19.78  ? 144 ASP   A CA  1 
ATOM   1073 C  C   . ASP   A 1 138 ? 26.320 2.601   1.920  1.00 24.34  ? 144 ASP   A C   1 
ATOM   1074 O  O   . ASP   A 1 138 ? 26.828 1.545   1.509  1.00 26.31  ? 144 ASP   A O   1 
ATOM   1075 C  CB  . ASP   A 1 138 ? 23.987 1.788   1.687  1.00 20.35  ? 144 ASP   A CB  1 
ATOM   1076 C  CG  . ASP   A 1 138 ? 22.634 1.476   2.270  1.00 22.40  ? 144 ASP   A CG  1 
ATOM   1077 O  OD1 . ASP   A 1 138 ? 22.478 1.585   3.508  1.00 25.07  ? 144 ASP   A OD1 1 
ATOM   1078 O  OD2 . ASP   A 1 138 ? 21.700 1.129   1.497  1.00 30.15  ? 144 ASP   A OD2 1 
ATOM   1079 N  N   . GLU   A 1 139 ? 26.871 3.789   1.680  1.00 25.35  ? 145 GLU   A N   1 
ATOM   1080 C  CA  . GLU   A 1 139 ? 28.140 3.901   0.939  1.00 29.28  ? 145 GLU   A CA  1 
ATOM   1081 C  C   . GLU   A 1 139 ? 29.088 4.931   1.554  1.00 31.86  ? 145 GLU   A C   1 
ATOM   1082 O  O   . GLU   A 1 139 ? 28.699 5.654   2.468  1.00 31.46  ? 145 GLU   A O   1 
ATOM   1083 C  CB  . GLU   A 1 139 ? 27.804 4.266   -0.510 1.00 34.08  ? 145 GLU   A CB  1 
ATOM   1084 C  CG  . GLU   A 1 139 ? 27.084 5.596   -0.618 1.00 42.25  ? 145 GLU   A CG  1 
ATOM   1085 C  CD  . GLU   A 1 139 ? 26.239 5.780   -1.864 1.00 50.96  ? 145 GLU   A CD  1 
ATOM   1086 O  OE1 . GLU   A 1 139 ? 25.773 6.921   -2.095 1.00 51.81  ? 145 GLU   A OE1 1 
ATOM   1087 O  OE2 . GLU   A 1 139 ? 26.041 4.791   -2.608 1.00 55.42  ? 145 GLU   A OE2 1 
ATOM   1088 N  N   . GLU   A 1 140 ? 30.330 5.004   1.035  1.00 34.64  ? 146 GLU   A N   1 
ATOM   1089 C  CA  . GLU   A 1 140 ? 31.417 5.957   1.345  1.00 37.80  ? 146 GLU   A CA  1 
ATOM   1090 C  C   . GLU   A 1 140 ? 31.215 6.820   2.557  1.00 39.28  ? 146 GLU   A C   1 
ATOM   1091 O  O   . GLU   A 1 140 ? 31.849 7.867   2.694  1.00 39.26  ? 146 GLU   A O   1 
ATOM   1092 C  CB  . GLU   A 1 140 ? 31.681 6.863   0.134  1.00 42.34  ? 146 GLU   A CB  1 
ATOM   1093 C  CG  . GLU   A 1 140 ? 30.509 7.766   -0.220 1.00 50.55  ? 146 GLU   A CG  1 
ATOM   1094 C  CD  . GLU   A 1 140 ? 30.777 9.255   -0.077 1.00 61.06  ? 146 GLU   A CD  1 
ATOM   1095 O  OE1 . GLU   A 1 140 ? 29.953 10.057  -0.575 1.00 63.22  ? 146 GLU   A OE1 1 
ATOM   1096 O  OE2 . GLU   A 1 140 ? 31.808 9.621   0.536  1.00 64.55  ? 146 GLU   A OE2 1 
ATOM   1097 N  N   . SER   B 1 1   ? 21.855 -21.247 7.636  1.00 15.88  ? 7   SER   C N   1 
ATOM   1098 C  CA  . SER   B 1 1   ? 20.718 -21.038 8.559  1.00 15.28  ? 7   SER   C CA  1 
ATOM   1099 C  C   . SER   B 1 1   ? 20.691 -22.161 9.620  1.00 16.06  ? 7   SER   C C   1 
ATOM   1100 O  O   . SER   B 1 1   ? 21.360 -23.200 9.474  1.00 18.30  ? 7   SER   C O   1 
ATOM   1101 C  CB  . SER   B 1 1   ? 19.403 -21.047 7.777  1.00 18.87  ? 7   SER   C CB  1 
ATOM   1102 O  OG  . SER   B 1 1   ? 19.277 -22.303 7.139  1.00 22.74  ? 7   SER   C OG  1 
ATOM   1103 N  N   . GLY   B 1 2   ? 19.918 -21.948 10.698 1.00 15.22  ? 8   GLY   C N   1 
ATOM   1104 C  CA  . GLY   B 1 2   ? 19.753 -22.955 11.741 1.00 14.70  ? 8   GLY   C CA  1 
ATOM   1105 C  C   . GLY   B 1 2   ? 19.472 -22.345 13.093 1.00 13.09  ? 8   GLY   C C   1 
ATOM   1106 O  O   . GLY   B 1 2   ? 19.846 -21.196 13.357 1.00 13.98  ? 8   GLY   C O   1 
ATOM   1107 N  N   . ALA   B 1 3   ? 18.804 -23.085 13.961 1.00 12.11  ? 9   ALA   C N   1 
ATOM   1108 C  CA  . ALA   B 1 3   ? 18.475 -22.588 15.304 1.00 12.76  ? 9   ALA   C CA  1 
ATOM   1109 C  C   . ALA   B 1 3   ? 18.600 -23.711 16.335 1.00 11.71  ? 9   ALA   C C   1 
ATOM   1110 O  O   . ALA   B 1 3   ? 18.662 -24.904 15.961 1.00 12.80  ? 9   ALA   C O   1 
ATOM   1111 C  CB  . ALA   B 1 3   ? 17.031 -22.069 15.296 1.00 14.81  ? 9   ALA   C CB  1 
ATOM   1112 N  N   . ILE   B 1 4   ? 18.616 -23.348 17.609 1.00 11.34  ? 10  ILE   C N   1 
ATOM   1113 C  CA  . ILE   B 1 4   ? 18.518 -24.277 18.750 1.00 11.55  ? 10  ILE   C CA  1 
ATOM   1114 C  C   . ILE   B 1 4   ? 17.113 -24.090 19.352 1.00 11.55  ? 10  ILE   C C   1 
ATOM   1115 O  O   . ILE   B 1 4   ? 16.676 -22.935 19.547 1.00 13.14  ? 10  ILE   C O   1 
ATOM   1116 C  CB  . ILE   B 1 4   ? 19.568 -23.955 19.815 1.00 11.47  ? 10  ILE   C CB  1 
ATOM   1117 C  CG1 . ILE   B 1 4   ? 20.996 -23.824 19.236 1.00 13.31  ? 10  ILE   C CG1 1 
ATOM   1118 C  CG2 . ILE   B 1 4   ? 19.511 -25.031 20.912 1.00 13.64  ? 10  ILE   C CG2 1 
ATOM   1119 C  CD1 . ILE   B 1 4   ? 21.967 -23.226 20.283 1.00 13.24  ? 10  ILE   C CD1 1 
ATOM   1120 N  N   . TYR   B 1 5   ? 16.407 -25.189 19.633 1.00 12.12  ? 11  TYR   C N   1 
ATOM   1121 C  CA  . TYR   B 1 5   ? 15.067 -25.129 20.217 1.00 12.87  ? 11  TYR   C CA  1 
ATOM   1122 C  C   . TYR   B 1 5   ? 15.143 -25.805 21.587 1.00 13.22  ? 11  TYR   C C   1 
ATOM   1123 O  O   . TYR   B 1 5   ? 15.236 -27.050 21.657 1.00 14.83  ? 11  TYR   C O   1 
ATOM   1124 C  CB  . TYR   B 1 5   ? 14.026 -25.843 19.308 1.00 13.77  ? 11  TYR   C CB  1 
ATOM   1125 C  CG  . TYR   B 1 5   ? 13.834 -25.081 18.010 1.00 13.82  ? 11  TYR   C CG  1 
ATOM   1126 C  CD1 . TYR   B 1 5   ? 12.999 -23.966 17.948 1.00 14.33  ? 11  TYR   C CD1 1 
ATOM   1127 C  CD2 . TYR   B 1 5   ? 14.537 -25.428 16.865 1.00 14.24  ? 11  TYR   C CD2 1 
ATOM   1128 C  CE1 . TYR   B 1 5   ? 12.871 -23.236 16.773 1.00 15.31  ? 11  TYR   C CE1 1 
ATOM   1129 C  CE2 . TYR   B 1 5   ? 14.412 -24.717 15.684 1.00 16.36  ? 11  TYR   C CE2 1 
ATOM   1130 C  CZ  . TYR   B 1 5   ? 13.584 -23.614 15.649 1.00 15.85  ? 11  TYR   C CZ  1 
ATOM   1131 O  OH  . TYR   B 1 5   ? 13.498 -22.851 14.504 1.00 18.31  ? 11  TYR   C OH  1 
ATOM   1132 N  N   . VAL   B 1 6   ? 15.167 -25.052 22.686 1.00 14.40  ? 12  VAL   C N   1 
ATOM   1133 C  CA  . VAL   B 1 6   ? 15.274 -25.600 24.059 1.00 14.65  ? 12  VAL   C CA  1 
ATOM   1134 C  C   . VAL   B 1 6   ? 14.142 -24.988 24.888 1.00 15.46  ? 12  VAL   C C   1 
ATOM   1135 O  O   . VAL   B 1 6   ? 13.961 -23.768 24.894 1.00 14.33  ? 12  VAL   C O   1 
ATOM   1136 C  CB  . VAL   B 1 6   ? 16.686 -25.329 24.648 1.00 16.54  ? 12  VAL   C CB  1 
ATOM   1137 C  CG1 . VAL   B 1 6   ? 17.042 -23.835 24.589 1.00 17.14  ? 12  VAL   C CG1 1 
ATOM   1138 C  CG2 . VAL   B 1 6   ? 16.764 -25.838 26.075 1.00 17.63  ? 12  VAL   C CG2 1 
ATOM   1139 N  N   . GLY   B 1 7   ? 13.321 -25.826 25.567 1.00 16.49  ? 13  GLY   C N   1 
ATOM   1140 C  CA  . GLY   B 1 7   ? 12.202 -25.292 26.343 1.00 16.87  ? 13  GLY   C CA  1 
ATOM   1141 C  C   . GLY   B 1 7   ? 11.263 -24.457 25.479 1.00 17.11  ? 13  GLY   C C   1 
ATOM   1142 O  O   . GLY   B 1 7   ? 10.993 -24.845 24.331 1.00 18.03  ? 13  GLY   C O   1 
ATOM   1143 N  N   . ASN   B 1 8   ? 10.935 -23.247 25.923 1.00 16.39  ? 14  ASN   C N   1 
ATOM   1144 C  CA  . ASN   B 1 8   ? 10.132 -22.346 25.078 1.00 16.54  ? 14  ASN   C CA  1 
ATOM   1145 C  C   . ASN   B 1 8   ? 11.003 -21.239 24.503 1.00 15.24  ? 14  ASN   C C   1 
ATOM   1146 O  O   . ASN   B 1 8   ? 10.535 -20.101 24.337 1.00 14.99  ? 14  ASN   C O   1 
ATOM   1147 C  CB  . ASN   B 1 8   ? 8.895  -21.772 25.821 1.00 19.11  ? 14  ASN   C CB  1 
ATOM   1148 C  CG  . ASN   B 1 8   ? 7.816  -22.836 25.963 1.00 25.21  ? 14  ASN   C CG  1 
ATOM   1149 O  OD1 . ASN   B 1 8   ? 6.960  -22.989 25.092 1.00 27.69  ? 14  ASN   C OD1 1 
ATOM   1150 N  ND2 . ASN   B 1 8   ? 7.909  -23.644 27.000 1.00 28.72  ? 14  ASN   C ND2 1 
ATOM   1151 N  N   . TYR   B 1 9   ? 12.229 -21.605 24.105 1.00 13.25  ? 15  TYR   C N   1 
ATOM   1152 C  CA  . TYR   B 1 9   ? 13.195 -20.647 23.515 1.00 12.99  ? 15  TYR   C CA  1 
ATOM   1153 C  C   . TYR   B 1 9   ? 13.655 -21.121 22.146 1.00 12.56  ? 15  TYR   C C   1 
ATOM   1154 O  O   . TYR   B 1 9   ? 13.840 -22.329 21.925 1.00 13.51  ? 15  TYR   C O   1 
ATOM   1155 C  CB  . TYR   B 1 9   ? 14.437 -20.474 24.425 1.00 13.87  ? 15  TYR   C CB  1 
ATOM   1156 C  CG  . TYR   B 1 9   ? 14.113 -19.950 25.816 1.00 14.46  ? 15  TYR   C CG  1 
ATOM   1157 C  CD1 . TYR   B 1 9   ? 13.536 -18.695 25.991 1.00 16.76  ? 15  TYR   C CD1 1 
ATOM   1158 C  CD2 . TYR   B 1 9   ? 14.430 -20.691 26.952 1.00 16.43  ? 15  TYR   C CD2 1 
ATOM   1159 C  CE1 . TYR   B 1 9   ? 13.249 -18.208 27.267 1.00 19.94  ? 15  TYR   C CE1 1 
ATOM   1160 C  CE2 . TYR   B 1 9   ? 14.164 -20.198 28.235 1.00 19.32  ? 15  TYR   C CE2 1 
ATOM   1161 C  CZ  . TYR   B 1 9   ? 13.591 -18.952 28.374 1.00 21.80  ? 15  TYR   C CZ  1 
ATOM   1162 O  OH  . TYR   B 1 9   ? 13.279 -18.413 29.616 1.00 27.76  ? 15  TYR   C OH  1 
ATOM   1163 N  N   . ARG   B 1 10  ? 13.895 -20.166 21.251 1.00 12.02  ? 16  ARG   C N   1 
ATOM   1164 C  CA  . ARG   B 1 10  ? 14.527 -20.384 19.942 1.00 11.78  ? 16  ARG   C CA  1 
ATOM   1165 C  C   . ARG   B 1 10  ? 15.790 -19.510 19.944 1.00 11.99  ? 16  ARG   C C   1 
ATOM   1166 O  O   . ARG   B 1 10  ? 15.703 -18.292 20.160 1.00 12.15  ? 16  ARG   C O   1 
ATOM   1167 C  CB  . ARG   B 1 10  ? 13.564 -19.964 18.813 1.00 13.07  ? 16  ARG   C CB  1 
ATOM   1168 C  CG  . ARG   B 1 10  ? 14.207 -19.780 17.428 1.00 13.80  ? 16  ARG   C CG  1 
ATOM   1169 C  CD  . ARG   B 1 10  ? 13.129 -19.466 16.384 1.00 13.60  ? 16  ARG   C CD  1 
ATOM   1170 N  NE  . ARG   B 1 10  ? 13.544 -18.533 15.341 1.00 14.48  ? 16  ARG   C NE  1 
ATOM   1171 C  CZ  . ARG   B 1 10  ? 14.065 -18.835 14.144 1.00 16.01  ? 16  ARG   C CZ  1 
ATOM   1172 N  NH1 . ARG   B 1 10  ? 14.282 -20.117 13.798 1.00 17.92  ? 16  ARG   C NH1 1 
ATOM   1173 N  NH2 . ARG   B 1 10  ? 14.420 -17.860 13.299 1.00 16.74  ? 16  ARG   C NH2 1 
ATOM   1174 N  N   . VAL   B 1 11  ? 16.960 -20.099 19.690 1.00 11.39  ? 17  VAL   C N   1 
ATOM   1175 C  CA  . VAL   B 1 11  ? 18.249 -19.391 19.665 1.00 11.05  ? 17  VAL   C CA  1 
ATOM   1176 C  C   . VAL   B 1 11  ? 18.720 -19.337 18.249 1.00 10.99  ? 17  VAL   C C   1 
ATOM   1177 O  O   . VAL   B 1 11  ? 18.889 -20.404 17.595 1.00 11.49  ? 17  VAL   C O   1 
ATOM   1178 C  CB  . VAL   B 1 11  ? 19.307 -20.120 20.531 1.00 11.92  ? 17  VAL   C CB  1 
ATOM   1179 C  CG1 . VAL   B 1 11  ? 20.561 -19.263 20.632 1.00 13.79  ? 17  VAL   C CG1 1 
ATOM   1180 C  CG2 . VAL   B 1 11  ? 18.764 -20.483 21.922 1.00 13.74  ? 17  VAL   C CG2 1 
ATOM   1181 N  N   . VAL   B 1 12  ? 18.975 -18.123 17.713 1.00 10.77  ? 18  VAL   C N   1 
ATOM   1182 C  CA  A VAL   B 1 12  ? 19.440 -17.968 16.324 0.50 10.89  ? 18  VAL   C CA  1 
ATOM   1183 C  CA  B VAL   B 1 12  ? 19.382 -17.974 16.318 0.50 12.19  ? 18  VAL   C CA  1 
ATOM   1184 C  C   . VAL   B 1 12  ? 20.568 -16.952 16.259 1.00 11.25  ? 18  VAL   C C   1 
ATOM   1185 O  O   . VAL   B 1 12  ? 20.819 -16.190 17.225 1.00 11.47  ? 18  VAL   C O   1 
ATOM   1186 C  CB  A VAL   B 1 12  ? 18.289 -17.445 15.401 0.50 11.01  ? 18  VAL   C CB  1 
ATOM   1187 C  CB  B VAL   B 1 12  ? 18.105 -17.430 15.546 0.50 15.01  ? 18  VAL   C CB  1 
ATOM   1188 C  CG1 A VAL   B 1 12  ? 17.282 -18.552 15.163 0.50 10.75  ? 18  VAL   C CG1 1 
ATOM   1189 C  CG1 B VAL   B 1 12  ? 17.700 -16.031 15.988 0.50 15.16  ? 18  VAL   C CG1 1 
ATOM   1190 C  CG2 A VAL   B 1 12  ? 17.630 -16.165 15.959 0.50 10.64  ? 18  VAL   C CG2 1 
ATOM   1191 C  CG2 B VAL   B 1 12  ? 18.248 -17.480 14.042 0.50 16.56  ? 18  VAL   C CG2 1 
ATOM   1192 N  N   . ASN   B 1 13  ? 21.274 -16.896 15.120 1.00 10.92  ? 19  ASN   C N   1 
ATOM   1193 C  CA  . ASN   B 1 13  ? 22.257 -15.833 14.922 1.00 10.79  ? 19  ASN   C CA  1 
ATOM   1194 C  C   . ASN   B 1 13  ? 21.448 -14.487 14.862 1.00 11.03  ? 19  ASN   C C   1 
ATOM   1195 O  O   . ASN   B 1 13  ? 20.431 -14.409 14.162 1.00 10.98  ? 19  ASN   C O   1 
ATOM   1196 C  CB  . ASN   B 1 13  ? 22.972 -15.976 13.559 1.00 11.71  ? 19  ASN   C CB  1 
ATOM   1197 C  CG  . ASN   B 1 13  ? 23.827 -17.240 13.481 1.00 10.70  ? 19  ASN   C CG  1 
ATOM   1198 O  OD1 . ASN   B 1 13  ? 23.359 -18.313 13.050 1.00 11.70  ? 19  ASN   C OD1 1 
ATOM   1199 N  ND2 . ASN   B 1 13  ? 25.072 -17.133 13.939 1.00 12.27  ? 19  ASN   C ND2 1 
ATOM   1200 N  N   . ARG   B 1 14  ? 21.945 -13.466 15.569 1.00 11.19  ? 20  ARG   C N   1 
ATOM   1201 C  CA  . ARG   B 1 14  ? 21.218 -12.173 15.581 1.00 11.05  ? 20  ARG   C CA  1 
ATOM   1202 C  C   . ARG   B 1 14  ? 21.055 -11.634 14.145 1.00 11.90  ? 20  ARG   C C   1 
ATOM   1203 O  O   . ARG   B 1 14  ? 19.972 -11.105 13.800 1.00 12.63  ? 20  ARG   C O   1 
ATOM   1204 C  CB  . ARG   B 1 14  ? 21.972 -11.170 16.435 1.00 11.19  ? 20  ARG   C CB  1 
ATOM   1205 C  CG  . ARG   B 1 14  ? 21.166 -9.836  16.662 1.00 11.69  ? 20  ARG   C CG  1 
ATOM   1206 C  CD  . ARG   B 1 14  ? 22.037 -8.876  17.432 1.00 12.28  ? 20  ARG   C CD  1 
ATOM   1207 N  NE  . ARG   B 1 14  ? 21.346 -7.628  17.880 1.00 12.77  ? 20  ARG   C NE  1 
ATOM   1208 C  CZ  . ARG   B 1 14  ? 21.232 -6.538  17.136 1.00 12.60  ? 20  ARG   C CZ  1 
ATOM   1209 N  NH1 . ARG   B 1 14  ? 21.649 -6.539  15.871 1.00 14.44  ? 20  ARG   C NH1 1 
ATOM   1210 N  NH2 . ARG   B 1 14  ? 20.738 -5.422  17.662 1.00 13.70  ? 20  ARG   C NH2 1 
ATOM   1211 N  N   . HIS   B 1 15  ? 22.084 -11.831 13.287 1.00 11.27  ? 21  HIS   C N   1 
ATOM   1212 C  CA  . HIS   B 1 15  ? 21.991 -11.300 11.924 1.00 12.11  ? 21  HIS   C CA  1 
ATOM   1213 C  C   . HIS   B 1 15  ? 20.976 -12.025 11.029 1.00 13.20  ? 21  HIS   C C   1 
ATOM   1214 O  O   . HIS   B 1 15  ? 20.689 -11.517 9.944  1.00 15.36  ? 21  HIS   C O   1 
ATOM   1215 C  CB  . HIS   B 1 15  ? 23.377 -11.196 11.238 1.00 13.46  ? 21  HIS   C CB  1 
ATOM   1216 C  CG  . HIS   B 1 15  ? 23.977 -12.518 10.808 1.00 12.61  ? 21  HIS   C CG  1 
ATOM   1217 N  ND1 . HIS   B 1 15  ? 24.697 -13.338 11.694 1.00 13.29  ? 21  HIS   C ND1 1 
ATOM   1218 C  CD2 . HIS   B 1 15  ? 23.999 -13.093 9.574  1.00 13.59  ? 21  HIS   C CD2 1 
ATOM   1219 C  CE1 . HIS   B 1 15  ? 25.098 -14.397 10.969 1.00 14.55  ? 21  HIS   C CE1 1 
ATOM   1220 N  NE2 . HIS   B 1 15  ? 24.713 -14.283 9.695  1.00 13.56  ? 21  HIS   C NE2 1 
ATOM   1221 N  N   . LEU   B 1 16  ? 20.462 -13.184 11.465 1.00 12.19  ? 22  LEU   C N   1 
ATOM   1222 C  CA  . LEU   B 1 16  ? 19.454 -13.959 10.722 1.00 13.64  ? 22  LEU   C CA  1 
ATOM   1223 C  C   . LEU   B 1 16  ? 18.061 -13.900 11.390 1.00 14.04  ? 22  LEU   C C   1 
ATOM   1224 O  O   . LEU   B 1 16  ? 17.131 -14.601 10.954 1.00 14.61  ? 22  LEU   C O   1 
ATOM   1225 C  CB  . LEU   B 1 16  ? 19.927 -15.413 10.527 1.00 13.16  ? 22  LEU   C CB  1 
ATOM   1226 C  CG  . LEU   B 1 16  ? 21.220 -15.546 9.716  1.00 13.55  ? 22  LEU   C CG  1 
ATOM   1227 C  CD1 . LEU   B 1 16  ? 21.649 -17.011 9.637  1.00 14.58  ? 22  LEU   C CD1 1 
ATOM   1228 C  CD2 . LEU   B 1 16  ? 21.101 -14.925 8.329  1.00 14.45  ? 22  LEU   C CD2 1 
ATOM   1229 N  N   . ALA   B 1 17  ? 17.901 -13.129 12.494 1.00 13.72  ? 23  ALA   C N   1 
ATOM   1230 C  CA  . ALA   B 1 17  ? 16.619 -13.072 13.206 1.00 13.07  ? 23  ALA   C CA  1 
ATOM   1231 C  C   . ALA   B 1 17  ? 15.511 -12.519 12.319 1.00 14.18  ? 23  ALA   C C   1 
ATOM   1232 O  O   . ALA   B 1 17  ? 15.740 -11.581 11.528 1.00 15.63  ? 23  ALA   C O   1 
ATOM   1233 C  CB  . ALA   B 1 17  ? 16.766 -12.207 14.471 1.00 14.68  ? 23  ALA   C CB  1 
ATOM   1234 N  N   . THR   B 1 18  ? 14.322 -13.066 12.484 1.00 14.69  ? 24  THR   C N   1 
ATOM   1235 C  CA  . THR   B 1 18  ? 13.176 -12.639 11.697 1.00 15.17  ? 24  THR   C CA  1 
ATOM   1236 C  C   . THR   B 1 18  ? 12.352 -11.589 12.479 1.00 14.45  ? 24  THR   C C   1 
ATOM   1237 O  O   . THR   B 1 18  ? 12.582 -11.294 13.657 1.00 15.12  ? 24  THR   C O   1 
ATOM   1238 C  CB  . THR   B 1 18  ? 12.258 -13.867 11.427 1.00 16.25  ? 24  THR   C CB  1 
ATOM   1239 O  OG1 . THR   B 1 18  ? 11.719 -14.294 12.664 1.00 16.68  ? 24  THR   C OG1 1 
ATOM   1240 C  CG2 . THR   B 1 18  ? 12.981 -15.039 10.703 1.00 17.78  ? 24  THR   C CG2 1 
ATOM   1241 N  N   . HIS   B 1 19  ? 11.345 -10.973 11.786 1.00 15.84  ? 25  HIS   C N   1 
ATOM   1242 C  CA  . HIS   B 1 19  ? 10.418 -10.064 12.477 1.00 16.30  ? 25  HIS   C CA  1 
ATOM   1243 C  C   . HIS   B 1 19  ? 9.719  -10.824 13.608 1.00 14.15  ? 25  HIS   C C   1 
ATOM   1244 O  O   . HIS   B 1 19  ? 9.630  -10.260 14.703 1.00 16.12  ? 25  HIS   C O   1 
ATOM   1245 C  CB  . HIS   B 1 19  ? 9.322  -9.525  11.524 1.00 18.56  ? 25  HIS   C CB  1 
ATOM   1246 C  CG  . HIS   B 1 19  ? 8.190  -8.835  12.253 1.00 18.32  ? 25  HIS   C CG  1 
ATOM   1247 N  ND1 . HIS   B 1 19  ? 8.340  -7.582  12.827 1.00 20.58  ? 25  HIS   C ND1 1 
ATOM   1248 C  CD2 . HIS   B 1 19  ? 6.984  -9.327  12.600 1.00 20.04  ? 25  HIS   C CD2 1 
ATOM   1249 C  CE1 . HIS   B 1 19  ? 7.163  -7.291  13.376 1.00 20.81  ? 25  HIS   C CE1 1 
ATOM   1250 N  NE2 . HIS   B 1 19  ? 6.329  -8.330  13.300 1.00 20.54  ? 25  HIS   C NE2 1 
ATOM   1251 N  N   . ASN   B 1 20  ? 9.296  -12.090 13.394 1.00 15.13  ? 26  ASN   C N   1 
ATOM   1252 C  CA  . ASN   B 1 20  ? 8.661  -12.821 14.482 1.00 16.13  ? 26  ASN   C CA  1 
ATOM   1253 C  C   . ASN   B 1 20  ? 9.574  -13.002 15.680 1.00 14.36  ? 26  ASN   C C   1 
ATOM   1254 O  O   . ASN   B 1 20  ? 9.162  -12.909 16.832 1.00 14.67  ? 26  ASN   C O   1 
ATOM   1255 C  CB  . ASN   B 1 20  ? 8.118  -14.180 14.028 1.00 18.39  ? 26  ASN   C CB  1 
ATOM   1256 C  CG  . ASN   B 1 20  ? 7.296  -14.861 15.118 1.00 24.40  ? 26  ASN   C CG  1 
ATOM   1257 O  OD1 . ASN   B 1 20  ? 6.160  -14.434 15.425 1.00 28.15  ? 26  ASN   C OD1 1 
ATOM   1258 N  ND2 . ASN   B 1 20  ? 7.837  -15.903 15.750 1.00 26.44  ? 26  ASN   C ND2 1 
ATOM   1259 N  N   . ASP   B 1 21  ? 10.901 -13.221 15.413 1.00 13.74  ? 27  ASP   C N   1 
ATOM   1260 C  CA  . ASP   B 1 21  ? 11.837 -13.308 16.520 1.00 13.22  ? 27  ASP   C CA  1 
ATOM   1261 C  C   . ASP   B 1 21  ? 11.899 -12.006 17.336 1.00 12.90  ? 27  ASP   C C   1 
ATOM   1262 O  O   . ASP   B 1 21  ? 11.835 -12.016 18.562 1.00 14.40  ? 27  ASP   C O   1 
ATOM   1263 C  CB  . ASP   B 1 21  ? 13.247 -13.615 16.004 1.00 13.53  ? 27  ASP   C CB  1 
ATOM   1264 C  CG  . ASP   B 1 21  ? 13.462 -15.036 15.521 1.00 14.47  ? 27  ASP   C CG  1 
ATOM   1265 O  OD1 . ASP   B 1 21  ? 12.885 -15.964 16.129 1.00 15.42  ? 27  ASP   C OD1 1 
ATOM   1266 O  OD2 . ASP   B 1 21  ? 14.171 -15.211 14.492 1.00 14.70  ? 27  ASP   C OD2 1 
ATOM   1267 N  N   . TRP   B 1 22  ? 11.990 -10.841 16.631 1.00 13.63  ? 28  TRP   C N   1 
ATOM   1268 C  CA  . TRP   B 1 22  ? 12.040 -9.554  17.315 1.00 13.95  ? 28  TRP   C CA  1 
ATOM   1269 C  C   . TRP   B 1 22  ? 10.706 -9.224  18.044 1.00 13.28  ? 28  TRP   C C   1 
ATOM   1270 O  O   . TRP   B 1 22  ? 10.731 -8.600  19.114 1.00 14.61  ? 28  TRP   C O   1 
ATOM   1271 C  CB  . TRP   B 1 22  ? 12.436 -8.427  16.351 1.00 14.30  ? 28  TRP   C CB  1 
ATOM   1272 C  CG  . TRP   B 1 22  ? 13.921 -8.370  16.080 1.00 14.17  ? 28  TRP   C CG  1 
ATOM   1273 C  CD1 . TRP   B 1 22  ? 14.585 -8.904  15.019 1.00 15.68  ? 28  TRP   C CD1 1 
ATOM   1274 C  CD2 . TRP   B 1 22  ? 14.927 -7.820  16.951 1.00 12.66  ? 28  TRP   C CD2 1 
ATOM   1275 N  NE1 . TRP   B 1 22  ? 15.940 -8.619  15.118 1.00 14.66  ? 28  TRP   C NE1 1 
ATOM   1276 C  CE2 . TRP   B 1 22  ? 16.162 -7.917  16.283 1.00 14.04  ? 28  TRP   C CE2 1 
ATOM   1277 C  CE3 . TRP   B 1 22  ? 14.875 -7.086  18.149 1.00 15.84  ? 28  TRP   C CE3 1 
ATOM   1278 C  CZ2 . TRP   B 1 22  ? 17.343 -7.405  16.809 1.00 14.15  ? 28  TRP   C CZ2 1 
ATOM   1279 C  CZ3 . TRP   B 1 22  ? 16.052 -6.573  18.661 1.00 16.63  ? 28  TRP   C CZ3 1 
ATOM   1280 C  CH2 . TRP   B 1 22  ? 17.268 -6.746  17.993 1.00 16.34  ? 28  TRP   C CH2 1 
ATOM   1281 N  N   . ALA   B 1 23  ? 9.592  -9.679  17.481 1.00 14.21  ? 29  ALA   C N   1 
ATOM   1282 C  CA  . ALA   B 1 23  ? 8.271  -9.445  18.092 1.00 14.51  ? 29  ALA   C CA  1 
ATOM   1283 C  C   . ALA   B 1 23  ? 8.009  -10.321 19.314 1.00 16.27  ? 29  ALA   C C   1 
ATOM   1284 O  O   . ALA   B 1 23  ? 7.022  -10.116 20.022 1.00 17.00  ? 29  ALA   C O   1 
ATOM   1285 C  CB  . ALA   B 1 23  ? 7.181  -9.697  17.065 1.00 16.37  ? 29  ALA   C CB  1 
ATOM   1286 N  N   . ASN   B 1 24  ? 8.840  -11.378 19.535 1.00 16.21  ? 30  ASN   C N   1 
ATOM   1287 C  CA  . ASN   B 1 24  ? 8.756  -12.305 20.672 1.00 15.02  ? 30  ASN   C CA  1 
ATOM   1288 C  C   . ASN   B 1 24  ? 10.134 -12.348 21.353 1.00 15.15  ? 30  ASN   C C   1 
ATOM   1289 O  O   . ASN   B 1 24  ? 10.565 -13.418 21.799 1.00 14.76  ? 30  ASN   C O   1 
ATOM   1290 C  CB  . ASN   B 1 24  ? 8.300  -13.681 20.152 1.00 16.54  ? 30  ASN   C CB  1 
ATOM   1291 C  CG  . ASN   B 1 24  ? 6.892  -13.625 19.673 1.00 17.69  ? 30  ASN   C CG  1 
ATOM   1292 O  OD1 . ASN   B 1 24  ? 5.930  -13.636 20.494 1.00 19.69  ? 30  ASN   C OD1 1 
ATOM   1293 N  ND2 . ASN   B 1 24  ? 6.701  -13.484 18.381 1.00 18.59  ? 30  ASN   C ND2 1 
ATOM   1294 N  N   . LEU   B 1 25  ? 10.832 -11.222 21.441 1.00 15.62  ? 31  LEU   C N   1 
ATOM   1295 C  CA  . LEU   B 1 25  ? 12.207 -11.196 21.935 1.00 14.27  ? 31  LEU   C CA  1 
ATOM   1296 C  C   . LEU   B 1 25  ? 12.340 -11.534 23.414 1.00 16.55  ? 31  LEU   C C   1 
ATOM   1297 O  O   . LEU   B 1 25  ? 11.581 -11.024 24.244 1.00 17.21  ? 31  LEU   C O   1 
ATOM   1298 C  CB  . LEU   B 1 25  ? 12.765 -9.793  21.674 1.00 15.26  ? 31  LEU   C CB  1 
ATOM   1299 C  CG  . LEU   B 1 25  ? 14.231 -9.625  22.045 1.00 15.45  ? 31  LEU   C CG  1 
ATOM   1300 C  CD1 . LEU   B 1 25  ? 15.142 -10.487 21.141 1.00 15.61  ? 31  LEU   C CD1 1 
ATOM   1301 C  CD2 . LEU   B 1 25  ? 14.636 -8.163  21.938 1.00 18.03  ? 31  LEU   C CD2 1 
ATOM   1302 N  N   . VAL   B 1 26  ? 13.332 -12.351 23.759 1.00 14.56  ? 32  VAL   C N   1 
ATOM   1303 C  CA  . VAL   B 1 26  ? 13.686 -12.633 25.152 1.00 15.16  ? 32  VAL   C CA  1 
ATOM   1304 C  C   . VAL   B 1 26  ? 15.003 -11.920 25.475 1.00 15.47  ? 32  VAL   C C   1 
ATOM   1305 O  O   . VAL   B 1 26  ? 15.121 -11.264 26.514 1.00 17.05  ? 32  VAL   C O   1 
ATOM   1306 C  CB  . VAL   B 1 26  ? 13.813 -14.143 25.378 1.00 15.64  ? 32  VAL   C CB  1 
ATOM   1307 C  CG1 . VAL   B 1 26  ? 14.392 -14.462 26.764 1.00 17.63  ? 32  VAL   C CG1 1 
ATOM   1308 C  CG2 . VAL   B 1 26  ? 12.469 -14.831 25.181 1.00 16.44  ? 32  VAL   C CG2 1 
ATOM   1309 N  N   . TRP   B 1 27  ? 16.024 -12.030 24.591 1.00 14.25  ? 33  TRP   C N   1 
ATOM   1310 C  CA  . TRP   B 1 27  ? 17.352 -11.472 24.873 1.00 14.44  ? 33  TRP   C CA  1 
ATOM   1311 C  C   . TRP   B 1 27  ? 18.141 -11.391 23.555 1.00 13.70  ? 33  TRP   C C   1 
ATOM   1312 O  O   . TRP   B 1 27  ? 17.961 -12.273 22.698 1.00 13.94  ? 33  TRP   C O   1 
ATOM   1313 C  CB  . TRP   B 1 27  ? 18.099 -12.362 25.922 1.00 15.83  ? 33  TRP   C CB  1 
ATOM   1314 C  CG  . TRP   B 1 27  ? 19.568 -12.099 26.104 1.00 16.23  ? 33  TRP   C CG  1 
ATOM   1315 C  CD1 . TRP   B 1 27  ? 20.147 -11.133 26.884 1.00 18.08  ? 33  TRP   C CD1 1 
ATOM   1316 C  CD2 . TRP   B 1 27  ? 20.649 -12.770 25.440 1.00 14.55  ? 33  TRP   C CD2 1 
ATOM   1317 N  NE1 . TRP   B 1 27  ? 21.522 -11.210 26.801 1.00 19.15  ? 33  TRP   C NE1 1 
ATOM   1318 C  CE2 . TRP   B 1 27  ? 21.856 -12.240 25.948 1.00 16.57  ? 33  TRP   C CE2 1 
ATOM   1319 C  CE3 . TRP   B 1 27  ? 20.720 -13.831 24.514 1.00 14.65  ? 33  TRP   C CE3 1 
ATOM   1320 C  CZ2 . TRP   B 1 27  ? 23.118 -12.729 25.557 1.00 16.69  ? 33  TRP   C CZ2 1 
ATOM   1321 C  CZ3 . TRP   B 1 27  ? 21.972 -14.317 24.150 1.00 15.71  ? 33  TRP   C CZ3 1 
ATOM   1322 C  CH2 . TRP   B 1 27  ? 23.144 -13.722 24.610 1.00 15.78  ? 33  TRP   C CH2 1 
ATOM   1323 N  N   . GLU   B 1 28  ? 18.993 -10.409 23.397 1.00 13.48  ? 34  GLU   C N   1 
ATOM   1324 C  CA  . GLU   B 1 28  ? 19.831 -10.304 22.212 1.00 14.89  ? 34  GLU   C CA  1 
ATOM   1325 C  C   . GLU   B 1 28  ? 21.119 -9.629  22.573 1.00 14.05  ? 34  GLU   C C   1 
ATOM   1326 O  O   . GLU   B 1 28  ? 21.148 -8.737  23.475 1.00 14.32  ? 34  GLU   C O   1 
ATOM   1327 C  CB  . GLU   B 1 28  ? 19.126 -9.633  21.030 1.00 15.81  ? 34  GLU   C CB  1 
ATOM   1328 C  CG  . GLU   B 1 28  ? 18.577 -8.243  21.301 1.00 16.48  ? 34  GLU   C CG  1 
ATOM   1329 C  CD  . GLU   B 1 28  ? 19.563 -7.095  21.242 1.00 17.78  ? 34  GLU   C CD  1 
ATOM   1330 O  OE1 . GLU   B 1 28  ? 19.293 -6.060  21.901 1.00 21.02  ? 34  GLU   C OE1 1 
ATOM   1331 O  OE2 . GLU   B 1 28  ? 20.580 -7.172  20.508 1.00 16.75  ? 34  GLU   C OE2 1 
ATOM   1332 N  N   . ASP   B 1 29  ? 22.205 -9.986  21.859 1.00 13.41  ? 35  ASP   C N   1 
ATOM   1333 C  CA  . ASP   B 1 29  ? 23.505 -9.354  22.086 1.00 13.49  ? 35  ASP   C CA  1 
ATOM   1334 C  C   . ASP   B 1 29  ? 24.278 -9.301  20.770 1.00 13.53  ? 35  ASP   C C   1 
ATOM   1335 O  O   . ASP   B 1 29  ? 24.721 -10.353 20.271 1.00 12.95  ? 35  ASP   C O   1 
ATOM   1336 C  CB  . ASP   B 1 29  ? 24.232 -10.120 23.198 1.00 15.33  ? 35  ASP   C CB  1 
ATOM   1337 C  CG  . ASP   B 1 29  ? 25.585 -9.588  23.591 1.00 18.15  ? 35  ASP   C CG  1 
ATOM   1338 O  OD1 . ASP   B 1 29  ? 26.322 -9.136  22.706 1.00 18.66  ? 35  ASP   C OD1 1 
ATOM   1339 O  OD2 . ASP   B 1 29  ? 25.961 -9.728  24.775 1.00 22.19  ? 35  ASP   C OD2 1 
ATOM   1340 N  N   . SER   B 1 30  ? 24.446 -8.088  20.194 1.00 13.79  ? 36  SER   C N   1 
ATOM   1341 C  CA  A SER   B 1 30  ? 25.166 -7.908  18.934 0.50 14.42  ? 36  SER   C CA  1 
ATOM   1342 C  CA  B SER   B 1 30  ? 25.131 -7.982  18.926 0.50 15.01  ? 36  SER   C CA  1 
ATOM   1343 C  C   . SER   B 1 30  ? 26.611 -8.373  19.016 1.00 14.55  ? 36  SER   C C   1 
ATOM   1344 O  O   . SER   B 1 30  ? 27.110 -8.993  18.065 1.00 14.30  ? 36  SER   C O   1 
ATOM   1345 C  CB  A SER   B 1 30  ? 25.159 -6.442  18.507 0.50 14.71  ? 36  SER   C CB  1 
ATOM   1346 C  CB  B SER   B 1 30  ? 24.951 -6.595  18.337 0.50 17.16  ? 36  SER   C CB  1 
ATOM   1347 O  OG  A SER   B 1 30  ? 26.076 -6.199  17.444 0.50 15.71  ? 36  SER   C OG  1 
ATOM   1348 O  OG  B SER   B 1 30  ? 25.422 -5.619  19.245 0.50 19.60  ? 36  SER   C OG  1 
ATOM   1349 N  N   . SER   B 1 31  ? 27.274 -8.115  20.150 1.00 14.06  ? 37  SER   C N   1 
ATOM   1350 C  CA  . SER   B 1 31  ? 28.681 -8.509  20.272 1.00 14.73  ? 37  SER   C CA  1 
ATOM   1351 C  C   . SER   B 1 31  ? 28.862 -10.026 20.225 1.00 14.09  ? 37  SER   C C   1 
ATOM   1352 O  O   . SER   B 1 31  ? 29.952 -10.470 19.844 1.00 15.10  ? 37  SER   C O   1 
ATOM   1353 C  CB  . SER   B 1 31  ? 29.306 -7.962  21.540 1.00 18.16  ? 37  SER   C CB  1 
ATOM   1354 O  OG  . SER   B 1 31  ? 28.947 -8.669  22.708 1.00 23.55  ? 37  SER   C OG  1 
ATOM   1355 N  N   . ARG   B 1 32  ? 27.814 -10.815 20.561 1.00 13.08  ? 38  ARG   C N   1 
ATOM   1356 C  CA  . ARG   B 1 32  ? 27.888 -12.274 20.494 1.00 12.36  ? 38  ARG   C CA  1 
ATOM   1357 C  C   . ARG   B 1 32  ? 27.255 -12.843 19.219 1.00 11.78  ? 38  ARG   C C   1 
ATOM   1358 O  O   . ARG   B 1 32  ? 27.318 -14.063 19.002 1.00 11.88  ? 38  ARG   C O   1 
ATOM   1359 C  CB  . ARG   B 1 32  ? 27.152 -12.873 21.724 1.00 14.65  ? 38  ARG   C CB  1 
ATOM   1360 C  CG  . ARG   B 1 32  ? 27.833 -12.526 23.047 1.00 15.11  ? 38  ARG   C CG  1 
ATOM   1361 C  CD  . ARG   B 1 32  ? 27.064 -13.075 24.238 1.00 13.10  ? 38  ARG   C CD  1 
ATOM   1362 N  NE  . ARG   B 1 32  ? 27.132 -14.558 24.273 1.00 12.86  ? 38  ARG   C NE  1 
ATOM   1363 C  CZ  . ARG   B 1 32  ? 27.098 -15.301 25.396 1.00 12.52  ? 38  ARG   C CZ  1 
ATOM   1364 N  NH1 . ARG   B 1 32  ? 26.969 -14.726 26.580 1.00 14.41  ? 38  ARG   C NH1 1 
ATOM   1365 N  NH2 . ARG   B 1 32  ? 27.236 -16.624 25.331 1.00 13.54  ? 38  ARG   C NH2 1 
ATOM   1366 N  N   . ASP   B 1 33  ? 26.593 -12.012 18.413 1.00 11.52  ? 39  ASP   C N   1 
ATOM   1367 C  CA  . ASP   B 1 33  ? 25.801 -12.452 17.278 1.00 11.30  ? 39  ASP   C CA  1 
ATOM   1368 C  C   . ASP   B 1 33  ? 24.711 -13.445 17.713 1.00 11.22  ? 39  ASP   C C   1 
ATOM   1369 O  O   . ASP   B 1 33  ? 24.423 -14.389 16.947 1.00 11.72  ? 39  ASP   C O   1 
ATOM   1370 C  CB  . ASP   B 1 33  ? 26.662 -13.076 16.155 1.00 12.07  ? 39  ASP   C CB  1 
ATOM   1371 C  CG  . ASP   B 1 33  ? 25.862 -13.402 14.883 1.00 12.94  ? 39  ASP   C CG  1 
ATOM   1372 O  OD1 . ASP   B 1 33  ? 24.974 -12.616 14.497 1.00 13.43  ? 39  ASP   C OD1 1 
ATOM   1373 O  OD2 . ASP   B 1 33  ? 26.182 -14.420 14.219 1.00 12.29  ? 39  ASP   C OD2 1 
ATOM   1374 N  N   . LEU   B 1 34  ? 24.047 -13.227 18.860 1.00 10.47  ? 40  LEU   C N   1 
ATOM   1375 C  CA  . LEU   B 1 34  ? 22.967 -14.128 19.292 1.00 11.15  ? 40  LEU   C CA  1 
ATOM   1376 C  C   . LEU   B 1 34  ? 21.658 -13.376 19.548 1.00 11.03  ? 40  LEU   C C   1 
ATOM   1377 O  O   . LEU   B 1 34  ? 21.676 -12.213 20.010 1.00 11.74  ? 40  LEU   C O   1 
ATOM   1378 C  CB  . LEU   B 1 34  ? 23.358 -14.827 20.595 1.00 12.37  ? 40  LEU   C CB  1 
ATOM   1379 C  CG  . LEU   B 1 34  ? 24.433 -15.943 20.499 1.00 12.19  ? 40  LEU   C CG  1 
ATOM   1380 C  CD1 . LEU   B 1 34  ? 24.680 -16.521 21.922 1.00 13.84  ? 40  LEU   C CD1 1 
ATOM   1381 C  CD2 . LEU   B 1 34  ? 24.006 -17.049 19.542 1.00 12.61  ? 40  LEU   C CD2 1 
ATOM   1382 N  N   . LEU   B 1 35  ? 20.563 -14.051 19.324 1.00 10.47  ? 41  LEU   C N   1 
ATOM   1383 C  CA  . LEU   B 1 35  ? 19.239 -13.550 19.691 1.00 11.68  ? 41  LEU   C CA  1 
ATOM   1384 C  C   . LEU   B 1 35  ? 18.409 -14.760 20.087 1.00 11.32  ? 41  LEU   C C   1 
ATOM   1385 O  O   . LEU   B 1 35  ? 18.502 -15.831 19.457 1.00 11.55  ? 41  LEU   C O   1 
ATOM   1386 C  CB  . LEU   B 1 35  ? 18.587 -12.819 18.480 1.00 12.48  ? 41  LEU   C CB  1 
ATOM   1387 C  CG  . LEU   B 1 35  ? 17.209 -12.218 18.743 1.00 12.13  ? 41  LEU   C CG  1 
ATOM   1388 C  CD1 . LEU   B 1 35  ? 17.022 -10.927 17.962 1.00 14.04  ? 41  LEU   C CD1 1 
ATOM   1389 C  CD2 . LEU   B 1 35  ? 16.100 -13.235 18.370 1.00 13.66  ? 41  LEU   C CD2 1 
ATOM   1390 N  N   . VAL   B 1 36  ? 17.615 -14.586 21.141 1.00 11.62  ? 42  VAL   C N   1 
ATOM   1391 C  CA  . VAL   B 1 36  ? 16.703 -15.606 21.661 1.00 11.65  ? 42  VAL   C CA  1 
ATOM   1392 C  C   . VAL   B 1 36  ? 15.285 -15.086 21.648 1.00 11.44  ? 42  VAL   C C   1 
ATOM   1393 O  O   . VAL   B 1 36  ? 15.060 -13.956 22.149 1.00 12.96  ? 42  VAL   C O   1 
ATOM   1394 C  CB  . VAL   B 1 36  ? 17.111 -16.052 23.083 1.00 12.37  ? 42  VAL   C CB  1 
ATOM   1395 C  CG1 . VAL   B 1 36  ? 16.141 -17.111 23.626 1.00 13.99  ? 42  VAL   C CG1 1 
ATOM   1396 C  CG2 . VAL   B 1 36  ? 18.553 -16.610 23.068 1.00 13.26  ? 42  VAL   C CG2 1 
ATOM   1397 N  N   . SER   B 1 37  ? 14.361 -15.843 21.106 1.00 11.94  ? 43  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 37  ? 12.943 -15.488 21.070 1.00 12.32  ? 43  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 37  ? 12.139 -16.588 21.757 1.00 12.89  ? 43  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 37  ? 12.616 -17.703 22.018 1.00 13.30  ? 43  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 37  ? 12.462 -15.278 19.638 1.00 12.70  ? 43  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 37  ? 12.614 -16.433 18.831 1.00 13.88  ? 43  SER   C OG  1 
ATOM   1403 N  N   . SER   B 1 38  ? 10.904 -16.261 22.151 1.00 13.58  ? 44  SER   C N   1 
ATOM   1404 C  CA  . SER   B 1 38  ? 10.025 -17.237 22.809 1.00 15.12  ? 44  SER   C CA  1 
ATOM   1405 C  C   . SER   B 1 38  ? 9.210  -18.023 21.776 1.00 17.00  ? 44  SER   C C   1 
ATOM   1406 O  O   . SER   B 1 38  ? 8.873  -17.520 20.703 1.00 18.95  ? 44  SER   C O   1 
ATOM   1407 C  CB  . SER   B 1 38  ? 9.109  -16.529 23.811 1.00 17.89  ? 44  SER   C CB  1 
ATOM   1408 O  OG  . SER   B 1 38  ? 8.298  -15.600 23.127 1.00 21.99  ? 44  SER   C OG  1 
ATOM   1409 N  N   . THR   B 1 39  ? 8.849  -19.257 22.112 1.00 17.13  ? 45  THR   C N   1 
ATOM   1410 C  CA  . THR   B 1 39  ? 8.097  -20.143 21.221 1.00 17.97  ? 45  THR   C CA  1 
ATOM   1411 C  C   . THR   B 1 39  ? 6.798  -20.590 21.917 1.00 20.56  ? 45  THR   C C   1 
ATOM   1412 O  O   . THR   B 1 39  ? 6.748  -20.709 23.136 1.00 20.25  ? 45  THR   C O   1 
ATOM   1413 C  CB  . THR   B 1 39  ? 8.931  -21.407 20.845 1.00 18.28  ? 45  THR   C CB  1 
ATOM   1414 O  OG1 . THR   B 1 39  ? 9.220  -22.155 22.007 1.00 19.39  ? 45  THR   C OG1 1 
ATOM   1415 C  CG2 . THR   B 1 39  ? 10.270 -21.061 20.175 1.00 19.95  ? 45  THR   C CG2 1 
ATOM   1416 N  N   . THR   B 1 40  ? 5.815  -20.971 21.108 1.00 22.49  ? 46  THR   C N   1 
ATOM   1417 C  CA  . THR   B 1 40  ? 4.573  -21.536 21.660 1.00 24.61  ? 46  THR   C CA  1 
ATOM   1418 C  C   . THR   B 1 40  ? 4.787  -23.010 22.016 1.00 24.94  ? 46  THR   C C   1 
ATOM   1419 O  O   . THR   B 1 40  ? 4.384  -23.465 23.095 1.00 27.23  ? 46  THR   C O   1 
ATOM   1420 C  CB  . THR   B 1 40  ? 3.419  -21.279 20.691 1.00 28.51  ? 46  THR   C CB  1 
ATOM   1421 O  OG1 . THR   B 1 40  ? 3.771  -21.832 19.421 1.00 32.33  ? 46  THR   C OG1 1 
ATOM   1422 C  CG2 . THR   B 1 40  ? 3.181  -19.805 20.497 1.00 27.64  ? 46  THR   C CG2 1 
ATOM   1423 N  N   . ALA   B 1 41  ? 5.489  -23.756 21.142 1.00 22.71  ? 47  ALA   C N   1 
ATOM   1424 C  CA  . ALA   B 1 41  ? 5.753  -25.161 21.381 1.00 23.15  ? 47  ALA   C CA  1 
ATOM   1425 C  C   . ALA   B 1 41  ? 7.066  -25.410 22.128 1.00 22.01  ? 47  ALA   C C   1 
ATOM   1426 O  O   . ALA   B 1 41  ? 8.008  -24.653 21.946 1.00 21.98  ? 47  ALA   C O   1 
ATOM   1427 C  CB  . ALA   B 1 41  ? 5.792  -25.901 20.057 1.00 25.13  ? 47  ALA   C CB  1 
ATOM   1428 N  N   . GLN   B 1 42  ? 7.164  -26.484 22.911 1.00 21.27  ? 48  GLN   C N   1 
ATOM   1429 C  CA  . GLN   B 1 42  ? 8.390  -26.827 23.605 1.00 21.34  ? 48  GLN   C CA  1 
ATOM   1430 C  C   . GLN   B 1 42  ? 9.367  -27.493 22.634 1.00 20.11  ? 48  GLN   C C   1 
ATOM   1431 O  O   . GLN   B 1 42  ? 8.977  -28.327 21.813 1.00 22.00  ? 48  GLN   C O   1 
ATOM   1432 C  CB  . GLN   B 1 42  ? 8.113  -27.746 24.807 1.00 26.84  ? 48  GLN   C CB  1 
ATOM   1433 C  CG  . GLN   B 1 42  ? 7.516  -26.997 26.001 1.00 36.16  ? 48  GLN   C CG  1 
ATOM   1434 C  CD  . GLN   B 1 42  ? 7.380  -27.961 27.149 1.00 46.63  ? 48  GLN   C CD  1 
ATOM   1435 O  OE1 . GLN   B 1 42  ? 6.486  -28.815 27.173 1.00 50.26  ? 48  GLN   C OE1 1 
ATOM   1436 N  NE2 . GLN   B 1 42  ? 8.280  -27.873 28.119 1.00 49.25  ? 48  GLN   C NE2 1 
ATOM   1437 N  N   . GLY   B 1 43  ? 10.643 -27.138 22.760 1.00 17.58  ? 49  GLY   C N   1 
ATOM   1438 C  CA  . GLY   B 1 43  ? 11.732 -27.707 21.981 1.00 16.90  ? 49  GLY   C CA  1 
ATOM   1439 C  C   . GLY   B 1 43  ? 12.438 -28.782 22.792 1.00 16.65  ? 49  GLY   C C   1 
ATOM   1440 O  O   . GLY   B 1 43  ? 12.259 -28.895 24.019 1.00 19.51  ? 49  GLY   C O   1 
ATOM   1441 N  N   . CYS   B 1 44  ? 13.246 -29.550 22.127 1.00 15.67  ? 50  CYS   C N   1 
ATOM   1442 C  CA  . CYS   B 1 44  ? 13.851 -30.767 22.687 1.00 16.88  ? 50  CYS   C CA  1 
ATOM   1443 C  C   . CYS   B 1 44  ? 15.339 -30.796 22.688 1.00 16.81  ? 50  CYS   C C   1 
ATOM   1444 O  O   . CYS   B 1 44  ? 15.920 -31.848 23.048 1.00 19.46  ? 50  CYS   C O   1 
ATOM   1445 C  CB  . CYS   B 1 44  ? 13.304 -31.981 21.942 1.00 17.25  ? 50  CYS   C CB  1 
ATOM   1446 S  SG  . CYS   B 1 44  ? 11.506 -32.118 22.046 1.00 23.16  ? 50  CYS   C SG  1 
ATOM   1447 N  N   . ASP   B 1 45  ? 16.013 -29.736 22.254 1.00 14.22  ? 51  ASP   C N   1 
ATOM   1448 C  CA  . ASP   B 1 45  ? 17.465 -29.728 22.259 1.00 14.95  ? 51  ASP   C CA  1 
ATOM   1449 C  C   . ASP   B 1 45  ? 17.900 -29.547 23.709 1.00 15.88  ? 51  ASP   C C   1 
ATOM   1450 O  O   . ASP   B 1 45  ? 17.216 -28.877 24.510 1.00 18.32  ? 51  ASP   C O   1 
ATOM   1451 C  CB  . ASP   B 1 45  ? 18.025 -28.577 21.412 1.00 14.95  ? 51  ASP   C CB  1 
ATOM   1452 C  CG  . ASP   B 1 45  ? 17.839 -28.769 19.929 1.00 17.42  ? 51  ASP   C CG  1 
ATOM   1453 O  OD1 . ASP   B 1 45  ? 17.887 -29.921 19.466 1.00 20.01  ? 51  ASP   C OD1 1 
ATOM   1454 O  OD2 . ASP   B 1 45  ? 17.693 -27.751 19.199 1.00 15.77  ? 51  ASP   C OD2 1 
ATOM   1455 N  N   . THR   B 1 46  ? 18.994 -30.198 24.065 1.00 13.43  ? 52  THR   C N   1 
ATOM   1456 C  CA  . THR   B 1 46  ? 19.616 -30.049 25.376 1.00 13.89  ? 52  THR   C CA  1 
ATOM   1457 C  C   . THR   B 1 46  ? 20.876 -29.187 25.219 1.00 13.10  ? 52  THR   C C   1 
ATOM   1458 O  O   . THR   B 1 46  ? 21.709 -29.486 24.324 1.00 14.23  ? 52  THR   C O   1 
ATOM   1459 C  CB  . THR   B 1 46  ? 20.019 -31.413 25.923 1.00 15.93  ? 52  THR   C CB  1 
ATOM   1460 O  OG1 . THR   B 1 46  ? 18.803 -32.192 26.139 1.00 18.24  ? 52  THR   C OG1 1 
ATOM   1461 C  CG2 . THR   B 1 46  ? 20.778 -31.289 27.267 1.00 18.49  ? 52  THR   C CG2 1 
ATOM   1462 N  N   . ILE   B 1 47  ? 21.052 -28.154 26.031 1.00 13.21  ? 53  ILE   C N   1 
ATOM   1463 C  CA  . ILE   B 1 47  ? 22.254 -27.333 25.978 1.00 12.84  ? 53  ILE   C CA  1 
ATOM   1464 C  C   . ILE   B 1 47  ? 23.339 -28.004 26.832 1.00 12.32  ? 53  ILE   C C   1 
ATOM   1465 O  O   . ILE   B 1 47  ? 23.117 -28.434 27.970 1.00 13.67  ? 53  ILE   C O   1 
ATOM   1466 C  CB  . ILE   B 1 47  ? 21.977 -25.947 26.564 1.00 13.67  ? 53  ILE   C CB  1 
ATOM   1467 C  CG1 . ILE   B 1 47  ? 20.766 -25.280 25.905 1.00 14.74  ? 53  ILE   C CG1 1 
ATOM   1468 C  CG2 . ILE   B 1 47  ? 23.226 -25.069 26.483 1.00 14.43  ? 53  ILE   C CG2 1 
ATOM   1469 C  CD1 . ILE   B 1 47  ? 20.960 -25.124 24.373 1.00 16.33  ? 53  ILE   C CD1 1 
ATOM   1470 N  N   . ALA   B 1 48  ? 24.539 -28.086 26.278 1.00 11.50  ? 54  ALA   C N   1 
ATOM   1471 C  CA  . ALA   B 1 48  ? 25.686 -28.633 27.031 1.00 11.14  ? 54  ALA   C CA  1 
ATOM   1472 C  C   . ALA   B 1 48  ? 26.030 -27.702 28.221 1.00 11.32  ? 54  ALA   C C   1 
ATOM   1473 O  O   . ALA   B 1 48  ? 26.026 -26.462 28.058 1.00 12.24  ? 54  ALA   C O   1 
ATOM   1474 C  CB  . ALA   B 1 48  ? 26.887 -28.722 26.097 1.00 11.45  ? 54  ALA   C CB  1 
ATOM   1475 N  N   . ARG   B 1 49  ? 26.403 -28.303 29.370 1.00 11.72  ? 55  ARG   C N   1 
ATOM   1476 C  CA  . ARG   B 1 49  ? 26.871 -27.543 30.522 1.00 11.62  ? 55  ARG   C CA  1 
ATOM   1477 C  C   . ARG   B 1 49  ? 28.186 -28.181 30.900 1.00 12.17  ? 55  ARG   C C   1 
ATOM   1478 O  O   . ARG   B 1 49  ? 28.216 -29.211 31.605 1.00 13.66  ? 55  ARG   C O   1 
ATOM   1479 C  CB  . ARG   B 1 49  ? 25.838 -27.592 31.654 1.00 12.67  ? 55  ARG   C CB  1 
ATOM   1480 C  CG  . ARG   B 1 49  ? 24.470 -27.025 31.226 1.00 12.04  ? 55  ARG   C CG  1 
ATOM   1481 C  CD  . ARG   B 1 49  ? 24.468 -25.544 30.877 1.00 14.62  ? 55  ARG   C CD  1 
ATOM   1482 N  NE  . ARG   B 1 49  ? 23.113 -25.107 30.501 1.00 13.90  ? 55  ARG   C NE  1 
ATOM   1483 C  CZ  . ARG   B 1 49  ? 22.848 -24.000 29.795 1.00 13.47  ? 55  ARG   C CZ  1 
ATOM   1484 N  NH1 . ARG   B 1 49  ? 23.814 -23.166 29.469 1.00 13.91  ? 55  ARG   C NH1 1 
ATOM   1485 N  NH2 . ARG   B 1 49  ? 21.589 -23.716 29.417 1.00 15.36  ? 55  ARG   C NH2 1 
ATOM   1486 N  N   . CYS   B 1 50  ? 29.287 -27.608 30.402 1.00 11.36  ? 56  CYS   C N   1 
ATOM   1487 C  CA  . CYS   B 1 50  ? 30.626 -28.238 30.418 1.00 11.73  ? 56  CYS   C CA  1 
ATOM   1488 C  C   . CYS   B 1 50  ? 31.668 -27.267 29.891 1.00 12.21  ? 56  CYS   C C   1 
ATOM   1489 O  O   . CYS   B 1 50  ? 31.341 -26.165 29.445 1.00 12.39  ? 56  CYS   C O   1 
ATOM   1490 C  CB  . CYS   B 1 50  ? 30.574 -29.463 29.494 1.00 11.21  ? 56  CYS   C CB  1 
ATOM   1491 S  SG  . CYS   B 1 50  ? 30.421 -29.035 27.717 1.00 12.01  ? 56  CYS   C SG  1 
ATOM   1492 N  N   . ASP   B 1 51  ? 32.961 -27.711 29.938 1.00 12.91  ? 57  ASP   C N   1 
ATOM   1493 C  CA  . ASP   B 1 51  ? 34.073 -26.987 29.335 1.00 14.31  ? 57  ASP   C CA  1 
ATOM   1494 C  C   . ASP   B 1 51  ? 34.730 -27.858 28.246 1.00 13.64  ? 57  ASP   C C   1 
ATOM   1495 O  O   . ASP   B 1 51  ? 35.939 -27.692 27.991 1.00 14.78  ? 57  ASP   C O   1 
ATOM   1496 C  CB  . ASP   B 1 51  ? 35.091 -26.539 30.394 1.00 17.05  ? 57  ASP   C CB  1 
ATOM   1497 C  CG  . ASP   B 1 51  ? 35.759 -27.652 31.141 1.00 20.48  ? 57  ASP   C CG  1 
ATOM   1498 O  OD1 . ASP   B 1 51  ? 35.479 -28.828 30.847 1.00 20.29  ? 57  ASP   C OD1 1 
ATOM   1499 O  OD2 . ASP   B 1 51  ? 36.682 -27.345 31.969 1.00 26.41  ? 57  ASP   C OD2 1 
ATOM   1500 N  N   . CYS   B 1 52  ? 33.956 -28.721 27.544 1.00 12.62  ? 58  CYS   C N   1 
ATOM   1501 C  CA  . CYS   B 1 52  ? 34.549 -29.484 26.418 1.00 11.69  ? 58  CYS   C CA  1 
ATOM   1502 C  C   . CYS   B 1 52  ? 35.225 -28.568 25.397 1.00 11.67  ? 58  CYS   C C   1 
ATOM   1503 O  O   . CYS   B 1 52  ? 34.759 -27.435 25.159 1.00 12.07  ? 58  CYS   C O   1 
ATOM   1504 C  CB  . CYS   B 1 52  ? 33.472 -30.310 25.695 1.00 12.30  ? 58  CYS   C CB  1 
ATOM   1505 S  SG  . CYS   B 1 52  ? 32.867 -31.740 26.626 1.00 13.02  ? 58  CYS   C SG  1 
ATOM   1506 N  N   . GLN   B 1 53  ? 36.268 -29.077 24.770 1.00 11.21  ? 59  GLN   C N   1 
ATOM   1507 C  CA  . GLN   B 1 53  ? 36.937 -28.466 23.630 1.00 11.99  ? 59  GLN   C CA  1 
ATOM   1508 C  C   . GLN   B 1 53  ? 37.015 -29.417 22.468 1.00 11.31  ? 59  GLN   C C   1 
ATOM   1509 O  O   . GLN   B 1 53  ? 37.777 -29.179 21.526 1.00 11.82  ? 59  GLN   C O   1 
ATOM   1510 C  CB  . GLN   B 1 53  ? 38.352 -27.998 24.022 1.00 13.02  ? 59  GLN   C CB  1 
ATOM   1511 C  CG  . GLN   B 1 53  ? 38.322 -26.743 24.926 1.00 16.79  ? 59  GLN   C CG  1 
ATOM   1512 C  CD  . GLN   B 1 53  ? 39.689 -26.173 25.152 1.00 18.16  ? 59  GLN   C CD  1 
ATOM   1513 O  OE1 . GLN   B 1 53  ? 40.200 -26.225 26.288 1.00 20.88  ? 59  GLN   C OE1 1 
ATOM   1514 N  NE2 . GLN   B 1 53  ? 40.315 -25.631 24.098 1.00 16.68  ? 59  GLN   C NE2 1 
ATOM   1515 N  N   . THR   B 1 54  ? 36.222 -30.512 22.482 1.00 11.02  ? 60  THR   C N   1 
ATOM   1516 C  CA  . THR   B 1 54  ? 36.126 -31.377 21.305 1.00 11.94  ? 60  THR   C CA  1 
ATOM   1517 C  C   . THR   B 1 54  ? 34.634 -31.644 21.043 1.00 11.33  ? 60  THR   C C   1 
ATOM   1518 O  O   . THR   B 1 54  ? 33.842 -31.759 21.986 1.00 11.57  ? 60  THR   C O   1 
ATOM   1519 C  CB  . THR   B 1 54  ? 36.851 -32.666 21.413 1.00 15.06  ? 60  THR   C CB  1 
ATOM   1520 O  OG1 . THR   B 1 54  ? 36.292 -33.442 22.390 1.00 19.05  ? 60  THR   C OG1 1 
ATOM   1521 C  CG2 . THR   B 1 54  ? 38.313 -32.487 21.702 1.00 14.86  ? 60  THR   C CG2 1 
ATOM   1522 N  N   . GLY   B 1 55  ? 34.248 -31.715 19.772 1.00 10.63  ? 61  GLY   C N   1 
ATOM   1523 C  CA  . GLY   B 1 55  ? 32.839 -31.917 19.429 1.00 10.52  ? 61  GLY   C CA  1 
ATOM   1524 C  C   . GLY   B 1 55  ? 32.722 -32.110 17.929 1.00 9.04   ? 61  GLY   C C   1 
ATOM   1525 O  O   . GLY   B 1 55  ? 33.710 -32.407 17.246 1.00 10.57  ? 61  GLY   C O   1 
ATOM   1526 N  N   . VAL   B 1 56  ? 31.498 -32.001 17.427 1.00 9.07   ? 62  VAL   C N   1 
ATOM   1527 C  CA  . VAL   B 1 56  ? 31.209 -32.206 15.997 1.00 8.64   ? 62  VAL   C CA  1 
ATOM   1528 C  C   . VAL   B 1 56  ? 30.291 -31.083 15.564 1.00 8.75   ? 62  VAL   C C   1 
ATOM   1529 O  O   . VAL   B 1 56  ? 29.347 -30.769 16.271 1.00 9.47   ? 62  VAL   C O   1 
ATOM   1530 C  CB  . VAL   B 1 56  ? 30.479 -33.563 15.827 1.00 9.47   ? 62  VAL   C CB  1 
ATOM   1531 C  CG1 . VAL   B 1 56  ? 29.978 -33.757 14.395 1.00 11.41  ? 62  VAL   C CG1 1 
ATOM   1532 C  CG2 . VAL   B 1 56  ? 31.388 -34.755 16.251 1.00 10.42  ? 62  VAL   C CG2 1 
ATOM   1533 N  N   . TYR   B 1 57  ? 30.573 -30.476 14.403 1.00 9.09   ? 63  TYR   C N   1 
ATOM   1534 C  CA  . TYR   B 1 57  ? 29.675 -29.414 13.892 1.00 8.50   ? 63  TYR   C CA  1 
ATOM   1535 C  C   . TYR   B 1 57  ? 29.121 -29.741 12.512 1.00 8.66   ? 63  TYR   C C   1 
ATOM   1536 O  O   . TYR   B 1 57  ? 29.781 -30.474 11.746 1.00 9.78   ? 63  TYR   C O   1 
ATOM   1537 C  CB  . TYR   B 1 57  ? 30.349 -27.989 13.887 1.00 9.59   ? 63  TYR   C CB  1 
ATOM   1538 C  CG  . TYR   B 1 57  ? 31.227 -27.679 12.677 1.00 9.22   ? 63  TYR   C CG  1 
ATOM   1539 C  CD1 . TYR   B 1 57  ? 32.508 -28.196 12.568 1.00 10.23  ? 63  TYR   C CD1 1 
ATOM   1540 C  CD2 . TYR   B 1 57  ? 30.764 -26.850 11.648 1.00 9.73   ? 63  TYR   C CD2 1 
ATOM   1541 C  CE1 . TYR   B 1 57  ? 33.322 -27.895 11.475 1.00 10.97  ? 63  TYR   C CE1 1 
ATOM   1542 C  CE2 . TYR   B 1 57  ? 31.586 -26.525 10.556 1.00 10.49  ? 63  TYR   C CE2 1 
ATOM   1543 C  CZ  . TYR   B 1 57  ? 32.866 -27.031 10.487 1.00 11.05  ? 63  TYR   C CZ  1 
ATOM   1544 O  OH  . TYR   B 1 57  ? 33.722 -26.749 9.424  1.00 12.99  ? 63  TYR   C OH  1 
ATOM   1545 N  N   . TYR   B 1 58  ? 27.946 -29.190 12.229 1.00 8.73   ? 64  TYR   C N   1 
ATOM   1546 C  CA  . TYR   B 1 58  ? 27.330 -29.354 10.905 1.00 9.54   ? 64  TYR   C CA  1 
ATOM   1547 C  C   . TYR   B 1 58  ? 27.731 -28.205 9.981  1.00 9.84   ? 64  TYR   C C   1 
ATOM   1548 O  O   . TYR   B 1 58  ? 27.492 -27.025 10.296 1.00 10.30  ? 64  TYR   C O   1 
ATOM   1549 C  CB  . TYR   B 1 58  ? 25.798 -29.467 10.979 1.00 10.54  ? 64  TYR   C CB  1 
ATOM   1550 C  CG  . TYR   B 1 58  ? 25.220 -29.729 9.599  1.00 11.21  ? 64  TYR   C CG  1 
ATOM   1551 C  CD1 . TYR   B 1 58  ? 25.551 -30.886 8.901  1.00 11.75  ? 64  TYR   C CD1 1 
ATOM   1552 C  CD2 . TYR   B 1 58  ? 24.344 -28.828 9.003  1.00 11.61  ? 64  TYR   C CD2 1 
ATOM   1553 C  CE1 . TYR   B 1 58  ? 25.040 -31.134 7.616  1.00 12.66  ? 64  TYR   C CE1 1 
ATOM   1554 C  CE2 . TYR   B 1 58  ? 23.806 -29.087 7.720  1.00 11.97  ? 64  TYR   C CE2 1 
ATOM   1555 C  CZ  . TYR   B 1 58  ? 24.186 -30.233 7.057  1.00 12.65  ? 64  TYR   C CZ  1 
ATOM   1556 O  OH  . TYR   B 1 58  ? 23.730 -30.486 5.761  1.00 15.82  ? 64  TYR   C OH  1 
ATOM   1557 N  N   . CYS   B 1 59  ? 28.240 -28.577 8.796  1.00 9.57   ? 65  CYS   C N   1 
ATOM   1558 C  CA  . CYS   B 1 59  ? 28.634 -27.633 7.744  1.00 9.87   ? 65  CYS   C CA  1 
ATOM   1559 C  C   . CYS   B 1 59  ? 27.715 -27.800 6.524  1.00 10.12  ? 65  CYS   C C   1 
ATOM   1560 O  O   . CYS   B 1 59  ? 27.879 -28.741 5.732  1.00 11.42  ? 65  CYS   C O   1 
ATOM   1561 C  CB  . CYS   B 1 59  ? 30.081 -27.873 7.383  1.00 10.53  ? 65  CYS   C CB  1 
ATOM   1562 S  SG  . CYS   B 1 59  ? 30.690 -26.830 6.031  1.00 12.70  ? 65  CYS   C SG  1 
ATOM   1563 N  N   . SER   B 1 60  ? 26.722 -26.931 6.403  1.00 11.34  ? 66  SER   C N   1 
ATOM   1564 C  CA  A SER   B 1 60  ? 25.738 -27.113 5.335  0.50 12.75  ? 66  SER   C CA  1 
ATOM   1565 C  CA  B SER   B 1 60  ? 25.733 -27.041 5.338  0.50 12.13  ? 66  SER   C CA  1 
ATOM   1566 C  C   . SER   B 1 60  ? 26.355 -26.986 3.932  1.00 12.63  ? 66  SER   C C   1 
ATOM   1567 O  O   . SER   B 1 60  ? 25.930 -27.719 3.058  1.00 14.36  ? 66  SER   C O   1 
ATOM   1568 C  CB  A SER   B 1 60  ? 24.541 -26.202 5.524  0.50 15.50  ? 66  SER   C CB  1 
ATOM   1569 C  CB  B SER   B 1 60  ? 24.685 -25.946 5.480  0.50 12.96  ? 66  SER   C CB  1 
ATOM   1570 O  OG  A SER   B 1 60  ? 24.941 -24.849 5.418  0.50 18.77  ? 66  SER   C OG  1 
ATOM   1571 O  OG  B SER   B 1 60  ? 23.691 -26.130 4.486  0.50 13.08  ? 66  SER   C OG  1 
ATOM   1572 N  N   . SER   B 1 61  ? 27.374 -26.140 3.768  1.00 12.00  ? 67  SER   C N   1 
ATOM   1573 C  CA  . SER   B 1 61  ? 28.045 -25.965 2.456  1.00 12.71  ? 67  SER   C CA  1 
ATOM   1574 C  C   . SER   B 1 61  ? 28.905 -27.147 2.064  1.00 13.72  ? 67  SER   C C   1 
ATOM   1575 O  O   . SER   B 1 61  ? 29.407 -27.163 0.929  1.00 15.79  ? 67  SER   C O   1 
ATOM   1576 C  CB  . SER   B 1 61  ? 28.869 -24.682 2.423  1.00 13.76  ? 67  SER   C CB  1 
ATOM   1577 O  OG  . SER   B 1 61  ? 29.974 -24.776 3.295  1.00 14.38  ? 67  SER   C OG  1 
ATOM   1578 N  N   . ARG   B 1 62  ? 29.007 -28.192 2.902  1.00 12.54  ? 68  ARG   C N   1 
ATOM   1579 C  CA  . ARG   B 1 62  ? 29.643 -29.449 2.533  1.00 12.74  ? 68  ARG   C CA  1 
ATOM   1580 C  C   . ARG   B 1 62  ? 28.705 -30.638 2.752  1.00 13.55  ? 68  ARG   C C   1 
ATOM   1581 O  O   . ARG   B 1 62  ? 29.114 -31.788 2.548  1.00 14.99  ? 68  ARG   C O   1 
ATOM   1582 C  CB  . ARG   B 1 62  ? 30.918 -29.641 3.345  1.00 13.22  ? 68  ARG   C CB  1 
ATOM   1583 C  CG  . ARG   B 1 62  ? 31.972 -28.569 3.122  1.00 16.30  ? 68  ARG   C CG  1 
ATOM   1584 C  CD  . ARG   B 1 62  ? 32.682 -28.804 1.806  1.00 17.37  ? 68  ARG   C CD  1 
ATOM   1585 N  NE  . ARG   B 1 62  ? 33.726 -27.802 1.545  1.00 18.17  ? 68  ARG   C NE  1 
ATOM   1586 C  CZ  . ARG   B 1 62  ? 33.535 -26.643 0.954  1.00 20.18  ? 68  ARG   C CZ  1 
ATOM   1587 N  NH1 . ARG   B 1 62  ? 32.348 -26.337 0.445  1.00 20.84  ? 68  ARG   C NH1 1 
ATOM   1588 N  NH2 . ARG   B 1 62  ? 34.574 -25.841 0.694  1.00 23.40  ? 68  ARG   C NH2 1 
ATOM   1589 N  N   . ARG   B 1 63  ? 27.472 -30.396 3.237  1.00 14.00  ? 69  ARG   C N   1 
ATOM   1590 C  CA  . ARG   B 1 63  ? 26.536 -31.475 3.680  1.00 15.22  ? 69  ARG   C CA  1 
ATOM   1591 C  C   . ARG   B 1 63  ? 27.247 -32.511 4.557  1.00 16.29  ? 69  ARG   C C   1 
ATOM   1592 O  O   . ARG   B 1 63  ? 27.109 -33.731 4.345  1.00 18.11  ? 69  ARG   C O   1 
ATOM   1593 C  CB  . ARG   B 1 63  ? 25.875 -32.162 2.463  1.00 17.54  ? 69  ARG   C CB  1 
ATOM   1594 C  CG  . ARG   B 1 63  ? 25.069 -31.243 1.592  1.00 19.91  ? 69  ARG   C CG  1 
ATOM   1595 C  CD  . ARG   B 1 63  ? 23.830 -30.836 2.292  1.00 24.96  ? 69  ARG   C CD  1 
ATOM   1596 N  NE  . ARG   B 1 63  ? 22.842 -30.369 1.329  1.00 27.49  ? 69  ARG   C NE  1 
ATOM   1597 C  CZ  . ARG   B 1 63  ? 22.618 -29.099 1.045  1.00 28.78  ? 69  ARG   C CZ  1 
ATOM   1598 N  NH1 . ARG   B 1 63  ? 23.341 -28.141 1.622  1.00 28.43  ? 69  ARG   C NH1 1 
ATOM   1599 N  NH2 . ARG   B 1 63  ? 21.680 -28.770 0.173  1.00 29.28  ? 69  ARG   C NH2 1 
ATOM   1600 N  N   . LYS   B 1 64  ? 28.042 -32.018 5.532  1.00 13.31  ? 70  LYS   C N   1 
ATOM   1601 C  CA  . LYS   B 1 64  ? 28.848 -32.946 6.324  1.00 13.67  ? 70  LYS   C CA  1 
ATOM   1602 C  C   . LYS   B 1 64  ? 28.954 -32.456 7.753  1.00 12.08  ? 70  LYS   C C   1 
ATOM   1603 O  O   . LYS   B 1 64  ? 28.990 -31.231 7.988  1.00 13.03  ? 70  LYS   C O   1 
ATOM   1604 C  CB  . LYS   B 1 64  ? 30.276 -32.974 5.746  1.00 17.75  ? 70  LYS   C CB  1 
ATOM   1605 C  CG  . LYS   B 1 64  ? 30.544 -34.026 4.686  1.00 29.09  ? 70  LYS   C CG  1 
ATOM   1606 C  CD  . LYS   B 1 64  ? 31.943 -34.651 4.905  1.00 36.60  ? 70  LYS   C CD  1 
ATOM   1607 C  CE  . LYS   B 1 64  ? 32.420 -35.322 3.643  1.00 43.74  ? 70  LYS   C CE  1 
ATOM   1608 N  NZ  . LYS   B 1 64  ? 32.207 -34.466 2.446  1.00 48.43  ? 70  LYS   C NZ  1 
ATOM   1609 N  N   . HIS   B 1 65  ? 29.066 -33.395 8.666  1.00 11.17  ? 71  HIS   C N   1 
ATOM   1610 C  CA  . HIS   B 1 65  ? 29.393 -33.132 10.074 1.00 10.98  ? 71  HIS   C CA  1 
ATOM   1611 C  C   . HIS   B 1 65  ? 30.863 -33.415 10.256 1.00 12.95  ? 71  HIS   C C   1 
ATOM   1612 O  O   . HIS   B 1 65  ? 31.355 -34.527 9.901  1.00 16.25  ? 71  HIS   C O   1 
ATOM   1613 C  CB  . HIS   B 1 65  ? 28.577 -34.033 10.995 1.00 11.85  ? 71  HIS   C CB  1 
ATOM   1614 C  CG  . HIS   B 1 65  ? 27.103 -33.779 10.972 1.00 10.86  ? 71  HIS   C CG  1 
ATOM   1615 N  ND1 . HIS   B 1 65  ? 26.432 -32.983 11.903 1.00 13.63  ? 71  HIS   C ND1 1 
ATOM   1616 C  CD2 . HIS   B 1 65  ? 26.188 -34.216 10.069 1.00 11.07  ? 71  HIS   C CD2 1 
ATOM   1617 C  CE1 . HIS   B 1 65  ? 25.133 -32.991 11.560 1.00 11.71  ? 71  HIS   C CE1 1 
ATOM   1618 N  NE2 . HIS   B 1 65  ? 24.940 -33.731 10.480 1.00 14.60  ? 71  HIS   C NE2 1 
ATOM   1619 N  N   . TYR   B 1 66  ? 31.613 -32.476 10.850 1.00 11.08  ? 72  TYR   C N   1 
ATOM   1620 C  CA  . TYR   B 1 66  ? 33.049 -32.641 11.026 1.00 10.01  ? 72  TYR   C CA  1 
ATOM   1621 C  C   . TYR   B 1 66  ? 33.419 -32.686 12.499 1.00 10.47  ? 72  TYR   C C   1 
ATOM   1622 O  O   . TYR   B 1 66  ? 32.973 -31.804 13.266 1.00 10.02  ? 72  TYR   C O   1 
ATOM   1623 C  CB  . TYR   B 1 66  ? 33.799 -31.411 10.449 1.00 10.84  ? 72  TYR   C CB  1 
ATOM   1624 C  CG  . TYR   B 1 66  ? 33.766 -31.312 8.930  1.00 12.08  ? 72  TYR   C CG  1 
ATOM   1625 C  CD1 . TYR   B 1 66  ? 34.617 -32.076 8.145  1.00 14.59  ? 72  TYR   C CD1 1 
ATOM   1626 C  CD2 . TYR   B 1 66  ? 32.945 -30.403 8.283  1.00 12.71  ? 72  TYR   C CD2 1 
ATOM   1627 C  CE1 . TYR   B 1 66  ? 34.618 -31.966 6.754  1.00 15.24  ? 72  TYR   C CE1 1 
ATOM   1628 C  CE2 . TYR   B 1 66  ? 32.938 -30.283 6.896  1.00 13.98  ? 72  TYR   C CE2 1 
ATOM   1629 C  CZ  . TYR   B 1 66  ? 33.771 -31.076 6.142  1.00 14.18  ? 72  TYR   C CZ  1 
ATOM   1630 O  OH  . TYR   B 1 66  ? 33.773 -30.898 4.764  1.00 16.98  ? 72  TYR   C OH  1 
ATOM   1631 N  N   . PRO   B 1 67  ? 34.229 -33.653 12.917 1.00 10.36  ? 73  PRO   C N   1 
ATOM   1632 C  CA  . PRO   B 1 67  ? 34.759 -33.629 14.296 1.00 10.44  ? 73  PRO   C CA  1 
ATOM   1633 C  C   . PRO   B 1 67  ? 35.863 -32.556 14.398 1.00 10.88  ? 73  PRO   C C   1 
ATOM   1634 O  O   . PRO   B 1 67  ? 36.753 -32.492 13.521 1.00 13.52  ? 73  PRO   C O   1 
ATOM   1635 C  CB  . PRO   B 1 67  ? 35.346 -35.051 14.490 1.00 12.26  ? 73  PRO   C CB  1 
ATOM   1636 C  CG  . PRO   B 1 67  ? 35.653 -35.522 13.113 1.00 15.14  ? 73  PRO   C CG  1 
ATOM   1637 C  CD  . PRO   B 1 67  ? 34.740 -34.816 12.127 1.00 11.85  ? 73  PRO   C CD  1 
ATOM   1638 N  N   . VAL   B 1 68  ? 35.819 -31.755 15.435 1.00 9.86   ? 74  VAL   C N   1 
ATOM   1639 C  CA  . VAL   B 1 68  ? 36.791 -30.661 15.598 1.00 10.61  ? 74  VAL   C CA  1 
ATOM   1640 C  C   . VAL   B 1 68  ? 37.172 -30.501 17.047 1.00 10.77  ? 74  VAL   C C   1 
ATOM   1641 O  O   . VAL   B 1 68  ? 36.429 -30.780 17.986 1.00 10.79  ? 74  VAL   C O   1 
ATOM   1642 C  CB  . VAL   B 1 68  ? 36.200 -29.277 15.116 1.00 12.67  ? 74  VAL   C CB  1 
ATOM   1643 C  CG1 . VAL   B 1 68  ? 36.095 -29.217 13.582 1.00 14.44  ? 74  VAL   C CG1 1 
ATOM   1644 C  CG2 . VAL   B 1 68  ? 34.837 -28.989 15.779 1.00 13.35  ? 74  VAL   C CG2 1 
ATOM   1645 N  N   . SER   B 1 69  ? 38.389 -29.939 17.243 1.00 10.20  ? 75  SER   C N   1 
ATOM   1646 C  CA  . SER   B 1 69  ? 38.829 -29.296 18.491 1.00 10.82  ? 75  SER   C CA  1 
ATOM   1647 C  C   . SER   B 1 69  ? 38.548 -27.820 18.388 1.00 10.26  ? 75  SER   C C   1 
ATOM   1648 O  O   . SER   B 1 69  ? 38.673 -27.208 17.301 1.00 11.00  ? 75  SER   C O   1 
ATOM   1649 C  CB  . SER   B 1 69  ? 40.335 -29.467 18.679 1.00 13.50  ? 75  SER   C CB  1 
ATOM   1650 O  OG  . SER   B 1 69  ? 40.603 -30.852 18.784 1.00 18.09  ? 75  SER   C OG  1 
ATOM   1651 N  N   . PHE   B 1 70  ? 38.070 -27.205 19.456 1.00 10.08  ? 76  PHE   C N   1 
ATOM   1652 C  CA  . PHE   B 1 70  ? 37.707 -25.786 19.424 1.00 10.02  ? 76  PHE   C CA  1 
ATOM   1653 C  C   . PHE   B 1 70  ? 38.190 -25.061 20.679 1.00 10.40  ? 76  PHE   C C   1 
ATOM   1654 O  O   . PHE   B 1 70  ? 38.347 -25.670 21.744 1.00 11.42  ? 76  PHE   C O   1 
ATOM   1655 C  CB  . PHE   B 1 70  ? 36.184 -25.580 19.163 1.00 10.55  ? 76  PHE   C CB  1 
ATOM   1656 C  CG  . PHE   B 1 70  ? 35.274 -26.283 20.167 1.00 10.26  ? 76  PHE   C CG  1 
ATOM   1657 C  CD1 . PHE   B 1 70  ? 34.864 -27.595 19.966 1.00 10.56  ? 76  PHE   C CD1 1 
ATOM   1658 C  CD2 . PHE   B 1 70  ? 34.840 -25.631 21.315 1.00 11.04  ? 76  PHE   C CD2 1 
ATOM   1659 C  CE1 . PHE   B 1 70  ? 34.022 -28.225 20.896 1.00 10.46  ? 76  PHE   C CE1 1 
ATOM   1660 C  CE2 . PHE   B 1 70  ? 33.951 -26.271 22.208 1.00 11.31  ? 76  PHE   C CE2 1 
ATOM   1661 C  CZ  . PHE   B 1 70  ? 33.603 -27.576 22.022 1.00 10.83  ? 76  PHE   C CZ  1 
ATOM   1662 N  N   . SER   B 1 71  ? 38.440 -23.776 20.541 1.00 10.01  ? 77  SER   C N   1 
ATOM   1663 C  CA  . SER   B 1 71  ? 39.030 -22.992 21.617 1.00 11.47  ? 77  SER   C CA  1 
ATOM   1664 C  C   . SER   B 1 71  ? 38.032 -22.621 22.699 1.00 12.23  ? 77  SER   C C   1 
ATOM   1665 O  O   . SER   B 1 71  ? 36.830 -22.858 22.590 1.00 13.54  ? 77  SER   C O   1 
ATOM   1666 C  CB  . SER   B 1 71  ? 39.747 -21.763 21.040 1.00 12.81  ? 77  SER   C CB  1 
ATOM   1667 O  OG  . SER   B 1 71  ? 38.847 -20.869 20.390 1.00 14.67  ? 77  SER   C OG  1 
ATOM   1668 N  N   . LYS   B 1 72  ? 38.518 -21.997 23.766 1.00 14.23  ? 78  LYS   C N   1 
ATOM   1669 C  CA  . LYS   B 1 72  ? 37.652 -21.570 24.868 1.00 14.18  ? 78  LYS   C CA  1 
ATOM   1670 C  C   . LYS   B 1 72  ? 36.931 -20.261 24.470 1.00 14.24  ? 78  LYS   C C   1 
ATOM   1671 O  O   . LYS   B 1 72  ? 37.504 -19.456 23.738 1.00 15.61  ? 78  LYS   C O   1 
ATOM   1672 C  CB  . LYS   B 1 72  ? 38.521 -21.305 26.114 1.00 18.21  ? 78  LYS   C CB  1 
ATOM   1673 C  CG  . LYS   B 1 72  ? 39.238 -22.558 26.568 1.00 21.17  ? 78  LYS   C CG  1 
ATOM   1674 C  CD  . LYS   B 1 72  ? 39.541 -22.535 28.082 1.00 33.53  ? 78  LYS   C CD  1 
ATOM   1675 C  CE  . LYS   B 1 72  ? 39.684 -23.952 28.607 1.00 42.46  ? 78  LYS   C CE  1 
ATOM   1676 N  NZ  . LYS   B 1 72  ? 39.483 -24.060 30.083 1.00 47.16  ? 78  LYS   C NZ  1 
ATOM   1677 N  N   . PRO   B 1 73  ? 35.695 -20.013 24.932 1.00 13.49  ? 79  PRO   C N   1 
ATOM   1678 C  CA  . PRO   B 1 73  ? 34.962 -18.784 24.492 1.00 13.93  ? 79  PRO   C CA  1 
ATOM   1679 C  C   . PRO   B 1 73  ? 35.742 -17.524 24.867 1.00 14.63  ? 79  PRO   C C   1 
ATOM   1680 O  O   . PRO   B 1 73  ? 36.193 -17.376 26.033 1.00 17.28  ? 79  PRO   C O   1 
ATOM   1681 C  CB  . PRO   B 1 73  ? 33.638 -18.839 25.262 1.00 15.89  ? 79  PRO   C CB  1 
ATOM   1682 C  CG  . PRO   B 1 73  ? 33.470 -20.262 25.659 1.00 19.23  ? 79  PRO   C CG  1 
ATOM   1683 C  CD  . PRO   B 1 73  ? 34.869 -20.871 25.801 1.00 15.38  ? 79  PRO   C CD  1 
ATOM   1684 N  N   A SER   B 1 74  ? 35.981 -16.637 23.884 0.50 14.29  ? 80  SER   C N   1 
ATOM   1685 N  N   B SER   B 1 74  ? 35.967 -16.624 23.892 0.50 14.45  ? 80  SER   C N   1 
ATOM   1686 C  CA  A SER   B 1 74  ? 36.830 -15.467 24.107 0.50 14.85  ? 80  SER   C CA  1 
ATOM   1687 C  CA  B SER   B 1 74  ? 36.785 -15.438 24.148 0.50 15.30  ? 80  SER   C CA  1 
ATOM   1688 C  C   A SER   B 1 74  ? 36.409 -14.285 23.218 0.50 14.63  ? 80  SER   C C   1 
ATOM   1689 C  C   B SER   B 1 74  ? 36.457 -14.297 23.167 0.50 14.67  ? 80  SER   C C   1 
ATOM   1690 O  O   A SER   B 1 74  ? 35.486 -14.411 22.413 0.50 14.40  ? 80  SER   C O   1 
ATOM   1691 O  O   B SER   B 1 74  ? 35.669 -14.478 22.231 0.50 14.08  ? 80  SER   C O   1 
ATOM   1692 C  CB  A SER   B 1 74  ? 38.277 -15.827 23.780 0.50 16.41  ? 80  SER   C CB  1 
ATOM   1693 C  CB  B SER   B 1 74  ? 38.266 -15.796 24.065 0.50 17.64  ? 80  SER   C CB  1 
ATOM   1694 O  OG  A SER   B 1 74  ? 38.697 -16.984 24.482 0.50 17.73  ? 80  SER   C OG  1 
ATOM   1695 O  OG  B SER   B 1 74  ? 38.636 -16.054 22.722 0.50 19.31  ? 80  SER   C OG  1 
ATOM   1696 N  N   . LEU   B 1 75  ? 37.090 -13.131 23.374 1.00 15.37  ? 81  LEU   C N   1 
ATOM   1697 C  CA  . LEU   B 1 75  ? 36.898 -11.933 22.571 1.00 16.26  ? 81  LEU   C CA  1 
ATOM   1698 C  C   . LEU   B 1 75  ? 37.915 -11.988 21.436 1.00 16.70  ? 81  LEU   C C   1 
ATOM   1699 O  O   . LEU   B 1 75  ? 39.143 -11.927 21.710 1.00 19.32  ? 81  LEU   C O   1 
ATOM   1700 C  CB  . LEU   B 1 75  ? 37.119 -10.668 23.461 1.00 18.13  ? 81  LEU   C CB  1 
ATOM   1701 C  CG  . LEU   B 1 75  ? 36.848 -9.338  22.798 1.00 21.10  ? 81  LEU   C CG  1 
ATOM   1702 C  CD1 . LEU   B 1 75  ? 35.375 -9.157  22.566 1.00 20.59  ? 81  LEU   C CD1 1 
ATOM   1703 C  CD2 . LEU   B 1 75  ? 37.370 -8.183  23.686 1.00 23.98  ? 81  LEU   C CD2 1 
ATOM   1704 N  N   . ILE   B 1 76  ? 37.468 -12.162 20.198 1.00 17.93  ? 82  ILE   C N   1 
ATOM   1705 C  CA  . ILE   B 1 76  ? 38.316 -12.380 19.024 1.00 19.56  ? 82  ILE   C CA  1 
ATOM   1706 C  C   . ILE   B 1 76  ? 38.048 -11.327 17.972 1.00 19.35  ? 82  ILE   C C   1 
ATOM   1707 O  O   . ILE   B 1 76  ? 36.869 -11.043 17.692 1.00 17.90  ? 82  ILE   C O   1 
ATOM   1708 C  CB  . ILE   B 1 76  ? 37.964 -13.779 18.473 1.00 21.76  ? 82  ILE   C CB  1 
ATOM   1709 C  CG1 . ILE   B 1 76  ? 38.174 -14.901 19.539 1.00 25.33  ? 82  ILE   C CG1 1 
ATOM   1710 C  CG2 . ILE   B 1 76  ? 38.677 -14.101 17.133 1.00 24.16  ? 82  ILE   C CG2 1 
ATOM   1711 C  CD1 . ILE   B 1 76  ? 39.567 -15.749 19.505 1.00 27.48  ? 82  ILE   C CD1 1 
ATOM   1712 N  N   . PHE   B 1 77  ? 39.106 -10.828 17.303 1.00 19.05  ? 83  PHE   C N   1 
ATOM   1713 C  CA  . PHE   B 1 77  ? 38.914 -9.921  16.184 1.00 19.10  ? 83  PHE   C CA  1 
ATOM   1714 C  C   . PHE   B 1 77  ? 38.591 -10.787 14.952 1.00 19.69  ? 83  PHE   C C   1 
ATOM   1715 O  O   . PHE   B 1 77  ? 39.354 -11.702 14.568 1.00 22.04  ? 83  PHE   C O   1 
ATOM   1716 C  CB  . PHE   B 1 77  ? 40.204 -9.108  15.901 1.00 19.40  ? 83  PHE   C CB  1 
ATOM   1717 C  CG  . PHE   B 1 77  ? 39.922 -7.971  14.945 1.00 21.02  ? 83  PHE   C CG  1 
ATOM   1718 C  CD1 . PHE   B 1 77  ? 39.191 -6.870  15.350 1.00 21.96  ? 83  PHE   C CD1 1 
ATOM   1719 C  CD2 . PHE   B 1 77  ? 40.288 -8.056  13.603 1.00 22.39  ? 83  PHE   C CD2 1 
ATOM   1720 C  CE1 . PHE   B 1 77  ? 38.875 -5.846  14.452 1.00 24.24  ? 83  PHE   C CE1 1 
ATOM   1721 C  CE2 . PHE   B 1 77  ? 39.991 -7.020  12.721 1.00 23.51  ? 83  PHE   C CE2 1 
ATOM   1722 C  CZ  . PHE   B 1 77  ? 39.319 -5.913  13.159 1.00 23.62  ? 83  PHE   C CZ  1 
ATOM   1723 N  N   . VAL   B 1 78  ? 37.445 -10.500 14.321 1.00 16.59  ? 84  VAL   C N   1 
ATOM   1724 C  CA  . VAL   B 1 78  ? 36.949 -11.231 13.163 1.00 16.54  ? 84  VAL   C CA  1 
ATOM   1725 C  C   . VAL   B 1 78  ? 37.021 -10.283 11.945 1.00 16.19  ? 84  VAL   C C   1 
ATOM   1726 O  O   . VAL   B 1 78  ? 36.534 -9.149  12.027 1.00 16.70  ? 84  VAL   C O   1 
ATOM   1727 C  CB  . VAL   B 1 78  ? 35.467 -11.672 13.447 1.00 17.31  ? 84  VAL   C CB  1 
ATOM   1728 C  CG1 . VAL   B 1 78  ? 34.919 -12.462 12.258 1.00 17.24  ? 84  VAL   C CG1 1 
ATOM   1729 C  CG2 . VAL   B 1 78  ? 35.361 -12.497 14.750 1.00 18.95  ? 84  VAL   C CG2 1 
ATOM   1730 N  N   . GLU   B 1 79  ? 37.530 -10.758 10.797 1.00 16.14  ? 85  GLU   C N   1 
ATOM   1731 C  CA  . GLU   B 1 79  ? 37.557 -9.944  9.579  1.00 16.63  ? 85  GLU   C CA  1 
ATOM   1732 C  C   . GLU   B 1 79  ? 36.158 -9.720  9.028  1.00 16.07  ? 85  GLU   C C   1 
ATOM   1733 O  O   . GLU   B 1 79  ? 35.188 -10.400 9.419  1.00 15.43  ? 85  GLU   C O   1 
ATOM   1734 C  CB  . GLU   B 1 79  ? 38.452 -10.574 8.500  1.00 18.84  ? 85  GLU   C CB  1 
ATOM   1735 C  CG  . GLU   B 1 79  ? 39.932 -10.589 8.874  1.00 23.67  ? 85  GLU   C CG  1 
ATOM   1736 C  CD  . GLU   B 1 79  ? 40.521 -9.206  9.128  1.00 28.02  ? 85  GLU   C CD  1 
ATOM   1737 O  OE1 . GLU   B 1 79  ? 40.147 -8.223  8.436  1.00 31.61  ? 85  GLU   C OE1 1 
ATOM   1738 O  OE2 . GLU   B 1 79  ? 41.378 -9.097  10.039 1.00 32.11  ? 85  GLU   C OE2 1 
ATOM   1739 N  N   . ALA   B 1 80  ? 36.007 -8.720  8.161  1.00 17.15  ? 86  ALA   C N   1 
ATOM   1740 C  CA  . ALA   B 1 80  ? 34.698 -8.402  7.593  1.00 18.05  ? 86  ALA   C CA  1 
ATOM   1741 C  C   . ALA   B 1 80  ? 34.088 -9.608  6.877  1.00 18.40  ? 86  ALA   C C   1 
ATOM   1742 O  O   . ALA   B 1 80  ? 34.816 -10.409 6.264  1.00 20.14  ? 86  ALA   C O   1 
ATOM   1743 C  CB  . ALA   B 1 80  ? 34.871 -7.263  6.587  1.00 19.29  ? 86  ALA   C CB  1 
ATOM   1744 N  N   . SER   B 1 81  ? 32.799 -9.776  7.048  1.00 17.11  ? 87  SER   C N   1 
ATOM   1745 C  CA  . SER   B 1 81  ? 32.088 -10.800 6.340  1.00 17.23  ? 87  SER   C CA  1 
ATOM   1746 C  C   . SER   B 1 81  ? 30.996 -10.149 5.512  1.00 17.69  ? 87  SER   C C   1 
ATOM   1747 O  O   . SER   B 1 81  ? 30.837 -8.899  5.520  1.00 18.90  ? 87  SER   C O   1 
ATOM   1748 C  CB  . SER   B 1 81  ? 31.465 -11.770 7.344  1.00 16.42  ? 87  SER   C CB  1 
ATOM   1749 O  OG  . SER   B 1 81  ? 30.433 -11.106 8.070  1.00 16.36  ? 87  SER   C OG  1 
ATOM   1750 N  N   . GLU   B 1 82  ? 30.154 -10.969 4.876  1.00 18.52  ? 88  GLU   C N   1 
ATOM   1751 C  CA  . GLU   B 1 82  ? 29.056 -10.351 4.134  1.00 20.35  ? 88  GLU   C CA  1 
ATOM   1752 C  C   . GLU   B 1 82  ? 28.001 -9.698  5.061  1.00 19.62  ? 88  GLU   C C   1 
ATOM   1753 O  O   . GLU   B 1 82  ? 27.220 -8.850  4.603  1.00 20.77  ? 88  GLU   C O   1 
ATOM   1754 C  CB  . GLU   B 1 82  ? 28.459 -11.371 3.170  1.00 26.16  ? 88  GLU   C CB  1 
ATOM   1755 C  CG  . GLU   B 1 82  ? 27.437 -12.318 3.735  1.00 34.51  ? 88  GLU   C CG  1 
ATOM   1756 C  CD  . GLU   B 1 82  ? 26.760 -13.137 2.653  1.00 39.75  ? 88  GLU   C CD  1 
ATOM   1757 O  OE1 . GLU   B 1 82  ? 27.405 -13.405 1.610  1.00 40.83  ? 88  GLU   C OE1 1 
ATOM   1758 O  OE2 . GLU   B 1 82  ? 25.580 -13.509 2.853  1.00 39.73  ? 88  GLU   C OE2 1 
ATOM   1759 N  N   . TYR   B 1 83  ? 27.999 -10.024 6.359  1.00 17.07  ? 89  TYR   C N   1 
ATOM   1760 C  CA  . TYR   B 1 83  ? 26.964 -9.531  7.275  1.00 16.30  ? 89  TYR   C CA  1 
ATOM   1761 C  C   . TYR   B 1 83  ? 27.469 -8.682  8.469  1.00 17.86  ? 89  TYR   C C   1 
ATOM   1762 O  O   . TYR   B 1 83  ? 26.631 -8.102  9.168  1.00 18.77  ? 89  TYR   C O   1 
ATOM   1763 C  CB  . TYR   B 1 83  ? 26.112 -10.729 7.759  1.00 15.64  ? 89  TYR   C CB  1 
ATOM   1764 C  CG  . TYR   B 1 83  ? 26.940 -11.924 8.239  1.00 14.96  ? 89  TYR   C CG  1 
ATOM   1765 C  CD1 . TYR   B 1 83  ? 27.372 -12.908 7.350  1.00 15.42  ? 89  TYR   C CD1 1 
ATOM   1766 C  CD2 . TYR   B 1 83  ? 27.315 -12.050 9.572  1.00 14.83  ? 89  TYR   C CD2 1 
ATOM   1767 C  CE1 . TYR   B 1 83  ? 28.114 -14.012 7.785  1.00 14.95  ? 89  TYR   C CE1 1 
ATOM   1768 C  CE2 . TYR   B 1 83  ? 28.088 -13.127 10.012 1.00 15.32  ? 89  TYR   C CE2 1 
ATOM   1769 C  CZ  . TYR   B 1 83  ? 28.487 -14.112 9.113  1.00 14.56  ? 89  TYR   C CZ  1 
ATOM   1770 O  OH  . TYR   B 1 83  ? 29.309 -15.159 9.486  1.00 15.51  ? 89  TYR   C OH  1 
ATOM   1771 N  N   . TYR   B 1 84  ? 28.775 -8.561  8.723  1.00 15.84  ? 90  TYR   C N   1 
ATOM   1772 C  CA  . TYR   B 1 84  ? 29.322 -7.647  9.736  1.00 15.86  ? 90  TYR   C CA  1 
ATOM   1773 C  C   . TYR   B 1 84  ? 30.650 -7.043  9.216  1.00 16.04  ? 90  TYR   C C   1 
ATOM   1774 O  O   . TYR   B 1 84  ? 31.379 -7.686  8.460  1.00 16.71  ? 90  TYR   C O   1 
ATOM   1775 C  CB  . TYR   B 1 84  ? 29.680 -8.403  11.058 1.00 14.66  ? 90  TYR   C CB  1 
ATOM   1776 C  CG  . TYR   B 1 84  ? 28.500 -8.831  11.903 1.00 13.78  ? 90  TYR   C CG  1 
ATOM   1777 C  CD1 . TYR   B 1 84  ? 27.566 -7.899  12.378 1.00 14.57  ? 90  TYR   C CD1 1 
ATOM   1778 C  CD2 . TYR   B 1 84  ? 28.328 -10.149 12.245 1.00 13.50  ? 90  TYR   C CD2 1 
ATOM   1779 C  CE1 . TYR   B 1 84  ? 26.475 -8.292  13.166 1.00 15.03  ? 90  TYR   C CE1 1 
ATOM   1780 C  CE2 . TYR   B 1 84  ? 27.243 -10.555 13.030 1.00 13.65  ? 90  TYR   C CE2 1 
ATOM   1781 C  CZ  . TYR   B 1 84  ? 26.340 -9.623  13.523 1.00 13.90  ? 90  TYR   C CZ  1 
ATOM   1782 O  OH  . TYR   B 1 84  ? 25.283 -10.006 14.348 1.00 13.47  ? 90  TYR   C OH  1 
ATOM   1783 N  N   . PRO   B 1 85  ? 31.008 -5.831  9.663  1.00 16.71  ? 91  PRO   C N   1 
ATOM   1784 C  CA  . PRO   B 1 85  ? 32.360 -5.323  9.378  1.00 16.47  ? 91  PRO   C CA  1 
ATOM   1785 C  C   . PRO   B 1 85  ? 33.378 -6.096  10.227 1.00 17.01  ? 91  PRO   C C   1 
ATOM   1786 O  O   . PRO   B 1 85  ? 33.019 -6.892  11.132 1.00 16.07  ? 91  PRO   C O   1 
ATOM   1787 C  CB  . PRO   B 1 85  ? 32.259 -3.863  9.840  1.00 18.01  ? 91  PRO   C CB  1 
ATOM   1788 C  CG  . PRO   B 1 85  ? 31.327 -3.927  10.977 1.00 18.29  ? 91  PRO   C CG  1 
ATOM   1789 C  CD  . PRO   B 1 85  ? 30.261 -4.976  10.618 1.00 17.48  ? 91  PRO   C CD  1 
ATOM   1790 N  N   . ALA   B 1 86  ? 34.681 -5.836  9.994  1.00 16.26  ? 92  ALA   C N   1 
ATOM   1791 C  CA  . ALA   B 1 86  ? 35.739 -6.356  10.848 1.00 17.58  ? 92  ALA   C CA  1 
ATOM   1792 C  C   . ALA   B 1 86  ? 35.532 -5.773  12.260 1.00 18.91  ? 92  ALA   C C   1 
ATOM   1793 O  O   . ALA   B 1 86  ? 35.234 -4.570  12.394 1.00 20.97  ? 92  ALA   C O   1 
ATOM   1794 C  CB  . ALA   B 1 86  ? 37.114 -5.946  10.298 1.00 18.37  ? 92  ALA   C CB  1 
ATOM   1795 N  N   . ARG   B 1 87  ? 35.528 -6.640  13.277 1.00 18.74  ? 93  ARG   C N   1 
ATOM   1796 C  CA  . ARG   B 1 87  ? 35.205 -6.201  14.628 1.00 18.32  ? 93  ARG   C CA  1 
ATOM   1797 C  C   . ARG   B 1 87  ? 35.594 -7.261  15.632 1.00 17.73  ? 93  ARG   C C   1 
ATOM   1798 O  O   . ARG   B 1 87  ? 35.866 -8.396  15.262 1.00 17.04  ? 93  ARG   C O   1 
ATOM   1799 C  CB  . ARG   B 1 87  ? 33.684 -5.945  14.754 1.00 19.11  ? 93  ARG   C CB  1 
ATOM   1800 C  CG  . ARG   B 1 87  ? 32.883 -7.258  14.737 1.00 16.88  ? 93  ARG   C CG  1 
ATOM   1801 C  CD  . ARG   B 1 87  ? 31.398 -7.023  14.685 1.00 16.62  ? 93  ARG   C CD  1 
ATOM   1802 N  NE  . ARG   B 1 87  ? 30.690 -8.280  15.001 1.00 16.86  ? 93  ARG   C NE  1 
ATOM   1803 C  CZ  . ARG   B 1 87  ? 29.612 -8.448  15.752 1.00 16.99  ? 93  ARG   C CZ  1 
ATOM   1804 N  NH1 . ARG   B 1 87  ? 28.995 -7.397  16.299 1.00 18.52  ? 93  ARG   C NH1 1 
ATOM   1805 N  NH2 . ARG   B 1 87  ? 29.167 -9.672  16.009 1.00 17.65  ? 93  ARG   C NH2 1 
ATOM   1806 N  N   . TYR   B 1 88  ? 35.530 -6.903  16.924 1.00 19.05  ? 94  TYR   C N   1 
ATOM   1807 C  CA  . TYR   B 1 88  ? 35.679 -7.887  17.977 1.00 20.27  ? 94  TYR   C CA  1 
ATOM   1808 C  C   . TYR   B 1 88  ? 34.305 -8.544  18.261 1.00 17.77  ? 94  TYR   C C   1 
ATOM   1809 O  O   . TYR   B 1 88  ? 33.308 -7.869  18.445 1.00 18.84  ? 94  TYR   C O   1 
ATOM   1810 C  CB  . TYR   B 1 88  ? 36.138 -7.211  19.277 1.00 22.27  ? 94  TYR   C CB  1 
ATOM   1811 C  CG  . TYR   B 1 88  ? 37.604 -6.875  19.216 1.00 24.62  ? 94  TYR   C CG  1 
ATOM   1812 C  CD1 . TYR   B 1 88  ? 38.564 -7.840  19.458 1.00 25.04  ? 94  TYR   C CD1 1 
ATOM   1813 C  CD2 . TYR   B 1 88  ? 38.030 -5.600  18.840 1.00 25.49  ? 94  TYR   C CD2 1 
ATOM   1814 C  CE1 . TYR   B 1 88  ? 39.922 -7.550  19.348 1.00 26.27  ? 94  TYR   C CE1 1 
ATOM   1815 C  CE2 . TYR   B 1 88  ? 39.373 -5.298  18.725 1.00 26.31  ? 94  TYR   C CE2 1 
ATOM   1816 C  CZ  . TYR   B 1 88  ? 40.322 -6.269  18.986 1.00 27.02  ? 94  TYR   C CZ  1 
ATOM   1817 O  OH  . TYR   B 1 88  ? 41.654 -5.904  18.861 1.00 29.68  ? 94  TYR   C OH  1 
ATOM   1818 N  N   . GLN   B 1 89  ? 34.283 -9.884  18.298 1.00 15.75  ? 95  GLN   C N   1 
ATOM   1819 C  CA  . GLN   B 1 89  ? 33.084 -10.635 18.683 1.00 14.98  ? 95  GLN   C CA  1 
ATOM   1820 C  C   . GLN   B 1 89  ? 33.394 -11.359 19.991 1.00 14.11  ? 95  GLN   C C   1 
ATOM   1821 O  O   . GLN   B 1 89  ? 34.496 -11.937 20.137 1.00 15.27  ? 95  GLN   C O   1 
ATOM   1822 C  CB  . GLN   B 1 89  ? 32.714 -11.591 17.551 1.00 15.24  ? 95  GLN   C CB  1 
ATOM   1823 C  CG  . GLN   B 1 89  ? 31.449 -12.388 17.864 1.00 15.80  ? 95  GLN   C CG  1 
ATOM   1824 C  CD  . GLN   B 1 89  ? 30.770 -12.961 16.652 1.00 14.73  ? 95  GLN   C CD  1 
ATOM   1825 O  OE1 . GLN   B 1 89  ? 30.752 -12.371 15.556 1.00 15.06  ? 95  GLN   C OE1 1 
ATOM   1826 N  NE2 . GLN   B 1 89  ? 30.203 -14.123 16.839 1.00 14.08  ? 95  GLN   C NE2 1 
ATOM   1827 N  N   . SER   B 1 90  ? 32.488 -11.333 20.940 1.00 13.53  ? 96  SER   C N   1 
ATOM   1828 C  CA  . SER   B 1 90  ? 32.668 -11.947 22.246 1.00 13.12  ? 96  SER   C CA  1 
ATOM   1829 C  C   . SER   B 1 90  ? 32.087 -13.362 22.318 1.00 12.82  ? 96  SER   C C   1 
ATOM   1830 O  O   . SER   B 1 90  ? 31.245 -13.735 21.500 1.00 12.35  ? 96  SER   C O   1 
ATOM   1831 C  CB  . SER   B 1 90  ? 32.108 -11.056 23.371 1.00 15.13  ? 96  SER   C CB  1 
ATOM   1832 O  OG  . SER   B 1 90  ? 30.707 -11.024 23.253 1.00 16.00  ? 96  SER   C OG  1 
ATOM   1833 N  N   . HIS   B 1 91  ? 32.542 -14.129 23.322 1.00 12.63  ? 97  HIS   C N   1 
ATOM   1834 C  CA  . HIS   B 1 91  ? 32.038 -15.494 23.575 1.00 12.25  ? 97  HIS   C CA  1 
ATOM   1835 C  C   . HIS   B 1 91  ? 32.155 -16.385 22.317 1.00 11.98  ? 97  HIS   C C   1 
ATOM   1836 O  O   . HIS   B 1 91  ? 31.249 -17.208 22.063 1.00 12.90  ? 97  HIS   C O   1 
ATOM   1837 C  CB  . HIS   B 1 91  ? 30.582 -15.469 24.129 1.00 12.68  ? 97  HIS   C CB  1 
ATOM   1838 C  CG  . HIS   B 1 91  ? 30.450 -14.727 25.445 1.00 14.45  ? 97  HIS   C CG  1 
ATOM   1839 N  ND1 . HIS   B 1 91  ? 30.442 -15.393 26.653 1.00 17.05  ? 97  HIS   C ND1 1 
ATOM   1840 C  CD2 . HIS   B 1 91  ? 30.364 -13.392 25.681 1.00 15.85  ? 97  HIS   C CD2 1 
ATOM   1841 C  CE1 . HIS   B 1 91  ? 30.335 -14.462 27.599 1.00 17.67  ? 97  HIS   C CE1 1 
ATOM   1842 N  NE2 . HIS   B 1 91  ? 30.279 -13.238 27.064 1.00 17.58  ? 97  HIS   C NE2 1 
ATOM   1843 N  N   . LEU   B 1 92  ? 33.250 -16.235 21.593 1.00 11.21  ? 98  LEU   C N   1 
ATOM   1844 C  CA  . LEU   B 1 92  ? 33.433 -16.931 20.324 1.00 11.63  ? 98  LEU   C CA  1 
ATOM   1845 C  C   . LEU   B 1 92  ? 34.506 -17.996 20.508 1.00 11.64  ? 98  LEU   C C   1 
ATOM   1846 O  O   . LEU   B 1 92  ? 35.495 -17.777 21.207 1.00 12.07  ? 98  LEU   C O   1 
ATOM   1847 C  CB  . LEU   B 1 92  ? 33.900 -15.909 19.227 1.00 12.47  ? 98  LEU   C CB  1 
ATOM   1848 C  CG  . LEU   B 1 92  ? 34.004 -16.469 17.811 1.00 13.70  ? 98  LEU   C CG  1 
ATOM   1849 C  CD1 . LEU   B 1 92  ? 32.687 -16.818 17.240 1.00 14.40  ? 98  LEU   C CD1 1 
ATOM   1850 C  CD2 . LEU   B 1 92  ? 34.687 -15.440 16.858 1.00 16.97  ? 98  LEU   C CD2 1 
ATOM   1851 N  N   . MET   B 1 93  ? 34.334 -19.135 19.845 1.00 11.32  ? 99  MET   C N   1 
ATOM   1852 C  CA  . MET   B 1 93  ? 35.267 -20.263 19.890 1.00 10.53  ? 99  MET   C CA  1 
ATOM   1853 C  C   . MET   B 1 93  ? 35.702 -20.575 18.465 1.00 11.10  ? 99  MET   C C   1 
ATOM   1854 O  O   . MET   B 1 93  ? 34.827 -20.626 17.594 1.00 12.12  ? 99  MET   C O   1 
ATOM   1855 C  CB  . MET   B 1 93  ? 34.563 -21.493 20.479 1.00 11.84  ? 99  MET   C CB  1 
ATOM   1856 C  CG  . MET   B 1 93  ? 34.074 -21.232 21.898 1.00 13.70  ? 99  MET   C CG  1 
ATOM   1857 S  SD  . MET   B 1 93  ? 33.070 -22.552 22.554 1.00 14.41  ? 99  MET   C SD  1 
ATOM   1858 C  CE  . MET   B 1 93  ? 31.594 -22.445 21.446 1.00 14.51  ? 99  MET   C CE  1 
ATOM   1859 N  N   . LEU   B 1 94  ? 36.979 -20.842 18.196 1.00 10.77  ? 100 LEU   C N   1 
ATOM   1860 C  CA  . LEU   B 1 94  ? 37.436 -21.139 16.835 1.00 11.47  ? 100 LEU   C CA  1 
ATOM   1861 C  C   . LEU   B 1 94  ? 37.880 -22.591 16.705 1.00 10.69  ? 100 LEU   C C   1 
ATOM   1862 O  O   . LEU   B 1 94  ? 38.403 -23.180 17.669 1.00 11.63  ? 100 LEU   C O   1 
ATOM   1863 C  CB  . LEU   B 1 94  ? 38.671 -20.270 16.444 1.00 12.76  ? 100 LEU   C CB  1 
ATOM   1864 C  CG  . LEU   B 1 94  ? 38.488 -18.771 16.418 1.00 14.60  ? 100 LEU   C CG  1 
ATOM   1865 C  CD1 . LEU   B 1 94  ? 39.803 -18.080 15.972 1.00 17.82  ? 100 LEU   C CD1 1 
ATOM   1866 C  CD2 . LEU   B 1 94  ? 37.319 -18.363 15.516 1.00 15.36  ? 100 LEU   C CD2 1 
ATOM   1867 N  N   . ALA   B 1 95  ? 37.731 -23.108 15.510 1.00 11.45  ? 101 ALA   C N   1 
ATOM   1868 C  CA  . ALA   B 1 95  ? 38.296 -24.401 15.105 1.00 11.11  ? 101 ALA   C CA  1 
ATOM   1869 C  C   . ALA   B 1 95  ? 38.869 -24.259 13.681 1.00 10.78  ? 101 ALA   C C   1 
ATOM   1870 O  O   . ALA   B 1 95  ? 38.471 -23.337 12.934 1.00 10.75  ? 101 ALA   C O   1 
ATOM   1871 C  CB  . ALA   B 1 95  ? 37.217 -25.517 15.122 1.00 11.37  ? 101 ALA   C CB  1 
ATOM   1872 N  N   . VAL   B 1 96  ? 39.727 -25.201 13.284 1.00 10.95  ? 102 VAL   C N   1 
ATOM   1873 C  CA  . VAL   B 1 96  ? 40.198 -25.264 11.911 1.00 11.95  ? 102 VAL   C CA  1 
ATOM   1874 C  C   . VAL   B 1 96  ? 39.123 -26.009 11.092 1.00 11.82  ? 102 VAL   C C   1 
ATOM   1875 O  O   . VAL   B 1 96  ? 38.799 -27.188 11.381 1.00 13.48  ? 102 VAL   C O   1 
ATOM   1876 C  CB  . VAL   B 1 96  ? 41.569 -25.992 11.876 1.00 13.24  ? 102 VAL   C CB  1 
ATOM   1877 C  CG1 . VAL   B 1 96  ? 42.041 -26.157 10.429 1.00 15.14  ? 102 VAL   C CG1 1 
ATOM   1878 C  CG2 . VAL   B 1 96  ? 42.590 -25.219 12.707 1.00 14.16  ? 102 VAL   C CG2 1 
ATOM   1879 N  N   . GLY   B 1 97  ? 38.526 -25.329 10.143 1.00 13.07  ? 103 GLY   C N   1 
ATOM   1880 C  CA  . GLY   B 1 97  ? 37.474 -25.958 9.341  1.00 14.07  ? 103 GLY   C CA  1 
ATOM   1881 C  C   . GLY   B 1 97  ? 36.802 -24.991 8.421  1.00 13.56  ? 103 GLY   C C   1 
ATOM   1882 O  O   . GLY   B 1 97  ? 37.065 -23.772 8.471  1.00 15.71  ? 103 GLY   C O   1 
ATOM   1883 N  N   . HIS   B 1 98  ? 35.937 -25.499 7.552  1.00 13.66  ? 104 HIS   C N   1 
ATOM   1884 C  CA  . HIS   B 1 98  ? 35.241 -24.683 6.594  1.00 13.46  ? 104 HIS   C CA  1 
ATOM   1885 C  C   . HIS   B 1 98  ? 33.968 -24.033 7.118  1.00 12.90  ? 104 HIS   C C   1 
ATOM   1886 O  O   . HIS   B 1 98  ? 33.143 -24.690 7.794  1.00 12.95  ? 104 HIS   C O   1 
ATOM   1887 C  CB  . HIS   B 1 98  ? 34.950 -25.560 5.387  1.00 15.85  ? 104 HIS   C CB  1 
ATOM   1888 C  CG  . HIS   B 1 98  ? 34.375 -24.774 4.278  1.00 16.73  ? 104 HIS   C CG  1 
ATOM   1889 N  ND1 . HIS   B 1 98  ? 35.124 -23.802 3.611  1.00 20.04  ? 104 HIS   C ND1 1 
ATOM   1890 C  CD2 . HIS   B 1 98  ? 33.104 -24.756 3.808  1.00 19.08  ? 104 HIS   C CD2 1 
ATOM   1891 C  CE1 . HIS   B 1 98  ? 34.278 -23.240 2.766  1.00 21.44  ? 104 HIS   C CE1 1 
ATOM   1892 N  NE2 . HIS   B 1 98  ? 33.064 -23.799 2.832  1.00 21.63  ? 104 HIS   C NE2 1 
ATOM   1893 N  N   . SER   B 1 99  ? 33.749 -22.772 6.749  1.00 12.91  ? 105 SER   C N   1 
ATOM   1894 C  CA  . SER   B 1 99  ? 32.507 -22.033 7.125  1.00 13.65  ? 105 SER   C CA  1 
ATOM   1895 C  C   . SER   B 1 99  ? 32.286 -20.880 6.128  1.00 14.66  ? 105 SER   C C   1 
ATOM   1896 O  O   . SER   B 1 99  ? 33.163 -20.004 6.003  1.00 16.86  ? 105 SER   C O   1 
ATOM   1897 C  CB  . SER   B 1 99  ? 32.724 -21.415 8.508  1.00 15.15  ? 105 SER   C CB  1 
ATOM   1898 O  OG  . SER   B 1 99  ? 31.604 -20.606 8.873  1.00 16.08  ? 105 SER   C OG  1 
ATOM   1899 N  N   . GLU   B 1 100 ? 31.161 -20.863 5.494  1.00 14.64  ? 106 GLU   C N   1 
ATOM   1900 C  CA  . GLU   B 1 100 ? 30.731 -19.787 4.599  1.00 15.80  ? 106 GLU   C CA  1 
ATOM   1901 C  C   . GLU   B 1 100 ? 29.530 -19.133 5.228  1.00 14.32  ? 106 GLU   C C   1 
ATOM   1902 O  O   . GLU   B 1 100 ? 28.936 -19.677 6.157  1.00 13.58  ? 106 GLU   C O   1 
ATOM   1903 C  CB  . GLU   B 1 100 ? 30.243 -20.442 3.303  1.00 19.43  ? 106 GLU   C CB  1 
ATOM   1904 C  CG  . GLU   B 1 100 ? 31.355 -20.983 2.473  1.00 26.44  ? 106 GLU   C CG  1 
ATOM   1905 C  CD  . GLU   B 1 100 ? 30.850 -21.760 1.285  1.00 27.75  ? 106 GLU   C CD  1 
ATOM   1906 O  OE1 . GLU   B 1 100 ? 29.742 -21.488 0.763  1.00 35.12  ? 106 GLU   C OE1 1 
ATOM   1907 O  OE2 . GLU   B 1 100 ? 31.614 -22.639 0.856  1.00 28.40  ? 106 GLU   C OE2 1 
ATOM   1908 N  N   . PRO   B 1 101 ? 29.092 -17.943 4.738  1.00 15.16  ? 107 PRO   C N   1 
ATOM   1909 C  CA  . PRO   B 1 101 ? 27.960 -17.285 5.387  1.00 14.76  ? 107 PRO   C CA  1 
ATOM   1910 C  C   . PRO   B 1 101 ? 26.718 -18.169 5.535  1.00 14.79  ? 107 PRO   C C   1 
ATOM   1911 O  O   . PRO   B 1 101 ? 26.096 -18.100 6.600  1.00 14.75  ? 107 PRO   C O   1 
ATOM   1912 C  CB  . PRO   B 1 101 ? 27.685 -16.058 4.458  1.00 16.18  ? 107 PRO   C CB  1 
ATOM   1913 C  CG  . PRO   B 1 101 ? 28.996 -15.735 3.972  1.00 19.45  ? 107 PRO   C CG  1 
ATOM   1914 C  CD  . PRO   B 1 101 ? 29.743 -17.043 3.750  1.00 17.42  ? 107 PRO   C CD  1 
ATOM   1915 N  N   . GLY   B 1 102 ? 26.408 -19.004 4.531  1.00 13.91  ? 108 GLY   C N   1 
ATOM   1916 C  CA  . GLY   B 1 102 ? 25.197 -19.838 4.600  1.00 14.29  ? 108 GLY   C CA  1 
ATOM   1917 C  C   . GLY   B 1 102 ? 25.293 -20.942 5.659  1.00 12.85  ? 108 GLY   C C   1 
ATOM   1918 O  O   . GLY   B 1 102 ? 24.293 -21.606 5.993  1.00 14.30  ? 108 GLY   C O   1 
ATOM   1919 N  N   . ASP   B 1 103 ? 26.502 -21.194 6.217  1.00 11.93  ? 109 ASP   C N   1 
ATOM   1920 C  CA  . ASP   B 1 103 ? 26.681 -22.206 7.268  1.00 11.14  ? 109 ASP   C CA  1 
ATOM   1921 C  C   . ASP   B 1 103 ? 26.282 -21.707 8.639  1.00 11.45  ? 109 ASP   C C   1 
ATOM   1922 O  O   . ASP   B 1 103 ? 26.188 -22.489 9.594  1.00 10.97  ? 109 ASP   C O   1 
ATOM   1923 C  CB  . ASP   B 1 103 ? 28.150 -22.661 7.309  1.00 12.24  ? 109 ASP   C CB  1 
ATOM   1924 C  CG  . ASP   B 1 103 ? 28.486 -23.449 6.070  1.00 13.56  ? 109 ASP   C CG  1 
ATOM   1925 O  OD1 . ASP   B 1 103 ? 27.639 -24.203 5.606  1.00 14.15  ? 109 ASP   C OD1 1 
ATOM   1926 O  OD2 . ASP   B 1 103 ? 29.619 -23.272 5.526  1.00 14.89  ? 109 ASP   C OD2 1 
ATOM   1927 N  N   . CYS   B 1 104 ? 26.093 -20.377 8.825  1.00 10.74  ? 110 CYS   C N   1 
ATOM   1928 C  CA  . CYS   B 1 104 ? 25.672 -19.850 10.113 1.00 10.60  ? 110 CYS   C CA  1 
ATOM   1929 C  C   . CYS   B 1 104 ? 24.437 -20.551 10.612 1.00 10.60  ? 110 CYS   C C   1 
ATOM   1930 O  O   . CYS   B 1 104 ? 23.486 -20.772 9.853  1.00 12.10  ? 110 CYS   C O   1 
ATOM   1931 C  CB  . CYS   B 1 104 ? 25.447 -18.332 10.034 1.00 10.99  ? 110 CYS   C CB  1 
ATOM   1932 S  SG  . CYS   B 1 104 ? 26.981 -17.363 9.922  1.00 13.41  ? 110 CYS   C SG  1 
ATOM   1933 N  N   . GLY   B 1 105 ? 24.432 -20.904 11.877 1.00 9.65   ? 111 GLY   C N   1 
ATOM   1934 C  CA  . GLY   B 1 105 ? 23.293 -21.578 12.505 1.00 10.59  ? 111 GLY   C CA  1 
ATOM   1935 C  C   . GLY   B 1 105 ? 23.511 -23.078 12.661 1.00 10.09  ? 111 GLY   C C   1 
ATOM   1936 O  O   . GLY   B 1 105 ? 22.733 -23.740 13.368 1.00 11.60  ? 111 GLY   C O   1 
ATOM   1937 N  N   . GLY   B 1 106 ? 24.538 -23.644 11.997 1.00 10.58  ? 112 GLY   C N   1 
ATOM   1938 C  CA  . GLY   B 1 106 ? 24.841 -25.077 12.163 1.00 11.12  ? 112 GLY   C CA  1 
ATOM   1939 C  C   . GLY   B 1 106 ? 25.247 -25.375 13.606 1.00 10.08  ? 112 GLY   C C   1 
ATOM   1940 O  O   . GLY   B 1 106 ? 25.974 -24.581 14.233 1.00 9.88   ? 112 GLY   C O   1 
ATOM   1941 N  N   . ILE   B 1 107 ? 24.813 -26.510 14.121 1.00 9.60   ? 113 ILE   C N   1 
ATOM   1942 C  CA  . ILE   B 1 107 ? 25.081 -26.835 15.513 1.00 9.60   ? 113 ILE   C CA  1 
ATOM   1943 C  C   . ILE   B 1 107 ? 26.457 -27.448 15.708 1.00 9.22   ? 113 ILE   C C   1 
ATOM   1944 O  O   . ILE   B 1 107 ? 26.882 -28.300 14.923 1.00 9.10   ? 113 ILE   C O   1 
ATOM   1945 C  CB  . ILE   B 1 107 ? 23.953 -27.803 16.025 1.00 11.77  ? 113 ILE   C CB  1 
ATOM   1946 C  CG1 . ILE   B 1 107 ? 22.717 -26.829 16.460 1.00 15.63  ? 113 ILE   C CG1 1 
ATOM   1947 C  CG2 . ILE   B 1 107 ? 24.398 -28.652 17.241 1.00 12.16  ? 113 ILE   C CG2 1 
ATOM   1948 C  CD1 . ILE   B 1 107 ? 21.388 -27.528 16.834 1.00 20.32  ? 113 ILE   C CD1 1 
ATOM   1949 N  N   . LEU   B 1 108 ? 27.114 -27.024 16.800 1.00 8.60   ? 114 LEU   C N   1 
ATOM   1950 C  CA  . LEU   B 1 108 ? 28.302 -27.679 17.369 1.00 8.48   ? 114 LEU   C CA  1 
ATOM   1951 C  C   . LEU   B 1 108 ? 27.797 -28.445 18.609 1.00 8.81   ? 114 LEU   C C   1 
ATOM   1952 O  O   . LEU   B 1 108 ? 27.139 -27.845 19.480 1.00 8.92   ? 114 LEU   C O   1 
ATOM   1953 C  CB  . LEU   B 1 108 ? 29.334 -26.616 17.798 1.00 9.21   ? 114 LEU   C CB  1 
ATOM   1954 C  CG  . LEU   B 1 108 ? 30.555 -27.135 18.576 1.00 9.77   ? 114 LEU   C CG  1 
ATOM   1955 C  CD1 . LEU   B 1 108 ? 31.421 -28.038 17.715 1.00 10.43  ? 114 LEU   C CD1 1 
ATOM   1956 C  CD2 . LEU   B 1 108 ? 31.363 -25.943 19.110 1.00 11.08  ? 114 LEU   C CD2 1 
ATOM   1957 N  N   . ARG   B 1 109 ? 28.092 -29.760 18.679 1.00 8.63   ? 115 ARG   C N   1 
ATOM   1958 C  CA  . ARG   B 1 109 ? 27.629 -30.567 19.830 1.00 9.07   ? 115 ARG   C CA  1 
ATOM   1959 C  C   . ARG   B 1 109 ? 28.786 -31.378 20.386 1.00 9.84   ? 115 ARG   C C   1 
ATOM   1960 O  O   . ARG   B 1 109 ? 29.696 -31.808 19.660 1.00 10.50  ? 115 ARG   C O   1 
ATOM   1961 C  CB  . ARG   B 1 109 ? 26.470 -31.486 19.385 1.00 12.44  ? 115 ARG   C CB  1 
ATOM   1962 C  CG  . ARG   B 1 109 ? 26.905 -32.489 18.337 1.00 15.75  ? 115 ARG   C CG  1 
ATOM   1963 C  CD  . ARG   B 1 109 ? 25.763 -33.390 17.862 1.00 19.83  ? 115 ARG   C CD  1 
ATOM   1964 N  NE  . ARG   B 1 109 ? 24.896 -32.638 16.959 1.00 24.74  ? 115 ARG   C NE  1 
ATOM   1965 C  CZ  . ARG   B 1 109 ? 23.582 -32.545 17.091 1.00 33.06  ? 115 ARG   C CZ  1 
ATOM   1966 N  NH1 . ARG   B 1 109 ? 22.970 -33.120 18.119 1.00 36.61  ? 115 ARG   C NH1 1 
ATOM   1967 N  NH2 . ARG   B 1 109 ? 22.866 -31.860 16.205 1.00 35.45  ? 115 ARG   C NH2 1 
ATOM   1968 N  N   . CYS   B 1 110 ? 28.685 -31.641 21.688 1.00 10.06  ? 116 CYS   C N   1 
ATOM   1969 C  CA  . CYS   B 1 110 ? 29.666 -32.517 22.393 1.00 10.81  ? 116 CYS   C CA  1 
ATOM   1970 C  C   . CYS   B 1 110 ? 28.803 -33.630 23.067 1.00 12.20  ? 116 CYS   C C   1 
ATOM   1971 O  O   . CYS   B 1 110 ? 27.565 -33.733 22.882 1.00 12.12  ? 116 CYS   C O   1 
ATOM   1972 C  CB  . CYS   B 1 110 ? 30.454 -31.709 23.427 1.00 10.67  ? 116 CYS   C CB  1 
ATOM   1973 S  SG  . CYS   B 1 110 ? 29.406 -31.087 24.789 1.00 11.07  ? 116 CYS   C SG  1 
ATOM   1974 N  N   . GLN   B 1 111 ? 29.444 -34.456 23.912 1.00 12.84  ? 117 GLN   C N   1 
ATOM   1975 C  CA  . GLN   B 1 111 ? 28.689 -35.501 24.613 1.00 14.51  ? 117 GLN   C CA  1 
ATOM   1976 C  C   . GLN   B 1 111 ? 27.601 -34.976 25.531 1.00 14.55  ? 117 GLN   C C   1 
ATOM   1977 O  O   . GLN   B 1 111 ? 26.664 -35.718 25.871 1.00 16.56  ? 117 GLN   C O   1 
ATOM   1978 C  CB  . GLN   B 1 111 ? 29.621 -36.439 25.435 1.00 15.74  ? 117 GLN   C CB  1 
ATOM   1979 C  CG  . GLN   B 1 111 ? 30.306 -35.736 26.595 1.00 17.31  ? 117 GLN   C CG  1 
ATOM   1980 C  CD  . GLN   B 1 111 ? 31.197 -36.673 27.368 1.00 28.02  ? 117 GLN   C CD  1 
ATOM   1981 O  OE1 . GLN   B 1 111 ? 32.401 -36.737 27.129 1.00 31.13  ? 117 GLN   C OE1 1 
ATOM   1982 N  NE2 . GLN   B 1 111 ? 30.608 -37.399 28.299 1.00 28.68  ? 117 GLN   C NE2 1 
ATOM   1983 N  N   . HIS   B 1 112 ? 27.674 -33.695 25.949 1.00 12.56  ? 118 HIS   C N   1 
ATOM   1984 C  CA  . HIS   B 1 112 ? 26.698 -33.142 26.879 1.00 12.74  ? 118 HIS   C CA  1 
ATOM   1985 C  C   . HIS   B 1 112 ? 25.524 -32.432 26.217 1.00 13.58  ? 118 HIS   C C   1 
ATOM   1986 O  O   . HIS   B 1 112 ? 24.573 -32.031 26.914 1.00 14.98  ? 118 HIS   C O   1 
ATOM   1987 C  CB  . HIS   B 1 112 ? 27.415 -32.164 27.803 1.00 13.72  ? 118 HIS   C CB  1 
ATOM   1988 C  CG  . HIS   B 1 112 ? 28.596 -32.777 28.517 1.00 12.86  ? 118 HIS   C CG  1 
ATOM   1989 N  ND1 . HIS   B 1 112 ? 29.910 -32.499 28.157 1.00 11.82  ? 118 HIS   C ND1 1 
ATOM   1990 C  CD2 . HIS   B 1 112 ? 28.614 -33.595 29.608 1.00 15.72  ? 118 HIS   C CD2 1 
ATOM   1991 C  CE1 . HIS   B 1 112 ? 30.679 -33.198 28.979 1.00 14.31  ? 118 HIS   C CE1 1 
ATOM   1992 N  NE2 . HIS   B 1 112 ? 29.940 -33.872 29.857 1.00 16.83  ? 118 HIS   C NE2 1 
ATOM   1993 N  N   . GLY   B 1 113 ? 25.603 -32.172 24.896 1.00 12.36  ? 119 GLY   C N   1 
ATOM   1994 C  CA  . GLY   B 1 113 ? 24.537 -31.487 24.185 1.00 12.49  ? 119 GLY   C CA  1 
ATOM   1995 C  C   . GLY   B 1 113 ? 25.054 -30.437 23.233 1.00 10.90  ? 119 GLY   C C   1 
ATOM   1996 O  O   . GLY   B 1 113 ? 26.188 -30.512 22.746 1.00 11.14  ? 119 GLY   C O   1 
ATOM   1997 N  N   . VAL   B 1 114 ? 24.202 -29.425 22.986 1.00 11.01  ? 120 VAL   C N   1 
ATOM   1998 C  CA  . VAL   B 1 114 ? 24.542 -28.366 22.039 1.00 10.59  ? 120 VAL   C CA  1 
ATOM   1999 C  C   . VAL   B 1 114 ? 25.468 -27.368 22.734 1.00 10.31  ? 120 VAL   C C   1 
ATOM   2000 O  O   . VAL   B 1 114 ? 25.143 -26.796 23.794 1.00 11.01  ? 120 VAL   C O   1 
ATOM   2001 C  CB  . VAL   B 1 114 ? 23.245 -27.668 21.570 1.00 10.96  ? 120 VAL   C CB  1 
ATOM   2002 C  CG1 . VAL   B 1 114 ? 23.568 -26.449 20.688 1.00 12.61  ? 120 VAL   C CG1 1 
ATOM   2003 C  CG2 . VAL   B 1 114 ? 22.325 -28.649 20.824 1.00 12.67  ? 120 VAL   C CG2 1 
ATOM   2004 N  N   . VAL   B 1 115 ? 26.596 -27.098 22.109 1.00 9.40   ? 121 VAL   C N   1 
ATOM   2005 C  CA  . VAL   B 1 115 ? 27.611 -26.158 22.618 1.00 10.26  ? 121 VAL   C CA  1 
ATOM   2006 C  C   . VAL   B 1 115 ? 27.397 -24.742 22.107 1.00 10.56  ? 121 VAL   C C   1 
ATOM   2007 O  O   . VAL   B 1 115 ? 27.614 -23.752 22.834 1.00 10.92  ? 121 VAL   C O   1 
ATOM   2008 C  CB  . VAL   B 1 115 ? 29.025 -26.667 22.228 1.00 9.99   ? 121 VAL   C CB  1 
ATOM   2009 C  CG1 . VAL   B 1 115 ? 30.099 -25.667 22.622 1.00 11.82  ? 121 VAL   C CG1 1 
ATOM   2010 C  CG2 . VAL   B 1 115 ? 29.301 -28.056 22.817 1.00 11.63  ? 121 VAL   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 116 ? 27.007 -24.636 20.827 1.00 9.74   ? 122 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 116 ? 26.817 -23.323 20.210 1.00 11.14  ? 122 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 116 ? 26.494 -23.501 18.736 1.00 9.42   ? 122 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 116 ? 26.168 -24.611 18.290 1.00 9.87   ? 122 GLY   C O   1 
ATOM   2015 N  N   . ILE   B 1 117 ? 26.477 -22.356 18.002 1.00 9.15   ? 123 ILE   C N   1 
ATOM   2016 C  CA  . ILE   B 1 117 ? 26.117 -22.375 16.592 1.00 9.58   ? 123 ILE   C CA  1 
ATOM   2017 C  C   . ILE   B 1 117 ? 27.169 -21.651 15.787 1.00 9.58   ? 123 ILE   C C   1 
ATOM   2018 O  O   . ILE   B 1 117 ? 27.812 -20.687 16.262 1.00 10.19  ? 123 ILE   C O   1 
ATOM   2019 C  CB  . ILE   B 1 117 ? 24.701 -21.735 16.308 1.00 10.33  ? 123 ILE   C CB  1 
ATOM   2020 C  CG1 . ILE   B 1 117 ? 24.602 -20.355 16.966 1.00 11.96  ? 123 ILE   C CG1 1 
ATOM   2021 C  CG2 . ILE   B 1 117 ? 23.586 -22.696 16.745 1.00 12.17  ? 123 ILE   C CG2 1 
ATOM   2022 C  CD1 . ILE   B 1 117 ? 23.244 -19.577 16.525 1.00 12.25  ? 123 ILE   C CD1 1 
ATOM   2023 N  N   . VAL   B 1 118 ? 27.353 -22.074 14.531 1.00 9.03   ? 124 VAL   C N   1 
ATOM   2024 C  CA  . VAL   B 1 118 ? 28.296 -21.390 13.631 1.00 9.13   ? 124 VAL   C CA  1 
ATOM   2025 C  C   . VAL   B 1 118 ? 27.903 -19.905 13.512 1.00 9.94   ? 124 VAL   C C   1 
ATOM   2026 O  O   . VAL   B 1 118 ? 26.706 -19.568 13.284 1.00 9.83   ? 124 VAL   C O   1 
ATOM   2027 C  CB  . VAL   B 1 118 ? 28.278 -22.047 12.233 1.00 9.51   ? 124 VAL   C CB  1 
ATOM   2028 C  CG1 . VAL   B 1 118 ? 29.125 -21.284 11.226 1.00 10.65  ? 124 VAL   C CG1 1 
ATOM   2029 C  CG2 . VAL   B 1 118 ? 28.752 -23.494 12.280 1.00 10.58  ? 124 VAL   C CG2 1 
ATOM   2030 N  N   . SER   B 1 119 ? 28.917 -19.039 13.596 1.00 9.79   ? 125 SER   C N   1 
ATOM   2031 C  CA  . SER   B 1 119 ? 28.717 -17.576 13.474 1.00 10.25  ? 125 SER   C CA  1 
ATOM   2032 C  C   . SER   B 1 119 ? 29.736 -16.894 12.558 1.00 11.68  ? 125 SER   C C   1 
ATOM   2033 O  O   . SER   B 1 119 ? 29.414 -15.803 12.037 1.00 11.59  ? 125 SER   C O   1 
ATOM   2034 C  CB  . SER   B 1 119 ? 28.750 -16.979 14.879 1.00 11.35  ? 125 SER   C CB  1 
ATOM   2035 O  OG  . SER   B 1 119 ? 28.637 -15.553 14.854 1.00 12.57  ? 125 SER   C OG  1 
ATOM   2036 N  N   . THR   B 1 120 ? 30.994 -17.399 12.460 1.00 11.27  ? 126 THR   C N   1 
ATOM   2037 C  CA  . THR   B 1 120 ? 32.023 -16.729 11.654 1.00 11.21  ? 126 THR   C CA  1 
ATOM   2038 C  C   . THR   B 1 120 ? 32.716 -17.735 10.743 1.00 10.65  ? 126 THR   C C   1 
ATOM   2039 O  O   . THR   B 1 120 ? 32.662 -18.966 10.988 1.00 10.86  ? 126 THR   C O   1 
ATOM   2040 C  CB  . THR   B 1 120 ? 33.077 -16.012 12.556 1.00 11.86  ? 126 THR   C CB  1 
ATOM   2041 O  OG1 . THR   B 1 120 ? 33.916 -16.963 13.216 1.00 12.11  ? 126 THR   C OG1 1 
ATOM   2042 C  CG2 . THR   B 1 120 ? 32.449 -15.057 13.561 1.00 13.30  ? 126 THR   C CG2 1 
ATOM   2043 N  N   . GLY   B 1 121 ? 33.413 -17.236 9.757  1.00 11.92  ? 127 GLY   C N   1 
ATOM   2044 C  CA  . GLY   B 1 121 ? 34.236 -18.066 8.885  1.00 14.29  ? 127 GLY   C CA  1 
ATOM   2045 C  C   . GLY   B 1 121 ? 35.253 -17.212 8.140  1.00 15.84  ? 127 GLY   C C   1 
ATOM   2046 O  O   . GLY   B 1 121 ? 34.944 -16.111 7.691  1.00 19.24  ? 127 GLY   C O   1 
ATOM   2047 N  N   . GLY   B 1 122 ? 36.454 -17.692 7.955  1.00 18.89  ? 128 GLY   C N   1 
ATOM   2048 C  CA  . GLY   B 1 122 ? 37.506 -16.940 7.254  1.00 20.91  ? 128 GLY   C CA  1 
ATOM   2049 C  C   . GLY   B 1 122 ? 38.831 -17.582 7.518  1.00 21.61  ? 128 GLY   C C   1 
ATOM   2050 O  O   . GLY   B 1 122 ? 39.053 -18.124 8.593  1.00 21.61  ? 128 GLY   C O   1 
ATOM   2051 N  N   . ASN   B 1 123 ? 39.775 -17.456 6.571  1.00 20.17  ? 129 ASN   C N   1 
ATOM   2052 C  CA  . ASN   B 1 123 ? 41.152 -17.915 6.722  1.00 20.41  ? 129 ASN   C CA  1 
ATOM   2053 C  C   . ASN   B 1 123 ? 41.220 -19.381 7.132  1.00 18.81  ? 129 ASN   C C   1 
ATOM   2054 O  O   . ASN   B 1 123 ? 42.157 -19.761 7.844  1.00 22.32  ? 129 ASN   C O   1 
ATOM   2055 C  CB  . ASN   B 1 123 ? 41.967 -17.006 7.727  1.00 23.26  ? 129 ASN   C CB  1 
ATOM   2056 C  CG  . ASN   B 1 123 ? 42.726 -15.852 7.095  1.00 29.37  ? 129 ASN   C CG  1 
ATOM   2057 O  OD1 . ASN   B 1 123 ? 43.118 -15.883 5.923  1.00 31.09  ? 129 ASN   C OD1 1 
ATOM   2058 N  ND2 . ASN   B 1 123 ? 42.956 -14.784 7.847  1.00 31.55  ? 129 ASN   C ND2 1 
ATOM   2059 N  N   . GLY   B 1 124 ? 40.260 -20.208 6.693  1.00 17.81  ? 130 GLY   C N   1 
ATOM   2060 C  CA  . GLY   B 1 124 ? 40.281 -21.635 7.074  1.00 16.63  ? 130 GLY   C CA  1 
ATOM   2061 C  C   . GLY   B 1 124 ? 39.882 -21.930 8.507  1.00 14.21  ? 130 GLY   C C   1 
ATOM   2062 O  O   . GLY   B 1 124 ? 40.182 -23.020 9.024  1.00 14.49  ? 130 GLY   C O   1 
ATOM   2063 N  N   . LEU   B 1 125 ? 39.245 -20.985 9.138  1.00 12.62  ? 131 LEU   C N   1 
ATOM   2064 C  CA  . LEU   B 1 125 ? 38.772 -21.112 10.518 1.00 12.56  ? 131 LEU   C CA  1 
ATOM   2065 C  C   . LEU   B 1 125 ? 37.251 -20.999 10.556 1.00 13.10  ? 131 LEU   C C   1 
ATOM   2066 O  O   . LEU   B 1 125 ? 36.655 -20.245 9.753  1.00 15.94  ? 131 LEU   C O   1 
ATOM   2067 C  CB  . LEU   B 1 125 ? 39.409 -20.035 11.433 1.00 15.06  ? 131 LEU   C CB  1 
ATOM   2068 C  CG  . LEU   B 1 125 ? 40.947 -20.105 11.507 1.00 17.51  ? 131 LEU   C CG  1 
ATOM   2069 C  CD1 . LEU   B 1 125 ? 41.583 -18.764 11.929 1.00 21.41  ? 131 LEU   C CD1 1 
ATOM   2070 C  CD2 . LEU   B 1 125 ? 41.414 -21.225 12.349 1.00 18.45  ? 131 LEU   C CD2 1 
ATOM   2071 N  N   . VAL   B 1 126 ? 36.620 -21.705 11.449 1.00 11.07  ? 132 VAL   C N   1 
ATOM   2072 C  CA  . VAL   B 1 126 ? 35.178 -21.600 11.695 1.00 10.34  ? 132 VAL   C CA  1 
ATOM   2073 C  C   . VAL   B 1 126 ? 35.018 -21.127 13.138 1.00 9.76   ? 132 VAL   C C   1 
ATOM   2074 O  O   . VAL   B 1 126 ? 35.686 -21.661 14.054 1.00 10.99  ? 132 VAL   C O   1 
ATOM   2075 C  CB  . VAL   B 1 126 ? 34.444 -22.935 11.449 1.00 10.45  ? 132 VAL   C CB  1 
ATOM   2076 C  CG1 . VAL   B 1 126 ? 35.053 -24.138 12.122 1.00 12.87  ? 132 VAL   C CG1 1 
ATOM   2077 C  CG2 . VAL   B 1 126 ? 32.953 -22.834 11.794 1.00 11.75  ? 132 VAL   C CG2 1 
ATOM   2078 N  N   . GLY   B 1 127 ? 34.124 -20.168 13.337 1.00 9.89   ? 133 GLY   C N   1 
ATOM   2079 C  CA  . GLY   B 1 127 ? 33.861 -19.676 14.687 1.00 10.01  ? 133 GLY   C CA  1 
ATOM   2080 C  C   . GLY   B 1 127 ? 32.430 -19.975 15.129 1.00 9.65   ? 133 GLY   C C   1 
ATOM   2081 O  O   . GLY   B 1 127 ? 31.479 -19.871 14.319 1.00 10.25  ? 133 GLY   C O   1 
ATOM   2082 N  N   . PHE   B 1 128 ? 32.298 -20.362 16.383 1.00 9.43   ? 134 PHE   C N   1 
ATOM   2083 C  CA  . PHE   B 1 128 ? 31.021 -20.740 17.024 1.00 9.55   ? 134 PHE   C CA  1 
ATOM   2084 C  C   . PHE   B 1 128 ? 30.672 -19.800 18.159 1.00 9.31   ? 134 PHE   C C   1 
ATOM   2085 O  O   . PHE   B 1 128 ? 31.533 -19.528 19.004 1.00 10.28  ? 134 PHE   C O   1 
ATOM   2086 C  CB  . PHE   B 1 128 ? 31.087 -22.171 17.596 1.00 9.98   ? 134 PHE   C CB  1 
ATOM   2087 C  CG  . PHE   B 1 128 ? 31.630 -23.182 16.590 1.00 9.59   ? 134 PHE   C CG  1 
ATOM   2088 C  CD1 . PHE   B 1 128 ? 30.781 -23.785 15.653 1.00 9.82   ? 134 PHE   C CD1 1 
ATOM   2089 C  CD2 . PHE   B 1 128 ? 32.974 -23.554 16.607 1.00 10.70  ? 134 PHE   C CD2 1 
ATOM   2090 C  CE1 . PHE   B 1 128 ? 31.265 -24.737 14.767 1.00 10.32  ? 134 PHE   C CE1 1 
ATOM   2091 C  CE2 . PHE   B 1 128 ? 33.459 -24.510 15.700 1.00 11.18  ? 134 PHE   C CE2 1 
ATOM   2092 C  CZ  . PHE   B 1 128 ? 32.609 -25.080 14.798 1.00 10.81  ? 134 PHE   C CZ  1 
ATOM   2093 N  N   . ALA   B 1 129 ? 29.431 -19.311 18.161 1.00 9.85   ? 135 ALA   C N   1 
ATOM   2094 C  CA  . ALA   B 1 129 ? 28.926 -18.507 19.268 1.00 10.29  ? 135 ALA   C CA  1 
ATOM   2095 C  C   . ALA   B 1 129 ? 28.539 -19.508 20.395 1.00 9.89   ? 135 ALA   C C   1 
ATOM   2096 O  O   . ALA   B 1 129 ? 27.620 -20.339 20.232 1.00 10.62  ? 135 ALA   C O   1 
ATOM   2097 C  CB  . ALA   B 1 129 ? 27.689 -17.729 18.804 1.00 11.04  ? 135 ALA   C CB  1 
ATOM   2098 N  N   . ASP   B 1 130 ? 29.213 -19.414 21.548 1.00 9.96   ? 136 ASP   C N   1 
ATOM   2099 C  CA  . ASP   B 1 130 ? 28.919 -20.282 22.693 1.00 10.43  ? 136 ASP   C CA  1 
ATOM   2100 C  C   . ASP   B 1 130 ? 27.575 -19.962 23.277 1.00 10.93  ? 136 ASP   C C   1 
ATOM   2101 O  O   . ASP   B 1 130 ? 27.183 -18.769 23.367 1.00 11.47  ? 136 ASP   C O   1 
ATOM   2102 C  CB  . ASP   B 1 130 ? 29.994 -20.063 23.781 1.00 11.92  ? 136 ASP   C CB  1 
ATOM   2103 C  CG  . ASP   B 1 130 ? 29.897 -20.996 24.971 1.00 13.73  ? 136 ASP   C CG  1 
ATOM   2104 O  OD1 . ASP   B 1 130 ? 29.770 -22.212 24.769 1.00 13.79  ? 136 ASP   C OD1 1 
ATOM   2105 O  OD2 . ASP   B 1 130 ? 29.810 -20.484 26.113 1.00 17.71  ? 136 ASP   C OD2 1 
ATOM   2106 N  N   . VAL   B 1 131 ? 26.877 -20.987 23.789 1.00 10.74  ? 137 VAL   C N   1 
ATOM   2107 C  CA  . VAL   B 1 131 ? 25.623 -20.811 24.544 1.00 10.85  ? 137 VAL   C CA  1 
ATOM   2108 C  C   . VAL   B 1 131 ? 25.692 -21.480 25.913 1.00 12.03  ? 137 VAL   C C   1 
ATOM   2109 O  O   . VAL   B 1 131 ? 24.709 -21.419 26.660 1.00 12.26  ? 137 VAL   C O   1 
ATOM   2110 C  CB  . VAL   B 1 131 ? 24.356 -21.280 23.782 1.00 11.50  ? 137 VAL   C CB  1 
ATOM   2111 C  CG1 . VAL   B 1 131 ? 24.197 -20.455 22.491 1.00 12.10  ? 137 VAL   C CG1 1 
ATOM   2112 C  CG2 . VAL   B 1 131 ? 24.388 -22.755 23.467 1.00 12.37  ? 137 VAL   C CG2 1 
ATOM   2113 N  N   . ARG   B 1 132 ? 26.824 -22.125 26.286 1.00 11.45  ? 138 ARG   C N   1 
ATOM   2114 C  CA  . ARG   B 1 132 ? 26.886 -22.915 27.522 1.00 11.37  ? 138 ARG   C CA  1 
ATOM   2115 C  C   . ARG   B 1 132 ? 26.831 -22.089 28.780 1.00 11.82  ? 138 ARG   C C   1 
ATOM   2116 O  O   . ARG   B 1 132 ? 26.494 -22.643 29.850 1.00 14.03  ? 138 ARG   C O   1 
ATOM   2117 C  CB  . ARG   B 1 132 ? 28.142 -23.758 27.521 1.00 11.24  ? 138 ARG   C CB  1 
ATOM   2118 C  CG  . ARG   B 1 132 ? 28.144 -24.835 26.382 1.00 11.39  ? 138 ARG   C CG  1 
ATOM   2119 C  CD  . ARG   B 1 132 ? 29.465 -25.591 26.436 1.00 11.29  ? 138 ARG   C CD  1 
ATOM   2120 N  NE  . ARG   B 1 132 ? 30.559 -24.698 26.026 1.00 11.56  ? 138 ARG   C NE  1 
ATOM   2121 C  CZ  . ARG   B 1 132 ? 31.816 -25.069 25.875 1.00 11.96  ? 138 ARG   C CZ  1 
ATOM   2122 N  NH1 . ARG   B 1 132 ? 32.194 -26.310 26.197 1.00 12.34  ? 138 ARG   C NH1 1 
ATOM   2123 N  NH2 . ARG   B 1 132 ? 32.713 -24.211 25.381 1.00 12.16  ? 138 ARG   C NH2 1 
ATOM   2124 N  N   . ASP   B 1 133 ? 27.127 -20.799 28.713 1.00 11.65  ? 139 ASP   C N   1 
ATOM   2125 C  CA  . ASP   B 1 133 ? 27.052 -19.920 29.880 1.00 13.11  ? 139 ASP   C CA  1 
ATOM   2126 C  C   . ASP   B 1 133 ? 25.634 -19.360 30.104 1.00 13.79  ? 139 ASP   C C   1 
ATOM   2127 O  O   . ASP   B 1 133 ? 25.410 -18.721 31.144 1.00 15.35  ? 139 ASP   C O   1 
ATOM   2128 C  CB  . ASP   B 1 133 ? 28.034 -18.723 29.727 1.00 15.11  ? 139 ASP   C CB  1 
ATOM   2129 C  CG  . ASP   B 1 133 ? 27.663 -17.812 28.577 1.00 15.63  ? 139 ASP   C CG  1 
ATOM   2130 O  OD1 . ASP   B 1 133 ? 27.294 -18.327 27.504 1.00 15.86  ? 139 ASP   C OD1 1 
ATOM   2131 O  OD2 . ASP   B 1 133 ? 27.706 -16.542 28.762 1.00 18.57  ? 139 ASP   C OD2 1 
ATOM   2132 N  N   . LEU   B 1 134 ? 24.679 -19.572 29.168 1.00 12.94  ? 140 LEU   C N   1 
ATOM   2133 C  CA  . LEU   B 1 134 ? 23.324 -19.002 29.245 1.00 13.46  ? 140 LEU   C CA  1 
ATOM   2134 C  C   . LEU   B 1 134 ? 22.471 -19.989 30.026 1.00 13.28  ? 140 LEU   C C   1 
ATOM   2135 O  O   . LEU   B 1 134 ? 21.668 -20.729 29.480 1.00 13.28  ? 140 LEU   C O   1 
ATOM   2136 C  CB  . LEU   B 1 134 ? 22.767 -18.751 27.837 1.00 13.03  ? 140 LEU   C CB  1 
ATOM   2137 C  CG  . LEU   B 1 134 ? 23.623 -17.795 26.970 1.00 13.23  ? 140 LEU   C CG  1 
ATOM   2138 C  CD1 . LEU   B 1 134 ? 23.033 -17.744 25.520 1.00 14.08  ? 140 LEU   C CD1 1 
ATOM   2139 C  CD2 . LEU   B 1 134 ? 23.736 -16.394 27.603 1.00 14.82  ? 140 LEU   C CD2 1 
ATOM   2140 N  N   . LEU   B 1 135 ? 22.687 -20.031 31.364 1.00 14.11  ? 141 LEU   C N   1 
ATOM   2141 C  CA  . LEU   B 1 135 ? 22.055 -21.075 32.192 1.00 14.63  ? 141 LEU   C CA  1 
ATOM   2142 C  C   . LEU   B 1 135 ? 20.544 -20.980 32.243 1.00 14.82  ? 141 LEU   C C   1 
ATOM   2143 O  O   . LEU   B 1 135 ? 19.859 -21.989 32.436 1.00 16.07  ? 141 LEU   C O   1 
ATOM   2144 C  CB  . LEU   B 1 135 ? 22.628 -21.063 33.626 1.00 14.89  ? 141 LEU   C CB  1 
ATOM   2145 C  CG  . LEU   B 1 135 ? 24.175 -21.066 33.716 1.00 15.24  ? 141 LEU   C CG  1 
ATOM   2146 C  CD1 . LEU   B 1 135 ? 24.677 -21.126 35.194 1.00 17.34  ? 141 LEU   C CD1 1 
ATOM   2147 C  CD2 . LEU   B 1 135 ? 24.817 -22.220 32.916 1.00 15.94  ? 141 LEU   C CD2 1 
ATOM   2148 N  N   . TRP   B 1 136 ? 20.021 -19.766 32.046 1.00 14.19  ? 142 TRP   C N   1 
ATOM   2149 C  CA  . TRP   B 1 136 ? 18.576 -19.519 32.088 1.00 15.32  ? 142 TRP   C CA  1 
ATOM   2150 C  C   . TRP   B 1 136 ? 17.845 -20.213 30.934 1.00 16.14  ? 142 TRP   C C   1 
ATOM   2151 O  O   . TRP   B 1 136 ? 16.622 -20.355 30.975 1.00 17.46  ? 142 TRP   C O   1 
ATOM   2152 C  CB  . TRP   B 1 136 ? 18.299 -18.002 32.076 1.00 15.52  ? 142 TRP   C CB  1 
ATOM   2153 C  CG  . TRP   B 1 136 ? 18.987 -17.257 30.973 1.00 15.27  ? 142 TRP   C CG  1 
ATOM   2154 C  CD1 . TRP   B 1 136 ? 20.161 -16.572 31.056 1.00 15.92  ? 142 TRP   C CD1 1 
ATOM   2155 C  CD2 . TRP   B 1 136 ? 18.484 -17.035 29.634 1.00 14.83  ? 142 TRP   C CD2 1 
ATOM   2156 N  NE1 . TRP   B 1 136 ? 20.449 -15.974 29.839 1.00 16.67  ? 142 TRP   C NE1 1 
ATOM   2157 C  CE2 . TRP   B 1 136 ? 19.420 -16.231 28.961 1.00 15.72  ? 142 TRP   C CE2 1 
ATOM   2158 C  CE3 . TRP   B 1 136 ? 17.332 -17.422 28.972 1.00 14.90  ? 142 TRP   C CE3 1 
ATOM   2159 C  CZ2 . TRP   B 1 136 ? 19.242 -15.831 27.621 1.00 16.05  ? 142 TRP   C CZ2 1 
ATOM   2160 C  CZ3 . TRP   B 1 136 ? 17.123 -16.976 27.677 1.00 15.98  ? 142 TRP   C CZ3 1 
ATOM   2161 C  CH2 . TRP   B 1 136 ? 18.096 -16.233 27.006 1.00 16.24  ? 142 TRP   C CH2 1 
ATOM   2162 N  N   . LEU   B 1 137 ? 18.544 -20.653 29.869 1.00 14.89  ? 143 LEU   C N   1 
ATOM   2163 C  CA  . LEU   B 1 137 ? 17.865 -21.423 28.803 1.00 15.37  ? 143 LEU   C CA  1 
ATOM   2164 C  C   . LEU   B 1 137 ? 17.249 -22.720 29.367 1.00 18.19  ? 143 LEU   C C   1 
ATOM   2165 O  O   . LEU   B 1 137 ? 16.330 -23.265 28.748 1.00 19.93  ? 143 LEU   C O   1 
ATOM   2166 C  CB  . LEU   B 1 137 ? 18.835 -21.783 27.659 1.00 14.24  ? 143 LEU   C CB  1 
ATOM   2167 C  CG  . LEU   B 1 137 ? 19.274 -20.593 26.798 1.00 13.33  ? 143 LEU   C CG  1 
ATOM   2168 C  CD1 . LEU   B 1 137 ? 20.421 -20.994 25.870 1.00 15.22  ? 143 LEU   C CD1 1 
ATOM   2169 C  CD2 . LEU   B 1 137 ? 18.118 -20.047 25.931 1.00 15.57  ? 143 LEU   C CD2 1 
ATOM   2170 N  N   . ASP   B 1 138 ? 17.781 -23.225 30.523 1.00 16.45  ? 144 ASP   C N   1 
ATOM   2171 C  CA  . ASP   B 1 138 ? 17.342 -24.507 31.118 1.00 18.92  ? 144 ASP   C CA  1 
ATOM   2172 C  C   . ASP   B 1 138 ? 16.088 -24.385 31.983 1.00 21.61  ? 144 ASP   C C   1 
ATOM   2173 O  O   . ASP   B 1 138 ? 15.659 -25.408 32.544 1.00 23.57  ? 144 ASP   C O   1 
ATOM   2174 C  CB  . ASP   B 1 138 ? 18.454 -25.155 31.982 1.00 19.73  ? 144 ASP   C CB  1 
ATOM   2175 C  CG  . ASP   B 1 138 ? 19.697 -25.566 31.208 1.00 19.96  ? 144 ASP   C CG  1 
ATOM   2176 O  OD1 . ASP   B 1 138 ? 19.652 -25.579 29.962 1.00 20.23  ? 144 ASP   C OD1 1 
ATOM   2177 O  OD2 . ASP   B 1 138 ? 20.728 -25.879 31.865 1.00 23.30  ? 144 ASP   C OD2 1 
ATOM   2178 N  N   . GLU   B 1 139 ? 15.536 -23.181 32.148 1.00 21.86  ? 145 GLU   C N   1 
ATOM   2179 C  CA  . GLU   B 1 139 ? 14.380 -22.990 33.027 1.00 26.82  ? 145 GLU   C CA  1 
ATOM   2180 C  C   . GLU   B 1 139 ? 13.350 -22.002 32.450 1.00 31.68  ? 145 GLU   C C   1 
ATOM   2181 O  O   . GLU   B 1 139 ? 13.607 -21.350 31.449 1.00 32.49  ? 145 GLU   C O   1 
ATOM   2182 C  CB  . GLU   B 1 139 ? 14.904 -22.505 34.389 1.00 31.97  ? 145 GLU   C CB  1 
ATOM   2183 C  CG  . GLU   B 1 139 ? 15.607 -21.165 34.290 1.00 40.25  ? 145 GLU   C CG  1 
ATOM   2184 C  CD  . GLU   B 1 139 ? 16.602 -20.850 35.390 1.00 49.79  ? 145 GLU   C CD  1 
ATOM   2185 O  OE1 . GLU   B 1 139 ? 17.095 -19.699 35.432 1.00 51.77  ? 145 GLU   C OE1 1 
ATOM   2186 O  OE2 . GLU   B 1 139 ? 16.881 -21.751 36.215 1.00 52.74  ? 145 GLU   C OE2 1 
ATOM   2187 N  N   . GLU   B 1 140 ? 12.188 -21.877 33.125 1.00 35.20  ? 146 GLU   C N   1 
ATOM   2188 C  CA  . GLU   B 1 140 ? 11.075 -20.938 32.879 1.00 38.88  ? 146 GLU   C CA  1 
ATOM   2189 C  C   . GLU   B 1 140 ? 11.118 -20.156 31.595 1.00 40.85  ? 146 GLU   C C   1 
ATOM   2190 O  O   . GLU   B 1 140 ? 10.459 -19.126 31.471 1.00 41.65  ? 146 GLU   C O   1 
ATOM   2191 C  CB  . GLU   B 1 140 ? 10.971 -19.948 34.045 1.00 43.42  ? 146 GLU   C CB  1 
ATOM   2192 C  CG  . GLU   B 1 140 ? 12.168 -19.022 34.168 1.00 50.67  ? 146 GLU   C CG  1 
ATOM   2193 C  CD  . GLU   B 1 140 ? 11.861 -17.546 33.965 1.00 60.48  ? 146 GLU   C CD  1 
ATOM   2194 O  OE1 . GLU   B 1 140 ? 12.733 -16.709 34.294 1.00 62.96  ? 146 GLU   C OE1 1 
ATOM   2195 O  OE2 . GLU   B 1 140 ? 10.752 -17.226 33.475 1.00 62.65  ? 146 GLU   C OE2 1 
HETATM 2196 N  N1  . A1B05 C 2 .   ? 7.943  11.563  23.878 1.00 24.21  ? 201 A1B05 A N1  1 
HETATM 2197 N  N3  . A1B05 C 2 .   ? 10.049 17.662  20.030 1.00 24.95  ? 201 A1B05 A N3  1 
HETATM 2198 C  C4  . A1B05 C 2 .   ? 11.583 15.682  21.615 1.00 24.26  ? 201 A1B05 A C4  1 
HETATM 2199 C  C5  . A1B05 C 2 .   ? 11.912 15.964  20.163 1.00 24.76  ? 201 A1B05 A C5  1 
HETATM 2200 C  C6  . A1B05 C 2 .   ? 10.741 16.588  19.474 1.00 25.46  ? 201 A1B05 A C6  1 
HETATM 2201 C  C7  . A1B05 C 2 .   ? 10.199 16.299  18.284 1.00 26.84  ? 201 A1B05 A C7  1 
HETATM 2202 C  C8  . A1B05 C 2 .   ? 9.157  17.943  19.154 1.00 25.42  ? 201 A1B05 A C8  1 
HETATM 2203 O  O   . A1B05 C 2 .   ? 9.637  15.490  23.628 1.00 26.06  ? 201 A1B05 A O   1 
HETATM 2204 C  C3  . A1B05 C 2 .   ? 9.784  14.553  22.834 1.00 24.18  ? 201 A1B05 A C3  1 
HETATM 2205 C  C2  . A1B05 C 2 .   ? 9.147  13.244  23.081 1.00 22.38  ? 201 A1B05 A C2  1 
HETATM 2206 C  C1  . A1B05 C 2 .   ? 8.104  12.881  23.943 1.00 23.20  ? 201 A1B05 A C1  1 
HETATM 2207 N  N4  . A1B05 C 2 .   ? 9.631  12.133  22.488 1.00 23.89  ? 201 A1B05 A N4  1 
HETATM 2208 N  N   . A1B05 C 2 .   ? 8.890  11.166  23.022 1.00 24.33  ? 201 A1B05 A N   1 
HETATM 2209 C  C   . A1B05 C 2 .   ? 9.130  9.761   22.724 1.00 25.01  ? 201 A1B05 A C   1 
HETATM 2210 N  N2  . A1B05 C 2 .   ? 10.599 14.613  21.769 1.00 23.38  ? 201 A1B05 A N2  1 
HETATM 2211 O  O1  . A1B05 C 2 .   ? 9.175  17.168  18.047 1.00 27.08  ? 201 A1B05 A O1  1 
HETATM 2212 ZN ZN  . ZN    D 3 .   ? 10.891 -3.671  5.775  1.00 17.20  2 202 ZN    A ZN  1 
HETATM 2213 S  S   . DMS   E 4 .   ? 19.340 -2.088  24.477 1.00 80.00  ? 203 DMS   A S   1 
HETATM 2214 O  O   . DMS   E 4 .   ? 20.125 -0.820  24.277 1.00 79.98  ? 203 DMS   A O   1 
HETATM 2215 C  C1  . DMS   E 4 .   ? 18.218 -2.261  23.068 1.00 79.89  ? 203 DMS   A C1  1 
HETATM 2216 C  C2  . DMS   E 4 .   ? 20.418 -3.480  24.041 1.00 80.09  ? 203 DMS   A C2  1 
HETATM 2217 ZN ZN  . ZN    F 3 .   ? 30.608 -31.134 26.737 1.00 11.97  2 201 ZN    C ZN  1 
HETATM 2218 S  S   . DMS   G 4 .   ? 20.506 -31.524 9.331  1.00 99.34  ? 202 DMS   C S   1 
HETATM 2219 O  O   . DMS   G 4 .   ? 20.883 -30.079 9.230  1.00 99.34  ? 202 DMS   C O   1 
HETATM 2220 C  C1  . DMS   G 4 .   ? 21.175 -32.150 10.888 1.00 99.26  ? 202 DMS   C C1  1 
HETATM 2221 C  C2  . DMS   G 4 .   ? 18.770 -31.572 9.862  1.00 99.38  ? 202 DMS   C C2  1 
HETATM 2222 S  S   . DMS   H 4 .   ? 27.818 -5.002  6.676  1.00 110.42 ? 203 DMS   C S   1 
HETATM 2223 O  O   . DMS   H 4 .   ? 27.104 -4.421  7.861  1.00 110.38 ? 203 DMS   C O   1 
HETATM 2224 C  C1  . DMS   H 4 .   ? 26.558 -5.494  5.468  1.00 110.44 ? 203 DMS   C C1  1 
HETATM 2225 C  C2  . DMS   H 4 .   ? 28.471 -3.617  5.703  1.00 110.45 ? 203 DMS   C C2  1 
HETATM 2226 O  O   . HOH   I 5 .   ? 2.192  22.791  21.630 1.00 25.50  ? 301 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 35.330 -3.882  7.788  1.00 23.15  ? 302 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 2.995  9.411   9.116  1.00 26.80  ? 303 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 14.226 17.408  4.410  1.00 36.62  ? 304 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 11.211 9.083   4.438  1.00 21.89  ? 305 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 7.905  16.457  25.660 1.00 34.65  ? 306 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 37.629 14.895  13.977 1.00 41.71  ? 307 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 27.832 7.998   1.645  1.00 29.97  ? 308 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 12.232 16.744  27.890 1.00 31.03  ? 309 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 1.114  9.413   9.496  1.00 30.01  ? 310 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 33.830 14.126  9.701  1.00 31.02  ? 311 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 30.528 10.526  15.573 1.00 28.84  ? 312 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 0.460  -0.890  19.446 1.00 19.69  ? 313 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 13.864 2.896   1.300  1.00 18.28  ? 314 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 17.497 0.910   28.279 1.00 23.82  ? 315 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 29.586 22.189  19.377 1.00 23.39  ? 316 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 10.643 10.136  31.512 1.00 21.85  ? 317 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 12.453 -5.991  30.475 1.00 46.59  ? 318 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 28.157 3.220   4.808  1.00 31.00  ? 319 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 0.496  -1.364  9.211  1.00 40.80  ? 320 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 12.488 22.321  13.138 1.00 25.39  ? 321 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 24.933 5.105   21.336 1.00 30.23  ? 322 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? -2.671 23.354  9.053  1.00 43.82  ? 323 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 19.946 20.049  5.764  1.00 44.57  ? 324 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 4.699  -3.637  28.959 1.00 26.22  ? 325 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 27.416 10.645  0.131  1.00 54.40  ? 326 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 19.445 10.032  19.704 1.00 12.21  ? 327 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 23.454 21.653  7.247  1.00 22.26  ? 328 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 21.837 2.400   -0.884 1.00 31.67  ? 329 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 7.443  20.153  17.535 1.00 20.03  ? 330 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 10.803 17.218  25.685 1.00 30.61  ? 331 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 2.626  -2.880  20.829 1.00 22.67  ? 332 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? -0.010 1.325   15.944 1.00 11.61  ? 333 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 20.912 -4.136  14.182 1.00 15.65  ? 334 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? -1.055 -4.343  11.177 1.00 53.69  ? 335 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 13.634 24.753  26.053 1.00 32.01  ? 336 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 22.666 0.828   17.384 1.00 14.88  ? 337 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 10.788 5.725   3.494  1.00 21.17  ? 338 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 14.372 -10.782 8.738  1.00 38.41  ? 339 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 33.735 11.097  15.432 1.00 36.91  ? 340 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 33.937 -2.400  13.567 1.00 29.99  ? 341 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 14.203 13.749  24.146 1.00 20.86  ? 342 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 13.802 3.947   23.585 1.00 11.33  ? 343 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 28.289 11.101  2.936  1.00 49.20  ? 344 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 16.913 -3.528  27.802 1.00 33.65  ? 345 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 28.938 3.338   12.574 1.00 16.03  ? 346 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 3.962  12.911  17.923 1.00 28.72  ? 347 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 16.658 3.818   23.734 1.00 16.35  ? 348 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 23.602 11.651  21.948 1.00 30.14  ? 349 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 18.449 21.908  9.608  1.00 17.59  ? 350 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 8.486  24.714  23.976 1.00 26.94  ? 351 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 11.313 12.802  11.357 1.00 13.84  ? 352 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 29.557 11.884  21.242 1.00 30.92  ? 353 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 26.825 -1.247  8.794  1.00 24.06  ? 354 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 20.585 -0.992  3.013  1.00 29.90  ? 355 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 6.609  -6.928  23.765 1.00 24.23  ? 356 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 30.060 -1.402  8.645  1.00 34.46  ? 357 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 31.627 19.923  11.647 1.00 18.89  ? 358 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 29.998 11.484  18.455 1.00 27.33  ? 359 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 31.814 7.038   5.374  1.00 29.38  ? 360 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 36.562 17.875  14.311 1.00 28.14  ? 361 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 9.139  3.525   3.087  1.00 24.83  ? 362 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 12.268 11.058  29.766 1.00 19.24  ? 363 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 32.254 2.076   5.946  1.00 35.58  ? 364 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 14.797 11.425  0.109  1.00 34.46  ? 365 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 30.542 2.836   14.715 1.00 22.54  ? 366 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 23.235 -6.519  11.940 1.00 28.23  ? 367 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 17.983 17.852  4.443  1.00 33.61  ? 368 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 20.749 -2.536  16.831 1.00 14.39  ? 369 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 25.529 19.513  21.707 1.00 23.45  ? 370 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 35.928 15.018  10.976 1.00 34.12  ? 371 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 17.692 19.971  17.119 1.00 15.92  ? 372 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 13.251 11.492  9.337  1.00 12.93  ? 373 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 28.832 15.705  4.264  1.00 30.36  ? 374 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 5.573  5.390   32.749 1.00 21.57  ? 375 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 9.648  3.986   33.565 1.00 13.72  ? 376 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 11.582 -7.009  24.752 1.00 26.02  ? 377 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 12.207 15.384  24.857 1.00 80.38  ? 378 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 31.135 15.569  22.719 1.00 22.18  ? 379 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 22.760 -0.591  5.349  1.00 21.85  ? 380 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 2.447  16.094  19.342 1.00 28.74  ? 381 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 19.505 2.894   19.390 1.00 18.67  ? 382 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 32.816 16.448  9.148  1.00 29.83  ? 383 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 5.800  11.032  25.715 1.00 98.35  ? 384 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 25.169 17.822  4.619  1.00 31.42  ? 385 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 27.156 -1.320  15.780 1.00 24.93  ? 386 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 14.424 -2.429  17.979 1.00 16.57  ? 387 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 3.224  20.597  24.496 1.00 41.64  ? 388 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 30.381 4.500   5.682  1.00 23.04  ? 389 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 17.157 6.028   26.954 1.00 26.49  ? 390 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 17.801 10.618  26.181 1.00 20.87  ? 391 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 1.316  11.536  27.658 1.00 42.12  ? 392 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 28.126 17.520  24.126 1.00 22.52  ? 393 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 24.143 -3.495  16.099 1.00 35.17  ? 394 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 17.103 -5.257  12.177 1.00 31.18  ? 395 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 5.180  26.311  20.234 1.00 26.36  ? 396 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 31.994 8.713   7.551  1.00 23.41  ? 397 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 0.254  6.136   6.222  1.00 23.58  ? 398 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 21.793 4.750   24.691 1.00 34.74  ? 399 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 4.187  0.311   24.099 1.00 18.01  ? 400 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 16.592 21.258  19.270 1.00 28.95  ? 401 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 3.332  7.627   24.401 1.00 29.93  ? 402 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 16.224 9.361   -1.655 1.00 23.67  ? 403 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 3.868  -3.861  6.084  1.00 27.35  ? 404 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 36.329 -0.347  12.421 1.00 33.96  ? 405 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 7.364  14.014  4.921  1.00 22.53  ? 406 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 25.165 10.489  22.852 1.00 33.45  ? 407 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 34.032 18.661  10.651 1.00 25.46  ? 408 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 8.531  -6.421  9.682  1.00 24.47  ? 409 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 6.237  24.062  10.735 1.00 34.32  ? 410 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 15.487 15.364  3.777  1.00 28.28  ? 411 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 7.360  26.603  14.781 1.00 37.61  ? 412 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 3.580  26.978  16.359 1.00 37.35  ? 413 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 18.350 -1.635  30.535 1.00 42.21  ? 414 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 3.422  -0.276  21.520 1.00 20.43  ? 415 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 17.457 0.653   20.211 1.00 17.51  ? 416 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 0.485  -1.268  16.753 1.00 17.15  ? 417 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 22.415 19.315  19.550 1.00 29.57  ? 418 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 19.418 -0.564  33.273 1.00 37.06  ? 419 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 1.122  -5.013  17.678 1.00 34.52  ? 420 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 33.976 5.047   16.551 1.00 30.78  ? 421 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 30.982 -2.422  15.698 1.00 39.01  ? 422 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 23.200 19.095  6.307  1.00 18.34  ? 423 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 19.765 13.370  2.253  1.00 31.39  ? 424 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 21.135 9.844   21.962 1.00 15.54  ? 425 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 6.077  16.776  21.610 1.00 35.51  ? 426 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 22.828 3.394   20.800 1.00 19.05  ? 427 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 23.507 8.178   21.651 1.00 23.75  ? 428 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 35.407 10.619  12.426 1.00 44.83  ? 429 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 8.399  6.491   33.858 1.00 20.89  ? 430 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 17.163 -2.394  19.676 1.00 17.15  ? 431 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 31.057 19.468  8.914  1.00 34.20  ? 432 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 16.773 -3.931  2.884  1.00 27.97  ? 433 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 15.862 21.486  7.392  1.00 22.95  ? 434 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 19.518 9.310   -0.871 1.00 28.28  ? 435 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 34.105 7.771   16.560 1.00 32.65  ? 436 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 20.895 -4.808  11.502 1.00 27.25  ? 437 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 7.694  11.763  3.480  1.00 40.26  ? 438 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? -1.376 -3.004  15.720 1.00 27.13  ? 439 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 2.106  14.583  16.915 1.00 31.15  ? 440 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 8.239  11.319  31.544 1.00 36.64  ? 441 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 14.888 13.126  28.719 1.00 35.41  ? 442 HOH   A O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 38.570 1.156   13.248 1.00 56.57  ? 443 HOH   A O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 18.575 2.059   22.692 1.00 35.05  ? 444 HOH   A O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 16.179 12.755  26.231 1.00 30.31  ? 445 HOH   A O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 13.754 -6.691  25.688 1.00 43.85  ? 446 HOH   A O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? -0.852 24.588  12.345 1.00 59.23  ? 447 HOH   A O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 2.256  -5.505  14.682 1.00 40.95  ? 448 HOH   A O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? 16.781 -5.051  34.365 1.00 28.70  ? 449 HOH   A O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 6.406  3.463   3.472  1.00 34.11  ? 450 HOH   A O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 21.646 19.755  4.213  1.00 36.67  ? 451 HOH   A O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 31.040 12.801  23.095 1.00 43.33  ? 452 HOH   A O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 29.711 0.541   16.429 1.00 33.71  ? 453 HOH   A O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 11.850 24.350  14.914 1.00 33.21  ? 454 HOH   A O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 23.854 0.947   19.830 1.00 28.46  ? 455 HOH   A O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 9.559  8.149   2.380  1.00 35.65  ? 456 HOH   A O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 11.412 23.189  10.877 1.00 33.54  ? 457 HOH   A O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 4.861  28.294  18.249 1.00 35.95  ? 458 HOH   A O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 5.423  12.227  27.851 1.00 56.78  ? 459 HOH   A O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 30.484 6.912   17.803 1.00 36.64  ? 460 HOH   A O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 33.491 16.674  23.436 1.00 42.89  ? 461 HOH   A O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 37.734 -4.555  6.693  1.00 32.08  ? 462 HOH   A O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 21.460 11.182  24.474 1.00 35.50  ? 463 HOH   A O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 12.417 -5.107  33.168 1.00 31.36  ? 464 HOH   A O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 31.338 4.448   16.933 1.00 25.16  ? 465 HOH   A O   1 
HETATM 2391 O  O   . HOH   I 5 .   ? 21.335 -1.046  18.929 1.00 27.88  ? 466 HOH   A O   1 
HETATM 2392 O  O   . HOH   I 5 .   ? -0.252 13.661  17.143 1.00 34.53  ? 467 HOH   A O   1 
HETATM 2393 O  O   . HOH   I 5 .   ? 34.976 -2.066  16.221 1.00 41.12  ? 468 HOH   A O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 2.390  -5.076  22.656 1.00 32.16  ? 469 HOH   A O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 32.217 11.294  6.526  1.00 31.66  ? 470 HOH   A O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 28.892 1.558   18.939 1.00 47.37  ? 471 HOH   A O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 1.124  26.449  17.516 1.00 39.57  ? 472 HOH   A O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 9.891  26.008  14.056 1.00 39.18  ? 473 HOH   A O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 26.485 0.375   20.144 1.00 46.46  ? 474 HOH   A O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 26.543 -5.464  9.907  1.00 21.47  ? 301 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 17.463 -33.393 24.088 1.00 41.42  ? 302 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 31.076 -23.701 -1.310 1.00 23.27  ? 303 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 38.281 -7.352  6.973  1.00 21.90  ? 304 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 38.426 -18.476 21.511 1.00 26.27  ? 305 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 14.544 -18.691 31.896 1.00 33.82  ? 306 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 19.696 -4.091  20.190 1.00 20.80  ? 307 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 42.588 -11.162 11.167 1.00 25.87  ? 308 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 36.114 -26.142 34.258 1.00 33.15  ? 309 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 16.225 -16.120 8.978  1.00 34.96  ? 310 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 22.826 -5.904  21.151 1.00 19.17  ? 311 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 24.518 -9.900  27.011 1.00 37.28  ? 312 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 28.158 -4.973  18.574 1.00 39.38  ? 313 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 17.798 -6.000  24.112 1.00 23.97  ? 314 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 30.698 -18.092 26.910 1.00 17.97  ? 315 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 20.701 -18.714 12.837 1.00 12.57  ? 316 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 24.632 -5.960  15.201 1.00 28.02  ? 317 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 17.860 -27.552 16.525 1.00 17.04  ? 318 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 18.487 -8.865  13.761 1.00 26.77  ? 319 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 36.103 -17.542 11.759 1.00 21.27  ? 320 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 10.185 -17.543 18.353 1.00 27.00  ? 321 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 21.652 -26.029 34.400 1.00 24.70  ? 322 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 7.310  -30.424 22.192 1.00 27.87  ? 323 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 32.435 -23.700 29.124 1.00 16.79  ? 324 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 38.225 -26.288 28.422 1.00 36.06  ? 325 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 14.711 -23.951 12.325 1.00 27.86  ? 326 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 40.142 -29.492 11.947 1.00 20.93  ? 327 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 37.458 -31.809 10.976 1.00 22.84  ? 328 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 34.253 -33.588 24.205 1.00 29.65  ? 329 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 10.046 -20.043 28.928 1.00 37.41  ? 330 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 37.142 -18.717 28.221 1.00 27.08  ? 331 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 22.043 -28.569 4.768  1.00 22.91  ? 332 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 31.066 -32.371 0.711  1.00 35.22  ? 333 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 33.465 -32.870 0.601  1.00 38.22  ? 334 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 40.535 -27.148 15.277 1.00 10.96  ? 335 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 24.737 -15.711 7.343  1.00 17.58  ? 336 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 16.308 -17.233 10.972 1.00 34.21  ? 337 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 30.904 -21.484 28.441 1.00 15.72  ? 338 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 26.034 -25.224 8.788  1.00 12.08  ? 339 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 41.277 -24.906 7.323  1.00 28.79  ? 340 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 13.846 -24.349 29.317 1.00 31.52  ? 341 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 26.313 -15.261 30.787 1.00 28.62  ? 342 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 9.821  -8.895  23.979 1.00 25.22  ? 343 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 6.757  -9.179  22.624 1.00 31.33  ? 344 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 25.960 -37.926 24.336 1.00 29.48  ? 345 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 9.159  -8.093  21.354 1.00 21.83  ? 346 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 11.090 -21.721 13.684 1.00 39.84  ? 347 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 35.211 -13.088 8.696  1.00 18.86  ? 348 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 37.252 -10.586 4.917  1.00 37.79  ? 349 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 29.618 -31.324 32.774 1.00 25.90  ? 350 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 11.846 -24.275 21.686 1.00 17.04  ? 351 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 29.830 -15.235 19.610 1.00 14.65  ? 352 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 32.012 -10.448 13.808 1.00 18.30  ? 353 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 35.373 -32.769 3.415  1.00 31.57  ? 354 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 10.578 -16.849 12.422 1.00 32.18  ? 355 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 13.250 -11.204 28.608 1.00 34.37  ? 356 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 20.728 -25.654 13.845 1.00 18.98  ? 357 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 23.829 -8.166  9.451  1.00 20.94  ? 358 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 16.799 -9.345  27.713 1.00 33.39  ? 359 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 36.066 -28.536 2.934  1.00 37.03  ? 360 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 23.724 -3.372  19.023 1.00 37.93  ? 361 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 34.765 -34.901 18.069 1.00 26.00  ? 362 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 14.612 -28.803 25.621 1.00 35.34  ? 363 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 23.155 -25.325 8.913  1.00 19.95  ? 364 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 5.911  -16.939 22.377 1.00 36.80  ? 365 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 39.931 -13.609 12.545 1.00 30.09  ? 366 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 31.188 -35.559 31.773 1.00 36.34  ? 367 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 29.833 -15.890 30.533 1.00 30.58  ? 368 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 10.395 -16.955 15.083 1.00 29.78  ? 369 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 29.756 -13.066 12.980 1.00 14.41  ? 370 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 27.211 -35.596 20.745 1.00 25.33  ? 371 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 32.156 -34.584 24.802 1.00 24.35  ? 372 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 19.179 -27.762 28.154 1.00 17.52  ? 373 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 41.783 -12.292 20.674 1.00 35.51  ? 374 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 22.940 -33.214 5.401  1.00 29.09  ? 375 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 22.872 -8.490  14.043 1.00 15.11  ? 376 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 17.491 -23.920 8.704  1.00 35.75  ? 377 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 36.335 -21.202 7.063  1.00 22.36  ? 378 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 23.566 -33.665 29.055 1.00 27.34  ? 379 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 11.370 -22.533 28.675 1.00 26.96  ? 380 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 31.076 -6.046  5.806  1.00 43.35  ? 381 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 22.332 -13.797 29.728 1.00 35.26  ? 382 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 28.880 -36.137 7.802  1.00 18.95  ? 383 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 34.520 -23.309 -0.683 1.00 34.38  ? 384 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 8.752  -13.246 10.809 1.00 20.60  ? 385 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 4.187  -10.410 19.563 1.00 28.83  ? 386 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 26.532 -6.021  22.002 1.00 27.41  ? 387 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 13.166 -29.547 19.235 1.00 26.12  ? 388 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 9.354  -27.430 19.086 1.00 28.48  ? 389 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 32.918 -9.815  11.124 1.00 14.48  ? 390 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 28.054 -16.314 22.094 1.00 12.83  ? 391 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 10.935 -6.358  13.249 1.00 20.94  ? 392 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 41.579 -13.719 10.172 1.00 29.10  ? 393 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 37.446 -31.562 25.708 1.00 29.83  ? 394 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 31.519 -13.497 4.438  1.00 31.10  ? 395 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 34.275 -13.368 25.531 1.00 19.34  ? 396 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 26.691 -12.029 27.638 1.00 26.24  ? 397 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 31.243 -12.145 10.669 1.00 14.25  ? 398 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 42.204 -11.908 13.979 1.00 29.36  ? 399 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 3.806  -8.175  14.762 1.00 24.76  ? 400 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 24.381 -13.774 5.503  1.00 34.42  ? 401 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 22.984 -28.202 12.597 1.00 19.05  ? 402 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 22.254 -23.701 6.032  1.00 32.96  ? 403 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 40.032 -28.378 28.260 1.00 44.39  ? 404 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 10.659 -11.838 9.074  1.00 26.66  ? 405 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 35.054 -13.701 6.029  1.00 31.66  ? 406 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 26.409 -31.198 14.845 1.00 17.34  ? 407 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 43.232 -25.402 23.817 1.00 22.14  ? 408 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? 27.776 -37.297 29.083 1.00 42.23  ? 409 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 20.382 -23.690 34.778 1.00 29.41  ? 410 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 35.557 -24.571 24.715 1.00 16.52  ? 411 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 21.683 -18.898 5.871  1.00 25.57  ? 412 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 35.803 -28.432 7.779  1.00 18.64  ? 413 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 36.992 -29.166 10.144 1.00 19.12  ? 414 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 9.992  -24.866 19.765 1.00 21.24  ? 415 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 25.990 -31.017 30.877 1.00 17.07  ? 416 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 38.971 -16.123 4.053  1.00 41.19  ? 417 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 33.019 -30.279 31.729 1.00 19.03  ? 418 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 34.838 -4.094  17.692 1.00 27.17  ? 419 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 14.662 -18.380 10.359 1.00 31.48  ? 420 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 32.795 -14.318 9.462  1.00 14.65  ? 421 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 16.957 -31.540 28.415 1.00 49.93  ? 422 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 17.158 -25.271 12.724 1.00 22.59  ? 423 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 30.360 -17.915 8.380  1.00 25.49  ? 424 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 38.794 -12.894 25.842 1.00 26.68  ? 425 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 4.623  -25.095 25.614 1.00 49.27  ? 426 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 4.537  -27.905 23.290 1.00 33.80  ? 427 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 20.232 -32.277 22.259 1.00 29.77  ? 428 HOH   C O   1 
HETATM 2528 O  O   . HOH   J 5 .   ? 38.000 -23.608 4.518  1.00 32.37  ? 429 HOH   C O   1 
HETATM 2529 O  O   . HOH   J 5 .   ? 9.728  -18.447 26.738 1.00 29.80  ? 430 HOH   C O   1 
HETATM 2530 O  O   . HOH   J 5 .   ? 6.389  -22.883 18.318 1.00 33.90  ? 431 HOH   C O   1 
HETATM 2531 O  O   . HOH   J 5 .   ? 29.882 -10.319 27.787 1.00 48.91  ? 432 HOH   C O   1 
HETATM 2532 O  O   . HOH   J 5 .   ? 3.955  -12.757 17.310 1.00 33.44  ? 433 HOH   C O   1 
HETATM 2533 O  O   . HOH   J 5 .   ? 18.786 -19.126 10.837 1.00 17.89  ? 434 HOH   C O   1 
HETATM 2534 O  O   . HOH   J 5 .   ? 18.539 -8.304  25.559 1.00 20.06  ? 435 HOH   C O   1 
HETATM 2535 O  O   . HOH   J 5 .   ? 16.325 -20.491 11.558 1.00 23.55  ? 436 HOH   C O   1 
HETATM 2536 O  O   . HOH   J 5 .   ? 37.838 -20.432 4.830  1.00 37.32  ? 437 HOH   C O   1 
HETATM 2537 O  O   . HOH   J 5 .   ? 40.072 -29.790 14.687 1.00 16.26  ? 438 HOH   C O   1 
HETATM 2538 O  O   . HOH   J 5 .   ? 41.649 -12.336 18.147 1.00 25.90  ? 439 HOH   C O   1 
HETATM 2539 O  O   . HOH   J 5 .   ? 10.418 -30.947 25.422 1.00 30.75  ? 440 HOH   C O   1 
HETATM 2540 O  O   . HOH   J 5 .   ? 23.354 -30.976 13.268 1.00 32.67  ? 441 HOH   C O   1 
HETATM 2541 O  O   . HOH   J 5 .   ? 33.961 -35.847 8.838  1.00 33.02  ? 442 HOH   C O   1 
HETATM 2542 O  O   . HOH   J 5 .   ? 37.526 -13.791 10.025 1.00 28.35  ? 443 HOH   C O   1 
HETATM 2543 O  O   . HOH   J 5 .   ? 6.457  -20.031 18.180 1.00 32.54  ? 444 HOH   C O   1 
HETATM 2544 O  O   . HOH   J 5 .   ? 33.988 -15.486 27.270 1.00 35.77  ? 445 HOH   C O   1 
HETATM 2545 O  O   . HOH   J 5 .   ? 23.229 -17.573 33.348 1.00 20.22  ? 446 HOH   C O   1 
HETATM 2546 O  O   . HOH   J 5 .   ? 14.927 -29.893 18.054 1.00 42.43  ? 447 HOH   C O   1 
HETATM 2547 O  O   . HOH   J 5 .   ? 20.315 -19.698 36.159 1.00 28.38  ? 448 HOH   C O   1 
HETATM 2548 O  O   . HOH   J 5 .   ? 21.489 -26.922 10.194 1.00 35.61  ? 449 HOH   C O   1 
HETATM 2549 O  O   . HOH   J 5 .   ? 31.671 -15.719 7.051  1.00 31.89  ? 450 HOH   C O   1 
HETATM 2550 O  O   . HOH   J 5 .   ? 24.148 -16.527 3.213  1.00 36.17  ? 451 HOH   C O   1 
HETATM 2551 O  O   . HOH   J 5 .   ? 39.614 -14.185 8.333  1.00 27.64  ? 452 HOH   C O   1 
HETATM 2552 O  O   . HOH   J 5 .   ? 34.205 -31.779 29.579 1.00 25.34  ? 453 HOH   C O   1 
HETATM 2553 O  O   . HOH   J 5 .   ? 34.521 -30.169 33.898 1.00 35.61  ? 454 HOH   C O   1 
HETATM 2554 O  O   . HOH   J 5 .   ? 36.573 -24.352 27.263 1.00 31.75  ? 455 HOH   C O   1 
HETATM 2555 O  O   . HOH   J 5 .   ? 38.933 -33.595 17.363 1.00 41.66  ? 456 HOH   C O   1 
HETATM 2556 O  O   . HOH   J 5 .   ? 41.158 -29.623 22.374 1.00 37.69  ? 457 HOH   C O   1 
HETATM 2557 O  O   . HOH   J 5 .   ? 23.668 -15.644 31.466 1.00 29.63  ? 458 HOH   C O   1 
HETATM 2558 O  O   . HOH   J 5 .   ? 21.011 -17.507 34.644 1.00 27.38  ? 459 HOH   C O   1 
HETATM 2559 O  O   . HOH   J 5 .   ? 26.179 -35.319 7.452  1.00 24.46  ? 460 HOH   C O   1 
HETATM 2560 O  O   . HOH   J 5 .   ? 8.797  -19.214 16.827 1.00 33.73  ? 461 HOH   C O   1 
HETATM 2561 O  O   . HOH   J 5 .   ? 24.343 -12.149 28.961 1.00 54.83  ? 462 HOH   C O   1 
HETATM 2562 O  O   . HOH   J 5 .   ? 22.866 -16.740 5.494  1.00 36.75  ? 463 HOH   C O   1 
HETATM 2563 O  O   . HOH   J 5 .   ? 28.302 -12.548 30.152 1.00 45.17  ? 464 HOH   C O   1 
HETATM 2564 O  O   . HOH   J 5 .   ? 37.103 -29.024 5.530  1.00 37.16  ? 465 HOH   C O   1 
HETATM 2565 O  O   . HOH   J 5 .   ? 16.353 -27.544 14.152 1.00 30.99  ? 466 HOH   C O   1 
HETATM 2566 O  O   . HOH   J 5 .   ? 11.966 -18.471 10.164 1.00 50.65  ? 467 HOH   C O   1 
HETATM 2567 O  O   . HOH   J 5 .   ? 9.997  -21.360 16.132 1.00 31.69  ? 468 HOH   C O   1 
HETATM 2568 O  O   . HOH   J 5 .   ? 32.392 -19.246 29.112 1.00 28.06  ? 469 HOH   C O   1 
HETATM 2569 O  O   . HOH   J 5 .   ? 18.431 -26.077 10.195 1.00 34.58  ? 470 HOH   C O   1 
HETATM 2570 O  O   . HOH   J 5 .   ? 43.287 -20.796 3.842  1.00 46.28  ? 471 HOH   C O   1 
HETATM 2571 O  O   . HOH   J 5 .   ? 40.590 -28.714 7.816  1.00 47.20  ? 472 HOH   C O   1 
HETATM 2572 O  O   . HOH   J 5 .   ? 31.946 -32.066 33.181 1.00 30.99  ? 473 HOH   C O   1 
HETATM 2573 O  O   . HOH   J 5 .   ? 18.073 -16.550 38.215 1.00 35.03  ? 474 HOH   C O   1 
HETATM 2574 O  O   . HOH   J 5 .   ? 22.313 -3.123  20.966 1.00 42.84  ? 475 HOH   C O   1 
HETATM 2575 O  O   . HOH   J 5 .   ? 5.221  -24.437 16.247 1.00 66.55  ? 476 HOH   C O   1 
HETATM 2576 O  O   . HOH   J 5 .   ? 22.602 -11.927 6.038  1.00 35.24  ? 477 HOH   C O   1 
HETATM 2577 O  O   . HOH   J 5 .   ? 18.086 -17.945 8.301  1.00 31.95  ? 478 HOH   C O   1 
HETATM 2578 O  O   . HOH   J 5 .   ? 16.895 -28.839 28.878 1.00 40.77  ? 479 HOH   C O   1 
HETATM 2579 O  O   . HOH   J 5 .   ? 38.085 -31.699 4.964  1.00 39.63  ? 480 HOH   C O   1 
HETATM 2580 O  O   . HOH   J 5 .   ? 8.925  -23.508 17.626 1.00 28.09  ? 481 HOH   C O   1 
HETATM 2581 O  O   . HOH   J 5 .   ? 35.136 -22.897 29.039 1.00 27.63  ? 482 HOH   C O   1 
HETATM 2582 O  O   . HOH   J 5 .   ? 35.387 -20.321 29.532 1.00 40.53  ? 483 HOH   C O   1 
HETATM 2583 O  O   . HOH   J 5 .   ? 3.173  -8.592  22.191 1.00 41.53  ? 484 HOH   C O   1 
HETATM 2584 O  O   . HOH   J 5 .   ? 19.303 -17.689 5.890  1.00 41.11  ? 485 HOH   C O   1 
HETATM 2585 O  O   . HOH   J 5 .   ? 11.540 -28.460 17.848 1.00 34.30  ? 486 HOH   C O   1 
HETATM 2586 O  O   . HOH   J 5 .   ? 39.222 -2.713  10.634 1.00 35.62  ? 487 HOH   C O   1 
HETATM 2587 O  O   . HOH   J 5 .   ? 34.442 -10.710 26.487 1.00 40.54  ? 488 HOH   C O   1 
HETATM 2588 O  O   . HOH   J 5 .   ? 7.287  -27.803 17.403 1.00 34.76  ? 489 HOH   C O   1 
HETATM 2589 O  O   . HOH   J 5 .   ? 3.274  -9.462  17.093 1.00 34.55  ? 490 HOH   C O   1 
HETATM 2590 O  O   . HOH   J 5 .   ? 19.410 -15.206 34.623 1.00 39.60  ? 491 HOH   C O   1 
HETATM 2591 O  O   . HOH   J 5 .   ? 13.809 -28.201 14.017 1.00 44.41  ? 492 HOH   C O   1 
HETATM 2592 O  O   . HOH   J 5 .   ? 36.238 -35.324 7.413  1.00 52.09  ? 493 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   ? 0.1910 0.1929 0.1713 -0.0161 -0.0072 -0.0082 7   SER   A N   
2    C CA  . SER   A 1   ? 0.1799 0.1838 0.1660 -0.0139 -0.0103 -0.0054 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1805 0.1854 0.1731 -0.0084 -0.0126 -0.0006 7   SER   A C   
4    O O   . SER   A 1   ? 0.1946 0.1995 0.1863 -0.0074 -0.0129 0.0013  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2116 0.2212 0.1940 -0.0201 -0.0144 -0.0035 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2549 0.2693 0.2353 -0.0219 -0.0187 0.0019  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1600 0.1653 0.1592 -0.0056 -0.0135 0.0009  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1569 0.1625 0.1626 -0.0015 -0.0142 0.0042  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1345 0.1384 0.1454 0.0014  -0.0123 0.0030  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1561 0.1579 0.1657 0.0013  -0.0103 0.0000  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1266 0.1313 0.1438 0.0034  -0.0125 0.0052  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1312 0.1347 0.1526 0.0050  -0.0103 0.0038  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1243 0.1266 0.1501 0.0067  -0.0080 0.0044  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1339 0.1364 0.1622 0.0072  -0.0082 0.0067  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1547 0.1610 0.1806 0.0041  -0.0121 0.0049  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1178 0.1191 0.1447 0.0068  -0.0052 0.0023  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1159 0.1159 0.1470 0.0067  -0.0015 0.0014  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1222 0.1231 0.1610 0.0070  -0.0005 0.0016  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1267 0.1287 0.1646 0.0064  -0.0014 0.0009  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1174 0.1167 0.1433 0.0048  0.0010  -0.0011 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1431 0.1427 0.1627 0.0045  -0.0003 -0.0007 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1382 0.1359 0.1668 0.0029  0.0060  -0.0034 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1556 0.1572 0.1711 0.0021  0.0006  -0.0011 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1220 0.1223 0.1698 0.0080  0.0020  0.0028  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1273 0.1288 0.1852 0.0086  0.0040  0.0032  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1358 0.1339 0.1974 0.0072  0.0112  -0.0007 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1459 0.1414 0.2142 0.0080  0.0150  -0.0004 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1379 0.1427 0.2066 0.0107  0.0011  0.0091  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1309 0.1401 0.1944 0.0099  -0.0057 0.0123  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1476 0.1602 0.2116 0.0088  -0.0081 0.0124  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1605 0.1704 0.2179 0.0094  -0.0092 0.0146  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1586 0.1747 0.2162 0.0065  -0.0133 0.0139  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1699 0.1837 0.2211 0.0070  -0.0144 0.0162  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1663 0.1829 0.2173 0.0053  -0.0162 0.0155  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.1981 0.2180 0.2417 0.0015  -0.0202 0.0158  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1409 0.1385 0.1976 0.0044  0.0138  -0.0047 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1481 0.1429 0.2053 0.0009  0.0212  -0.0096 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1534 0.1493 0.2165 -0.0002 0.0241  -0.0113 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1445 0.1431 0.2034 -0.0005 0.0203  -0.0104 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1746 0.1695 0.2183 -0.0036 0.0215  -0.0124 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1805 0.1789 0.2166 -0.0041 0.0163  -0.0106 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2013 0.1943 0.2437 -0.0094 0.0295  -0.0181 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1633 0.1567 0.2374 -0.0007 0.0314  -0.0138 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1829 0.1774 0.2643 -0.0016 0.0349  -0.0155 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1572 0.1564 0.2442 0.0023  0.0280  -0.0101 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1559 0.1571 0.2493 0.0062  0.0234  -0.0046 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1509 0.1523 0.2334 0.0004  0.0265  -0.0112 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1429 0.1487 0.2282 0.0027  0.0200  -0.0069 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1389 0.1453 0.2105 0.0019  0.0138  -0.0061 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1379 0.1465 0.2080 0.0014  0.0107  -0.0052 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1648 0.1728 0.2584 0.0017  0.0229  -0.0080 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2005 0.2092 0.3129 0.0041  0.0279  -0.0066 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2332 0.2468 0.3571 0.0073  0.0237  -0.0006 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1924 0.1969 0.3092 0.0022  0.0370  -0.0115 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1237 0.1282 0.1870 0.0019  0.0124  -0.0060 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1252 0.1300 0.1780 0.0016  0.0076  -0.0050 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1216 0.1266 0.1731 0.0039  0.0035  -0.0022 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1358 0.1398 0.1904 0.0051  0.0048  -0.0015 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1342 0.1375 0.1776 -0.0015 0.0097  -0.0070 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1490 0.1530 0.1910 -0.0055 0.0133  -0.0094 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1617 0.1670 0.2040 -0.0060 0.0117  -0.0085 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1842 0.1874 0.2238 -0.0098 0.0188  -0.0129 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1780 0.1841 0.2184 -0.0103 0.0150  -0.0103 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1954 0.1997 0.2319 -0.0150 0.0223  -0.0152 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1954 0.2014 0.2323 -0.0150 0.0201  -0.0135 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2532 0.2607 0.2867 -0.0205 0.0233  -0.0153 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1146 0.1202 0.1607 0.0040  -0.0006 -0.0011 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1135 0.1192 0.1557 0.0049  -0.0039 0.0005  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1183 0.1219 0.1525 0.0042  -0.0040 -0.0007 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1226 0.1258 0.1555 0.0033  -0.0040 -0.0013 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1363 0.1452 0.1806 0.0042  -0.0078 0.0025  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1431 0.1521 0.1806 0.0031  -0.0107 0.0029  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1533 0.1669 0.1920 0.0004  -0.0145 0.0049  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1543 0.1667 0.1847 -0.0027 -0.0152 0.0023  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1795 0.1925 0.2039 -0.0049 -0.0168 0.0025  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1946 0.2096 0.2204 -0.0038 -0.0185 0.0060  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1877 0.1988 0.2052 -0.0086 -0.0157 -0.0011 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1168 0.1193 0.1472 0.0047  -0.0036 -0.0007 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1120 0.1135 0.1372 0.0044  -0.0035 -0.0006 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1241 0.1248 0.1467 0.0051  -0.0051 -0.0005 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1265 0.1274 0.1482 0.0055  -0.0059 0.0000  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1205 0.1224 0.1432 0.0034  -0.0017 -0.0006 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1339 0.1368 0.1540 0.0030  -0.0021 0.0012  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1418 0.1444 0.1660 0.0012  0.0012  -0.0020 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1125 0.1118 0.1341 0.0047  -0.0050 -0.0011 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1123 0.1103 0.1310 0.0041  -0.0051 -0.0023 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1330 0.1311 0.1517 0.0040  -0.0052 -0.0023 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1142 0.1100 0.1337 0.0047  -0.0026 -0.0026 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1315 0.1274 0.1544 0.0055  -0.0016 -0.0007 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1109 0.1093 0.1288 0.0015  -0.0062 -0.0039 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1749 0.1736 0.1934 0.0015  -0.0064 -0.0038 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1348 0.1368 0.1535 0.0008  -0.0094 -0.0020 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.1826 0.1806 0.1961 -0.0013 -0.0064 -0.0058 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0729 0.0700 0.0937 0.0009  -0.0049 -0.0049 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2139 0.2161 0.2355 0.0014  -0.0090 -0.0019 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1194 0.1135 0.1368 0.0041  -0.0012 -0.0042 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1196 0.1110 0.1409 0.0050  0.0025  -0.0044 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1256 0.1141 0.1497 0.0037  0.0046  -0.0063 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1284 0.1163 0.1488 0.0006  0.0041  -0.0094 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1293 0.1186 0.1479 0.0037  0.0050  -0.0074 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1282 0.1199 0.1441 0.0047  0.0034  -0.0058 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1404 0.1337 0.1508 0.0033  0.0007  -0.0062 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1431 0.1358 0.1636 0.0069  0.0049  -0.0033 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1319 0.1192 0.1630 0.0055  0.0067  -0.0037 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1312 0.1149 0.1659 0.0043  0.0093  -0.0052 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1480 0.1269 0.1810 0.0011  0.0137  -0.0111 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1584 0.1358 0.1888 -0.0022 0.0142  -0.0145 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1460 0.1293 0.1901 0.0067  0.0113  -0.0002 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1459 0.1253 0.1950 0.0058  0.0141  -0.0008 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1624 0.1418 0.2228 0.0084  0.0161  0.0059  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1702 0.1462 0.2364 0.0078  0.0184  0.0070  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.1876 0.1565 0.2604 0.0072  0.0247  0.0038  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.1914 0.1557 0.2638 0.0063  0.0296  -0.0021 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.1994 0.1653 0.2787 0.0069  0.0269  0.0059  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1426 0.1198 0.1759 0.0013  0.0169  -0.0128 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1631 0.1352 0.1941 -0.0030 0.0226  -0.0195 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.1717 0.1462 0.1908 -0.0087 0.0195  -0.0236 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2046 0.1759 0.2194 -0.0145 0.0238  -0.0298 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.1758 0.1450 0.2117 -0.0018 0.0283  -0.0207 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1682 0.1412 0.1976 -0.0017 0.0253  -0.0202 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.1659 0.1436 0.1977 0.0027  0.0210  -0.0142 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.1829 0.1558 0.2033 -0.0063 0.0263  -0.0251 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.1744 0.1540 0.1995 0.0013  0.0198  -0.0156 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.1816 0.1585 0.2000 -0.0039 0.0228  -0.0217 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.1713 0.1518 0.1856 -0.0078 0.0125  -0.0200 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1682 0.1530 0.1738 -0.0126 0.0083  -0.0211 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.1820 0.1706 0.1883 -0.0132 0.0038  -0.0189 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.1891 0.1828 0.1908 -0.0168 -0.0005 -0.0180 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1618 0.1505 0.1635 -0.0115 0.0046  -0.0183 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.1734 0.1592 0.1737 -0.0118 0.0089  -0.0208 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.1842 0.1739 0.1806 -0.0107 0.0049  -0.0175 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2015 0.1845 0.1955 -0.0193 0.0138  -0.0276 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1658 0.1525 0.1786 -0.0101 0.0049  -0.0176 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1706 0.1607 0.1850 -0.0105 0.0013  -0.0157 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.1766 0.1679 0.1867 -0.0172 0.0013  -0.0193 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.1906 0.1771 0.1986 -0.0211 0.0064  -0.0244 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1656 0.1530 0.1868 -0.0070 0.0033  -0.0140 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.1698 0.1676 0.1794 -0.0189 -0.0039 -0.0166 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1618 0.1633 0.1673 -0.0263 -0.0053 -0.0188 24  THR   A CA  
140  C C   . THR   A 18  ? 0.1690 0.1690 0.1789 -0.0267 -0.0038 -0.0200 24  THR   A C   
141  O O   . THR   A 18  ? 0.1579 0.1551 0.1743 -0.0211 -0.0026 -0.0181 24  THR   A O   
142  C CB  . THR   A 18  ? 0.1908 0.2019 0.1961 -0.0280 -0.0123 -0.0135 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.1860 0.1994 0.2001 -0.0225 -0.0145 -0.0091 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2016 0.2147 0.2031 -0.0276 -0.0144 -0.0111 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.1723 0.1751 0.1787 -0.0341 -0.0043 -0.0228 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.1745 0.1767 0.1851 -0.0350 -0.0033 -0.0236 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.1636 0.1715 0.1818 -0.0299 -0.0080 -0.0176 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.1694 0.1742 0.1930 -0.0265 -0.0060 -0.0173 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.1915 0.1976 0.1962 -0.0451 -0.0037 -0.0273 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.2609 0.2695 0.2706 -0.0463 -0.0048 -0.0266 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3078 0.3082 0.3211 -0.0450 0.0010  -0.0301 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3041 0.3227 0.3179 -0.0472 -0.0109 -0.0216 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3167 0.3222 0.3336 -0.0468 -0.0016 -0.0285 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3266 0.3432 0.3449 -0.0475 -0.0088 -0.0232 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1625 0.1784 0.1820 -0.0293 -0.0136 -0.0126 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1578 0.1781 0.1865 -0.0244 -0.0163 -0.0076 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1387 0.1529 0.1708 -0.0173 -0.0130 -0.0074 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1466 0.1606 0.1845 -0.0147 -0.0120 -0.0064 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.1820 0.2111 0.2143 -0.0244 -0.0218 -0.0015 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2496 0.2829 0.2939 -0.0201 -0.0229 0.0029  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.2933 0.3313 0.3428 -0.0224 -0.0241 0.0039  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.2803 0.3117 0.3295 -0.0142 -0.0218 0.0052  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1439 0.1534 0.1718 -0.0151 -0.0112 -0.0084 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1383 0.1432 0.1686 -0.0099 -0.0084 -0.0078 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1328 0.1331 0.1648 -0.0097 -0.0049 -0.0095 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1420 0.1422 0.1777 -0.0073 -0.0042 -0.0078 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1385 0.1399 0.1645 -0.0082 -0.0071 -0.0084 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1546 0.1597 0.1795 -0.0074 -0.0100 -0.0060 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1601 0.1688 0.1901 -0.0053 -0.0119 -0.0029 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1566 0.1607 0.1763 -0.0089 -0.0098 -0.0072 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1302 0.1264 0.1597 -0.0128 -0.0022 -0.0129 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1403 0.1315 0.1730 -0.0126 0.0016  -0.0137 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1337 0.1281 0.1696 -0.0142 0.0003  -0.0132 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1459 0.1378 0.1853 -0.0127 0.0023  -0.0118 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1519 0.1372 0.1825 -0.0163 0.0061  -0.0183 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1453 0.1258 0.1766 -0.0136 0.0094  -0.0184 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.1649 0.1446 0.1916 -0.0153 0.0105  -0.0211 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1490 0.1258 0.1868 -0.0091 0.0122  -0.0149 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1636 0.1389 0.1943 -0.0117 0.0142  -0.0201 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1551 0.1289 0.1932 -0.0078 0.0150  -0.0157 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.1612 0.1375 0.2049 -0.0067 0.0126  -0.0106 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.1747 0.1461 0.2204 -0.0036 0.0177  -0.0115 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.1752 0.1498 0.2247 -0.0031 0.0143  -0.0059 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.1782 0.1501 0.2299 -0.0016 0.0172  -0.0063 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1356 0.1359 0.1709 -0.0175 -0.0030 -0.0135 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1394 0.1435 0.1790 -0.0190 -0.0041 -0.0128 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1506 0.1584 0.1958 -0.0151 -0.0053 -0.0094 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1678 0.1782 0.2177 -0.0157 -0.0051 -0.0089 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1646 0.1754 0.2030 -0.0245 -0.0075 -0.0134 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1458 0.1537 0.1907 -0.0115 -0.0059 -0.0076 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1414 0.1516 0.1912 -0.0086 -0.0054 -0.0055 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1380 0.1439 0.1842 -0.0062 -0.0032 -0.0052 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1447 0.1516 0.1914 -0.0042 -0.0029 -0.0043 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1562 0.1719 0.2103 -0.0075 -0.0082 -0.0031 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1643 0.1864 0.2237 -0.0104 -0.0109 -0.0018 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2060 0.2309 0.2729 -0.0102 -0.0099 -0.0011 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.1797 0.2046 0.2352 -0.0139 -0.0142 -0.0015 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1388 0.1405 0.1823 -0.0066 -0.0014 -0.0055 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1287 0.1278 0.1697 -0.0049 -0.0002 -0.0038 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1466 0.1474 0.1878 -0.0053 0.0010  -0.0022 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1685 0.1702 0.2116 -0.0071 0.0022  -0.0021 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1376 0.1321 0.1789 -0.0054 0.0017  -0.0034 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1473 0.1402 0.1886 -0.0035 0.0026  0.0001  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1510 0.1438 0.1898 -0.0017 0.0018  -0.0005 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1747 0.1629 0.2203 -0.0036 0.0054  0.0016  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1299 0.1316 0.1686 -0.0044 0.0010  -0.0010 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1356 0.1393 0.1723 -0.0066 0.0026  0.0002  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1405 0.1443 0.1750 -0.0071 0.0020  0.0045  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1633 0.1689 0.1970 -0.0100 0.0025  0.0073  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1363 0.1416 0.1720 -0.0065 0.0036  -0.0016 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1690 0.1765 0.2004 -0.0106 0.0059  -0.0012 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1656 0.1717 0.2071 -0.0056 0.0045  -0.0042 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1428 0.1452 0.1770 -0.0046 0.0009  0.0058  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1404 0.1441 0.1752 -0.0047 0.0003  0.0110  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1392 0.1401 0.1763 -0.0013 0.0002  0.0110  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1393 0.1389 0.1742 0.0000  -0.0001 0.0072  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1514 0.1602 0.1812 -0.0078 -0.0002 0.0127  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1660 0.1783 0.1964 -0.0083 -0.0018 0.0190  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1897 0.2061 0.2226 -0.0108 -0.0030 0.0261  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1564 0.1697 0.1866 -0.0064 -0.0027 0.0198  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2006 0.2211 0.2355 -0.0105 -0.0048 0.0318  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1781 0.1967 0.2109 -0.0080 -0.0045 0.0276  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1709 0.1817 0.1991 -0.0040 -0.0024 0.0154  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.1967 0.2184 0.2304 -0.0072 -0.0057 0.0305  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1841 0.1972 0.2120 -0.0033 -0.0033 0.0177  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.1961 0.2144 0.2272 -0.0046 -0.0049 0.0249  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1400 0.1398 0.1824 -0.0001 0.0010  0.0153  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1487 0.1455 0.1943 0.0027  0.0022  0.0149  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1525 0.1516 0.2052 0.0037  0.0024  0.0224  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1553 0.1565 0.2125 0.0025  0.0021  0.0282  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1729 0.1634 0.2207 0.0034  0.0050  0.0101  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.1830 0.1703 0.2367 0.0027  0.0074  0.0116  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.1788 0.1635 0.2431 0.0045  0.0105  0.0170  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2026 0.1866 0.2727 0.0039  0.0115  0.0211  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1780 0.1612 0.2463 0.0067  0.0126  0.0174  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1499 0.1493 0.2048 0.0058  0.0029  0.0233  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1458 0.1485 0.2101 0.0072  0.0031  0.0314  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1391 0.1378 0.2093 0.0104  0.0066  0.0294  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1472 0.1469 0.2119 0.0107  0.0058  0.0262  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1707 0.1826 0.2306 0.0043  -0.0011 0.0368  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2016 0.2200 0.2713 0.0047  -0.0025 0.0472  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2158 0.2316 0.2956 0.0085  0.0003  0.0489  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2499 0.2769 0.3171 0.0004  -0.0062 0.0537  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1440 0.1373 0.2254 0.0125  0.0114  0.0305  36  SER   A N   
245  C CA  . SER   A 30  ? 0.1499 0.1380 0.2378 0.0149  0.0167  0.0273  36  SER   A CA  
246  C C   . SER   A 30  ? 0.1544 0.1486 0.2491 0.0169  0.0157  0.0338  36  SER   A C   
247  O O   . SER   A 30  ? 0.1662 0.1586 0.2589 0.0177  0.0178  0.0292  36  SER   A O   
248  C CB  . SER   A 30  ? 0.1769 0.1575 0.2773 0.0161  0.0234  0.0272  36  SER   A CB  
249  O OG  . SER   A 30  ? 0.2230 0.1983 0.3314 0.0180  0.0302  0.0239  36  SER   A OG  
250  N N   . SER   A 31  ? 0.1569 0.1593 0.2578 0.0168  0.0118  0.0443  37  SER   A N   
251  C CA  . SER   A 31  ? 0.1489 0.1589 0.2565 0.0179  0.0101  0.0515  37  SER   A CA  
252  C C   . SER   A 31  ? 0.1460 0.1599 0.2397 0.0158  0.0064  0.0470  37  SER   A C   
253  O O   . SER   A 31  ? 0.1681 0.1859 0.2662 0.0170  0.0065  0.0496  37  SER   A O   
254  C CB  . SER   A 31  ? 0.1807 0.2008 0.2971 0.0166  0.0057  0.0649  37  SER   A CB  
255  O OG  . SER   A 31  ? 0.2347 0.2622 0.3377 0.0115  -0.0006 0.0664  37  SER   A OG  
256  N N   . ARG   A 32  ? 0.1317 0.1445 0.2104 0.0129  0.0038  0.0406  38  ARG   A N   
257  C CA  . ARG   A 32  ? 0.1340 0.1490 0.2004 0.0110  0.0012  0.0360  38  ARG   A CA  
258  C C   . ARG   A 32  ? 0.1381 0.1455 0.1978 0.0121  0.0039  0.0262  38  ARG   A C   
259  O O   . ARG   A 32  ? 0.1360 0.1445 0.1870 0.0109  0.0022  0.0227  38  ARG   A O   
260  C CB  . ARG   A 32  ? 0.1403 0.1596 0.1962 0.0066  -0.0028 0.0358  38  ARG   A CB  
261  C CG  . ARG   A 32  ? 0.1657 0.1947 0.2246 0.0031  -0.0063 0.0455  38  ARG   A CG  
262  C CD  . ARG   A 32  ? 0.1612 0.1937 0.2089 -0.0025 -0.0087 0.0440  38  ARG   A CD  
263  N NE  . ARG   A 32  ? 0.1382 0.1715 0.1755 -0.0050 -0.0090 0.0383  38  ARG   A NE  
264  C CZ  . ARG   A 32  ? 0.1416 0.1801 0.1699 -0.0113 -0.0104 0.0378  38  ARG   A CZ  
265  N NH1 . ARG   A 32  ? 0.1711 0.2156 0.1982 -0.0164 -0.0122 0.0430  38  ARG   A NH1 
266  N NH2 . ARG   A 32  ? 0.1519 0.1899 0.1725 -0.0133 -0.0096 0.0323  38  ARG   A NH2 
267  N N   . ASP   A 33  ? 0.1318 0.1319 0.1944 0.0132  0.0078  0.0218  39  ASP   A N   
268  C CA  . ASP   A 33  ? 0.1250 0.1193 0.1798 0.0124  0.0095  0.0133  39  ASP   A CA  
269  C C   . ASP   A 33  ? 0.1267 0.1225 0.1705 0.0103  0.0055  0.0102  39  ASP   A C   
270  O O   . ASP   A 33  ? 0.1342 0.1287 0.1710 0.0094  0.0049  0.0057  39  ASP   A O   
271  C CB  . ASP   A 33  ? 0.1420 0.1351 0.1962 0.0131  0.0119  0.0104  39  ASP   A CB  
272  C CG  . ASP   A 33  ? 0.1387 0.1267 0.1844 0.0109  0.0135  0.0023  39  ASP   A CG  
273  O OD1 . ASP   A 33  ? 0.1487 0.1322 0.1942 0.0093  0.0159  -0.0015 39  ASP   A OD1 
274  O OD2 . ASP   A 33  ? 0.1572 0.1461 0.1966 0.0101  0.0127  -0.0001 39  ASP   A OD2 
275  N N   . LEU   A 34  ? 0.1230 0.1211 0.1662 0.0091  0.0033  0.0127  40  LEU   A N   
276  C CA  . LEU   A 34  ? 0.1274 0.1266 0.1628 0.0073  0.0008  0.0098  40  LEU   A CA  
277  C C   . LEU   A 34  ? 0.1195 0.1164 0.1553 0.0063  0.0011  0.0079  40  LEU   A C   
278  O O   . LEU   A 34  ? 0.1322 0.1284 0.1735 0.0063  0.0023  0.0109  40  LEU   A O   
279  C CB  . LEU   A 34  ? 0.1385 0.1433 0.1711 0.0054  -0.0015 0.0132  40  LEU   A CB  
280  C CG  . LEU   A 34  ? 0.1468 0.1548 0.1764 0.0050  -0.0024 0.0138  40  LEU   A CG  
281  C CD1 . LEU   A 34  ? 0.1596 0.1732 0.1853 0.0012  -0.0039 0.0162  40  LEU   A CD1 
282  C CD2 . LEU   A 34  ? 0.1526 0.1575 0.1774 0.0058  -0.0022 0.0087  40  LEU   A CD2 
283  N N   . LEU   A 35  ? 0.1174 0.1138 0.1486 0.0053  0.0000  0.0041  41  LEU   A N   
284  C CA  . LEU   A 35  ? 0.1156 0.1113 0.1471 0.0039  -0.0002 0.0026  41  LEU   A CA  
285  C C   . LEU   A 35  ? 0.1134 0.1116 0.1421 0.0032  -0.0019 0.0012  41  LEU   A C   
286  O O   . LEU   A 35  ? 0.1212 0.1199 0.1476 0.0037  -0.0028 0.0000  41  LEU   A O   
287  C CB  . LEU   A 35  ? 0.1286 0.1205 0.1608 0.0032  0.0013  -0.0010 41  LEU   A CB  
288  C CG  . LEU   A 35  ? 0.1282 0.1197 0.1611 0.0013  0.0011  -0.0026 41  LEU   A CG  
289  C CD1 . LEU   A 35  ? 0.1527 0.1397 0.1877 -0.0002 0.0043  -0.0052 41  LEU   A CD1 
290  C CD2 . LEU   A 35  ? 0.1345 0.1290 0.1646 0.0000  -0.0016 -0.0045 41  LEU   A CD2 
291  N N   . VAL   A 36  ? 0.1174 0.1169 0.1473 0.0019  -0.0017 0.0014  42  VAL   A N   
292  C CA  . VAL   A 36  ? 0.1155 0.1169 0.1455 0.0012  -0.0018 -0.0001 42  VAL   A CA  
293  C C   . VAL   A 36  ? 0.1155 0.1171 0.1488 0.0004  -0.0019 -0.0014 42  VAL   A C   
294  O O   . VAL   A 36  ? 0.1285 0.1295 0.1628 -0.0008 -0.0011 -0.0009 42  VAL   A O   
295  C CB  . VAL   A 36  ? 0.1170 0.1205 0.1453 -0.0009 -0.0002 0.0007  42  VAL   A CB  
296  C CG1 . VAL   A 36  ? 0.1352 0.1394 0.1657 -0.0018 0.0017  -0.0019 42  VAL   A CG1 
297  C CG2 . VAL   A 36  ? 0.1345 0.1392 0.1595 -0.0010 -0.0006 0.0023  42  VAL   A CG2 
298  N N   . SER   A 37  ? 0.1087 0.1117 0.1444 0.0008  -0.0030 -0.0023 43  SER   A N   
299  C CA  . SER   A 37  ? 0.1185 0.1234 0.1588 -0.0003 -0.0036 -0.0028 43  SER   A CA  
300  C C   . SER   A 37  ? 0.1197 0.1271 0.1660 0.0003  -0.0023 -0.0026 43  SER   A C   
301  O O   . SER   A 37  ? 0.1266 0.1336 0.1734 0.0013  -0.0009 -0.0025 43  SER   A O   
302  C CB  . SER   A 37  ? 0.1347 0.1407 0.1742 -0.0012 -0.0063 -0.0029 43  SER   A CB  
303  O OG  . SER   A 37  ? 0.1384 0.1461 0.1776 -0.0004 -0.0083 -0.0016 43  SER   A OG  
304  N N   . SER   A 38  ? 0.1314 0.1411 0.1834 -0.0007 -0.0019 -0.0027 44  SER   A N   
305  C CA  . SER   A 38  ? 0.1459 0.1579 0.2067 0.0000  0.0005  -0.0025 44  SER   A CA  
306  C C   . SER   A 38  ? 0.1619 0.1781 0.2305 0.0014  -0.0025 0.0008  44  SER   A C   
307  O O   . SER   A 38  ? 0.1928 0.2117 0.2595 0.0003  -0.0069 0.0025  44  SER   A O   
308  C CB  . SER   A 38  ? 0.1676 0.1806 0.2324 -0.0018 0.0030  -0.0039 44  SER   A CB  
309  O OG  . SER   A 38  ? 0.2069 0.2223 0.2728 -0.0028 -0.0004 -0.0029 44  SER   A OG  
310  N N   . THR   A 39  ? 0.1588 0.1758 0.2366 0.0033  0.0001  0.0021  45  THR   A N   
311  C CA  . THR   A 39  ? 0.1819 0.2038 0.2697 0.0049  -0.0028 0.0072  45  THR   A CA  
312  C C   . THR   A 39  ? 0.2001 0.2254 0.3040 0.0060  0.0005  0.0089  45  THR   A C   
313  O O   . THR   A 39  ? 0.1933 0.2151 0.3002 0.0059  0.0070  0.0049  45  THR   A O   
314  C CB  . THR   A 39  ? 0.1898 0.2094 0.2773 0.0068  -0.0024 0.0087  45  THR   A CB  
315  O OG1 . THR   A 39  ? 0.1992 0.2146 0.2909 0.0077  0.0045  0.0056  45  THR   A OG1 
316  C CG2 . THR   A 39  ? 0.1951 0.2117 0.2682 0.0059  -0.0049 0.0070  45  THR   A CG2 
317  N N   . THR   A 40  ? 0.2050 0.2373 0.3197 0.0067  -0.0036 0.0152  46  THR   A N   
318  C CA  . THR   A 40  ? 0.2196 0.2562 0.3535 0.0084  -0.0006 0.0185  46  THR   A CA  
319  C C   . THR   A 40  ? 0.2175 0.2510 0.3631 0.0118  0.0047  0.0201  46  THR   A C   
320  O O   . THR   A 40  ? 0.2488 0.2795 0.4057 0.0130  0.0126  0.0174  46  THR   A O   
321  C CB  . THR   A 40  ? 0.2647 0.3119 0.4068 0.0071  -0.0077 0.0260  46  THR   A CB  
322  O OG1 . THR   A 40  ? 0.3213 0.3723 0.4607 0.0066  -0.0139 0.0318  46  THR   A OG1 
323  C CG2 . THR   A 40  ? 0.2766 0.3256 0.4078 0.0030  -0.0111 0.0230  46  THR   A CG2 
324  N N   . ALA   A 41  ? 0.2209 0.2540 0.3630 0.0129  0.0014  0.0235  47  ALA   A N   
325  C CA  . ALA   A 41  ? 0.2341 0.2636 0.3874 0.0159  0.0067  0.0252  47  ALA   A CA  
326  C C   . ALA   A 41  ? 0.2183 0.2380 0.3588 0.0151  0.0128  0.0169  47  ALA   A C   
327  O O   . ALA   A 41  ? 0.2208 0.2383 0.3432 0.0129  0.0096  0.0133  47  ALA   A O   
328  C CB  . ALA   A 41  ? 0.2695 0.3038 0.4261 0.0170  0.0001  0.0339  47  ALA   A CB  
329  N N   . GLN   A 42  ? 0.1992 0.2136 0.3497 0.0164  0.0213  0.0146  48  GLN   A N   
330  C CA  . GLN   A 42  ? 0.2107 0.2170 0.3493 0.0142  0.0271  0.0071  48  GLN   A CA  
331  C C   . GLN   A 42  ? 0.2096 0.2145 0.3422 0.0153  0.0234  0.0101  48  GLN   A C   
332  O O   . GLN   A 42  ? 0.2201 0.2276 0.3653 0.0183  0.0213  0.0174  48  GLN   A O   
333  C CB  . GLN   A 42  ? 0.2421 0.2426 0.3925 0.0136  0.0391  0.0019  48  GLN   A CB  
334  C CG  . GLN   A 42  ? 0.3116 0.3120 0.4631 0.0106  0.0445  -0.0039 48  GLN   A CG  
335  C CD  . GLN   A 42  ? 0.3937 0.3880 0.5574 0.0091  0.0578  -0.0098 48  GLN   A CD  
336  O OE1 . GLN   A 42  ? 0.3764 0.3709 0.5629 0.0128  0.0627  -0.0060 48  GLN   A OE1 
337  N NE2 . GLN   A 42  ? 0.4226 0.4115 0.5721 0.0031  0.0641  -0.0189 48  GLN   A NE2 
338  N N   . GLY   A 43  ? 0.1797 0.1812 0.2942 0.0127  0.0225  0.0052  49  GLY   A N   
339  C CA  . GLY   A 43  ? 0.1904 0.1903 0.2973 0.0132  0.0194  0.0070  49  GLY   A CA  
340  C C   . GLY   A 43  ? 0.1766 0.1700 0.2865 0.0126  0.0272  0.0035  49  GLY   A C   
341  O O   . GLY   A 43  ? 0.1813 0.1706 0.2946 0.0103  0.0357  -0.0024 49  GLY   A O   
342  N N   . CYS   A 44  ? 0.1559 0.1482 0.2615 0.0134  0.0245  0.0061  50  CYS   A N   
343  C CA  . CYS   A 44  ? 0.1651 0.1510 0.2740 0.0127  0.0318  0.0033  50  CYS   A CA  
344  C C   . CYS   A 44  ? 0.1741 0.1572 0.2655 0.0089  0.0322  -0.0022 50  CYS   A C   
345  O O   . CYS   A 44  ? 0.1823 0.1600 0.2747 0.0070  0.0387  -0.0056 50  CYS   A O   
346  C CB  . CYS   A 44  ? 0.1820 0.1686 0.3041 0.0165  0.0299  0.0116  50  CYS   A CB  
347  S SG  . CYS   A 44  ? 0.2169 0.2074 0.3654 0.0208  0.0313  0.0195  50  CYS   A SG  
348  N N   . ASP   A 45  ? 0.1578 0.1445 0.2346 0.0077  0.0255  -0.0024 51  ASP   A N   
349  C CA  . ASP   A 45  ? 0.1537 0.1393 0.2160 0.0042  0.0253  -0.0062 51  ASP   A CA  
350  C C   . ASP   A 45  ? 0.1675 0.1513 0.2244 -0.0012 0.0317  -0.0131 51  ASP   A C   
351  O O   . ASP   A 45  ? 0.1938 0.1788 0.2532 -0.0023 0.0335  -0.0149 51  ASP   A O   
352  C CB  . ASP   A 45  ? 0.1425 0.1325 0.1939 0.0049  0.0171  -0.0038 51  ASP   A CB  
353  C CG  . ASP   A 45  ? 0.1552 0.1472 0.2084 0.0081  0.0113  0.0019  51  ASP   A CG  
354  O OD1 . ASP   A 45  ? 0.1637 0.1534 0.2205 0.0090  0.0126  0.0039  51  ASP   A OD1 
355  O OD2 . ASP   A 45  ? 0.1563 0.1519 0.2064 0.0090  0.0057  0.0043  51  ASP   A OD2 
356  N N   . THR   A 46  ? 0.1798 0.1617 0.2288 -0.0055 0.0350  -0.0170 52  THR   A N   
357  C CA  . THR   A 46  ? 0.2061 0.1881 0.2464 -0.0130 0.0403  -0.0233 52  THR   A CA  
358  C C   . THR   A 46  ? 0.1900 0.1771 0.2159 -0.0158 0.0342  -0.0219 52  THR   A C   
359  O O   . THR   A 46  ? 0.1965 0.1843 0.2199 -0.0134 0.0300  -0.0189 52  THR   A O   
360  C CB  . THR   A 46  ? 0.2866 0.2627 0.3298 -0.0174 0.0500  -0.0289 52  THR   A CB  
361  O OG1 . THR   A 46  ? 0.3467 0.3179 0.4061 -0.0147 0.0570  -0.0301 52  THR   A OG1 
362  C CG2 . THR   A 46  ? 0.3309 0.3082 0.3615 -0.0274 0.0548  -0.0356 52  THR   A CG2 
363  N N   . ILE   A 47  ? 0.1822 0.1736 0.2001 -0.0208 0.0334  -0.0232 53  ILE   A N   
364  C CA  . ILE   A 47  ? 0.1686 0.1659 0.1760 -0.0234 0.0278  -0.0204 53  ILE   A CA  
365  C C   . ILE   A 47  ? 0.1711 0.1702 0.1698 -0.0318 0.0315  -0.0239 53  ILE   A C   
366  O O   . ILE   A 47  ? 0.1877 0.1857 0.1834 -0.0392 0.0383  -0.0295 53  ILE   A O   
367  C CB  . ILE   A 47  ? 0.1670 0.1692 0.1712 -0.0247 0.0242  -0.0179 53  ILE   A CB  
368  C CG1 . ILE   A 47  ? 0.1759 0.1764 0.1883 -0.0178 0.0215  -0.0155 53  ILE   A CG1 
369  C CG2 . ILE   A 47  ? 0.1649 0.1738 0.1621 -0.0261 0.0180  -0.0129 53  ILE   A CG2 
370  C CD1 . ILE   A 47  ? 0.1800 0.1798 0.1957 -0.0107 0.0158  -0.0112 53  ILE   A CD1 
371  N N   . ALA   A 48  ? 0.1559 0.1580 0.1497 -0.0318 0.0275  -0.0210 54  ALA   A N   
372  C CA  . ALA   A 48  ? 0.1649 0.1710 0.1495 -0.0405 0.0294  -0.0231 54  ALA   A CA  
373  C C   . ALA   A 48  ? 0.1634 0.1782 0.1397 -0.0483 0.0271  -0.0214 54  ALA   A C   
374  O O   . ALA   A 48  ? 0.1707 0.1902 0.1480 -0.0450 0.0210  -0.0154 54  ALA   A O   
375  C CB  . ALA   A 48  ? 0.1593 0.1681 0.1425 -0.0376 0.0243  -0.0189 54  ALA   A CB  
376  N N   . ARG   A 49  ? 0.1914 0.2087 0.1591 -0.0595 0.0322  -0.0262 55  ARG   A N   
377  C CA  . ARG   A 49  ? 0.2111 0.2385 0.1693 -0.0691 0.0297  -0.0237 55  ARG   A CA  
378  C C   . ARG   A 49  ? 0.2318 0.2659 0.1807 -0.0783 0.0294  -0.0237 55  ARG   A C   
379  O O   . ARG   A 49  ? 0.2553 0.2880 0.1969 -0.0887 0.0368  -0.0313 55  ARG   A O   
380  C CB  . ARG   A 49  ? 0.2292 0.2542 0.1844 -0.0762 0.0369  -0.0302 55  ARG   A CB  
381  C CG  . ARG   A 49  ? 0.2278 0.2462 0.1935 -0.0669 0.0376  -0.0303 55  ARG   A CG  
382  C CD  . ARG   A 49  ? 0.2083 0.2317 0.1772 -0.0605 0.0288  -0.0216 55  ARG   A CD  
383  N NE  . ARG   A 49  ? 0.1992 0.2166 0.1773 -0.0530 0.0300  -0.0226 55  ARG   A NE  
384  C CZ  . ARG   A 49  ? 0.1935 0.2119 0.1769 -0.0454 0.0237  -0.0166 55  ARG   A CZ  
385  N NH1 . ARG   A 49  ? 0.1973 0.2218 0.1791 -0.0439 0.0166  -0.0093 55  ARG   A NH1 
386  N NH2 . ARG   A 49  ? 0.2264 0.2397 0.2181 -0.0394 0.0249  -0.0178 55  ARG   A NH2 
387  N N   . CYS   A 50  ? 0.2239 0.2658 0.1735 -0.0754 0.0212  -0.0153 56  CYS   A N   
388  C CA  . CYS   A 50  ? 0.2147 0.2629 0.1586 -0.0815 0.0198  -0.0141 56  CYS   A CA  
389  C C   . CYS   A 50  ? 0.2154 0.2737 0.1631 -0.0774 0.0103  -0.0029 56  CYS   A C   
390  O O   . CYS   A 50  ? 0.2371 0.2963 0.1925 -0.0694 0.0055  0.0034  56  CYS   A O   
391  C CB  . CYS   A 50  ? 0.2074 0.2448 0.1553 -0.0763 0.0249  -0.0201 56  CYS   A CB  
392  S SG  . CYS   A 50  ? 0.2152 0.2472 0.1756 -0.0598 0.0194  -0.0145 56  CYS   A SG  
393  N N   . ASP   A 51  ? 0.2451 0.3110 0.1889 -0.0829 0.0082  -0.0006 57  ASP   A N   
394  C CA  . ASP   A 51  ? 0.2668 0.3423 0.2169 -0.0788 0.0004  0.0099  57  ASP   A CA  
395  C C   . ASP   A 51  ? 0.2594 0.3300 0.2129 -0.0732 0.0014  0.0079  57  ASP   A C   
396  O O   . ASP   A 51  ? 0.2654 0.3452 0.2210 -0.0743 -0.0031 0.0143  57  ASP   A O   
397  C CB  . ASP   A 51  ? 0.3337 0.4265 0.2779 -0.0907 -0.0049 0.0178  57  ASP   A CB  
398  C CG  . ASP   A 51  ? 0.4226 0.5201 0.3548 -0.1040 -0.0016 0.0125  57  ASP   A CG  
399  O OD1 . ASP   A 51  ? 0.4435 0.5295 0.3724 -0.1039 0.0059  0.0020  57  ASP   A OD1 
400  O OD2 . ASP   A 51  ? 0.4751 0.5884 0.4017 -0.1153 -0.0063 0.0193  57  ASP   A OD2 
401  N N   . CYS   A 52  ? 0.2168 0.2735 0.1721 -0.0671 0.0070  -0.0001 58  CYS   A N   
402  C CA  . CYS   A 52  ? 0.1988 0.2507 0.1575 -0.0617 0.0077  -0.0013 58  CYS   A CA  
403  C C   . CYS   A 52  ? 0.2037 0.2600 0.1713 -0.0531 0.0015  0.0070  58  CYS   A C   
404  O O   . CYS   A 52  ? 0.1948 0.2511 0.1687 -0.0470 -0.0014 0.0112  58  CYS   A O   
405  C CB  . CYS   A 52  ? 0.2177 0.2551 0.1797 -0.0551 0.0133  -0.0082 58  CYS   A CB  
406  S SG  . CYS   A 52  ? 0.2371 0.2665 0.1928 -0.0639 0.0234  -0.0190 58  CYS   A SG  
407  N N   . GLN   A 53  ? 0.1853 0.2444 0.1540 -0.0528 0.0005  0.0085  59  GLN   A N   
408  C CA  . GLN   A 53  ? 0.1718 0.2331 0.1494 -0.0449 -0.0032 0.0143  59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.1531 0.2055 0.1315 -0.0399 -0.0003 0.0099  59  GLN   A C   
410  O O   . GLN   A 53  ? 0.1598 0.2145 0.1439 -0.0354 -0.0022 0.0135  59  GLN   A O   
411  C CB  . GLN   A 53  ? 0.1895 0.2657 0.1702 -0.0494 -0.0080 0.0229  59  GLN   A CB  
412  C CG  . GLN   A 53  ? 0.2008 0.2869 0.1847 -0.0522 -0.0124 0.0306  59  GLN   A CG  
413  C CD  . GLN   A 53  ? 0.2707 0.3725 0.2613 -0.0554 -0.0177 0.0412  59  GLN   A CD  
414  O OE1 . GLN   A 53  ? 0.3082 0.4227 0.2933 -0.0663 -0.0206 0.0454  59  GLN   A OE1 
415  N NE2 . GLN   A 53  ? 0.2292 0.3317 0.2326 -0.0470 -0.0189 0.0463  59  GLN   A NE2 
416  N N   . THR   A 54  ? 0.1520 0.1946 0.1255 -0.0409 0.0046  0.0025  60  THR   A N   
417  C CA  . THR   A 54  ? 0.1584 0.1920 0.1336 -0.0355 0.0070  -0.0005 60  THR   A CA  
418  C C   . THR   A 54  ? 0.1426 0.1656 0.1195 -0.0313 0.0101  -0.0045 60  THR   A C   
419  O O   . THR   A 54  ? 0.1681 0.1891 0.1428 -0.0349 0.0128  -0.0076 60  THR   A O   
420  C CB  . THR   A 54  ? 0.2034 0.2364 0.1737 -0.0413 0.0102  -0.0039 60  THR   A CB  
421  O OG1 . THR   A 54  ? 0.2969 0.3261 0.2618 -0.0481 0.0153  -0.0097 60  THR   A OG1 
422  C CG2 . THR   A 54  ? 0.1900 0.2347 0.1589 -0.0465 0.0072  0.0002  60  THR   A CG2 
423  N N   . GLY   A 55  ? 0.1377 0.1547 0.1186 -0.0242 0.0095  -0.0039 61  GLY   A N   
424  C CA  . GLY   A 55  ? 0.1440 0.1529 0.1281 -0.0200 0.0112  -0.0058 61  GLY   A CA  
425  C C   . GLY   A 55  ? 0.1267 0.1315 0.1136 -0.0142 0.0097  -0.0041 61  GLY   A C   
426  O O   . GLY   A 55  ? 0.1346 0.1409 0.1201 -0.0143 0.0091  -0.0031 61  GLY   A O   
427  N N   . VAL   A 56  ? 0.1206 0.1208 0.1112 -0.0100 0.0092  -0.0036 62  VAL   A N   
428  C CA  . VAL   A 56  ? 0.1179 0.1151 0.1102 -0.0060 0.0075  -0.0017 62  VAL   A CA  
429  C C   . VAL   A 56  ? 0.1149 0.1126 0.1094 -0.0026 0.0047  -0.0002 62  VAL   A C   
430  O O   . VAL   A 56  ? 0.1237 0.1207 0.1207 -0.0023 0.0051  -0.0008 62  VAL   A O   
431  C CB  . VAL   A 56  ? 0.1371 0.1280 0.1328 -0.0058 0.0105  -0.0020 62  VAL   A CB  
432  C CG1 . VAL   A 56  ? 0.1701 0.1593 0.1678 -0.0027 0.0079  0.0016  62  VAL   A CG1 
433  C CG2 . VAL   A 56  ? 0.1440 0.1332 0.1374 -0.0098 0.0144  -0.0042 62  VAL   A CG2 
434  N N   . TYR   A 57  ? 0.1150 0.1137 0.1084 -0.0008 0.0025  0.0012  63  TYR   A N   
435  C CA  . TYR   A 57  ? 0.1142 0.1129 0.1090 0.0014  0.0004  0.0019  63  TYR   A CA  
436  C C   . TYR   A 57  ? 0.1175 0.1145 0.1111 0.0018  -0.0012 0.0034  63  TYR   A C   
437  O O   . TYR   A 57  ? 0.1279 0.1244 0.1188 0.0008  -0.0010 0.0041  63  TYR   A O   
438  C CB  . TYR   A 57  ? 0.1218 0.1238 0.1170 0.0020  0.0000  0.0017  63  TYR   A CB  
439  C CG  . TYR   A 57  ? 0.1153 0.1178 0.1089 0.0020  0.0005  0.0014  63  TYR   A CG  
440  C CD1 . TYR   A 57  ? 0.1281 0.1325 0.1207 0.0009  0.0017  0.0016  63  TYR   A CD1 
441  C CD2 . TYR   A 57  ? 0.1293 0.1305 0.1221 0.0024  0.0005  0.0004  63  TYR   A CD2 
442  C CE1 . TYR   A 57  ? 0.1485 0.1533 0.1402 0.0007  0.0031  0.0009  63  TYR   A CE1 
443  C CE2 . TYR   A 57  ? 0.1420 0.1432 0.1331 0.0015  0.0024  -0.0010 63  TYR   A CE2 
444  C CZ  . TYR   A 57  ? 0.1553 0.1582 0.1465 0.0010  0.0038  -0.0007 63  TYR   A CZ  
445  O OH  . TYR   A 57  ? 0.1843 0.1872 0.1744 -0.0002 0.0065  -0.0024 63  TYR   A OH  
446  N N   . TYR   A 58  ? 0.1141 0.1110 0.1093 0.0026  -0.0031 0.0042  64  TYR   A N   
447  C CA  . TYR   A 58  ? 0.1177 0.1150 0.1109 0.0015  -0.0055 0.0064  64  TYR   A CA  
448  C C   . TYR   A 58  ? 0.1233 0.1217 0.1116 -0.0001 -0.0054 0.0041  64  TYR   A C   
449  O O   . TYR   A 58  ? 0.1267 0.1253 0.1163 0.0006  -0.0048 0.0021  64  TYR   A O   
450  C CB  . TYR   A 58  ? 0.1297 0.1276 0.1277 0.0022  -0.0077 0.0091  64  TYR   A CB  
451  C CG  . TYR   A 58  ? 0.1370 0.1373 0.1328 -0.0003 -0.0111 0.0129  64  TYR   A CG  
452  C CD1 . TYR   A 58  ? 0.1389 0.1393 0.1339 -0.0015 -0.0119 0.0166  64  TYR   A CD1 
453  C CD2 . TYR   A 58  ? 0.1407 0.1437 0.1342 -0.0025 -0.0135 0.0129  64  TYR   A CD2 
454  C CE1 . TYR   A 58  ? 0.1573 0.1614 0.1491 -0.0051 -0.0157 0.0210  64  TYR   A CE1 
455  C CE2 . TYR   A 58  ? 0.1506 0.1574 0.1402 -0.0066 -0.0170 0.0165  64  TYR   A CE2 
456  C CZ  . TYR   A 58  ? 0.1637 0.1715 0.1525 -0.0080 -0.0184 0.0210  64  TYR   A CZ  
457  O OH  . TYR   A 58  ? 0.2004 0.2134 0.1846 -0.0133 -0.0224 0.0256  64  TYR   A OH  
458  N N   . CYS   A 59  ? 0.1245 0.1234 0.1077 -0.0027 -0.0056 0.0044  65  CYS   A N   
459  C CA  . CYS   A 59  ? 0.1360 0.1353 0.1140 -0.0056 -0.0040 0.0012  65  CYS   A CA  
460  C C   . CYS   A 59  ? 0.1399 0.1412 0.1124 -0.0102 -0.0068 0.0030  65  CYS   A C   
461  O O   . CYS   A 59  ? 0.1467 0.1494 0.1153 -0.0129 -0.0084 0.0059  65  CYS   A O   
462  C CB  . CYS   A 59  ? 0.1432 0.1421 0.1189 -0.0062 -0.0011 -0.0005 65  CYS   A CB  
463  S SG  . CYS   A 59  ? 0.1580 0.1565 0.1284 -0.0105 0.0030  -0.0054 65  CYS   A SG  
464  N N   . SER   A 60  ? 0.1406 0.1429 0.1128 -0.0118 -0.0077 0.0018  66  SER   A N   
465  C CA  . SER   A 60  ? 0.1582 0.1643 0.1248 -0.0176 -0.0113 0.0043  66  SER   A CA  
466  C C   . SER   A 60  ? 0.1547 0.1617 0.1113 -0.0242 -0.0094 0.0015  66  SER   A C   
467  O O   . SER   A 60  ? 0.1794 0.1908 0.1305 -0.0296 -0.0132 0.0058  66  SER   A O   
468  C CB  . SER   A 60  ? 0.1833 0.1906 0.1512 -0.0187 -0.0124 0.0031  66  SER   A CB  
469  O OG  . SER   A 60  ? 0.2118 0.2164 0.1766 -0.0209 -0.0077 -0.0037 66  SER   A OG  
470  N N   . SER   A 61  ? 0.1491 0.1525 0.1043 -0.0242 -0.0034 -0.0049 67  SER   A N   
471  C CA  . SER   A 61  ? 0.1627 0.1662 0.1091 -0.0308 0.0001  -0.0088 67  SER   A CA  
472  C C   . SER   A 61  ? 0.1638 0.1683 0.1070 -0.0315 -0.0009 -0.0057 67  SER   A C   
473  O O   . SER   A 61  ? 0.1752 0.1803 0.1102 -0.0378 0.0018  -0.0085 67  SER   A O   
474  C CB  . SER   A 61  ? 0.1767 0.1757 0.1254 -0.0304 0.0079  -0.0166 67  SER   A CB  
475  O OG  . SER   A 61  ? 0.1737 0.1705 0.1309 -0.0235 0.0102  -0.0162 67  SER   A OG  
476  N N   . ARG   A 62  ? 0.1621 0.1667 0.1114 -0.0260 -0.0042 -0.0002 68  ARG   A N   
477  C CA  . ARG   A 62  ? 0.1693 0.1747 0.1167 -0.0266 -0.0056 0.0039  68  ARG   A CA  
478  C C   . ARG   A 62  ? 0.1764 0.1843 0.1278 -0.0255 -0.0115 0.0124  68  ARG   A C   
479  O O   . ARG   A 62  ? 0.1832 0.1913 0.1347 -0.0256 -0.0127 0.0168  68  ARG   A O   
480  C CB  . ARG   A 62  ? 0.1731 0.1753 0.1260 -0.0213 -0.0019 0.0016  68  ARG   A CB  
481  C CG  . ARG   A 62  ? 0.1809 0.1816 0.1329 -0.0220 0.0043  -0.0050 68  ARG   A CG  
482  C CD  . ARG   A 62  ? 0.1907 0.1922 0.1339 -0.0283 0.0065  -0.0066 68  ARG   A CD  
483  N NE  . ARG   A 62  ? 0.2144 0.2141 0.1588 -0.0290 0.0137  -0.0133 68  ARG   A NE  
484  C CZ  . ARG   A 62  ? 0.1919 0.1903 0.1333 -0.0334 0.0184  -0.0192 68  ARG   A CZ  
485  N NH1 . ARG   A 62  ? 0.2165 0.2159 0.1518 -0.0381 0.0159  -0.0194 68  ARG   A NH1 
486  N NH2 . ARG   A 62  ? 0.2266 0.2229 0.1718 -0.0337 0.0262  -0.0250 68  ARG   A NH2 
487  N N   . ARG   A 63  ? 0.1799 0.1893 0.1364 -0.0237 -0.0147 0.0150  69  ARG   A N   
488  C CA  . ARG   A 63  ? 0.1847 0.1959 0.1499 -0.0208 -0.0190 0.0232  69  ARG   A CA  
489  C C   . ARG   A 63  ? 0.2105 0.2172 0.1825 -0.0155 -0.0165 0.0242  69  ARG   A C   
490  O O   . ARG   A 63  ? 0.2446 0.2517 0.2207 -0.0154 -0.0183 0.0307  69  ARG   A O   
491  C CB  . ARG   A 63  ? 0.2267 0.2440 0.1886 -0.0268 -0.0243 0.0314  69  ARG   A CB  
492  C CG  . ARG   A 63  ? 0.2506 0.2735 0.2083 -0.0321 -0.0275 0.0319  69  ARG   A CG  
493  C CD  . ARG   A 63  ? 0.2673 0.2982 0.2256 -0.0371 -0.0343 0.0431  69  ARG   A CD  
494  N NE  . ARG   A 63  ? 0.2741 0.3121 0.2250 -0.0450 -0.0378 0.0434  69  ARG   A NE  
495  C CZ  . ARG   A 63  ? 0.2349 0.2774 0.1713 -0.0553 -0.0384 0.0415  69  ARG   A CZ  
496  N NH1 . ARG   A 63  ? 0.2477 0.2886 0.1764 -0.0584 -0.0362 0.0404  69  ARG   A NH1 
497  N NH2 . ARG   A 63  ? 0.2593 0.3081 0.1885 -0.0634 -0.0410 0.0409  69  ARG   A NH2 
498  N N   . LYS   A 64  ? 0.1734 0.1763 0.1468 -0.0119 -0.0124 0.0181  70  LYS   A N   
499  C CA  . LYS   A 64  ? 0.1858 0.1851 0.1635 -0.0088 -0.0097 0.0180  70  LYS   A CA  
500  C C   . LYS   A 64  ? 0.1672 0.1643 0.1498 -0.0049 -0.0071 0.0140  70  LYS   A C   
501  O O   . LYS   A 64  ? 0.1656 0.1634 0.1467 -0.0045 -0.0063 0.0101  70  LYS   A O   
502  C CB  . LYS   A 64  ? 0.2261 0.2249 0.1969 -0.0111 -0.0071 0.0150  70  LYS   A CB  
503  C CG  . LYS   A 64  ? 0.3549 0.3510 0.3281 -0.0100 -0.0050 0.0161  70  LYS   A CG  
504  C CD  . LYS   A 64  ? 0.4678 0.4648 0.4340 -0.0140 -0.0049 0.0173  70  LYS   A CD  
505  C CE  . LYS   A 64  ? 0.5306 0.5249 0.4988 -0.0133 -0.0023 0.0175  70  LYS   A CE  
506  N NZ  . LYS   A 64  ? 0.5418 0.5327 0.5187 -0.0107 -0.0021 0.0213  70  LYS   A NZ  
507  N N   . HIS   A 65  ? 0.1530 0.1472 0.1411 -0.0029 -0.0051 0.0147  71  HIS   A N   
508  C CA  . HIS   A 65  ? 0.1466 0.1394 0.1376 -0.0011 -0.0021 0.0108  71  HIS   A CA  
509  C C   . HIS   A 65  ? 0.1628 0.1554 0.1500 -0.0024 0.0004  0.0081  71  HIS   A C   
510  O O   . HIS   A 65  ? 0.2039 0.1949 0.1904 -0.0036 0.0015  0.0096  71  HIS   A O   
511  C CB  . HIS   A 65  ? 0.1423 0.1320 0.1414 0.0004  -0.0002 0.0122  71  HIS   A CB  
512  C CG  . HIS   A 65  ? 0.1483 0.1389 0.1534 0.0020  -0.0025 0.0152  71  HIS   A CG  
513  N ND1 . HIS   A 65  ? 0.1874 0.1782 0.1955 0.0033  -0.0017 0.0127  71  HIS   A ND1 
514  C CD2 . HIS   A 65  ? 0.1470 0.1394 0.1559 0.0020  -0.0058 0.0212  71  HIS   A CD2 
515  C CE1 . HIS   A 65  ? 0.1627 0.1549 0.1769 0.0044  -0.0041 0.0168  71  HIS   A CE1 
516  N NE2 . HIS   A 65  ? 0.1892 0.1829 0.2043 0.0036  -0.0068 0.0223  71  HIS   A NE2 
517  N N   . TYR   A 66  ? 0.1369 0.1318 0.1228 -0.0022 0.0014  0.0049  72  TYR   A N   
518  C CA  . TYR   A 66  ? 0.1364 0.1332 0.1201 -0.0037 0.0033  0.0033  72  TYR   A CA  
519  C C   . TYR   A 66  ? 0.1349 0.1331 0.1205 -0.0046 0.0049  0.0017  72  TYR   A C   
520  O O   . TYR   A 66  ? 0.1337 0.1338 0.1214 -0.0037 0.0042  0.0013  72  TYR   A O   
521  C CB  . TYR   A 66  ? 0.1470 0.1470 0.1293 -0.0035 0.0033  0.0021  72  TYR   A CB  
522  C CG  . TYR   A 66  ? 0.1575 0.1568 0.1357 -0.0047 0.0030  0.0022  72  TYR   A CG  
523  C CD1 . TYR   A 66  ? 0.1862 0.1852 0.1608 -0.0069 0.0040  0.0025  72  TYR   A CD1 
524  C CD2 . TYR   A 66  ? 0.1616 0.1607 0.1387 -0.0048 0.0020  0.0016  72  TYR   A CD2 
525  C CE1 . TYR   A 66  ? 0.1956 0.1945 0.1650 -0.0094 0.0040  0.0024  72  TYR   A CE1 
526  C CE2 . TYR   A 66  ? 0.1858 0.1848 0.1573 -0.0078 0.0021  0.0011  72  TYR   A CE2 
527  C CZ  . TYR   A 66  ? 0.1926 0.1917 0.1601 -0.0103 0.0031  0.0015  72  TYR   A CZ  
528  O OH  . TYR   A 66  ? 0.2275 0.2272 0.1881 -0.0147 0.0035  0.0007  72  TYR   A OH  
529  N N   . PRO   A 67  ? 0.1327 0.1311 0.1169 -0.0073 0.0070  0.0008  73  PRO   A N   
530  C CA  . PRO   A 67  ? 0.1367 0.1385 0.1208 -0.0102 0.0083  -0.0008 73  PRO   A CA  
531  C C   . PRO   A 67  ? 0.1422 0.1513 0.1268 -0.0104 0.0067  0.0004  73  PRO   A C   
532  O O   . PRO   A 67  ? 0.1695 0.1804 0.1540 -0.0098 0.0065  0.0012  73  PRO   A O   
533  C CB  . PRO   A 67  ? 0.1658 0.1653 0.1477 -0.0140 0.0115  -0.0024 73  PRO   A CB  
534  C CG  . PRO   A 67  ? 0.1930 0.1902 0.1738 -0.0124 0.0110  -0.0007 73  PRO   A CG  
535  C CD  . PRO   A 67  ? 0.1474 0.1432 0.1295 -0.0086 0.0083  0.0014  73  PRO   A CD  
536  N N   . VAL   A 68  ? 0.1198 0.1332 0.1059 -0.0115 0.0057  0.0011  74  VAL   A N   
537  C CA  . VAL   A 68  ? 0.1363 0.1576 0.1261 -0.0113 0.0039  0.0041  74  VAL   A CA  
538  C C   . VAL   A 68  ? 0.1311 0.1595 0.1203 -0.0162 0.0031  0.0056  74  VAL   A C   
539  O O   . VAL   A 68  ? 0.1418 0.1685 0.1279 -0.0191 0.0039  0.0036  74  VAL   A O   
540  C CB  . VAL   A 68  ? 0.1743 0.1949 0.1688 -0.0068 0.0027  0.0055  74  VAL   A CB  
541  C CG1 . VAL   A 68  ? 0.1971 0.2132 0.1915 -0.0038 0.0037  0.0042  74  VAL   A CG1 
542  C CG2 . VAL   A 68  ? 0.1734 0.1908 0.1672 -0.0063 0.0022  0.0045  74  VAL   A CG2 
543  N N   . SER   A 69  ? 0.1313 0.1688 0.1246 -0.0175 0.0013  0.0098  75  SER   A N   
544  C CA  A SER   A 69  ? 0.1256 0.1730 0.1204 -0.0220 -0.0011 0.0140  75  SER   A CA  
545  C CA  B SER   A 69  ? 0.1295 0.1771 0.1243 -0.0221 -0.0011 0.0141  75  SER   A CA  
546  C C   . SER   A 69  ? 0.1194 0.1694 0.1226 -0.0174 -0.0031 0.0187  75  SER   A C   
547  O O   . SER   A 69  ? 0.1340 0.1818 0.1438 -0.0120 -0.0022 0.0195  75  SER   A O   
548  C CB  A SER   A 69  ? 0.1374 0.1949 0.1340 -0.0262 -0.0024 0.0178  75  SER   A CB  
549  C CB  B SER   A 69  ? 0.1525 0.2095 0.1501 -0.0252 -0.0022 0.0178  75  SER   A CB  
550  O OG  A SER   A 69  ? 0.1825 0.2370 0.1716 -0.0306 0.0000  0.0133  75  SER   A OG  
551  O OG  B SER   A 69  ? 0.1887 0.2577 0.1886 -0.0304 -0.0055 0.0238  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1316 0.1853 0.1345 -0.0199 -0.0049 0.0209  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1287 0.1838 0.1401 -0.0155 -0.0064 0.0254  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1284 0.1952 0.1431 -0.0202 -0.0099 0.0328  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1439 0.2164 0.1510 -0.0280 -0.0111 0.0327  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1352 0.1800 0.1438 -0.0119 -0.0048 0.0205  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1251 0.1673 0.1250 -0.0165 -0.0041 0.0164  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1307 0.1658 0.1242 -0.0176 -0.0013 0.0104  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1311 0.1772 0.1303 -0.0197 -0.0055 0.0186  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1454 0.1772 0.1335 -0.0216 0.0009  0.0063  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1550 0.1979 0.1468 -0.0243 -0.0035 0.0139  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1459 0.1816 0.1329 -0.0251 0.0002  0.0076  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1240 0.1949 0.1507 -0.0162 -0.0113 0.0396  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1305 0.2140 0.1627 -0.0204 -0.0155 0.0491  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1332 0.2159 0.1587 -0.0240 -0.0167 0.0484  77  SER   A C   
566  O O   . SER   A 71  ? 0.1453 0.2170 0.1651 -0.0214 -0.0140 0.0410  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1416 0.2293 0.1919 -0.0143 -0.0157 0.0575  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1641 0.2413 0.2190 -0.0076 -0.0127 0.0543  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1394 0.2342 0.1656 -0.0305 -0.0208 0.0563  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1443 0.2392 0.1644 -0.0346 -0.0218 0.0563  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1488 0.2387 0.1799 -0.0268 -0.0214 0.0595  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1592 0.2505 0.2049 -0.0205 -0.0214 0.0655  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.1629 0.2740 0.1803 -0.0451 -0.0267 0.0651  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.1927 0.3084 0.1972 -0.0548 -0.0263 0.0605  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.2758 0.4084 0.2748 -0.0677 -0.0313 0.0685  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.3608 0.4964 0.3455 -0.0784 -0.0295 0.0620  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4274 0.5740 0.3993 -0.0934 -0.0314 0.0635  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1412 0.2252 0.1670 -0.0272 -0.0204 0.0558  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1448 0.2233 0.1805 -0.0202 -0.0195 0.0581  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.1555 0.2449 0.2057 -0.0199 -0.0230 0.0715  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.1767 0.2787 0.2252 -0.0275 -0.0275 0.0795  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.1740 0.2475 0.1997 -0.0234 -0.0185 0.0526  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2191 0.2906 0.2312 -0.0291 -0.0167 0.0445  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.1716 0.2525 0.1824 -0.0340 -0.0188 0.0481  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1495 0.2343 0.2145 -0.0116 -0.0206 0.0740  80  SER   A N   
586  C CA  . SER   A 74  ? 0.1614 0.2557 0.2453 -0.0095 -0.0227 0.0875  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1403 0.2249 0.2378 -0.0014 -0.0182 0.0876  80  SER   A C   
588  O O   . SER   A 74  ? 0.1339 0.2052 0.2259 0.0025  -0.0136 0.0768  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2085 0.3096 0.3020 -0.0081 -0.0227 0.0919  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.2990 0.4027 0.3785 -0.0135 -0.0239 0.0863  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.1476 0.2397 0.2652 0.0011  -0.0190 0.1005  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.1622 0.2459 0.2965 0.0084  -0.0137 0.1019  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.1695 0.2508 0.3182 0.0142  -0.0084 0.1014  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.1878 0.2811 0.3503 0.0139  -0.0108 0.1124  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.1714 0.2654 0.3209 0.0073  -0.0174 0.1177  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2156 0.3005 0.3831 0.0142  -0.0115 0.1199  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2298 0.3012 0.3839 0.0145  -0.0085 0.1082  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2322 0.3292 0.4184 0.0133  -0.0155 0.1383  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.1618 0.2291 0.3071 0.0184  -0.0016 0.0891  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.1742 0.2375 0.3294 0.0227  0.0046  0.0856  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.1868 0.2380 0.3552 0.0283  0.0136  0.0812  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.1801 0.2209 0.3390 0.0282  0.0159  0.0730  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2038 0.2616 0.3383 0.0204  0.0047  0.0729  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2319 0.3004 0.3521 0.0139  -0.0032 0.0756  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2217 0.2742 0.3628 0.0238  0.0116  0.0672  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.2209 0.2868 0.3262 0.0117  -0.0034 0.0672  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.1865 0.2379 0.3764 0.0326  0.0199  0.0854  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2047 0.2433 0.4074 0.0370  0.0307  0.0794  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2314 0.2593 0.4185 0.0358  0.0359  0.0638  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.2763 0.3074 0.4595 0.0351  0.0357  0.0615  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2070 0.2498 0.4404 0.0419  0.0368  0.0894  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2419 0.2712 0.4913 0.0459  0.0488  0.0846  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.2707 0.2966 0.5278 0.0470  0.0494  0.0893  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.2870 0.3061 0.5411 0.0473  0.0600  0.0738  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.2976 0.3101 0.5691 0.0499  0.0614  0.0838  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.2978 0.3038 0.5655 0.0495  0.0724  0.0678  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.2996 0.3021 0.5766 0.0510  0.0732  0.0729  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2068 0.2227 0.3834 0.0348  0.0399  0.0533  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2017 0.2081 0.3617 0.0323  0.0440  0.0390  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.1940 0.1886 0.3654 0.0335  0.0563  0.0318  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.2027 0.1923 0.3842 0.0349  0.0600  0.0334  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.1928 0.1962 0.3294 0.0285  0.0377  0.0327  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2050 0.2002 0.3249 0.0252  0.0410  0.0196  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2042 0.2182 0.3302 0.0266  0.0273  0.0388  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.1950 0.1846 0.3634 0.0321  0.0631  0.0229  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.2078 0.1859 0.3856 0.0316  0.0764  0.0142  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.2125 0.1810 0.3752 0.0272  0.0783  0.0041  85  GLU   A C   
628  O O   . GLU   A 79  ? 0.2222 0.1928 0.3650 0.0243  0.0695  0.0023  85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.2557 0.2316 0.4314 0.0296  0.0831  0.0066  85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.3203 0.3047 0.5167 0.0343  0.0842  0.0162  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.4056 0.3904 0.6337 0.0400  0.0910  0.0258  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.4207 0.3943 0.6594 0.0400  0.1025  0.0198  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.4580 0.4548 0.7010 0.0439  0.0848  0.0399  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.2190 0.1770 0.3926 0.0263  0.0905  -0.0024 86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.2355 0.1843 0.3962 0.0210  0.0938  -0.0125 86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.2589 0.2068 0.3931 0.0140  0.0907  -0.0230 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.2768 0.2262 0.4053 0.0120  0.0922  -0.0267 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.2521 0.1892 0.4296 0.0200  0.1099  -0.0194 86  ALA   A CB  
639  N N   A SER   A 81  ? 0.2421 0.1879 0.3601 0.0097  0.0861  -0.0272 87  SER   A N   
640  N N   B SER   A 81  ? 0.2708 0.2165 0.3895 0.0098  0.0864  -0.0272 87  SER   A N   
641  C CA  A SER   A 81  ? 0.2442 0.1896 0.3384 0.0022  0.0831  -0.0362 87  SER   A CA  
642  C CA  B SER   A 81  ? 0.2992 0.2447 0.3938 0.0024  0.0829  -0.0358 87  SER   A CA  
643  C C   A SER   A 81  ? 0.2724 0.2096 0.3609 -0.0042 0.0891  -0.0451 87  SER   A C   
644  C C   B SER   A 81  ? 0.3019 0.2394 0.3905 -0.0039 0.0885  -0.0445 87  SER   A C   
645  O O   A SER   A 81  ? 0.2691 0.2000 0.3731 -0.0022 0.0967  -0.0449 87  SER   A O   
646  O O   B SER   A 81  ? 0.3042 0.2358 0.4080 -0.0017 0.0953  -0.0438 87  SER   A O   
647  C CB  A SER   A 81  ? 0.2213 0.1755 0.3012 0.0033  0.0689  -0.0303 87  SER   A CB  
648  C CB  B SER   A 81  ? 0.3486 0.3031 0.4302 0.0040  0.0687  -0.0293 87  SER   A CB  
649  O OG  A SER   A 81  ? 0.1566 0.1112 0.2361 0.0044  0.0640  -0.0269 87  SER   A OG  
650  O OG  B SER   A 81  ? 0.4198 0.3772 0.4845 -0.0004 0.0648  -0.0333 87  SER   A OG  
651  N N   . GLU   A 82  ? 0.3041 0.2421 0.3715 -0.0119 0.0852  -0.0518 88  GLU   A N   
652  C CA  . GLU   A 82  ? 0.3158 0.2478 0.3770 -0.0188 0.0895  -0.0594 88  GLU   A CA  
653  C C   . GLU   A 82  ? 0.2720 0.2064 0.3355 -0.0148 0.0818  -0.0525 88  GLU   A C   
654  O O   . GLU   A 82  ? 0.2849 0.2138 0.3489 -0.0185 0.0861  -0.0570 88  GLU   A O   
655  C CB  . GLU   A 82  ? 0.4151 0.3476 0.4545 -0.0301 0.0893  -0.0687 88  GLU   A CB  
656  C CG  . GLU   A 82  ? 0.5045 0.4461 0.5278 -0.0315 0.0754  -0.0642 88  GLU   A CG  
657  C CD  . GLU   A 82  ? 0.6137 0.5574 0.6172 -0.0435 0.0743  -0.0715 88  GLU   A CD  
658  O OE1 . GLU   A 82  ? 0.6420 0.5848 0.6399 -0.0491 0.0739  -0.0748 88  GLU   A OE1 
659  O OE2 . GLU   A 82  ? 0.6142 0.5611 0.6076 -0.0478 0.0734  -0.0734 88  GLU   A OE2 
660  N N   . TYR   A 83  ? 0.2472 0.1895 0.3136 -0.0075 0.0714  -0.0419 89  TYR   A N   
661  C CA  . TYR   A 83  ? 0.2271 0.1724 0.2942 -0.0045 0.0640  -0.0357 89  TYR   A CA  
662  C C   . TYR   A 83  ? 0.2132 0.1584 0.2995 0.0029  0.0651  -0.0267 89  TYR   A C   
663  O O   . TYR   A 83  ? 0.2197 0.1648 0.3084 0.0039  0.0624  -0.0234 89  TYR   A O   
664  C CB  . TYR   A 83  ? 0.2283 0.1825 0.2822 -0.0038 0.0518  -0.0312 89  TYR   A CB  
665  C CG  . TYR   A 83  ? 0.2392 0.1948 0.2756 -0.0113 0.0495  -0.0380 89  TYR   A CG  
666  C CD1 . TYR   A 83  ? 0.2730 0.2282 0.3007 -0.0170 0.0479  -0.0418 89  TYR   A CD1 
667  C CD2 . TYR   A 83  ? 0.2573 0.2152 0.2864 -0.0134 0.0492  -0.0399 89  TYR   A CD2 
668  C CE1 . TYR   A 83  ? 0.3027 0.2614 0.3149 -0.0244 0.0444  -0.0459 89  TYR   A CE1 
669  C CE2 . TYR   A 83  ? 0.2938 0.2544 0.3070 -0.0208 0.0461  -0.0443 89  TYR   A CE2 
670  C CZ  . TYR   A 83  ? 0.3352 0.2965 0.3404 -0.0266 0.0438  -0.0471 89  TYR   A CZ  
671  O OH  . TYR   A 83  ? 0.3910 0.3569 0.3814 -0.0344 0.0398  -0.0495 89  TYR   A OH  
672  N N   . TYR   A 84  ? 0.2255 0.1719 0.3254 0.0077  0.0683  -0.0218 90  TYR   A N   
673  C CA  . TYR   A 84  ? 0.2079 0.1563 0.3277 0.0142  0.0686  -0.0112 90  TYR   A CA  
674  C C   . TYR   A 84  ? 0.2145 0.1588 0.3538 0.0171  0.0792  -0.0106 90  TYR   A C   
675  O O   . TYR   A 84  ? 0.2190 0.1637 0.3548 0.0158  0.0818  -0.0148 90  TYR   A O   
676  C CB  . TYR   A 84  ? 0.1922 0.1520 0.3099 0.0181  0.0572  -0.0007 90  TYR   A CB  
677  C CG  . TYR   A 84  ? 0.1762 0.1407 0.2776 0.0161  0.0473  0.0000  90  TYR   A CG  
678  C CD1 . TYR   A 84  ? 0.1821 0.1468 0.2861 0.0166  0.0447  0.0040  90  TYR   A CD1 
679  C CD2 . TYR   A 84  ? 0.1781 0.1470 0.2630 0.0139  0.0409  -0.0029 90  TYR   A CD2 
680  C CE1 . TYR   A 84  ? 0.1750 0.1439 0.2656 0.0148  0.0366  0.0043  90  TYR   A CE1 
681  C CE2 . TYR   A 84  ? 0.1802 0.1530 0.2531 0.0124  0.0330  -0.0022 90  TYR   A CE2 
682  C CZ  . TYR   A 84  ? 0.1627 0.1356 0.2386 0.0129  0.0311  0.0012  90  TYR   A CZ  
683  O OH  . TYR   A 84  ? 0.1669 0.1433 0.2324 0.0113  0.0246  0.0013  90  TYR   A OH  
684  N N   . PRO   A 85  ? 0.2259 0.1673 0.3869 0.0213  0.0846  -0.0039 91  PRO   A N   
685  C CA  . PRO   A 85  ? 0.2298 0.1695 0.4141 0.0256  0.0938  -0.0002 91  PRO   A CA  
686  C C   . PRO   A 85  ? 0.2349 0.1873 0.4237 0.0301  0.0851  0.0112  91  PRO   A C   
687  O O   . PRO   A 85  ? 0.2262 0.1876 0.4010 0.0298  0.0726  0.0163  91  PRO   A O   
688  C CB  . PRO   A 85  ? 0.2416 0.1769 0.4484 0.0293  0.0992  0.0070  91  PRO   A CB  
689  C CG  . PRO   A 85  ? 0.2571 0.1987 0.4533 0.0292  0.0872  0.0136  91  PRO   A CG  
690  C CD  . PRO   A 85  ? 0.2367 0.1780 0.4040 0.0231  0.0816  0.0027  91  PRO   A CD  
691  N N   . ALA   A 86  ? 0.2393 0.1931 0.4480 0.0339  0.0914  0.0156  92  ALA   A N   
692  C CA  . ALA   A 86  ? 0.2371 0.2040 0.4522 0.0377  0.0833  0.0276  92  ALA   A CA  
693  C C   . ALA   A 86  ? 0.2380 0.2133 0.4623 0.0407  0.0747  0.0423  92  ALA   A C   
694  O O   . ALA   A 86  ? 0.2585 0.2290 0.4993 0.0429  0.0799  0.0466  92  ALA   A O   
695  C CB  . ALA   A 86  ? 0.2399 0.2063 0.4796 0.0415  0.0933  0.0304  92  ALA   A CB  
696  N N   . ARG   A 87  ? 0.2358 0.2226 0.4465 0.0396  0.0620  0.0486  93  ARG   A N   
697  C CA  . ARG   A 87  ? 0.2218 0.2171 0.4358 0.0402  0.0534  0.0610  93  ARG   A CA  
698  C C   . ARG   A 87  ? 0.2142 0.2232 0.4159 0.0381  0.0417  0.0673  93  ARG   A C   
699  O O   . ARG   A 87  ? 0.2231 0.2333 0.4118 0.0364  0.0402  0.0609  93  ARG   A O   
700  C CB  . ARG   A 87  ? 0.2321 0.2204 0.4303 0.0370  0.0517  0.0541  93  ARG   A CB  
701  C CG  . ARG   A 87  ? 0.2636 0.2532 0.4331 0.0325  0.0445  0.0449  93  ARG   A CG  
702  C CD  . ARG   A 87  ? 0.2564 0.2382 0.4114 0.0294  0.0448  0.0359  93  ARG   A CD  
703  N NE  . ARG   A 87  ? 0.2361 0.2224 0.3696 0.0260  0.0357  0.0333  93  ARG   A NE  
704  C CZ  . ARG   A 87  ? 0.2746 0.2631 0.3919 0.0237  0.0317  0.0278  93  ARG   A CZ  
705  N NH1 . ARG   A 87  ? 0.2583 0.2472 0.3765 0.0243  0.0344  0.0252  93  ARG   A NH1 
706  N NH2 . ARG   A 87  ? 0.2208 0.2119 0.3224 0.0210  0.0251  0.0258  93  ARG   A NH2 
707  N N   . TYR   A 88  ? 0.2129 0.2319 0.4172 0.0373  0.0336  0.0794  94  TYR   A N   
708  C CA  . TYR   A 88  ? 0.2156 0.2470 0.4055 0.0334  0.0229  0.0842  94  TYR   A CA  
709  C C   . TYR   A 88  ? 0.1915 0.2187 0.3558 0.0291  0.0186  0.0744  94  TYR   A C   
710  O O   . TYR   A 88  ? 0.2092 0.2316 0.3712 0.0285  0.0189  0.0734  94  TYR   A O   
711  C CB  . TYR   A 88  ? 0.2213 0.2661 0.4243 0.0327  0.0164  0.1015  94  TYR   A CB  
712  C CG  . TYR   A 88  ? 0.2286 0.2824 0.4560 0.0361  0.0178  0.1135  94  TYR   A CG  
713  C CD1 . TYR   A 88  ? 0.2438 0.3081 0.4671 0.0340  0.0131  0.1162  94  TYR   A CD1 
714  C CD2 . TYR   A 88  ? 0.2393 0.2902 0.4950 0.0415  0.0250  0.1215  94  TYR   A CD2 
715  C CE1 . TYR   A 88  ? 0.2590 0.3324 0.5057 0.0370  0.0145  0.1274  94  TYR   A CE1 
716  C CE2 . TYR   A 88  ? 0.2456 0.3049 0.5265 0.0451  0.0271  0.1329  94  TYR   A CE2 
717  C CZ  . TYR   A 88  ? 0.2599 0.3310 0.5360 0.0428  0.0214  0.1360  94  TYR   A CZ  
718  O OH  . TYR   A 88  ? 0.2962 0.3773 0.5970 0.0460  0.0229  0.1475  94  TYR   A OH  
719  N N   . GLN   A 89  ? 0.1645 0.1936 0.3106 0.0262  0.0149  0.0676  95  GLN   A N   
720  C CA  . GLN   A 89  ? 0.1493 0.1757 0.2732 0.0223  0.0108  0.0594  95  GLN   A CA  
721  C C   . GLN   A 89  ? 0.1489 0.1876 0.2649 0.0179  0.0026  0.0664  95  GLN   A C   
722  O O   . GLN   A 89  ? 0.1545 0.2017 0.2732 0.0169  0.0002  0.0714  95  GLN   A O   
723  C CB  . GLN   A 89  ? 0.1607 0.1795 0.2717 0.0220  0.0137  0.0470  95  GLN   A CB  
724  C CG  . GLN   A 89  ? 0.1721 0.1885 0.2638 0.0187  0.0098  0.0399  95  GLN   A CG  
725  C CD  . GLN   A 89  ? 0.1580 0.1657 0.2392 0.0183  0.0130  0.0286  95  GLN   A CD  
726  O OE1 . GLN   A 89  ? 0.1747 0.1751 0.2607 0.0196  0.0192  0.0236  95  GLN   A OE1 
727  N NE2 . GLN   A 89  ? 0.1500 0.1585 0.2166 0.0158  0.0091  0.0243  95  GLN   A NE2 
728  N N   . SER   A 90  ? 0.1378 0.1778 0.2440 0.0143  -0.0012 0.0665  96  SER   A N   
729  C CA  . SER   A 90  ? 0.1376 0.1885 0.2350 0.0084  -0.0078 0.0719  96  SER   A CA  
730  C C   . SER   A 90  ? 0.1329 0.1812 0.2107 0.0049  -0.0090 0.0616  96  SER   A C   
731  O O   . SER   A 90  ? 0.1329 0.1713 0.2040 0.0070  -0.0059 0.0517  96  SER   A O   
732  C CB  . SER   A 90  ? 0.1629 0.2175 0.2618 0.0056  -0.0106 0.0786  96  SER   A CB  
733  O OG  . SER   A 90  ? 0.1997 0.2444 0.2893 0.0059  -0.0083 0.0694  96  SER   A OG  
734  N N   . HIS   A 91  ? 0.1279 0.1858 0.1977 -0.0011 -0.0135 0.0649  97  HIS   A N   
735  C CA  . HIS   A 91  ? 0.1299 0.1861 0.1831 -0.0053 -0.0140 0.0564  97  HIS   A CA  
736  C C   . HIS   A 91  ? 0.1215 0.1703 0.1720 -0.0015 -0.0108 0.0482  97  HIS   A C   
737  O O   . HIS   A 91  ? 0.1411 0.1831 0.1812 -0.0019 -0.0094 0.0395  97  HIS   A O   
738  C CB  . HIS   A 91  ? 0.1525 0.2030 0.1966 -0.0073 -0.0133 0.0505  97  HIS   A CB  
739  C CG  . HIS   A 91  ? 0.1650 0.2231 0.2092 -0.0125 -0.0162 0.0578  97  HIS   A CG  
740  N ND1 . HIS   A 91  ? 0.1914 0.2566 0.2243 -0.0210 -0.0184 0.0579  97  HIS   A ND1 
741  C CD2 . HIS   A 91  ? 0.1920 0.2518 0.2465 -0.0109 -0.0170 0.0655  97  HIS   A CD2 
742  C CE1 . HIS   A 91  ? 0.1997 0.2714 0.2351 -0.0249 -0.0210 0.0657  97  HIS   A CE1 
743  N NE2 . HIS   A 91  ? 0.2066 0.2754 0.2555 -0.0186 -0.0205 0.0710  97  HIS   A NE2 
744  N N   . LEU   A 92  ? 0.1153 0.1658 0.1755 0.0018  -0.0097 0.0515  98  LEU   A N   
745  C CA  . LEU   A 92  ? 0.1189 0.1627 0.1774 0.0051  -0.0064 0.0445  98  LEU   A CA  
746  C C   . LEU   A 92  ? 0.1208 0.1718 0.1755 0.0018  -0.0084 0.0460  98  LEU   A C   
747  O O   . LEU   A 92  ? 0.1241 0.1859 0.1854 -0.0007 -0.0113 0.0548  98  LEU   A O   
748  C CB  . LEU   A 92  ? 0.1365 0.1765 0.2099 0.0107  -0.0020 0.0462  98  LEU   A CB  
749  C CG  . LEU   A 92  ? 0.1565 0.1890 0.2275 0.0132  0.0024  0.0381  98  LEU   A CG  
750  C CD1 . LEU   A 92  ? 0.1584 0.1816 0.2178 0.0130  0.0037  0.0289  98  LEU   A CD1 
751  C CD2 . LEU   A 92  ? 0.1864 0.2158 0.2734 0.0176  0.0082  0.0397  98  LEU   A CD2 
752  N N   . MET   A 93  ? 0.1214 0.1668 0.1666 0.0017  -0.0068 0.0380  99  MET   A N   
753  C CA  . MET   A 93  ? 0.1266 0.1770 0.1672 -0.0015 -0.0078 0.0379  99  MET   A CA  
754  C C   . MET   A 93  ? 0.1240 0.1689 0.1673 0.0026  -0.0044 0.0339  99  MET   A C   
755  O O   . MET   A 93  ? 0.1307 0.1663 0.1704 0.0052  -0.0018 0.0274  99  MET   A O   
756  C CB  . MET   A 93  ? 0.1325 0.1802 0.1590 -0.0060 -0.0083 0.0318  99  MET   A CB  
757  C CG  . MET   A 93  ? 0.1526 0.2051 0.1749 -0.0112 -0.0105 0.0342  99  MET   A CG  
758  S SD  . MET   A 93  ? 0.1853 0.2325 0.1935 -0.0163 -0.0087 0.0256  99  MET   A SD  
759  C CE  . MET   A 93  ? 0.2267 0.2615 0.2362 -0.0093 -0.0061 0.0194  99  MET   A CE  
760  N N   . LEU   A 94  ? 0.1193 0.1701 0.1682 0.0024  -0.0043 0.0374  100 LEU   A N   
761  C CA  . LEU   A 94  ? 0.1236 0.1695 0.1748 0.0055  -0.0004 0.0333  100 LEU   A CA  
762  C C   . LEU   A 94  ? 0.1235 0.1702 0.1651 0.0023  -0.0010 0.0298  100 LEU   A C   
763  O O   . LEU   A 94  ? 0.1338 0.1882 0.1717 -0.0024 -0.0041 0.0329  100 LEU   A O   
764  C CB  . LEU   A 94  ? 0.1413 0.1928 0.2097 0.0085  0.0017  0.0399  100 LEU   A CB  
765  C CG  . LEU   A 94  ? 0.1890 0.2387 0.2710 0.0124  0.0042  0.0436  100 LEU   A CG  
766  C CD1 . LEU   A 94  ? 0.2164 0.2701 0.3183 0.0161  0.0083  0.0494  100 LEU   A CD1 
767  C CD2 . LEU   A 94  ? 0.2184 0.2556 0.2954 0.0147  0.0084  0.0350  100 LEU   A CD2 
768  N N   . ALA   A 95  ? 0.1246 0.1639 0.1620 0.0040  0.0021  0.0237  101 ALA   A N   
769  C CA  . ALA   A 95  ? 0.1198 0.1589 0.1496 0.0016  0.0023  0.0206  101 ALA   A CA  
770  C C   . ALA   A 95  ? 0.1167 0.1517 0.1497 0.0041  0.0065  0.0176  101 ALA   A C   
771  O O   . ALA   A 95  ? 0.1243 0.1545 0.1623 0.0070  0.0097  0.0157  101 ALA   A O   
772  C CB  . ALA   A 95  ? 0.1313 0.1637 0.1484 -0.0004 0.0015  0.0152  101 ALA   A CB  
773  N N   . VAL   A 96  ? 0.1154 0.1516 0.1444 0.0021  0.0070  0.0162  102 VAL   A N   
774  C CA  . VAL   A 96  ? 0.1156 0.1477 0.1448 0.0032  0.0112  0.0125  102 VAL   A CA  
775  C C   . VAL   A 96  ? 0.1398 0.1634 0.1563 0.0020  0.0111  0.0068  102 VAL   A C   
776  O O   . VAL   A 96  ? 0.1669 0.1897 0.1754 -0.0003 0.0088  0.0061  102 VAL   A O   
777  C CB  . VAL   A 96  ? 0.1190 0.1572 0.1507 0.0013  0.0117  0.0144  102 VAL   A CB  
778  C CG1 . VAL   A 96  ? 0.1437 0.1771 0.1733 0.0014  0.0163  0.0097  102 VAL   A CG1 
779  C CG2 . VAL   A 96  ? 0.1206 0.1691 0.1669 0.0023  0.0110  0.0218  102 VAL   A CG2 
780  N N   . GLY   A 97  ? 0.1525 0.1706 0.1686 0.0031  0.0140  0.0033  103 GLY   A N   
781  C CA  . GLY   A 97  ? 0.1727 0.1847 0.1779 0.0013  0.0132  -0.0006 103 GLY   A CA  
782  C C   . GLY   A 97  ? 0.1889 0.1963 0.1938 0.0011  0.0166  -0.0044 103 GLY   A C   
783  O O   . GLY   A 97  ? 0.2001 0.2074 0.2136 0.0029  0.0199  -0.0046 103 GLY   A O   
784  N N   . HIS   A 98  ? 0.2171 0.2209 0.2119 -0.0020 0.0161  -0.0072 104 HIS   A N   
785  C CA  . HIS   A 98  ? 0.2430 0.2431 0.2345 -0.0044 0.0192  -0.0114 104 HIS   A CA  
786  C C   . HIS   A 98  ? 0.2347 0.2331 0.2264 -0.0036 0.0169  -0.0113 104 HIS   A C   
787  O O   . HIS   A 98  ? 0.2304 0.2294 0.2195 -0.0027 0.0119  -0.0085 104 HIS   A O   
788  C CB  . HIS   A 98  ? 0.2465 0.2453 0.2264 -0.0094 0.0184  -0.0132 104 HIS   A CB  
789  C CG  . HIS   A 98  ? 0.2564 0.2525 0.2312 -0.0141 0.0219  -0.0180 104 HIS   A CG  
790  N ND1 . HIS   A 98  ? 0.2512 0.2454 0.2292 -0.0159 0.0295  -0.0231 104 HIS   A ND1 
791  C CD2 . HIS   A 98  ? 0.2713 0.2666 0.2388 -0.0177 0.0192  -0.0186 104 HIS   A CD2 
792  C CE1 . HIS   A 98  ? 0.2675 0.2592 0.2388 -0.0212 0.0317  -0.0276 104 HIS   A CE1 
793  N NE2 . HIS   A 98  ? 0.2797 0.2727 0.2440 -0.0227 0.0251  -0.0247 104 HIS   A NE2 
794  N N   . SER   A 99  ? 0.2531 0.2491 0.2486 -0.0040 0.0212  -0.0145 105 SER   A N   
795  C CA  . SER   A 99  ? 0.2478 0.2417 0.2421 -0.0046 0.0201  -0.0156 105 SER   A CA  
796  C C   . SER   A 99  ? 0.2453 0.2352 0.2389 -0.0084 0.0265  -0.0217 105 SER   A C   
797  O O   . SER   A 99  ? 0.2832 0.2717 0.2819 -0.0088 0.0332  -0.0247 105 SER   A O   
798  C CB  . SER   A 99  ? 0.2702 0.2656 0.2726 0.0001  0.0176  -0.0116 105 SER   A CB  
799  O OG  . SER   A 99  ? 0.2908 0.2869 0.3050 0.0030  0.0219  -0.0106 105 SER   A OG  
800  N N   . GLU   A 100 ? 0.1993 0.1876 0.1875 -0.0114 0.0250  -0.0236 106 GLU   A N   
801  C CA  . GLU   A 100 ? 0.2093 0.1936 0.1951 -0.0165 0.0309  -0.0301 106 GLU   A CA  
802  C C   . GLU   A 100 ? 0.2209 0.2043 0.2094 -0.0151 0.0285  -0.0291 106 GLU   A C   
803  O O   . GLU   A 100 ? 0.2022 0.1885 0.1917 -0.0114 0.0218  -0.0238 106 GLU   A O   
804  C CB  . GLU   A 100 ? 0.2258 0.2112 0.1968 -0.0251 0.0299  -0.0332 106 GLU   A CB  
805  C CG  . GLU   A 100 ? 0.2713 0.2574 0.2392 -0.0271 0.0329  -0.0345 106 GLU   A CG  
806  C CD  . GLU   A 100 ? 0.2854 0.2738 0.2382 -0.0361 0.0312  -0.0362 106 GLU   A CD  
807  O OE1 . GLU   A 100 ? 0.3467 0.3355 0.2910 -0.0432 0.0307  -0.0389 106 GLU   A OE1 
808  O OE2 . GLU   A 100 ? 0.2800 0.2704 0.2290 -0.0368 0.0300  -0.0342 106 GLU   A OE2 
809  N N   . PRO   A 101 ? 0.2232 0.2023 0.2135 -0.0182 0.0346  -0.0346 107 PRO   A N   
810  C CA  . PRO   A 101 ? 0.2153 0.1933 0.2097 -0.0164 0.0327  -0.0334 107 PRO   A CA  
811  C C   . PRO   A 101 ? 0.2045 0.1868 0.1911 -0.0176 0.0240  -0.0298 107 PRO   A C   
812  O O   . PRO   A 101 ? 0.2042 0.1879 0.1962 -0.0127 0.0198  -0.0253 107 PRO   A O   
813  C CB  . PRO   A 101 ? 0.2451 0.2171 0.2397 -0.0220 0.0417  -0.0415 107 PRO   A CB  
814  C CG  . PRO   A 101 ? 0.2699 0.2389 0.2696 -0.0223 0.0500  -0.0452 107 PRO   A CG  
815  C CD  . PRO   A 101 ? 0.2363 0.2103 0.2277 -0.0229 0.0449  -0.0424 107 PRO   A CD  
816  N N   . GLY   A 102 ? 0.2036 0.1888 0.1785 -0.0241 0.0210  -0.0308 108 GLY   A N   
817  C CA  . GLY   A 102 ? 0.1964 0.1867 0.1661 -0.0255 0.0128  -0.0261 108 GLY   A CA  
818  C C   . GLY   A 102 ? 0.1720 0.1656 0.1451 -0.0195 0.0067  -0.0190 108 GLY   A C   
819  O O   . GLY   A 102 ? 0.1779 0.1752 0.1504 -0.0193 0.0008  -0.0146 108 GLY   A O   
820  N N   . ASP   A 103 ? 0.1548 0.1472 0.1327 -0.0148 0.0086  -0.0179 109 ASP   A N   
821  C CA  . ASP   A 103 ? 0.1484 0.1431 0.1297 -0.0097 0.0041  -0.0124 109 ASP   A CA  
822  C C   . ASP   A 103 ? 0.1464 0.1408 0.1354 -0.0049 0.0029  -0.0103 109 ASP   A C   
823  O O   . ASP   A 103 ? 0.1377 0.1339 0.1290 -0.0020 -0.0003 -0.0066 109 ASP   A O   
824  C CB  . ASP   A 103 ? 0.1449 0.1393 0.1279 -0.0076 0.0066  -0.0122 109 ASP   A CB  
825  C CG  . ASP   A 103 ? 0.1614 0.1568 0.1361 -0.0123 0.0064  -0.0129 109 ASP   A CG  
826  O OD1 . ASP   A 103 ? 0.1686 0.1665 0.1378 -0.0154 0.0019  -0.0102 109 ASP   A OD1 
827  O OD2 . ASP   A 103 ? 0.1683 0.1625 0.1427 -0.0132 0.0109  -0.0156 109 ASP   A OD2 
828  N N   . CYS   A 104 ? 0.1414 0.1334 0.1346 -0.0045 0.0061  -0.0128 110 CYS   A N   
829  C CA  . CYS   A 104 ? 0.1424 0.1347 0.1421 -0.0008 0.0047  -0.0103 110 CYS   A CA  
830  C C   . CYS   A 104 ? 0.1372 0.1320 0.1351 -0.0011 -0.0003 -0.0078 110 CYS   A C   
831  O O   . CYS   A 104 ? 0.1460 0.1420 0.1393 -0.0047 -0.0023 -0.0083 110 CYS   A O   
832  C CB  . CYS   A 104 ? 0.1397 0.1287 0.1439 -0.0012 0.0088  -0.0131 110 CYS   A CB  
833  S SG  . CYS   A 104 ? 0.1647 0.1513 0.1783 0.0015  0.0154  -0.0135 110 CYS   A SG  
834  N N   . GLY   A 105 ? 0.1225 0.1185 0.1244 0.0021  -0.0020 -0.0048 111 GLY   A N   
835  C CA  . GLY   A 105 ? 0.1335 0.1313 0.1363 0.0025  -0.0052 -0.0026 111 GLY   A CA  
836  C C   . GLY   A 105 ? 0.1262 0.1252 0.1286 0.0033  -0.0067 -0.0002 111 GLY   A C   
837  O O   . GLY   A 105 ? 0.1333 0.1331 0.1393 0.0043  -0.0079 0.0016  111 GLY   A O   
838  N N   . GLY   A 106 ? 0.1239 0.1226 0.1230 0.0027  -0.0060 -0.0004 112 GLY   A N   
839  C CA  . GLY   A 106 ? 0.1234 0.1224 0.1226 0.0033  -0.0066 0.0017  112 GLY   A CA  
840  C C   . GLY   A 106 ? 0.1083 0.1071 0.1107 0.0050  -0.0051 0.0018  112 GLY   A C   
841  O O   . GLY   A 106 ? 0.1163 0.1158 0.1193 0.0055  -0.0037 0.0010  112 GLY   A O   
842  N N   . ILE   A 107 ? 0.1088 0.1070 0.1137 0.0053  -0.0049 0.0030  113 ILE   A N   
843  C CA  . ILE   A 107 ? 0.1104 0.1084 0.1170 0.0051  -0.0026 0.0020  113 ILE   A CA  
844  C C   . ILE   A 107 ? 0.1066 0.1050 0.1102 0.0039  -0.0011 0.0014  113 ILE   A C   
845  O O   . ILE   A 107 ? 0.1160 0.1133 0.1182 0.0037  -0.0010 0.0021  113 ILE   A O   
846  C CB  . ILE   A 107 ? 0.1175 0.1138 0.1296 0.0054  -0.0013 0.0025  113 ILE   A CB  
847  C CG1 . ILE   A 107 ? 0.1388 0.1360 0.1547 0.0062  -0.0023 0.0026  113 ILE   A CG1 
848  C CG2 . ILE   A 107 ? 0.1302 0.1251 0.1428 0.0036  0.0028  0.0002  113 ILE   A CG2 
849  C CD1 . ILE   A 107 ? 0.1738 0.1699 0.1979 0.0070  -0.0008 0.0039  113 ILE   A CD1 
850  N N   . LEU   A 108 ? 0.1051 0.1058 0.1078 0.0024  0.0000  0.0007  114 LEU   A N   
851  C CA  . LEU   A 108 ? 0.1075 0.1101 0.1075 -0.0003 0.0015  0.0003  114 LEU   A CA  
852  C C   . LEU   A 108 ? 0.1045 0.1058 0.1047 -0.0033 0.0045  -0.0019 114 LEU   A C   
853  O O   . LEU   A 108 ? 0.1148 0.1170 0.1162 -0.0041 0.0049  -0.0025 114 LEU   A O   
854  C CB  . LEU   A 108 ? 0.1113 0.1192 0.1111 -0.0012 0.0004  0.0021  114 LEU   A CB  
855  C CG  . LEU   A 108 ? 0.1093 0.1217 0.1063 -0.0054 0.0011  0.0026  114 LEU   A CG  
856  C CD1 . LEU   A 108 ? 0.1350 0.1465 0.1303 -0.0053 0.0017  0.0023  114 LEU   A CD1 
857  C CD2 . LEU   A 108 ? 0.1361 0.1556 0.1355 -0.0064 -0.0009 0.0067  114 LEU   A CD2 
858  N N   . ARG   A 109 ? 0.1136 0.1126 0.1129 -0.0054 0.0074  -0.0036 115 ARG   A N   
859  C CA  . ARG   A 109 ? 0.1205 0.1170 0.1204 -0.0091 0.0123  -0.0071 115 ARG   A CA  
860  C C   . ARG   A 109 ? 0.1275 0.1251 0.1226 -0.0143 0.0150  -0.0092 115 ARG   A C   
861  O O   . ARG   A 109 ? 0.1288 0.1271 0.1219 -0.0138 0.0137  -0.0079 115 ARG   A O   
862  C CB  . ARG   A 109 ? 0.1378 0.1283 0.1453 -0.0062 0.0148  -0.0073 115 ARG   A CB  
863  C CG  . ARG   A 109 ? 0.1444 0.1319 0.1535 -0.0045 0.0150  -0.0055 115 ARG   A CG  
864  C CD  . ARG   A 109 ? 0.1570 0.1401 0.1761 -0.0014 0.0167  -0.0034 115 ARG   A CD  
865  N NE  . ARG   A 109 ? 0.1675 0.1530 0.1894 0.0024  0.0116  0.0006  115 ARG   A NE  
866  C CZ  . ARG   A 109 ? 0.1564 0.1416 0.1858 0.0042  0.0118  0.0018  115 ARG   A CZ  
867  N NH1 . ARG   A 109 ? 0.1786 0.1610 0.2136 0.0029  0.0175  -0.0015 115 ARG   A NH1 
868  N NH2 . ARG   A 109 ? 0.1776 0.1659 0.2088 0.0066  0.0067  0.0057  115 ARG   A NH2 
869  N N   . CYS   A 110 ? 0.1618 0.1594 0.1545 -0.0202 0.0195  -0.0131 116 CYS   A N   
870  C CA  . CYS   A 110 ? 0.1982 0.1971 0.1850 -0.0274 0.0230  -0.0163 116 CYS   A CA  
871  C C   . CYS   A 110 ? 0.2150 0.2062 0.2052 -0.0302 0.0312  -0.0219 116 CYS   A C   
872  O O   . CYS   A 110 ? 0.2019 0.1874 0.2005 -0.0257 0.0335  -0.0221 116 CYS   A O   
873  C CB  . CYS   A 110 ? 0.1725 0.1804 0.1521 -0.0342 0.0210  -0.0156 116 CYS   A CB  
874  S SG  . CYS   A 110 ? 0.1899 0.1979 0.1680 -0.0394 0.0248  -0.0193 116 CYS   A SG  
875  N N   . GLN   A 111 ? 0.2299 0.2210 0.2144 -0.0385 0.0365  -0.0267 117 GLN   A N   
876  C CA  . GLN   A 111 ? 0.2600 0.2429 0.2480 -0.0425 0.0463  -0.0334 117 GLN   A CA  
877  C C   . GLN   A 111 ? 0.2809 0.2621 0.2718 -0.0443 0.0506  -0.0368 117 GLN   A C   
878  O O   . GLN   A 111 ? 0.3091 0.2819 0.3086 -0.0441 0.0588  -0.0410 117 GLN   A O   
879  C CB  . GLN   A 111 ? 0.2997 0.2833 0.2791 -0.0531 0.0518  -0.0390 117 GLN   A CB  
880  C CG  . GLN   A 111 ? 0.3501 0.3431 0.3178 -0.0633 0.0507  -0.0409 117 GLN   A CG  
881  C CD  . GLN   A 111 ? 0.4338 0.4281 0.3924 -0.0751 0.0563  -0.0467 117 GLN   A CD  
882  O OE1 . GLN   A 111 ? 0.4724 0.4745 0.4246 -0.0781 0.0512  -0.0435 117 GLN   A OE1 
883  N NE2 . GLN   A 111 ? 0.4293 0.4161 0.3878 -0.0824 0.0675  -0.0557 117 GLN   A NE2 
884  N N   . HIS   A 112 ? 0.2315 0.2200 0.2172 -0.0457 0.0455  -0.0346 118 HIS   A N   
885  C CA  . HIS   A 112 ? 0.2327 0.2207 0.2195 -0.0485 0.0493  -0.0379 118 HIS   A CA  
886  C C   . HIS   A 112 ? 0.2373 0.2232 0.2343 -0.0388 0.0458  -0.0337 118 HIS   A C   
887  O O   . HIS   A 112 ? 0.2681 0.2526 0.2683 -0.0399 0.0494  -0.0363 118 HIS   A O   
888  C CB  . HIS   A 112 ? 0.2314 0.2297 0.2063 -0.0564 0.0452  -0.0367 118 HIS   A CB  
889  C CG  . HIS   A 112 ? 0.2640 0.2667 0.2279 -0.0677 0.0478  -0.0401 118 HIS   A CG  
890  N ND1 . HIS   A 112 ? 0.2456 0.2577 0.2032 -0.0694 0.0404  -0.0345 118 HIS   A ND1 
891  C CD2 . HIS   A 112 ? 0.3023 0.3024 0.2603 -0.0789 0.0573  -0.0487 118 HIS   A CD2 
892  C CE1 . HIS   A 112 ? 0.2899 0.3049 0.2383 -0.0811 0.0448  -0.0393 118 HIS   A CE1 
893  N NE2 . HIS   A 112 ? 0.3295 0.3371 0.2771 -0.0875 0.0553  -0.0484 118 HIS   A NE2 
894  N N   . GLY   A 113 ? 0.2079 0.1946 0.2087 -0.0303 0.0385  -0.0273 119 GLY   A N   
895  C CA  . GLY   A 113 ? 0.1937 0.1797 0.2026 -0.0227 0.0347  -0.0233 119 GLY   A CA  
896  C C   . GLY   A 113 ? 0.1622 0.1537 0.1681 -0.0180 0.0256  -0.0173 119 GLY   A C   
897  O O   . GLY   A 113 ? 0.1629 0.1573 0.1635 -0.0186 0.0225  -0.0154 119 GLY   A O   
898  N N   . VAL   A 114 ? 0.1444 0.1369 0.1541 -0.0138 0.0222  -0.0147 120 VAL   A N   
899  C CA  . VAL   A 114 ? 0.1468 0.1433 0.1546 -0.0098 0.0151  -0.0100 120 VAL   A CA  
900  C C   . VAL   A 114 ? 0.1239 0.1266 0.1249 -0.0136 0.0126  -0.0087 120 VAL   A C   
901  O O   . VAL   A 114 ? 0.1400 0.1450 0.1387 -0.0179 0.0142  -0.0101 120 VAL   A O   
902  C CB  . VAL   A 114 ? 0.1460 0.1416 0.1601 -0.0052 0.0128  -0.0081 120 VAL   A CB  
903  C CG1 . VAL   A 114 ? 0.1570 0.1558 0.1688 -0.0024 0.0071  -0.0047 120 VAL   A CG1 
904  C CG2 . VAL   A 114 ? 0.1578 0.1494 0.1802 -0.0015 0.0140  -0.0070 120 VAL   A CG2 
905  N N   . VAL   A 115 ? 0.1202 0.1262 0.1189 -0.0122 0.0088  -0.0055 121 VAL   A N   
906  C CA  . VAL   A 115 ? 0.1203 0.1333 0.1155 -0.0150 0.0058  -0.0022 121 VAL   A CA  
907  C C   . VAL   A 115 ? 0.1186 0.1331 0.1178 -0.0105 0.0021  0.0016  121 VAL   A C   
908  O O   . VAL   A 115 ? 0.1309 0.1502 0.1301 -0.0125 0.0004  0.0048  121 VAL   A O   
909  C CB  . VAL   A 115 ? 0.1359 0.1521 0.1284 -0.0165 0.0049  -0.0008 121 VAL   A CB  
910  C CG1 . VAL   A 115 ? 0.1651 0.1900 0.1575 -0.0183 0.0011  0.0048  121 VAL   A CG1 
911  C CG2 . VAL   A 115 ? 0.1610 0.1759 0.1488 -0.0223 0.0092  -0.0051 121 VAL   A CG2 
912  N N   . GLY   A 116 ? 0.1171 0.1276 0.1196 -0.0052 0.0010  0.0017  122 GLY   A N   
913  C CA  . GLY   A 116 ? 0.1248 0.1356 0.1309 -0.0017 -0.0012 0.0043  122 GLY   A CA  
914  C C   . GLY   A 116 ? 0.1126 0.1192 0.1200 0.0020  -0.0017 0.0031  122 GLY   A C   
915  O O   . GLY   A 116 ? 0.1178 0.1217 0.1241 0.0023  -0.0010 0.0014  122 GLY   A O   
916  N N   . ILE   A 117 ? 0.1100 0.1162 0.1200 0.0042  -0.0024 0.0041  123 ILE   A N   
917  C CA  . ILE   A 117 ? 0.1111 0.1140 0.1206 0.0060  -0.0026 0.0025  123 ILE   A CA  
918  C C   . ILE   A 117 ? 0.1101 0.1132 0.1212 0.0069  -0.0015 0.0030  123 ILE   A C   
919  O O   . ILE   A 117 ? 0.1164 0.1216 0.1322 0.0075  -0.0008 0.0054  123 ILE   A O   
920  C CB  . ILE   A 117 ? 0.1196 0.1204 0.1304 0.0064  -0.0032 0.0013  123 ILE   A CB  
921  C CG1 . ILE   A 117 ? 0.1466 0.1480 0.1610 0.0067  -0.0027 0.0023  123 ILE   A CG1 
922  C CG2 . ILE   A 117 ? 0.1444 0.1448 0.1556 0.0060  -0.0038 0.0009  123 ILE   A CG2 
923  C CD1 . ILE   A 117 ? 0.1438 0.1429 0.1591 0.0067  -0.0030 0.0006  123 ILE   A CD1 
924  N N   . VAL   A 118 ? 0.1104 0.1115 0.1188 0.0068  -0.0010 0.0011  124 VAL   A N   
925  C CA  . VAL   A 118 ? 0.1157 0.1162 0.1262 0.0072  0.0016  0.0004  124 VAL   A CA  
926  C C   . VAL   A 118 ? 0.1194 0.1179 0.1348 0.0079  0.0037  -0.0004 124 VAL   A C   
927  O O   . VAL   A 118 ? 0.1193 0.1157 0.1326 0.0069  0.0030  -0.0023 124 VAL   A O   
928  C CB  . VAL   A 118 ? 0.1204 0.1189 0.1253 0.0055  0.0021  -0.0023 124 VAL   A CB  
929  C CG1 . VAL   A 118 ? 0.1310 0.1279 0.1380 0.0051  0.0063  -0.0046 124 VAL   A CG1 
930  C CG2 . VAL   A 118 ? 0.1310 0.1308 0.1322 0.0050  0.0006  -0.0012 124 VAL   A CG2 
931  N N   . SER   A 119 ? 0.1187 0.1179 0.1415 0.0093  0.0064  0.0014  125 SER   A N   
932  C CA  . SER   A 119 ? 0.1314 0.1280 0.1615 0.0103  0.0097  0.0012  125 SER   A CA  
933  C C   . SER   A 119 ? 0.1386 0.1329 0.1756 0.0110  0.0153  -0.0001 125 SER   A C   
934  O O   . SER   A 119 ? 0.1592 0.1485 0.2003 0.0105  0.0200  -0.0033 125 SER   A O   
935  C CB  . SER   A 119 ? 0.1239 0.1240 0.1600 0.0116  0.0076  0.0067  125 SER   A CB  
936  O OG  . SER   A 119 ? 0.1572 0.1549 0.2025 0.0130  0.0109  0.0079  125 SER   A OG  
937  N N   . THR   A 120 ? 0.1453 0.1428 0.1855 0.0120  0.0160  0.0021  126 THR   A N   
938  C CA  . THR   A 120 ? 0.1590 0.1547 0.2090 0.0131  0.0225  0.0012  126 THR   A CA  
939  C C   . THR   A 120 ? 0.1738 0.1701 0.2179 0.0115  0.0234  -0.0016 126 THR   A C   
940  O O   . THR   A 120 ? 0.1494 0.1487 0.1846 0.0104  0.0185  -0.0008 126 THR   A O   
941  C CB  . THR   A 120 ? 0.1615 0.1622 0.2272 0.0166  0.0231  0.0092  126 THR   A CB  
942  O OG1 . THR   A 120 ? 0.1693 0.1778 0.2340 0.0166  0.0186  0.0143  126 THR   A OG1 
943  C CG2 . THR   A 120 ? 0.1614 0.1626 0.2322 0.0177  0.0211  0.0135  126 THR   A CG2 
944  N N   . GLY   A 121 ? 0.1996 0.1927 0.2492 0.0111  0.0303  -0.0051 127 GLY   A N   
945  C CA  . GLY   A 121 ? 0.2305 0.2243 0.2753 0.0093  0.0319  -0.0077 127 GLY   A CA  
946  C C   . GLY   A 121 ? 0.2589 0.2497 0.3139 0.0094  0.0410  -0.0109 127 GLY   A C   
947  O O   . GLY   A 121 ? 0.2892 0.2755 0.3537 0.0101  0.0472  -0.0128 127 GLY   A O   
948  N N   . GLY   A 122 ? 0.2873 0.2801 0.3396 0.0081  0.0423  -0.0121 128 GLY   A N   
949  C CA  . GLY   A 122 ? 0.2921 0.2822 0.3525 0.0073  0.0517  -0.0163 128 GLY   A CA  
950  C C   . GLY   A 122 ? 0.3169 0.3134 0.3827 0.0091  0.0508  -0.0120 128 GLY   A C   
951  O O   . GLY   A 122 ? 0.3360 0.3397 0.4068 0.0122  0.0446  -0.0040 128 GLY   A O   
952  N N   . ASN   A 123 ? 0.3015 0.2956 0.3662 0.0062  0.0575  -0.0175 129 ASN   A N   
953  C CA  . ASN   A 123 ? 0.2974 0.2970 0.3693 0.0074  0.0589  -0.0147 129 ASN   A CA  
954  C C   . ASN   A 123 ? 0.2671 0.2743 0.3320 0.0081  0.0494  -0.0085 129 ASN   A C   
955  O O   . ASN   A 123 ? 0.2566 0.2710 0.3325 0.0105  0.0485  -0.0025 129 ASN   A O   
956  C CB  . ASN   A 123 ? 0.3240 0.3261 0.4207 0.0124  0.0651  -0.0097 129 ASN   A CB  
957  C CG  . ASN   A 123 ? 0.3711 0.3647 0.4773 0.0114  0.0774  -0.0169 129 ASN   A CG  
958  O OD1 . ASN   A 123 ? 0.4149 0.4036 0.5152 0.0068  0.0849  -0.0255 129 ASN   A OD1 
959  N ND2 . ASN   A 123 ? 0.3607 0.3522 0.4822 0.0152  0.0804  -0.0137 129 ASN   A ND2 
960  N N   . GLY   A 124 ? 0.2320 0.2375 0.2789 0.0049  0.0434  -0.0106 130 GLY   A N   
961  C CA  . GLY   A 124 ? 0.2112 0.2219 0.2507 0.0046  0.0360  -0.0065 130 GLY   A CA  
962  C C   . GLY   A 124 ? 0.1582 0.1738 0.2018 0.0074  0.0297  0.0002  130 GLY   A C   
963  O O   . GLY   A 124 ? 0.1855 0.2054 0.2240 0.0065  0.0246  0.0032  130 GLY   A O   
964  N N   . LEU   A 125 ? 0.1643 0.1784 0.2152 0.0097  0.0302  0.0017  131 LEU   A N   
965  C CA  . LEU   A 125 ? 0.1613 0.1797 0.2135 0.0111  0.0239  0.0076  131 LEU   A CA  
966  C C   . LEU   A 125 ? 0.1797 0.1924 0.2219 0.0102  0.0216  0.0042  131 LEU   A C   
967  O O   . LEU   A 125 ? 0.2141 0.2202 0.2543 0.0094  0.0257  -0.0012 131 LEU   A O   
968  C CB  . LEU   A 125 ? 0.1621 0.1850 0.2321 0.0145  0.0255  0.0141  131 LEU   A CB  
969  C CG  . LEU   A 125 ? 0.1637 0.1949 0.2467 0.0156  0.0268  0.0198  131 LEU   A CG  
970  C CD1 . LEU   A 125 ? 0.1997 0.2335 0.3048 0.0196  0.0313  0.0258  131 LEU   A CD1 
971  C CD2 . LEU   A 125 ? 0.1737 0.2141 0.2512 0.0131  0.0195  0.0253  131 LEU   A CD2 
972  N N   . VAL   A 126 ? 0.1338 0.1491 0.1703 0.0097  0.0157  0.0070  132 VAL   A N   
973  C CA  . VAL   A 126 ? 0.1298 0.1410 0.1597 0.0092  0.0133  0.0050  132 VAL   A CA  
974  C C   . VAL   A 126 ? 0.1305 0.1465 0.1659 0.0102  0.0100  0.0106  132 VAL   A C   
975  O O   . VAL   A 126 ? 0.1322 0.1548 0.1685 0.0091  0.0071  0.0149  132 VAL   A O   
976  C CB  . VAL   A 126 ? 0.1450 0.1537 0.1620 0.0068  0.0103  0.0020  132 VAL   A CB  
977  C CG1 . VAL   A 126 ? 0.1606 0.1735 0.1743 0.0055  0.0075  0.0044  132 VAL   A CG1 
978  C CG2 . VAL   A 126 ? 0.1487 0.1542 0.1610 0.0065  0.0079  0.0008  132 VAL   A CG2 
979  N N   . GLY   A 127 ? 0.1256 0.1389 0.1636 0.0113  0.0102  0.0105  133 GLY   A N   
980  C CA  . GLY   A 127 ? 0.1240 0.1417 0.1659 0.0115  0.0071  0.0158  133 GLY   A CA  
981  C C   . GLY   A 127 ? 0.1195 0.1339 0.1528 0.0102  0.0045  0.0131  133 GLY   A C   
982  O O   . GLY   A 127 ? 0.1377 0.1461 0.1666 0.0103  0.0059  0.0082  133 GLY   A O   
983  N N   . PHE   A 128 ? 0.1116 0.1306 0.1423 0.0083  0.0011  0.0161  134 PHE   A N   
984  C CA  . PHE   A 128 ? 0.1102 0.1268 0.1340 0.0068  -0.0007 0.0137  134 PHE   A CA  
985  C C   . PHE   A 128 ? 0.1095 0.1293 0.1371 0.0060  -0.0021 0.0177  134 PHE   A C   
986  O O   . PHE   A 128 ? 0.1141 0.1412 0.1455 0.0043  -0.0037 0.0235  134 PHE   A O   
987  C CB  . PHE   A 128 ? 0.1179 0.1360 0.1339 0.0037  -0.0020 0.0123  134 PHE   A CB  
988  C CG  . PHE   A 128 ? 0.1183 0.1344 0.1309 0.0039  -0.0010 0.0097  134 PHE   A CG  
989  C CD1 . PHE   A 128 ? 0.1095 0.1198 0.1177 0.0047  -0.0004 0.0058  134 PHE   A CD1 
990  C CD2 . PHE   A 128 ? 0.1309 0.1517 0.1448 0.0027  -0.0009 0.0119  134 PHE   A CD2 
991  C CE1 . PHE   A 128 ? 0.1175 0.1264 0.1223 0.0043  0.0003  0.0043  134 PHE   A CE1 
992  C CE2 . PHE   A 128 ? 0.1360 0.1547 0.1463 0.0025  0.0002  0.0095  134 PHE   A CE2 
993  C CZ  . PHE   A 128 ? 0.1290 0.1415 0.1345 0.0033  0.0008  0.0057  134 PHE   A CZ  
994  N N   . ALA   A 129 ? 0.1083 0.1237 0.1347 0.0067  -0.0018 0.0152  135 ALA   A N   
995  C CA  . ALA   A 129 ? 0.1209 0.1387 0.1495 0.0055  -0.0030 0.0184  135 ALA   A CA  
996  C C   . ALA   A 129 ? 0.1096 0.1301 0.1305 0.0013  -0.0046 0.0173  135 ALA   A C   
997  O O   . ALA   A 129 ? 0.1221 0.1383 0.1379 0.0011  -0.0038 0.0123  135 ALA   A O   
998  C CB  . ALA   A 129 ? 0.1253 0.1372 0.1551 0.0073  -0.0017 0.0153  135 ALA   A CB  
999  N N   . ASP   A 130 ? 0.1148 0.1427 0.1354 -0.0026 -0.0063 0.0220  136 ASP   A N   
1000 C CA  . ASP   A 130 ? 0.1217 0.1520 0.1343 -0.0083 -0.0063 0.0199  136 ASP   A CA  
1001 C C   . ASP   A 130 ? 0.1216 0.1489 0.1325 -0.0091 -0.0054 0.0174  136 ASP   A C   
1002 O O   . ASP   A 130 ? 0.1397 0.1669 0.1555 -0.0074 -0.0062 0.0204  136 ASP   A O   
1003 C CB  . ASP   A 130 ? 0.1522 0.1929 0.1642 -0.0140 -0.0088 0.0264  136 ASP   A CB  
1004 C CG  . ASP   A 130 ? 0.1730 0.2169 0.1755 -0.0219 -0.0079 0.0235  136 ASP   A CG  
1005 O OD1 . ASP   A 130 ? 0.2003 0.2401 0.1976 -0.0230 -0.0053 0.0175  136 ASP   A OD1 
1006 O OD2 . ASP   A 130 ? 0.2385 0.2881 0.2386 -0.0273 -0.0092 0.0268  136 ASP   A OD2 
1007 N N   . VAL   A 131 ? 0.1174 0.1421 0.1224 -0.0122 -0.0032 0.0121  137 VAL   A N   
1008 C CA  . VAL   A 131 ? 0.1269 0.1495 0.1308 -0.0140 -0.0014 0.0094  137 VAL   A CA  
1009 C C   . VAL   A 131 ? 0.1347 0.1608 0.1317 -0.0220 0.0009  0.0072  137 VAL   A C   
1010 O O   . VAL   A 131 ? 0.1319 0.1566 0.1277 -0.0246 0.0034  0.0043  137 VAL   A O   
1011 C CB  . VAL   A 131 ? 0.1256 0.1408 0.1320 -0.0097 0.0005  0.0045  137 VAL   A CB  
1012 C CG1 . VAL   A 131 ? 0.1370 0.1493 0.1482 -0.0039 -0.0015 0.0060  137 VAL   A CG1 
1013 C CG2 . VAL   A 131 ? 0.1407 0.1527 0.1455 -0.0099 0.0030  0.0004  137 VAL   A CG2 
1014 N N   . ARG   A 132 ? 0.1324 0.1634 0.1247 -0.0268 0.0007  0.0081  138 ARG   A N   
1015 C CA  . ARG   A 132 ? 0.1388 0.1724 0.1232 -0.0360 0.0041  0.0043  138 ARG   A CA  
1016 C C   . ARG   A 132 ? 0.1526 0.1930 0.1328 -0.0431 0.0032  0.0072  138 ARG   A C   
1017 O O   . ARG   A 132 ? 0.1728 0.2139 0.1459 -0.0515 0.0076  0.0022  138 ARG   A O   
1018 C CB  . ARG   A 132 ? 0.1465 0.1845 0.1262 -0.0404 0.0038  0.0047  138 ARG   A CB  
1019 C CG  . ARG   A 132 ? 0.1390 0.1694 0.1213 -0.0350 0.0061  0.0005  138 ARG   A CG  
1020 C CD  . ARG   A 132 ? 0.1655 0.2007 0.1431 -0.0398 0.0058  0.0010  138 ARG   A CD  
1021 N NE  . ARG   A 132 ? 0.1588 0.2015 0.1401 -0.0374 0.0000  0.0091  138 ARG   A NE  
1022 C CZ  . ARG   A 132 ? 0.1765 0.2248 0.1568 -0.0395 -0.0018 0.0118  138 ARG   A CZ  
1023 N NH1 . ARG   A 132 ? 0.1917 0.2397 0.1652 -0.0457 0.0015  0.0071  138 ARG   A NH1 
1024 N NH2 . ARG   A 132 ? 0.1825 0.2369 0.1695 -0.0360 -0.0063 0.0194  138 ARG   A NH2 
1025 N N   . ASP   A 133 ? 0.1483 0.1943 0.1328 -0.0412 -0.0019 0.0155  139 ASP   A N   
1026 C CA  . ASP   A 133 ? 0.1644 0.2173 0.1455 -0.0481 -0.0034 0.0197  139 ASP   A CA  
1027 C C   . ASP   A 133 ? 0.1613 0.2084 0.1443 -0.0460 -0.0008 0.0163  139 ASP   A C   
1028 O O   . ASP   A 133 ? 0.1889 0.2409 0.1681 -0.0523 -0.0012 0.0187  139 ASP   A O   
1029 C CB  . ASP   A 133 ? 0.1939 0.2554 0.1816 -0.0464 -0.0097 0.0314  139 ASP   A CB  
1030 C CG  . ASP   A 133 ? 0.2103 0.2654 0.2096 -0.0354 -0.0108 0.0338  139 ASP   A CG  
1031 O OD1 . ASP   A 133 ? 0.1992 0.2460 0.2013 -0.0287 -0.0087 0.0283  139 ASP   A OD1 
1032 O OD2 . ASP   A 133 ? 0.2369 0.2956 0.2427 -0.0343 -0.0135 0.0414  139 ASP   A OD2 
1033 N N   . LEU   A 134 ? 0.1452 0.1828 0.1341 -0.0376 0.0013  0.0115  140 LEU   A N   
1034 C CA  . LEU   A 134 ? 0.1478 0.1804 0.1401 -0.0349 0.0032  0.0089  140 LEU   A CA  
1035 C C   . LEU   A 134 ? 0.1558 0.1851 0.1439 -0.0400 0.0095  0.0007  140 LEU   A C   
1036 O O   . LEU   A 134 ? 0.1620 0.1842 0.1545 -0.0356 0.0130  -0.0048 140 LEU   A O   
1037 C CB  . LEU   A 134 ? 0.1450 0.1707 0.1456 -0.0250 0.0021  0.0082  140 LEU   A CB  
1038 C CG  . LEU   A 134 ? 0.1605 0.1879 0.1667 -0.0200 -0.0022 0.0149  140 LEU   A CG  
1039 C CD1 . LEU   A 134 ? 0.1719 0.1923 0.1837 -0.0124 -0.0021 0.0123  140 LEU   A CD1 
1040 C CD2 . LEU   A 134 ? 0.1784 0.2104 0.1874 -0.0216 -0.0047 0.0218  140 LEU   A CD2 
1041 N N   . LEU   A 135 ? 0.1544 0.1892 0.1343 -0.0502 0.0115  0.0001  141 LEU   A N   
1042 C CA  . LEU   A 135 ? 0.1669 0.1983 0.1423 -0.0567 0.0194  -0.0089 141 LEU   A CA  
1043 C C   . LEU   A 135 ? 0.1745 0.1995 0.1567 -0.0530 0.0236  -0.0135 141 LEU   A C   
1044 O O   . LEU   A 135 ? 0.1923 0.2115 0.1771 -0.0537 0.0308  -0.0211 141 LEU   A O   
1045 C CB  . LEU   A 135 ? 0.1845 0.2243 0.1477 -0.0706 0.0210  -0.0090 141 LEU   A CB  
1046 C CG  . LEU   A 135 ? 0.1935 0.2425 0.1504 -0.0757 0.0156  -0.0026 141 LEU   A CG  
1047 C CD1 . LEU   A 135 ? 0.2295 0.2869 0.1728 -0.0917 0.0184  -0.0044 141 LEU   A CD1 
1048 C CD2 . LEU   A 135 ? 0.2210 0.2665 0.1795 -0.0721 0.0165  -0.0054 141 LEU   A CD2 
1049 N N   . TRP   A 136 ? 0.1564 0.1823 0.1427 -0.0488 0.0196  -0.0088 142 TRP   A N   
1050 C CA  . TRP   A 136 ? 0.1663 0.1875 0.1593 -0.0455 0.0227  -0.0122 142 TRP   A CA  
1051 C C   . TRP   A 136 ? 0.1700 0.1843 0.1731 -0.0365 0.0239  -0.0150 142 TRP   A C   
1052 O O   . TRP   A 136 ? 0.1815 0.1923 0.1917 -0.0345 0.0277  -0.0185 142 TRP   A O   
1053 C CB  . TRP   A 136 ? 0.1751 0.1989 0.1698 -0.0436 0.0178  -0.0060 142 TRP   A CB  
1054 C CG  . TRP   A 136 ? 0.1609 0.1852 0.1598 -0.0365 0.0112  0.0007  142 TRP   A CG  
1055 C CD1 . TRP   A 136 ? 0.1694 0.1995 0.1658 -0.0381 0.0064  0.0081  142 TRP   A CD1 
1056 C CD2 . TRP   A 136 ? 0.1580 0.1771 0.1651 -0.0274 0.0093  0.0007  142 TRP   A CD2 
1057 N NE1 . TRP   A 136 ? 0.1843 0.2119 0.1877 -0.0300 0.0027  0.0119  142 TRP   A NE1 
1058 C CE2 . TRP   A 136 ? 0.1643 0.1852 0.1730 -0.0241 0.0044  0.0070  142 TRP   A CE2 
1059 C CE3 . TRP   A 136 ? 0.1731 0.1871 0.1868 -0.0225 0.0113  -0.0035 142 TRP   A CE3 
1060 C CZ2 . TRP   A 136 ? 0.1791 0.1957 0.1940 -0.0168 0.0025  0.0076  142 TRP   A CZ2 
1061 C CZ3 . TRP   A 136 ? 0.1913 0.2025 0.2103 -0.0158 0.0080  -0.0017 142 TRP   A CZ3 
1062 C CH2 . TRP   A 136 ? 0.1847 0.1967 0.2034 -0.0134 0.0041  0.0030  142 TRP   A CH2 
1063 N N   . LEU   A 137 ? 0.1566 0.1696 0.1613 -0.0314 0.0206  -0.0129 143 LEU   A N   
1064 C CA  . LEU   A 137 ? 0.1696 0.1772 0.1833 -0.0242 0.0215  -0.0147 143 LEU   A CA  
1065 C C   . LEU   A 137 ? 0.1990 0.2027 0.2171 -0.0265 0.0296  -0.0211 143 LEU   A C   
1066 O O   . LEU   A 137 ? 0.2114 0.2115 0.2400 -0.0211 0.0311  -0.0217 143 LEU   A O   
1067 C CB  . LEU   A 137 ? 0.1637 0.1710 0.1766 -0.0202 0.0175  -0.0119 143 LEU   A CB  
1068 C CG  . LEU   A 137 ? 0.1528 0.1620 0.1657 -0.0159 0.0110  -0.0064 143 LEU   A CG  
1069 C CD1 . LEU   A 137 ? 0.1796 0.1890 0.1907 -0.0136 0.0084  -0.0044 143 LEU   A CD1 
1070 C CD2 . LEU   A 137 ? 0.1684 0.1751 0.1886 -0.0104 0.0093  -0.0059 143 LEU   A CD2 
1071 N N   . ASP   A 138 ? 0.2201 0.2247 0.2308 -0.0352 0.0352  -0.0255 144 ASP   A N   
1072 C CA  . ASP   A 138 ? 0.2456 0.2452 0.2607 -0.0386 0.0449  -0.0328 144 ASP   A CA  
1073 C C   . ASP   A 138 ? 0.3021 0.3001 0.3227 -0.0413 0.0517  -0.0373 144 ASP   A C   
1074 O O   . ASP   A 138 ? 0.3268 0.3202 0.3528 -0.0445 0.0615  -0.0440 144 ASP   A O   
1075 C CB  . ASP   A 138 ? 0.2561 0.2571 0.2598 -0.0485 0.0494  -0.0371 144 ASP   A CB  
1076 C CG  . ASP   A 138 ? 0.2833 0.2858 0.2821 -0.0471 0.0445  -0.0339 144 ASP   A CG  
1077 O OD1 . ASP   A 138 ? 0.3154 0.3162 0.3209 -0.0380 0.0393  -0.0294 144 ASP   A OD1 
1078 O OD2 . ASP   A 138 ? 0.3838 0.3900 0.3718 -0.0558 0.0458  -0.0356 144 ASP   A OD2 
1079 N N   . GLU   A 139 ? 0.3141 0.3155 0.3337 -0.0409 0.0478  -0.0343 145 GLU   A N   
1080 C CA  . GLU   A 139 ? 0.3626 0.3630 0.3868 -0.0441 0.0544  -0.0387 145 GLU   A CA  
1081 C C   . GLU   A 139 ? 0.3922 0.3937 0.4246 -0.0373 0.0493  -0.0342 145 GLU   A C   
1082 O O   . GLU   A 139 ? 0.3865 0.3897 0.4190 -0.0312 0.0409  -0.0282 145 GLU   A O   
1083 C CB  . GLU   A 139 ? 0.4267 0.4315 0.4366 -0.0558 0.0568  -0.0412 145 GLU   A CB  
1084 C CG  . GLU   A 139 ? 0.5310 0.5425 0.5318 -0.0563 0.0469  -0.0333 145 GLU   A CG  
1085 C CD  . GLU   A 139 ? 0.6443 0.6623 0.6297 -0.0681 0.0467  -0.0328 145 GLU   A CD  
1086 O OE1 . GLU   A 139 ? 0.6548 0.6789 0.6350 -0.0690 0.0392  -0.0252 145 GLU   A OE1 
1087 O OE2 . GLU   A 139 ? 0.7030 0.7204 0.6821 -0.0770 0.0541  -0.0395 145 GLU   A OE2 
1088 N N   . GLU   A 140 ? 0.4255 0.4262 0.4647 -0.0390 0.0552  -0.0378 146 GLU   A N   
1089 C CA  . GLU   A 140 ? 0.4624 0.4648 0.5092 -0.0348 0.0522  -0.0349 146 GLU   A CA  
1090 C C   . GLU   A 140 ? 0.4798 0.4839 0.5285 -0.0271 0.0422  -0.0278 146 GLU   A C   
1091 O O   . GLU   A 140 ? 0.4784 0.4844 0.5288 -0.0255 0.0386  -0.0252 146 GLU   A O   
1092 C CB  . GLU   A 140 ? 0.5220 0.5275 0.5594 -0.0424 0.0534  -0.0361 146 GLU   A CB  
1093 C CG  . GLU   A 140 ? 0.6293 0.6391 0.6522 -0.0460 0.0462  -0.0311 146 GLU   A CG  
1094 C CD  . GLU   A 140 ? 0.7617 0.7743 0.7840 -0.0436 0.0395  -0.0252 146 GLU   A CD  
1095 O OE1 . GLU   A 140 ? 0.7910 0.8075 0.8037 -0.0474 0.0348  -0.0205 146 GLU   A OE1 
1096 O OE2 . GLU   A 140 ? 0.8030 0.8142 0.8354 -0.0383 0.0389  -0.0249 146 GLU   A OE2 
1097 N N   . SER   B 1   ? 0.1910 0.2079 0.2046 0.0074  -0.0128 0.0336  7   SER   C N   
1098 C CA  . SER   B 1   ? 0.1804 0.1981 0.2019 0.0058  -0.0136 0.0333  7   SER   C CA  
1099 C C   . SER   B 1   ? 0.1912 0.2065 0.2124 0.0044  -0.0134 0.0296  7   SER   C C   
1100 O O   . SER   B 1   ? 0.2223 0.2356 0.2374 0.0045  -0.0137 0.0272  7   SER   C O   
1101 C CB  . SER   B 1   ? 0.2249 0.2446 0.2475 0.0057  -0.0177 0.0349  7   SER   C CB  
1102 O OG  . SER   B 1   ? 0.2765 0.2952 0.2925 0.0055  -0.0211 0.0322  7   SER   C OG  
1103 N N   . GLY   B 2   ? 0.1784 0.1936 0.2064 0.0034  -0.0125 0.0294  8   GLY   C N   
1104 C CA  . GLY   B 2   ? 0.1725 0.1853 0.2006 0.0025  -0.0117 0.0268  8   GLY   C CA  
1105 C C   . GLY   B 2   ? 0.1506 0.1627 0.1842 0.0024  -0.0088 0.0268  8   GLY   C C   
1106 O O   . GLY   B 2   ? 0.1605 0.1736 0.1969 0.0030  -0.0070 0.0278  8   GLY   C O   
1107 N N   . ALA   B 3   ? 0.1382 0.1485 0.1736 0.0018  -0.0079 0.0258  9   ALA   C N   
1108 C CA  . ALA   B 3   ? 0.1455 0.1546 0.1847 0.0023  -0.0046 0.0258  9   ALA   C CA  
1109 C C   . ALA   B 3   ? 0.1345 0.1403 0.1703 0.0027  -0.0028 0.0240  9   ALA   C C   
1110 O O   . ALA   B 3   ? 0.1496 0.1542 0.1825 0.0022  -0.0041 0.0232  9   ALA   C O   
1111 C CB  . ALA   B 3   ? 0.1680 0.1788 0.2158 0.0015  -0.0045 0.0280  9   ALA   C CB  
1112 N N   . ILE   B 4   ? 0.1304 0.1343 0.1662 0.0039  0.0004  0.0236  10  ILE   C N   
1113 C CA  . ILE   B 4   ? 0.1352 0.1357 0.1680 0.0050  0.0029  0.0228  10  ILE   C CA  
1114 C C   . ILE   B 4   ? 0.1332 0.1331 0.1728 0.0048  0.0057  0.0247  10  ILE   C C   
1115 O O   . ILE   B 4   ? 0.1514 0.1525 0.1954 0.0050  0.0069  0.0255  10  ILE   C O   
1116 C CB  . ILE   B 4   ? 0.1368 0.1355 0.1636 0.0071  0.0045  0.0209  10  ILE   C CB  
1117 C CG1 . ILE   B 4   ? 0.1609 0.1610 0.1836 0.0073  0.0020  0.0192  10  ILE   C CG1 
1118 C CG2 . ILE   B 4   ? 0.1670 0.1620 0.1890 0.0088  0.0070  0.0207  10  ILE   C CG2 
1119 C CD1 . ILE   B 4   ? 0.1616 0.1608 0.1808 0.0093  0.0026  0.0169  10  ILE   C CD1 
1120 N N   . TYR   B 5   ? 0.1403 0.1383 0.1818 0.0046  0.0072  0.0255  11  TYR   C N   
1121 C CA  . TYR   B 5   ? 0.1476 0.1448 0.1967 0.0045  0.0106  0.0276  11  TYR   C CA  
1122 C C   . TYR   B 5   ? 0.1551 0.1478 0.1993 0.0069  0.0154  0.0279  11  TYR   C C   
1123 O O   . TYR   B 5   ? 0.1768 0.1674 0.2194 0.0069  0.0159  0.0281  11  TYR   C O   
1124 C CB  . TYR   B 5   ? 0.1554 0.1543 0.2134 0.0021  0.0083  0.0288  11  TYR   C CB  
1125 C CG  . TYR   B 5   ? 0.1533 0.1566 0.2152 0.0005  0.0036  0.0290  11  TYR   C CG  
1126 C CD1 . TYR   B 5   ? 0.1565 0.1622 0.2260 0.0003  0.0041  0.0309  11  TYR   C CD1 
1127 C CD2 . TYR   B 5   ? 0.1597 0.1644 0.2169 -0.0004 -0.0010 0.0275  11  TYR   C CD2 
1128 C CE1 . TYR   B 5   ? 0.1665 0.1762 0.2389 -0.0007 -0.0002 0.0316  11  TYR   C CE1 
1129 C CE2 . TYR   B 5   ? 0.1847 0.1932 0.2438 -0.0012 -0.0051 0.0281  11  TYR   C CE2 
1130 C CZ  . TYR   B 5   ? 0.1748 0.1858 0.2415 -0.0013 -0.0047 0.0303  11  TYR   C CZ  
1131 O OH  . TYR   B 5   ? 0.2044 0.2189 0.2723 -0.0015 -0.0085 0.0315  11  TYR   C OH  
1132 N N   . VAL   B 6   ? 0.1717 0.1626 0.2129 0.0092  0.0189  0.0278  12  VAL   C N   
1133 C CA  . VAL   B 6   ? 0.1786 0.1649 0.2130 0.0123  0.0237  0.0282  12  VAL   C CA  
1134 C C   . VAL   B 6   ? 0.1879 0.1726 0.2271 0.0136  0.0290  0.0302  12  VAL   C C   
1135 O O   . VAL   B 6   ? 0.1721 0.1584 0.2139 0.0136  0.0289  0.0294  12  VAL   C O   
1136 C CB  . VAL   B 6   ? 0.2068 0.1920 0.2296 0.0147  0.0223  0.0254  12  VAL   C CB  
1137 C CG1 . VAL   B 6   ? 0.2135 0.2008 0.2368 0.0146  0.0206  0.0232  12  VAL   C CG1 
1138 C CG2 . VAL   B 6   ? 0.2250 0.2055 0.2395 0.0186  0.0268  0.0259  12  VAL   C CG2 
1139 N N   . GLY   B 7   ? 0.2011 0.1827 0.2428 0.0148  0.0341  0.0329  13  GLY   C N   
1140 C CA  . GLY   B 7   ? 0.2047 0.1846 0.2517 0.0163  0.0400  0.0351  13  GLY   C CA  
1141 C C   . GLY   B 7   ? 0.2020 0.1860 0.2621 0.0134  0.0383  0.0360  13  GLY   C C   
1142 O O   . GLY   B 7   ? 0.2099 0.1974 0.2779 0.0102  0.0340  0.0364  13  GLY   C O   
1143 N N   . ASN   B 8   ? 0.1925 0.1765 0.2539 0.0146  0.0407  0.0358  14  ASN   C N   
1144 C CA  . ASN   B 8   ? 0.1889 0.1770 0.2627 0.0121  0.0387  0.0368  14  ASN   C CA  
1145 C C   . ASN   B 8   ? 0.1726 0.1635 0.2429 0.0114  0.0340  0.0341  14  ASN   C C   
1146 O O   . ASN   B 8   ? 0.1666 0.1593 0.2436 0.0110  0.0344  0.0345  14  ASN   C O   
1147 C CB  . ASN   B 8   ? 0.2192 0.2058 0.3012 0.0135  0.0453  0.0393  14  ASN   C CB  
1148 C CG  . ASN   B 8   ? 0.2935 0.2792 0.3850 0.0131  0.0492  0.0428  14  ASN   C CG  
1149 O OD1 . ASN   B 8   ? 0.3191 0.3085 0.4243 0.0103  0.0469  0.0446  14  ASN   C OD1 
1150 N ND2 . ASN   B 8   ? 0.3421 0.3227 0.4265 0.0159  0.0547  0.0438  14  ASN   C ND2 
1151 N N   . TYR   B 9   ? 0.1502 0.1416 0.2118 0.0110  0.0295  0.0317  15  TYR   C N   
1152 C CA  . TYR   B 9   ? 0.1469 0.1408 0.2058 0.0103  0.0252  0.0293  15  TYR   C CA  
1153 C C   . TYR   B 9   ? 0.1400 0.1374 0.1998 0.0078  0.0195  0.0294  15  TYR   C C   
1154 O O   . TYR   B 9   ? 0.1532 0.1499 0.2101 0.0072  0.0183  0.0294  15  TYR   C O   
1155 C CB  . TYR   B 9   ? 0.1630 0.1541 0.2099 0.0128  0.0256  0.0258  15  TYR   C CB  
1156 C CG  . TYR   B 9   ? 0.1731 0.1601 0.2163 0.0160  0.0308  0.0249  15  TYR   C CG  
1157 C CD1 . TYR   B 9   ? 0.2001 0.1874 0.2494 0.0162  0.0330  0.0247  15  TYR   C CD1 
1158 C CD2 . TYR   B 9   ? 0.2029 0.1856 0.2356 0.0191  0.0337  0.0241  15  TYR   C CD2 
1159 C CE1 . TYR   B 9   ? 0.2431 0.2263 0.2881 0.0193  0.0380  0.0234  15  TYR   C CE1 
1160 C CE2 . TYR   B 9   ? 0.2427 0.2214 0.2701 0.0226  0.0385  0.0230  15  TYR   C CE2 
1161 C CZ  . TYR   B 9   ? 0.2721 0.2509 0.3054 0.0226  0.0406  0.0224  15  TYR   C CZ  
1162 O OH  . TYR   B 9   ? 0.3509 0.3253 0.3787 0.0262  0.0457  0.0210  15  TYR   C OH  
1163 N N   . ARG   B 10  ? 0.1308 0.1316 0.1941 0.0066  0.0163  0.0293  16  ARG   C N   
1164 C CA  . ARG   B 10  ? 0.1273 0.1311 0.1894 0.0049  0.0112  0.0292  16  ARG   C CA  
1165 C C   . ARG   B 10  ? 0.1314 0.1355 0.1886 0.0056  0.0102  0.0271  16  ARG   C C   
1166 O O   . ARG   B 10  ? 0.1320 0.1366 0.1932 0.0061  0.0115  0.0271  16  ARG   C O   
1167 C CB  . ARG   B 10  ? 0.1390 0.1467 0.2107 0.0032  0.0086  0.0320  16  ARG   C CB  
1168 C CG  . ARG   B 10  ? 0.1479 0.1588 0.2177 0.0022  0.0038  0.0322  16  ARG   C CG  
1169 C CD  . ARG   B 10  ? 0.1412 0.1559 0.2197 0.0011  0.0009  0.0351  16  ARG   C CD  
1170 N NE  . ARG   B 10  ? 0.1514 0.1689 0.2299 0.0012  -0.0016 0.0366  16  ARG   C NE  
1171 C CZ  . ARG   B 10  ? 0.1718 0.1911 0.2454 0.0010  -0.0057 0.0368  16  ARG   C CZ  
1172 N NH1 . ARG   B 10  ? 0.1981 0.2166 0.2662 0.0003  -0.0081 0.0350  16  ARG   C NH1 
1173 N NH2 . ARG   B 10  ? 0.1802 0.2018 0.2542 0.0017  -0.0068 0.0389  16  ARG   C NH2 
1174 N N   . VAL   B 11  ? 0.1264 0.1302 0.1762 0.0058  0.0079  0.0252  17  VAL   C N   
1175 C CA  . VAL   B 11  ? 0.1231 0.1272 0.1695 0.0064  0.0068  0.0231  17  VAL   C CA  
1176 C C   . VAL   B 11  ? 0.1211 0.1282 0.1683 0.0051  0.0036  0.0244  17  VAL   C C   
1177 O O   . VAL   B 11  ? 0.1286 0.1359 0.1720 0.0045  0.0016  0.0246  17  VAL   C O   
1178 C CB  . VAL   B 11  ? 0.1379 0.1395 0.1756 0.0080  0.0069  0.0202  17  VAL   C CB  
1179 C CG1 . VAL   B 11  ? 0.1618 0.1640 0.1984 0.0086  0.0058  0.0176  17  VAL   C CG1 
1180 C CG2 . VAL   B 11  ? 0.1632 0.1612 0.1975 0.0098  0.0103  0.0195  17  VAL   C CG2 
1181 N N   . VAL   B 12  ? 0.1160 0.1252 0.1680 0.0049  0.0034  0.0253  18  VAL   C N   
1182 C CA  A VAL   B 12  ? 0.1166 0.1284 0.1687 0.0043  0.0010  0.0272  18  VAL   C CA  
1183 C CA  B VAL   B 12  ? 0.1330 0.1449 0.1853 0.0043  0.0010  0.0273  18  VAL   C CA  
1184 C C   . VAL   B 12  ? 0.1204 0.1327 0.1742 0.0049  0.0018  0.0264  18  VAL   C C   
1185 O O   . VAL   B 12  ? 0.1227 0.1338 0.1793 0.0055  0.0036  0.0243  18  VAL   C O   
1186 C CB  A VAL   B 12  ? 0.1151 0.1295 0.1736 0.0037  0.0001  0.0310  18  VAL   C CB  
1187 C CB  B VAL   B 12  ? 0.1656 0.1799 0.2248 0.0036  0.0004  0.0310  18  VAL   C CB  
1188 C CG1 A VAL   B 12  ? 0.1120 0.1266 0.1700 0.0028  -0.0017 0.0316  18  VAL   C CG1 
1189 C CG1 B VAL   B 12  ? 0.1648 0.1794 0.2320 0.0040  0.0029  0.0320  18  VAL   C CG1 
1190 C CG2 A VAL   B 12  ? 0.1076 0.1223 0.1745 0.0040  0.0026  0.0320  18  VAL   C CG2 
1191 C CG2 B VAL   B 12  ? 0.1848 0.2016 0.2426 0.0035  -0.0025 0.0334  18  VAL   C CG2 
1192 N N   . ASN   B 13  ? 0.1160 0.1301 0.1687 0.0049  0.0006  0.0280  19  ASN   C N   
1193 C CA  . ASN   B 13  ? 0.1127 0.1275 0.1696 0.0053  0.0019  0.0281  19  ASN   C CA  
1194 C C   . ASN   B 13  ? 0.1124 0.1283 0.1783 0.0053  0.0035  0.0306  19  ASN   C C   
1195 O O   . ASN   B 13  ? 0.1107 0.1281 0.1784 0.0051  0.0028  0.0340  19  ASN   C O   
1196 C CB  . ASN   B 13  ? 0.1247 0.1410 0.1790 0.0057  0.0012  0.0306  19  ASN   C CB  
1197 C CG  . ASN   B 13  ? 0.1151 0.1303 0.1613 0.0059  0.0000  0.0284  19  ASN   C CG  
1198 O OD1 . ASN   B 13  ? 0.1298 0.1447 0.1701 0.0056  -0.0018 0.0286  19  ASN   C OD1 
1199 N ND2 . ASN   B 13  ? 0.1348 0.1495 0.1818 0.0063  0.0008  0.0261  19  ASN   C ND2 
1200 N N   . ARG   B 14  ? 0.1127 0.1278 0.1845 0.0055  0.0055  0.0287  20  ARG   C N   
1201 C CA  . ARG   B 14  ? 0.1077 0.1233 0.1888 0.0055  0.0075  0.0308  20  ARG   C CA  
1202 C C   . ARG   B 14  ? 0.1165 0.1346 0.2011 0.0058  0.0076  0.0363  20  ARG   C C   
1203 O O   . ARG   B 14  ? 0.1237 0.1431 0.2132 0.0060  0.0080  0.0397  20  ARG   C O   
1204 C CB  . ARG   B 14  ? 0.1079 0.1221 0.1951 0.0057  0.0093  0.0273  20  ARG   C CB  
1205 C CG  . ARG   B 14  ? 0.1110 0.1249 0.2084 0.0058  0.0119  0.0286  20  ARG   C CG  
1206 C CD  . ARG   B 14  ? 0.1168 0.1291 0.2206 0.0059  0.0132  0.0244  20  ARG   C CD  
1207 N NE  . ARG   B 14  ? 0.1202 0.1314 0.2337 0.0061  0.0159  0.0243  20  ARG   C NE  
1208 C CZ  . ARG   B 14  ? 0.1143 0.1265 0.2379 0.0060  0.0181  0.0282  20  ARG   C CZ  
1209 N NH1 . ARG   B 14  ? 0.1365 0.1511 0.2611 0.0061  0.0180  0.0331  20  ARG   C NH1 
1210 N NH2 . ARG   B 14  ? 0.1256 0.1364 0.2584 0.0062  0.0207  0.0272  20  ARG   C NH2 
1211 N N   . HIS   B 15  ? 0.1092 0.1281 0.1909 0.0063  0.0074  0.0375  21  HIS   C N   
1212 C CA  . HIS   B 15  ? 0.1185 0.1394 0.2021 0.0072  0.0080  0.0432  21  HIS   C CA  
1213 C C   . HIS   B 15  ? 0.1339 0.1564 0.2112 0.0076  0.0050  0.0462  21  HIS   C C   
1214 O O   . HIS   B 15  ? 0.1604 0.1846 0.2387 0.0089  0.0051  0.0511  21  HIS   C O   
1215 C CB  . HIS   B 15  ? 0.1359 0.1569 0.2187 0.0080  0.0095  0.0441  21  HIS   C CB  
1216 C CG  . HIS   B 15  ? 0.1288 0.1495 0.2008 0.0082  0.0076  0.0428  21  HIS   C CG  
1217 N ND1 . HIS   B 15  ? 0.1391 0.1584 0.2075 0.0075  0.0067  0.0377  21  HIS   C ND1 
1218 C CD2 . HIS   B 15  ? 0.1435 0.1651 0.2079 0.0094  0.0067  0.0459  21  HIS   C CD2 
1219 C CE1 . HIS   B 15  ? 0.1580 0.1773 0.2176 0.0080  0.0054  0.0381  21  HIS   C CE1 
1220 N NE2 . HIS   B 15  ? 0.1460 0.1664 0.2026 0.0091  0.0054  0.0426  21  HIS   C NE2 
1221 N N   . LEU   B 16  ? 0.1234 0.1452 0.1947 0.0067  0.0025  0.0434  22  LEU   C N   
1222 C CA  . LEU   B 16  ? 0.1427 0.1659 0.2095 0.0067  -0.0010 0.0452  22  LEU   C CA  
1223 C C   . LEU   B 16  ? 0.1457 0.1694 0.2184 0.0059  -0.0016 0.0452  22  LEU   C C   
1224 O O   . LEU   B 16  ? 0.1531 0.1781 0.2241 0.0055  -0.0047 0.0459  22  LEU   C O   
1225 C CB  . LEU   B 16  ? 0.1404 0.1626 0.1972 0.0064  -0.0033 0.0424  22  LEU   C CB  
1226 C CG  . LEU   B 16  ? 0.1473 0.1692 0.1983 0.0075  -0.0024 0.0430  22  LEU   C CG  
1227 C CD1 . LEU   B 16  ? 0.1640 0.1844 0.2057 0.0072  -0.0044 0.0398  22  LEU   C CD1 
1228 C CD2 . LEU   B 16  ? 0.1585 0.1822 0.2085 0.0093  -0.0026 0.0481  22  LEU   C CD2 
1229 N N   . ALA   B 17  ? 0.1397 0.1621 0.2194 0.0055  0.0014  0.0438  23  ALA   C N   
1230 C CA  . ALA   B 17  ? 0.1297 0.1520 0.2151 0.0050  0.0019  0.0437  23  ALA   C CA  
1231 C C   . ALA   B 17  ? 0.1405 0.1660 0.2322 0.0055  0.0003  0.0486  23  ALA   C C   
1232 O O   . ALA   B 17  ? 0.1573 0.1843 0.2521 0.0066  0.0008  0.0522  23  ALA   C O   
1233 C CB  . ALA   B 17  ? 0.1490 0.1690 0.2399 0.0051  0.0058  0.0413  23  ALA   C CB  
1234 N N   . THR   B 18  ? 0.1458 0.1721 0.2402 0.0048  -0.0013 0.0489  24  THR   C N   
1235 C CA  . THR   B 18  ? 0.1485 0.1782 0.2498 0.0053  -0.0036 0.0532  24  THR   C CA  
1236 C C   . THR   B 18  ? 0.1355 0.1651 0.2484 0.0055  0.0001  0.0546  24  THR   C C   
1237 O O   . THR   B 18  ? 0.1444 0.1710 0.2590 0.0052  0.0042  0.0517  24  THR   C O   
1238 C CB  . THR   B 18  ? 0.1621 0.1932 0.2623 0.0043  -0.0078 0.0525  24  THR   C CB  
1239 O OG1 . THR   B 18  ? 0.1669 0.1959 0.2710 0.0033  -0.0051 0.0499  24  THR   C OG1 
1240 C CG2 . THR   B 18  ? 0.1853 0.2161 0.2741 0.0041  -0.0114 0.0504  24  THR   C CG2 
1241 N N   . HIS   B 19  ? 0.1493 0.1823 0.2704 0.0063  -0.0016 0.0592  25  HIS   C N   
1242 C CA  . HIS   B 19  ? 0.1511 0.1840 0.2842 0.0065  0.0019  0.0607  25  HIS   C CA  
1243 C C   . HIS   B 19  ? 0.1238 0.1548 0.2590 0.0054  0.0037  0.0576  25  HIS   C C   
1244 O O   . HIS   B 19  ? 0.1483 0.1765 0.2877 0.0056  0.0087  0.0559  25  HIS   C O   
1245 C CB  . HIS   B 19  ? 0.1753 0.2126 0.3171 0.0076  -0.0010 0.0663  25  HIS   C CB  
1246 C CG  . HIS   B 19  ? 0.1678 0.2054 0.3229 0.0077  0.0023  0.0677  25  HIS   C CG  
1247 N ND1 . HIS   B 19  ? 0.1948 0.2304 0.3568 0.0085  0.0076  0.0685  25  HIS   C ND1 
1248 C CD2 . HIS   B 19  ? 0.1867 0.2256 0.3492 0.0070  0.0016  0.0680  25  HIS   C CD2 
1249 C CE1 . HIS   B 19  ? 0.1938 0.2299 0.3668 0.0086  0.0097  0.0697  25  HIS   C CE1 
1250 N NE2 . HIS   B 19  ? 0.1894 0.2275 0.3634 0.0077  0.0065  0.0695  25  HIS   C NE2 
1251 N N   . ASN   B 20  ? 0.1369 0.1689 0.2689 0.0043  0.0001  0.0565  26  ASN   C N   
1252 C CA  . ASN   B 20  ? 0.1495 0.1794 0.2841 0.0035  0.0027  0.0541  26  ASN   C CA  
1253 C C   . ASN   B 20  ? 0.1312 0.1562 0.2581 0.0036  0.0072  0.0498  26  ASN   C C   
1254 O O   . ASN   B 20  ? 0.1351 0.1574 0.2651 0.0039  0.0118  0.0485  26  ASN   C O   
1255 C CB  . ASN   B 20  ? 0.1778 0.2093 0.3114 0.0022  -0.0017 0.0535  26  ASN   C CB  
1256 C CG  . ASN   B 20  ? 0.2529 0.2823 0.3920 0.0015  0.0018  0.0522  26  ASN   C CG  
1257 O OD1 . ASN   B 20  ? 0.2959 0.3267 0.4471 0.0017  0.0038  0.0545  26  ASN   C OD1 
1258 N ND2 . ASN   B 20  ? 0.2825 0.3086 0.4135 0.0010  0.0031  0.0489  26  ASN   C ND2 
1259 N N   . ASP   B 21  ? 0.1273 0.1511 0.2437 0.0036  0.0058  0.0476  27  ASP   C N   
1260 C CA  . ASP   B 21  ? 0.1244 0.1440 0.2338 0.0040  0.0092  0.0435  27  ASP   C CA  
1261 C C   . ASP   B 21  ? 0.1193 0.1369 0.2339 0.0050  0.0137  0.0428  27  ASP   C C   
1262 O O   . ASP   B 21  ? 0.1399 0.1541 0.2532 0.0057  0.0175  0.0400  27  ASP   C O   
1263 C CB  . ASP   B 21  ? 0.1316 0.1510 0.2314 0.0039  0.0068  0.0417  27  ASP   C CB  
1264 C CG  . ASP   B 21  ? 0.1459 0.1656 0.2381 0.0031  0.0033  0.0407  27  ASP   C CG  
1265 O OD1 . ASP   B 21  ? 0.1586 0.1769 0.2504 0.0026  0.0040  0.0395  27  ASP   C OD1 
1266 O OD2 . ASP   B 21  ? 0.1500 0.1712 0.2371 0.0031  0.0002  0.0413  27  ASP   C OD2 
1267 N N   . TRP   B 22  ? 0.1258 0.1455 0.2465 0.0054  0.0135  0.0455  28  TRP   C N   
1268 C CA  . TRP   B 22  ? 0.1285 0.1462 0.2555 0.0063  0.0177  0.0447  28  TRP   C CA  
1269 C C   . TRP   B 22  ? 0.1172 0.1341 0.2531 0.0068  0.0214  0.0458  28  TRP   C C   
1270 O O   . TRP   B 22  ? 0.1348 0.1482 0.2721 0.0077  0.0258  0.0429  28  TRP   C O   
1271 C CB  . TRP   B 22  ? 0.1303 0.1502 0.2630 0.0067  0.0171  0.0479  28  TRP   C CB  
1272 C CG  . TRP   B 22  ? 0.1311 0.1502 0.2573 0.0066  0.0162  0.0458  28  TRP   C CG  
1273 C CD1 . TRP   B 22  ? 0.1515 0.1726 0.2716 0.0064  0.0128  0.0475  28  TRP   C CD1 
1274 C CD2 . TRP   B 22  ? 0.1134 0.1292 0.2386 0.0067  0.0187  0.0412  28  TRP   C CD2 
1275 N NE1 . TRP   B 22  ? 0.1402 0.1598 0.2572 0.0064  0.0136  0.0450  28  TRP   C NE1 
1276 C CE2 . TRP   B 22  ? 0.1319 0.1485 0.2529 0.0065  0.0169  0.0410  28  TRP   C CE2 
1277 C CE3 . TRP   B 22  ? 0.1535 0.1659 0.2826 0.0073  0.0223  0.0374  28  TRP   C CE3 
1278 C CZ2 . TRP   B 22  ? 0.1340 0.1485 0.2552 0.0065  0.0181  0.0370  28  TRP   C CZ2 
1279 C CZ3 . TRP   B 22  ? 0.1645 0.1747 0.2927 0.0074  0.0230  0.0329  28  TRP   C CZ3 
1280 C CH2 . TRP   B 22  ? 0.1614 0.1728 0.2864 0.0069  0.0208  0.0328  28  TRP   C CH2 
1281 N N   . ALA   B 23  ? 0.1261 0.1461 0.2676 0.0064  0.0195  0.0494  29  ALA   C N   
1282 C CA  . ALA   B 23  ? 0.1268 0.1465 0.2782 0.0068  0.0230  0.0510  29  ALA   C CA  
1283 C C   . ALA   B 23  ? 0.1518 0.1677 0.2986 0.0071  0.0265  0.0479  29  ALA   C C   
1284 O O   . ALA   B 23  ? 0.1591 0.1737 0.3132 0.0079  0.0309  0.0488  29  ALA   C O   
1285 C CB  . ALA   B 23  ? 0.1457 0.1705 0.3058 0.0063  0.0192  0.0559  29  ALA   C CB  
1286 N N   . ASN   B 24  ? 0.1555 0.1698 0.2905 0.0067  0.0248  0.0448  30  ASN   C N   
1287 C CA  . ASN   B 24  ? 0.1439 0.1542 0.2725 0.0073  0.0281  0.0422  30  ASN   C CA  
1288 C C   . ASN   B 24  ? 0.1510 0.1578 0.2670 0.0082  0.0285  0.0374  30  ASN   C C   
1289 O O   . ASN   B 24  ? 0.1497 0.1545 0.2566 0.0084  0.0282  0.0354  30  ASN   C O   
1290 C CB  . ASN   B 24  ? 0.1626 0.1750 0.2910 0.0060  0.0249  0.0437  30  ASN   C CB  
1291 C CG  . ASN   B 24  ? 0.1714 0.1872 0.3135 0.0053  0.0246  0.0478  30  ASN   C CG  
1292 O OD1 . ASN   B 24  ? 0.1950 0.2090 0.3440 0.0061  0.0297  0.0488  30  ASN   C OD1 
1293 N ND2 . ASN   B 24  ? 0.1797 0.2003 0.3265 0.0041  0.0190  0.0504  30  ASN   C ND2 
1294 N N   . LEU   B 25  ? 0.1572 0.1631 0.2734 0.0088  0.0290  0.0355  31  LEU   C N   
1295 C CA  . LEU   B 25  ? 0.1443 0.1477 0.2504 0.0094  0.0282  0.0308  31  LEU   C CA  
1296 C C   . LEU   B 25  ? 0.1775 0.1759 0.2752 0.0115  0.0318  0.0268  31  LEU   C C   
1297 O O   . LEU   B 25  ? 0.1857 0.1814 0.2866 0.0130  0.0365  0.0264  31  LEU   C O   
1298 C CB  . LEU   B 25  ? 0.1547 0.1586 0.2664 0.0094  0.0283  0.0300  31  LEU   C CB  
1299 C CG  . LEU   B 25  ? 0.1603 0.1623 0.2645 0.0097  0.0267  0.0251  31  LEU   C CG  
1300 C CD1 . LEU   B 25  ? 0.1634 0.1680 0.2618 0.0085  0.0221  0.0258  31  LEU   C CD1 
1301 C CD2 . LEU   B 25  ? 0.1902 0.1920 0.3026 0.0098  0.0278  0.0240  31  LEU   C CD2 
1302 N N   . VAL   B 26  ? 0.1566 0.1535 0.2431 0.0119  0.0298  0.0238  32  VAL   C N   
1303 C CA  . VAL   B 26  ? 0.1692 0.1613 0.2455 0.0144  0.0324  0.0196  32  VAL   C CA  
1304 C C   . VAL   B 26  ? 0.1749 0.1660 0.2468 0.0151  0.0301  0.0145  32  VAL   C C   
1305 O O   . VAL   B 26  ? 0.1971 0.1845 0.2661 0.0172  0.0325  0.0105  32  VAL   C O   
1306 C CB  . VAL   B 26  ? 0.1786 0.1698 0.2460 0.0149  0.0317  0.0202  32  VAL   C CB  
1307 C CG1 . VAL   B 26  ? 0.2095 0.1959 0.2644 0.0180  0.0336  0.0161  32  VAL   C CG1 
1308 C CG2 . VAL   B 26  ? 0.1864 0.1783 0.2600 0.0143  0.0343  0.0248  32  VAL   C CG2 
1309 N N   . TRP   B 27  ? 0.1586 0.1526 0.2303 0.0134  0.0255  0.0143  33  TRP   C N   
1310 C CA  . TRP   B 27  ? 0.1621 0.1555 0.2311 0.0138  0.0231  0.0095  33  TRP   C CA  
1311 C C   . TRP   B 27  ? 0.1499 0.1474 0.2234 0.0115  0.0194  0.0115  33  TRP   C C   
1312 O O   . TRP   B 27  ? 0.1526 0.1524 0.2249 0.0103  0.0178  0.0151  33  TRP   C O   
1313 C CB  . TRP   B 27  ? 0.1851 0.1756 0.2409 0.0160  0.0219  0.0054  33  TRP   C CB  
1314 C CG  . TRP   B 27  ? 0.1911 0.1817 0.2438 0.0163  0.0181  0.0006  33  TRP   C CG  
1315 C CD1 . TRP   B 27  ? 0.2151 0.2037 0.2683 0.0175  0.0176  -0.0050 33  TRP   C CD1 
1316 C CD2 . TRP   B 27  ? 0.1697 0.1630 0.2201 0.0151  0.0140  0.0007  33  TRP   C CD2 
1317 N NE1 . TRP   B 27  ? 0.2286 0.2186 0.2803 0.0173  0.0132  -0.0084 33  TRP   C NE1 
1318 C CE2 . TRP   B 27  ? 0.1958 0.1886 0.2454 0.0159  0.0113  -0.0047 33  TRP   C CE2 
1319 C CE3 . TRP   B 27  ? 0.1707 0.1665 0.2195 0.0137  0.0125  0.0046  33  TRP   C CE3 
1320 C CZ2 . TRP   B 27  ? 0.1971 0.1920 0.2451 0.0154  0.0073  -0.0059 33  TRP   C CZ2 
1321 C CZ3 . TRP   B 27  ? 0.1845 0.1819 0.2304 0.0134  0.0090  0.0033  33  TRP   C CZ3 
1322 C CH2 . TRP   B 27  ? 0.1853 0.1825 0.2317 0.0141  0.0066  -0.0015 33  TRP   C CH2 
1323 N N   . GLU   B 28  ? 0.1451 0.1432 0.2238 0.0111  0.0183  0.0091  34  GLU   C N   
1324 C CA  . GLU   B 28  ? 0.1605 0.1619 0.2433 0.0095  0.0157  0.0111  34  GLU   C CA  
1325 C C   . GLU   B 28  ? 0.1494 0.1503 0.2343 0.0097  0.0142  0.0062  34  GLU   C C   
1326 O O   . GLU   B 28  ? 0.1527 0.1510 0.2405 0.0106  0.0154  0.0019  34  GLU   C O   
1327 C CB  . GLU   B 28  ? 0.1678 0.1721 0.2606 0.0082  0.0168  0.0167  34  GLU   C CB  
1328 C CG  . GLU   B 28  ? 0.1733 0.1765 0.2763 0.0085  0.0199  0.0165  34  GLU   C CG  
1329 C CD  . GLU   B 28  ? 0.1873 0.1903 0.2980 0.0082  0.0199  0.0139  34  GLU   C CD  
1330 O OE1 . GLU   B 28  ? 0.2269 0.2276 0.3440 0.0088  0.0224  0.0113  34  GLU   C OE1 
1331 O OE2 . GLU   B 28  ? 0.1733 0.1783 0.2849 0.0074  0.0180  0.0147  34  GLU   C OE2 
1332 N N   . ASP   B 29  ? 0.1406 0.1437 0.2251 0.0088  0.0115  0.0067  35  ASP   C N   
1333 C CA  . ASP   B 29  ? 0.1401 0.1434 0.2291 0.0088  0.0099  0.0023  35  ASP   C CA  
1334 C C   . ASP   B 29  ? 0.1377 0.1442 0.2323 0.0074  0.0093  0.0060  35  ASP   C C   
1335 O O   . ASP   B 29  ? 0.1321 0.1400 0.2201 0.0073  0.0075  0.0076  35  ASP   C O   
1336 C CB  . ASP   B 29  ? 0.1673 0.1687 0.2464 0.0103  0.0071  -0.0032 35  ASP   C CB  
1337 C CG  . ASP   B 29  ? 0.2016 0.2032 0.2850 0.0105  0.0044  -0.0086 35  ASP   C CG  
1338 O OD1 . ASP   B 29  ? 0.2041 0.2082 0.2967 0.0091  0.0042  -0.0070 35  ASP   C OD1 
1339 O OD2 . ASP   B 29  ? 0.2555 0.2550 0.3328 0.0123  0.0022  -0.0144 35  ASP   C OD2 
1340 N N   . SER   B 30  ? 0.1367 0.1441 0.2434 0.0067  0.0111  0.0076  36  SER   C N   
1341 C CA  A SER   B 30  ? 0.1417 0.1518 0.2542 0.0059  0.0116  0.0118  36  SER   C CA  
1342 C CA  B SER   B 30  ? 0.1495 0.1596 0.2613 0.0059  0.0115  0.0119  36  SER   C CA  
1343 C C   . SER   B 30  ? 0.1435 0.1543 0.2549 0.0058  0.0093  0.0086  36  SER   C C   
1344 O O   . SER   B 30  ? 0.1406 0.1534 0.2495 0.0057  0.0091  0.0121  36  SER   C O   
1345 C CB  A SER   B 30  ? 0.1406 0.1509 0.2674 0.0054  0.0146  0.0137  36  SER   C CB  
1346 C CB  B SER   B 30  ? 0.1721 0.1827 0.2973 0.0054  0.0147  0.0150  36  SER   C CB  
1347 O OG  A SER   B 30  ? 0.1505 0.1629 0.2835 0.0050  0.0156  0.0172  36  SER   C OG  
1348 O OG  B SER   B 30  ? 0.2007 0.2095 0.3344 0.0053  0.0150  0.0093  36  SER   C OG  
1349 N N   . SER   B 31  ? 0.1374 0.1468 0.2502 0.0062  0.0073  0.0019  37  SER   C N   
1350 C CA  . SER   B 31  ? 0.1452 0.1558 0.2588 0.0063  0.0046  -0.0014 37  SER   C CA  
1351 C C   . SER   B 31  ? 0.1413 0.1524 0.2418 0.0070  0.0024  -0.0006 37  SER   C C   
1352 O O   . SER   B 31  ? 0.1531 0.1659 0.2548 0.0069  0.0011  -0.0007 37  SER   C O   
1353 C CB  . SER   B 31  ? 0.1879 0.1970 0.3052 0.0068  0.0019  -0.0093 37  SER   C CB  
1354 O OG  . SER   B 31  ? 0.2611 0.2680 0.3658 0.0084  -0.0006 -0.0135 37  SER   C OG  
1355 N N   . ARG   B 32  ? 0.1327 0.1423 0.2222 0.0076  0.0024  0.0005  38  ARG   C N   
1356 C CA  . ARG   B 32  ? 0.1273 0.1370 0.2052 0.0082  0.0008  0.0015  38  ARG   C CA  
1357 C C   . ARG   B 32  ? 0.1204 0.1315 0.1956 0.0075  0.0024  0.0078  38  ARG   C C   
1358 O O   . ARG   B 32  ? 0.1246 0.1357 0.1913 0.0078  0.0012  0.0088  38  ARG   C O   
1359 C CB  . ARG   B 32  ? 0.1606 0.1676 0.2285 0.0097  -0.0001 -0.0013 38  ARG   C CB  
1360 C CG  . ARG   B 32  ? 0.1672 0.1726 0.2342 0.0112  -0.0025 -0.0080 38  ARG   C CG  
1361 C CD  . ARG   B 32  ? 0.1465 0.1487 0.2024 0.0133  -0.0025 -0.0101 38  ARG   C CD  
1362 N NE  . ARG   B 32  ? 0.1472 0.1492 0.1924 0.0143  -0.0034 -0.0083 38  ARG   C NE  
1363 C CZ  . ARG   B 32  ? 0.1473 0.1467 0.1817 0.0168  -0.0045 -0.0107 38  ARG   C CZ  
1364 N NH1 . ARG   B 32  ? 0.1731 0.1700 0.2044 0.0189  -0.0049 -0.0153 38  ARG   C NH1 
1365 N NH2 . ARG   B 32  ? 0.1629 0.1622 0.1893 0.0176  -0.0051 -0.0086 38  ARG   C NH2 
1366 N N   . ASP   B 33  ? 0.1146 0.1266 0.1965 0.0067  0.0048  0.0118  39  ASP   C N   
1367 C CA  . ASP   B 33  ? 0.1124 0.1256 0.1912 0.0063  0.0056  0.0174  39  ASP   C CA  
1368 C C   . ASP   B 33  ? 0.1148 0.1267 0.1848 0.0065  0.0048  0.0175  39  ASP   C C   
1369 O O   . ASP   B 33  ? 0.1228 0.1354 0.1870 0.0063  0.0039  0.0202  39  ASP   C O   
1370 C CB  . ASP   B 33  ? 0.1225 0.1373 0.1987 0.0063  0.0053  0.0200  39  ASP   C CB  
1371 C CG  . ASP   B 33  ? 0.1343 0.1503 0.2070 0.0063  0.0058  0.0254  39  ASP   C CG  
1372 O OD1 . ASP   B 33  ? 0.1387 0.1553 0.2161 0.0062  0.0071  0.0286  39  ASP   C OD1 
1373 O OD2 . ASP   B 33  ? 0.1284 0.1446 0.1938 0.0065  0.0048  0.0264  39  ASP   C OD2 
1374 N N   . LEU   B 34  ? 0.1062 0.1161 0.1757 0.0070  0.0053  0.0148  40  LEU   C N   
1375 C CA  . LEU   B 34  ? 0.1174 0.1259 0.1802 0.0073  0.0055  0.0155  40  LEU   C CA  
1376 C C   . LEU   B 34  ? 0.1145 0.1223 0.1825 0.0072  0.0078  0.0170  40  LEU   C C   
1377 O O   . LEU   B 34  ? 0.1215 0.1286 0.1961 0.0074  0.0093  0.0154  40  LEU   C O   
1378 C CB  . LEU   B 34  ? 0.1364 0.1423 0.1914 0.0087  0.0046  0.0111  40  LEU   C CB  
1379 C CG  . LEU   B 34  ? 0.1363 0.1424 0.1845 0.0091  0.0023  0.0098  40  LEU   C CG  
1380 C CD1 . LEU   B 34  ? 0.1608 0.1641 0.2011 0.0111  0.0016  0.0059  40  LEU   C CD1 
1381 C CD2 . LEU   B 34  ? 0.1426 0.1496 0.1869 0.0082  0.0019  0.0134  40  LEU   C CD2 
1382 N N   . LEU   B 35  ? 0.1079 0.1159 0.1739 0.0069  0.0081  0.0198  41  LEU   C N   
1383 C CA  . LEU   B 35  ? 0.1218 0.1292 0.1927 0.0070  0.0105  0.0213  41  LEU   C CA  
1384 C C   . LEU   B 35  ? 0.1195 0.1256 0.1851 0.0072  0.0108  0.0220  41  LEU   C C   
1385 O O   . LEU   B 35  ? 0.1235 0.1306 0.1848 0.0065  0.0087  0.0233  41  LEU   C O   
1386 C CB  . LEU   B 35  ? 0.1282 0.1385 0.2074 0.0060  0.0104  0.0261  41  LEU   C CB  
1387 C CG  . LEU   B 35  ? 0.1214 0.1317 0.2079 0.0062  0.0128  0.0282  41  LEU   C CG  
1388 C CD1 . LEU   B 35  ? 0.1416 0.1539 0.2378 0.0060  0.0136  0.0315  41  LEU   C CD1 
1389 C CD2 . LEU   B 35  ? 0.1407 0.1521 0.2262 0.0056  0.0118  0.0311  41  LEU   C CD2 
1390 N N   . VAL   B 36  ? 0.1239 0.1275 0.1900 0.0083  0.0138  0.0210  42  VAL   C N   
1391 C CA  . VAL   B 36  ? 0.1259 0.1278 0.1889 0.0087  0.0154  0.0221  42  VAL   C CA  
1392 C C   . VAL   B 36  ? 0.1202 0.1226 0.1921 0.0085  0.0182  0.0251  42  VAL   C C   
1393 O O   . VAL   B 36  ? 0.1382 0.1396 0.2147 0.0093  0.0207  0.0241  42  VAL   C O   
1394 C CB  . VAL   B 36  ? 0.1393 0.1371 0.1934 0.0110  0.0174  0.0185  42  VAL   C CB  
1395 C CG1 . VAL   B 36  ? 0.1614 0.1571 0.2130 0.0118  0.0201  0.0204  42  VAL   C CG1 
1396 C CG2 . VAL   B 36  ? 0.1532 0.1510 0.1994 0.0114  0.0141  0.0157  42  VAL   C CG2 
1397 N N   . SER   B 37  ? 0.1249 0.1288 0.2000 0.0074  0.0176  0.0282  43  SER   C N   
1398 C CA  . SER   B 37  ? 0.1261 0.1310 0.2111 0.0071  0.0200  0.0313  43  SER   C CA  
1399 C C   . SER   B 37  ? 0.1344 0.1371 0.2185 0.0076  0.0227  0.0321  43  SER   C C   
1400 O O   . SER   B 37  ? 0.1427 0.1437 0.2190 0.0079  0.0221  0.0309  43  SER   C O   
1401 C CB  . SER   B 37  ? 0.1268 0.1363 0.2194 0.0054  0.0163  0.0349  43  SER   C CB  
1402 O OG  . SER   B 37  ? 0.1424 0.1535 0.2314 0.0042  0.0123  0.0354  43  SER   C OG  
1403 N N   . SER   B 38  ? 0.1403 0.1427 0.2330 0.0080  0.0264  0.0343  44  SER   C N   
1404 C CA  . SER   B 38  ? 0.1600 0.1602 0.2542 0.0086  0.0301  0.0357  44  SER   C CA  
1405 C C   . SER   B 38  ? 0.1798 0.1837 0.2826 0.0063  0.0267  0.0386  44  SER   C C   
1406 O O   . SER   B 38  ? 0.2006 0.2087 0.3108 0.0047  0.0229  0.0404  44  SER   C O   
1407 C CB  . SER   B 38  ? 0.1942 0.1918 0.2937 0.0105  0.0365  0.0366  44  SER   C CB  
1408 O OG  . SER   B 38  ? 0.2407 0.2419 0.3529 0.0094  0.0359  0.0391  44  SER   C OG  
1409 N N   . THR   B 39  ? 0.1821 0.1843 0.2845 0.0062  0.0282  0.0392  45  THR   C N   
1410 C CA  . THR   B 39  ? 0.1889 0.1941 0.2999 0.0039  0.0248  0.0411  45  THR   C CA  
1411 C C   . THR   B 39  ? 0.2187 0.2224 0.3401 0.0043  0.0303  0.0437  45  THR   C C   
1412 O O   . THR   B 39  ? 0.2176 0.2169 0.3350 0.0066  0.0368  0.0438  45  THR   C O   
1413 C CB  . THR   B 39  ? 0.1960 0.2003 0.2984 0.0030  0.0214  0.0391  45  THR   C CB  
1414 O OG1 . THR   B 39  ? 0.2140 0.2135 0.3093 0.0049  0.0263  0.0385  45  THR   C OG1 
1415 C CG2 . THR   B 39  ? 0.2200 0.2256 0.3123 0.0029  0.0167  0.0368  45  THR   C CG2 
1416 N N   . THR   B 40  ? 0.2376 0.2451 0.3720 0.0022  0.0273  0.0456  46  THR   C N   
1417 C CA  . THR   B 40  ? 0.2606 0.2670 0.4073 0.0021  0.0322  0.0483  46  THR   C CA  
1418 C C   . THR   B 40  ? 0.2672 0.2704 0.4102 0.0020  0.0336  0.0476  46  THR   C C   
1419 O O   . THR   B 40  ? 0.2971 0.2962 0.4413 0.0037  0.0410  0.0493  46  THR   C O   
1420 C CB  . THR   B 40  ? 0.3024 0.3145 0.4662 0.0000  0.0280  0.0504  46  THR   C CB  
1421 O OG1 . THR   B 40  ? 0.3502 0.3658 0.5125 -0.0022 0.0194  0.0487  46  THR   C OG1 
1422 C CG2 . THR   B 40  ? 0.2893 0.3038 0.4570 0.0008  0.0279  0.0518  46  THR   C CG2 
1423 N N   . ALA   B 41  ? 0.2403 0.2449 0.3778 0.0002  0.0272  0.0453  47  ALA   C N   
1424 C CA  . ALA   B 41  ? 0.2478 0.2493 0.3823 0.0000  0.0282  0.0446  47  ALA   C CA  
1425 C C   . ALA   B 41  ? 0.2407 0.2378 0.3576 0.0023  0.0306  0.0428  47  ALA   C C   
1426 O O   . ALA   B 41  ? 0.2436 0.2413 0.3504 0.0029  0.0279  0.0408  47  ALA   C O   
1427 C CB  . ALA   B 41  ? 0.2706 0.2755 0.4086 -0.0030 0.0202  0.0427  47  ALA   C CB  
1428 N N   . GLN   B 42  ? 0.2338 0.2265 0.3477 0.0035  0.0352  0.0435  48  GLN   C N   
1429 C CA  . GLN   B 42  ? 0.2414 0.2301 0.3391 0.0060  0.0368  0.0420  48  GLN   C CA  
1430 C C   . GLN   B 42  ? 0.2275 0.2176 0.3191 0.0042  0.0300  0.0391  48  GLN   C C   
1431 O O   . GLN   B 42  ? 0.2483 0.2400 0.3476 0.0017  0.0267  0.0388  48  GLN   C O   
1432 C CB  . GLN   B 42  ? 0.3133 0.2966 0.4098 0.0086  0.0446  0.0445  48  GLN   C CB  
1433 C CG  . GLN   B 42  ? 0.4324 0.4128 0.5288 0.0117  0.0523  0.0469  48  GLN   C CG  
1434 C CD  . GLN   B 42  ? 0.5682 0.5428 0.6608 0.0149  0.0601  0.0498  48  GLN   C CD  
1435 O OE1 . GLN   B 42  ? 0.6105 0.5842 0.7151 0.0140  0.0637  0.0527  48  GLN   C OE1 
1436 N NE2 . GLN   B 42  ? 0.6081 0.5787 0.6843 0.0188  0.0628  0.0490  48  GLN   C NE2 
1437 N N   . GLY   B 43  ? 0.2002 0.1896 0.2781 0.0056  0.0282  0.0368  49  GLY   C N   
1438 C CA  . GLY   B 43  ? 0.1938 0.1839 0.2643 0.0046  0.0229  0.0342  49  GLY   C CA  
1439 C C   . GLY   B 43  ? 0.1950 0.1806 0.2569 0.0067  0.0260  0.0342  49  GLY   C C   
1440 O O   . GLY   B 43  ? 0.2335 0.2154 0.2923 0.0096  0.0321  0.0361  49  GLY   C O   
1441 N N   . CYS   B 44  ? 0.1841 0.1698 0.2416 0.0058  0.0222  0.0323  50  CYS   C N   
1442 C CA  . CYS   B 44  ? 0.2027 0.1844 0.2542 0.0074  0.0246  0.0325  50  CYS   C CA  
1443 C C   . CYS   B 44  ? 0.2061 0.1874 0.2452 0.0089  0.0220  0.0302  50  CYS   C C   
1444 O O   . CYS   B 44  ? 0.2423 0.2206 0.2766 0.0103  0.0234  0.0305  50  CYS   C O   
1445 C CB  . CYS   B 44  ? 0.2045 0.1859 0.2649 0.0049  0.0232  0.0324  50  CYS   C CB  
1446 S SG  . CYS   B 44  ? 0.2735 0.2553 0.3514 0.0032  0.0266  0.0353  50  CYS   C SG  
1447 N N   . ASP   B 45  ? 0.1736 0.1580 0.2085 0.0086  0.0184  0.0282  51  ASP   C N   
1448 C CA  . ASP   B 45  ? 0.1863 0.1705 0.2110 0.0099  0.0160  0.0261  51  ASP   C CA  
1449 C C   . ASP   B 45  ? 0.2019 0.1831 0.2185 0.0138  0.0197  0.0266  51  ASP   C C   
1450 O O   . ASP   B 45  ? 0.2327 0.2129 0.2503 0.0151  0.0231  0.0278  51  ASP   C O   
1451 C CB  . ASP   B 45  ? 0.1852 0.1734 0.2093 0.0087  0.0117  0.0241  51  ASP   C CB  
1452 C CG  . ASP   B 45  ? 0.2140 0.2051 0.2427 0.0057  0.0075  0.0234  51  ASP   C CG  
1453 O OD1 . ASP   B 45  ? 0.2471 0.2369 0.2761 0.0049  0.0066  0.0229  51  ASP   C OD1 
1454 O OD2 . ASP   B 45  ? 0.1911 0.1855 0.2227 0.0045  0.0051  0.0233  51  ASP   C OD2 
1455 N N   . THR   B 46  ? 0.1741 0.1536 0.1826 0.0157  0.0191  0.0257  52  THR   C N   
1456 C CA  . THR   B 46  ? 0.1839 0.1609 0.1829 0.0198  0.0212  0.0257  52  THR   C CA  
1457 C C   . THR   B 46  ? 0.1748 0.1544 0.1687 0.0202  0.0168  0.0223  52  THR   C C   
1458 O O   . THR   B 46  ? 0.1883 0.1699 0.1824 0.0187  0.0132  0.0209  52  THR   C O   
1459 C CB  . THR   B 46  ? 0.2126 0.1860 0.2066 0.0222  0.0233  0.0273  52  THR   C CB  
1460 O OG1 . THR   B 46  ? 0.2407 0.2113 0.2411 0.0219  0.0282  0.0307  52  THR   C OG1 
1461 C CG2 . THR   B 46  ? 0.2497 0.2206 0.2321 0.0270  0.0246  0.0272  52  THR   C CG2 
1462 N N   . ILE   B 47  ? 0.1775 0.1571 0.1673 0.0223  0.0171  0.0208  53  ILE   C N   
1463 C CA  . ILE   B 47  ? 0.1732 0.1551 0.1597 0.0227  0.0129  0.0174  53  ILE   C CA  
1464 C C   . ILE   B 47  ? 0.1703 0.1504 0.1475 0.0263  0.0120  0.0165  53  ILE   C C   
1465 O O   . ILE   B 47  ? 0.1909 0.1674 0.1612 0.0299  0.0149  0.0178  53  ILE   C O   
1466 C CB  . ILE   B 47  ? 0.1834 0.1657 0.1702 0.0235  0.0135  0.0156  53  ILE   C CB  
1467 C CG1 . ILE   B 47  ? 0.1933 0.1771 0.1895 0.0206  0.0151  0.0172  53  ILE   C CG1 
1468 C CG2 . ILE   B 47  ? 0.1926 0.1775 0.1782 0.0237  0.0091  0.0117  53  ILE   C CG2 
1469 C CD1 . ILE   B 47  ? 0.2097 0.1976 0.2131 0.0169  0.0116  0.0172  53  ILE   C CD1 
1470 N N   . ALA   B 48  ? 0.1591 0.1416 0.1361 0.0257  0.0079  0.0145  54  ALA   C N   
1471 C CA  . ALA   B 48  ? 0.1575 0.1390 0.1268 0.0291  0.0061  0.0134  54  ALA   C CA  
1472 C C   . ALA   B 48  ? 0.1620 0.1430 0.1251 0.0324  0.0049  0.0106  54  ALA   C C   
1473 O O   . ALA   B 48  ? 0.1717 0.1547 0.1388 0.0310  0.0033  0.0080  54  ALA   C O   
1474 C CB  . ALA   B 48  ? 0.1593 0.1440 0.1317 0.0275  0.0021  0.0117  54  ALA   C CB  
1475 N N   . ARG   B 49  ? 0.1712 0.1494 0.1246 0.0369  0.0052  0.0110  55  ARG   C N   
1476 C CA  . ARG   B 49  ? 0.1727 0.1502 0.1185 0.0407  0.0031  0.0076  55  ARG   C CA  
1477 C C   . ARG   B 49  ? 0.1813 0.1595 0.1217 0.0436  -0.0010 0.0065  55  ARG   C C   
1478 O O   . ARG   B 49  ? 0.2038 0.1790 0.1361 0.0473  0.0007  0.0092  55  ARG   C O   
1479 C CB  . ARG   B 49  ? 0.1902 0.1630 0.1280 0.0442  0.0081  0.0096  55  ARG   C CB  
1480 C CG  . ARG   B 49  ? 0.1799 0.1523 0.1251 0.0411  0.0125  0.0112  55  ARG   C CG  
1481 C CD  . ARG   B 49  ? 0.2097 0.1849 0.1611 0.0387  0.0101  0.0073  55  ARG   C CD  
1482 N NE  . ARG   B 49  ? 0.1983 0.1729 0.1568 0.0362  0.0146  0.0095  55  ARG   C NE  
1483 C CZ  . ARG   B 49  ? 0.1890 0.1664 0.1565 0.0329  0.0135  0.0079  55  ARG   C CZ  
1484 N NH1 . ARG   B 49  ? 0.1925 0.1730 0.1628 0.0317  0.0088  0.0039  55  ARG   C NH1 
1485 N NH2 . ARG   B 49  ? 0.2106 0.1878 0.1852 0.0308  0.0174  0.0105  55  ARG   C NH2 
1486 N N   . CYS   B 50  ? 0.1679 0.1502 0.1136 0.0420  -0.0063 0.0028  56  CYS   C N   
1487 C CA  . CYS   B 50  ? 0.1722 0.1565 0.1168 0.0437  -0.0105 0.0019  56  CYS   C CA  
1488 C C   . CYS   B 50  ? 0.1740 0.1629 0.1270 0.0415  -0.0156 -0.0025 56  CYS   C C   
1489 O O   . CYS   B 50  ? 0.1736 0.1640 0.1332 0.0386  -0.0155 -0.0045 56  CYS   C O   
1490 C CB  . CYS   B 50  ? 0.1645 0.1484 0.1128 0.0417  -0.0080 0.0060  56  CYS   C CB  
1491 S SG  . CYS   B 50  ? 0.1692 0.1565 0.1305 0.0354  -0.0076 0.0059  56  CYS   C SG  
1492 N N   . ASP   B 51  ? 0.1819 0.1731 0.1355 0.0431  -0.0199 -0.0038 57  ASP   C N   
1493 C CA  . ASP   B 51  ? 0.1947 0.1905 0.1584 0.0410  -0.0242 -0.0073 57  ASP   C CA  
1494 C C   . ASP   B 51  ? 0.1836 0.1812 0.1535 0.0391  -0.0236 -0.0047 57  ASP   C C   
1495 O O   . ASP   B 51  ? 0.1947 0.1958 0.1712 0.0391  -0.0273 -0.0068 57  ASP   C O   
1496 C CB  . ASP   B 51  ? 0.2298 0.2273 0.1908 0.0447  -0.0304 -0.0120 57  ASP   C CB  
1497 C CG  . ASP   B 51  ? 0.2762 0.2728 0.2291 0.0493  -0.0327 -0.0107 57  ASP   C CG  
1498 O OD1 . ASP   B 51  ? 0.2754 0.2700 0.2253 0.0496  -0.0291 -0.0060 57  ASP   C OD1 
1499 O OD2 . ASP   B 51  ? 0.3513 0.3498 0.3023 0.0525  -0.0388 -0.0148 57  ASP   C OD2 
1500 N N   . CYS   B 52  ? 0.1718 0.1671 0.1407 0.0374  -0.0189 -0.0005 58  CYS   C N   
1501 C CA  . CYS   B 52  ? 0.1576 0.1542 0.1322 0.0355  -0.0180 0.0013  58  CYS   C CA  
1502 C C   . CYS   B 52  ? 0.1524 0.1531 0.1377 0.0323  -0.0194 -0.0007 58  CYS   C C   
1503 O O   . CYS   B 52  ? 0.1558 0.1575 0.1452 0.0302  -0.0191 -0.0020 58  CYS   C O   
1504 C CB  . CYS   B 52  ? 0.1667 0.1604 0.1401 0.0334  -0.0132 0.0051  58  CYS   C CB  
1505 S SG  . CYS   B 52  ? 0.1808 0.1695 0.1446 0.0369  -0.0103 0.0086  58  CYS   C SG  
1506 N N   . GLN   B 53  ? 0.1444 0.1470 0.1345 0.0322  -0.0202 -0.0003 59  GLN   C N   
1507 C CA  . GLN   B 53  ? 0.1498 0.1556 0.1500 0.0295  -0.0201 -0.0010 59  GLN   C CA  
1508 C C   . GLN   B 53  ? 0.1413 0.1461 0.1424 0.0282  -0.0168 0.0018  59  GLN   C C   
1509 O O   . GLN   B 53  ? 0.1445 0.1516 0.1528 0.0268  -0.0162 0.0018  59  GLN   C O   
1510 C CB  . GLN   B 53  ? 0.1593 0.1688 0.1666 0.0310  -0.0244 -0.0040 59  GLN   C CB  
1511 C CG  . GLN   B 53  ? 0.2060 0.2169 0.2150 0.0315  -0.0280 -0.0079 59  GLN   C CG  
1512 C CD  . GLN   B 53  ? 0.2187 0.2338 0.2375 0.0323  -0.0326 -0.0114 59  GLN   C CD  
1513 O OE1 . GLN   B 53  ? 0.2539 0.2697 0.2697 0.0355  -0.0375 -0.0143 59  GLN   C OE1 
1514 N NE2 . GLN   B 53  ? 0.1950 0.2129 0.2257 0.0298  -0.0311 -0.0112 59  GLN   C NE2 
1515 N N   . THR   B 54  ? 0.1411 0.1423 0.1352 0.0286  -0.0143 0.0042  60  THR   C N   
1516 C CA  . THR   B 54  ? 0.1532 0.1529 0.1477 0.0270  -0.0113 0.0062  60  THR   C CA  
1517 C C   . THR   B 54  ? 0.1478 0.1445 0.1380 0.0252  -0.0086 0.0078  60  THR   C C   
1518 O O   . THR   B 54  ? 0.1532 0.1478 0.1387 0.0263  -0.0084 0.0083  60  THR   C O   
1519 C CB  . THR   B 54  ? 0.1936 0.1920 0.1865 0.0292  -0.0109 0.0072  60  THR   C CB  
1520 O OG1 . THR   B 54  ? 0.2475 0.2428 0.2337 0.0313  -0.0107 0.0085  60  THR   C OG1 
1521 C CG2 . THR   B 54  ? 0.1882 0.1899 0.1864 0.0311  -0.0138 0.0058  60  THR   C CG2 
1522 N N   . GLY   B 55  ? 0.1386 0.1349 0.1305 0.0226  -0.0067 0.0085  61  GLY   C N   
1523 C CA  . GLY   B 55  ? 0.1387 0.1328 0.1283 0.0207  -0.0049 0.0096  61  GLY   C CA  
1524 C C   . GLY   B 55  ? 0.1195 0.1135 0.1104 0.0186  -0.0037 0.0099  61  GLY   C C   
1525 O O   . GLY   B 55  ? 0.1382 0.1328 0.1304 0.0190  -0.0033 0.0095  61  GLY   C O   
1526 N N   . VAL   B 56  ? 0.1204 0.1135 0.1107 0.0165  -0.0031 0.0104  62  VAL   C N   
1527 C CA  . VAL   B 56  ? 0.1152 0.1079 0.1052 0.0148  -0.0025 0.0104  62  VAL   C CA  
1528 C C   . VAL   B 56  ? 0.1152 0.1099 0.1072 0.0129  -0.0032 0.0110  62  VAL   C C   
1529 O O   . VAL   B 56  ? 0.1241 0.1186 0.1170 0.0124  -0.0034 0.0116  62  VAL   C O   
1530 C CB  . VAL   B 56  ? 0.1277 0.1167 0.1153 0.0142  -0.0018 0.0103  62  VAL   C CB  
1531 C CG1 . VAL   B 56  ? 0.1528 0.1413 0.1393 0.0125  -0.0021 0.0095  62  VAL   C CG1 
1532 C CG2 . VAL   B 56  ? 0.1410 0.1278 0.1272 0.0163  -0.0007 0.0100  62  VAL   C CG2 
1533 N N   . TYR   B 57  ? 0.1188 0.1152 0.1114 0.0123  -0.0031 0.0113  63  TYR   C N   
1534 C CA  . TYR   B 57  ? 0.1101 0.1084 0.1046 0.0108  -0.0037 0.0124  63  TYR   C CA  
1535 C C   . TYR   B 57  ? 0.1133 0.1110 0.1048 0.0099  -0.0042 0.0126  63  TYR   C C   
1536 O O   . TYR   B 57  ? 0.1292 0.1254 0.1171 0.0106  -0.0035 0.0118  63  TYR   C O   
1537 C CB  . TYR   B 57  ? 0.1213 0.1227 0.1204 0.0111  -0.0033 0.0132  63  TYR   C CB  
1538 C CG  . TYR   B 57  ? 0.1162 0.1188 0.1155 0.0116  -0.0019 0.0141  63  TYR   C CG  
1539 C CD1 . TYR   B 57  ? 0.1291 0.1314 0.1284 0.0130  -0.0007 0.0135  63  TYR   C CD1 
1540 C CD2 . TYR   B 57  ? 0.1220 0.1259 0.1216 0.0111  -0.0015 0.0161  63  TYR   C CD2 
1541 C CE1 . TYR   B 57  ? 0.1380 0.1410 0.1377 0.0138  0.0015  0.0147  63  TYR   C CE1 
1542 C CE2 . TYR   B 57  ? 0.1316 0.1362 0.1307 0.0121  0.0006  0.0175  63  TYR   C CE2 
1543 C CZ  . TYR   B 57  ? 0.1388 0.1429 0.1382 0.0134  0.0023  0.0168  63  TYR   C CZ  
1544 O OH  . TYR   B 57  ? 0.1633 0.1677 0.1626 0.0148  0.0053  0.0185  63  TYR   C OH  
1545 N N   . TYR   B 58  ? 0.1134 0.1121 0.1062 0.0086  -0.0054 0.0136  64  TYR   C N   
1546 C CA  . TYR   B 58  ? 0.1248 0.1234 0.1145 0.0080  -0.0068 0.0137  64  TYR   C CA  
1547 C C   . TYR   B 58  ? 0.1278 0.1288 0.1172 0.0087  -0.0062 0.0157  64  TYR   C C   
1548 O O   . TYR   B 58  ? 0.1314 0.1347 0.1255 0.0084  -0.0059 0.0175  64  TYR   C O   
1549 C CB  . TYR   B 58  ? 0.1366 0.1352 0.1286 0.0063  -0.0090 0.0137  64  TYR   C CB  
1550 C CG  . TYR   B 58  ? 0.1463 0.1449 0.1346 0.0059  -0.0115 0.0131  64  TYR   C CG  
1551 C CD1 . TYR   B 58  ? 0.1559 0.1518 0.1388 0.0063  -0.0121 0.0106  64  TYR   C CD1 
1552 C CD2 . TYR   B 58  ? 0.1501 0.1512 0.1400 0.0055  -0.0135 0.0149  64  TYR   C CD2 
1553 C CE1 . TYR   B 58  ? 0.1691 0.1647 0.1474 0.0064  -0.0149 0.0094  64  TYR   C CE1 
1554 C CE2 . TYR   B 58  ? 0.1560 0.1572 0.1415 0.0056  -0.0166 0.0141  64  TYR   C CE2 
1555 C CZ  . TYR   B 58  ? 0.1676 0.1660 0.1469 0.0061  -0.0174 0.0112  64  TYR   C CZ  
1556 O OH  . TYR   B 58  ? 0.2098 0.2079 0.1832 0.0066  -0.0208 0.0098  64  TYR   C OH  
1557 N N   . CYS   B 59  ? 0.1266 0.1266 0.1103 0.0098  -0.0058 0.0155  65  CYS   C N   
1558 C CA  . CYS   B 59  ? 0.1305 0.1322 0.1124 0.0111  -0.0045 0.0179  65  CYS   C CA  
1559 C C   . CYS   B 59  ? 0.1358 0.1372 0.1116 0.0113  -0.0071 0.0181  65  CYS   C C   
1560 O O   . CYS   B 59  ? 0.1554 0.1544 0.1240 0.0121  -0.0077 0.0160  65  CYS   C O   
1561 C CB  . CYS   B 59  ? 0.1399 0.1406 0.1198 0.0128  -0.0013 0.0179  65  CYS   C CB  
1562 S SG  . CYS   B 59  ? 0.1677 0.1697 0.1451 0.0151  0.0018  0.0216  65  CYS   C SG  
1563 N N   . SER   B 60  ? 0.1496 0.1532 0.1282 0.0106  -0.0090 0.0201  66  SER   C N   
1564 C CA  A SER   B 60  ? 0.1691 0.1728 0.1424 0.0109  -0.0126 0.0199  66  SER   C CA  
1565 C CA  B SER   B 60  ? 0.1612 0.1651 0.1348 0.0109  -0.0125 0.0201  66  SER   C CA  
1566 C C   . SER   B 60  ? 0.1709 0.1740 0.1351 0.0136  -0.0114 0.0212  66  SER   C C   
1567 O O   . SER   B 60  ? 0.1958 0.1973 0.1524 0.0143  -0.0144 0.0190  66  SER   C O   
1568 C CB  A SER   B 60  ? 0.2010 0.2077 0.1803 0.0098  -0.0148 0.0221  66  SER   C CB  
1569 C CB  B SER   B 60  ? 0.1687 0.1757 0.1482 0.0101  -0.0142 0.0229  66  SER   C CB  
1570 O OG  A SER   B 60  ? 0.2407 0.2495 0.2230 0.0110  -0.0122 0.0261  66  SER   C OG  
1571 O OG  B SER   B 60  ? 0.1714 0.1790 0.1466 0.0105  -0.0185 0.0226  66  SER   C OG  
1572 N N   . SER   B 61  ? 0.1624 0.1662 0.1275 0.0153  -0.0071 0.0243  67  SER   C N   
1573 C CA  . SER   B 61  ? 0.1746 0.1773 0.1309 0.0184  -0.0047 0.0263  67  SER   C CA  
1574 C C   . SER   B 61  ? 0.1910 0.1903 0.1401 0.0196  -0.0030 0.0232  67  SER   C C   
1575 O O   . SER   B 61  ? 0.2207 0.2184 0.1608 0.0225  -0.0009 0.0244  67  SER   C O   
1576 C CB  . SER   B 61  ? 0.1855 0.1901 0.1472 0.0198  0.0003  0.0311  67  SER   C CB  
1577 O OG  . SER   B 61  ? 0.1912 0.1955 0.1597 0.0191  0.0037  0.0302  67  SER   C OG  
1578 N N   . ARG   B 62  ? 0.1757 0.1734 0.1274 0.0177  -0.0040 0.0193  68  ARG   C N   
1579 C CA  . ARG   B 62  ? 0.1816 0.1756 0.1267 0.0187  -0.0030 0.0159  68  ARG   C CA  
1580 C C   . ARG   B 62  ? 0.1931 0.1851 0.1368 0.0167  -0.0076 0.0113  68  ARG   C C   
1581 O O   . ARG   B 62  ? 0.2138 0.2024 0.1533 0.0171  -0.0071 0.0079  68  ARG   C O   
1582 C CB  . ARG   B 62  ? 0.1859 0.1795 0.1369 0.0187  0.0012  0.0160  68  ARG   C CB  
1583 C CG  . ARG   B 62  ? 0.2232 0.2185 0.1775 0.0205  0.0061  0.0201  68  ARG   C CG  
1584 C CD  . ARG   B 62  ? 0.2407 0.2336 0.1855 0.0238  0.0096  0.0209  68  ARG   C CD  
1585 N NE  . ARG   B 62  ? 0.2489 0.2433 0.1982 0.0257  0.0152  0.0253  68  ARG   C NE  
1586 C CZ  . ARG   B 62  ? 0.2739 0.2700 0.2231 0.0271  0.0168  0.0297  68  ARG   C CZ  
1587 N NH1 . ARG   B 62  ? 0.2839 0.2806 0.2273 0.0271  0.0129  0.0303  68  ARG   C NH1 
1588 N NH2 . ARG   B 62  ? 0.3126 0.3096 0.2669 0.0289  0.0227  0.0337  68  ARG   C NH2 
1589 N N   . ARG   B 63  ? 0.1963 0.1903 0.1453 0.0145  -0.0116 0.0112  69  ARG   C N   
1590 C CA  . ARG   B 63  ? 0.2114 0.2038 0.1629 0.0122  -0.0154 0.0073  69  ARG   C CA  
1591 C C   . ARG   B 63  ? 0.2249 0.2146 0.1793 0.0115  -0.0129 0.0051  69  ARG   C C   
1592 O O   . ARG   B 63  ? 0.2500 0.2364 0.2018 0.0111  -0.0142 0.0013  69  ARG   C O   
1593 C CB  . ARG   B 63  ? 0.2443 0.2348 0.1874 0.0129  -0.0197 0.0039  69  ARG   C CB  
1594 C CG  . ARG   B 63  ? 0.2745 0.2678 0.2142 0.0139  -0.0231 0.0059  69  ARG   C CG  
1595 C CD  . ARG   B 63  ? 0.3342 0.3305 0.2837 0.0113  -0.0265 0.0069  69  ARG   C CD  
1596 N NE  . ARG   B 63  ? 0.3666 0.3651 0.3128 0.0121  -0.0315 0.0073  69  ARG   C NE  
1597 C CZ  . ARG   B 63  ? 0.3817 0.3835 0.3283 0.0134  -0.0314 0.0120  69  ARG   C CZ  
1598 N NH1 . ARG   B 63  ? 0.3755 0.3786 0.3262 0.0138  -0.0263 0.0162  69  ARG   C NH1 
1599 N NH2 . ARG   B 63  ? 0.3884 0.3922 0.3318 0.0144  -0.0366 0.0123  69  ARG   C NH2 
1600 N N   . LYS   B 64  ? 0.1849 0.1759 0.1448 0.0116  -0.0095 0.0074  70  LYS   C N   
1601 C CA  . LYS   B 64  ? 0.1896 0.1783 0.1516 0.0116  -0.0071 0.0059  70  LYS   C CA  
1602 C C   . LYS   B 64  ? 0.1661 0.1568 0.1361 0.0108  -0.0061 0.0078  70  LYS   C C   
1603 O O   . LYS   B 64  ? 0.1760 0.1698 0.1494 0.0108  -0.0056 0.0104  70  LYS   C O   
1604 C CB  . LYS   B 64  ? 0.2429 0.2306 0.2008 0.0140  -0.0033 0.0064  70  LYS   C CB  
1605 C CG  . LYS   B 64  ? 0.3907 0.3745 0.3403 0.0154  -0.0030 0.0033  70  LYS   C CG  
1606 C CD  . LYS   B 64  ? 0.4862 0.4681 0.4363 0.0170  0.0012  0.0030  70  LYS   C CD  
1607 C CE  . LYS   B 64  ? 0.5809 0.5593 0.5218 0.0191  0.0029  0.0007  70  LYS   C CE  
1608 N NZ  . LYS   B 64  ? 0.6424 0.6218 0.5758 0.0207  0.0028  0.0023  70  LYS   C NZ  
1609 N N   . HIS   B 65  ? 0.1544 0.1430 0.1269 0.0104  -0.0055 0.0064  71  HIS   C N   
1610 C CA  . HIS   B 65  ? 0.1498 0.1395 0.1278 0.0104  -0.0043 0.0077  71  HIS   C CA  
1611 C C   . HIS   B 65  ? 0.1750 0.1642 0.1526 0.0123  -0.0018 0.0077  71  HIS   C C   
1612 O O   . HIS   B 65  ? 0.2188 0.2050 0.1935 0.0131  -0.0007 0.0060  71  HIS   C O   
1613 C CB  . HIS   B 65  ? 0.1606 0.1481 0.1413 0.0094  -0.0050 0.0068  71  HIS   C CB  
1614 C CG  . HIS   B 65  ? 0.1470 0.1352 0.1304 0.0074  -0.0073 0.0070  71  HIS   C CG  
1615 N ND1 . HIS   B 65  ? 0.1799 0.1701 0.1679 0.0068  -0.0073 0.0089  71  HIS   C ND1 
1616 C CD2 . HIS   B 65  ? 0.1503 0.1376 0.1327 0.0062  -0.0098 0.0053  71  HIS   C CD2 
1617 C CE1 . HIS   B 65  ? 0.1546 0.1450 0.1452 0.0051  -0.0094 0.0087  71  HIS   C CE1 
1618 N NE2 . HIS   B 65  ? 0.1927 0.1817 0.1804 0.0046  -0.0113 0.0064  71  HIS   C NE2 
1619 N N   . TYR   B 66  ? 0.1491 0.1411 0.1306 0.0130  -0.0008 0.0094  72  TYR   C N   
1620 C CA  . TYR   B 66  ? 0.1350 0.1272 0.1181 0.0148  0.0013  0.0094  72  TYR   C CA  
1621 C C   . TYR   B 66  ? 0.1393 0.1323 0.1264 0.0154  0.0007  0.0095  72  TYR   C C   
1622 O O   . TYR   B 66  ? 0.1318 0.1268 0.1219 0.0148  -0.0006 0.0102  72  TYR   C O   
1623 C CB  . TYR   B 66  ? 0.1436 0.1388 0.1294 0.0155  0.0028  0.0112  72  TYR   C CB  
1624 C CG  . TYR   B 66  ? 0.1613 0.1558 0.1419 0.0160  0.0043  0.0117  72  TYR   C CG  
1625 C CD1 . TYR   B 66  ? 0.1952 0.1874 0.1720 0.0176  0.0068  0.0110  72  TYR   C CD1 
1626 C CD2 . TYR   B 66  ? 0.1693 0.1651 0.1484 0.0153  0.0034  0.0133  72  TYR   C CD2 
1627 C CE1 . TYR   B 66  ? 0.2059 0.1969 0.1763 0.0187  0.0084  0.0115  72  TYR   C CE1 
1628 C CE2 . TYR   B 66  ? 0.1877 0.1827 0.1606 0.0164  0.0046  0.0141  72  TYR   C CE2 
1629 C CZ  . TYR   B 66  ? 0.1927 0.1852 0.1607 0.0182  0.0072  0.0131  72  TYR   C CZ  
1630 O OH  . TYR   B 66  ? 0.2311 0.2225 0.1916 0.0198  0.0087  0.0141  72  TYR   C OH  
1631 N N   . PRO   B 67  ? 0.1384 0.1298 0.1256 0.0169  0.0015  0.0088  73  PRO   C N   
1632 C CA  . PRO   B 67  ? 0.1379 0.1304 0.1283 0.0183  0.0005  0.0091  73  PRO   C CA  
1633 C C   . PRO   B 67  ? 0.1404 0.1367 0.1363 0.0191  0.0004  0.0094  73  PRO   C C   
1634 O O   . PRO   B 67  ? 0.1729 0.1699 0.1707 0.0197  0.0024  0.0096  73  PRO   C O   
1635 C CB  . PRO   B 67  ? 0.1625 0.1520 0.1514 0.0199  0.0016  0.0086  73  PRO   C CB  
1636 C CG  . PRO   B 67  ? 0.2003 0.1882 0.1870 0.0197  0.0037  0.0078  73  PRO   C CG  
1637 C CD  . PRO   B 67  ? 0.1593 0.1477 0.1433 0.0178  0.0033  0.0078  73  PRO   C CD  
1638 N N   . VAL   B 68  ? 0.1258 0.1242 0.1247 0.0193  -0.0015 0.0092  74  VAL   C N   
1639 C CA  . VAL   B 68  ? 0.1316 0.1338 0.1376 0.0197  -0.0022 0.0090  74  VAL   C CA  
1640 C C   . VAL   B 68  ? 0.1326 0.1360 0.1406 0.0213  -0.0051 0.0077  74  VAL   C C   
1641 O O   . VAL   B 68  ? 0.1349 0.1368 0.1385 0.0217  -0.0064 0.0074  74  VAL   C O   
1642 C CB  . VAL   B 68  ? 0.1562 0.1603 0.1650 0.0179  -0.0019 0.0096  74  VAL   C CB  
1643 C CG1 . VAL   B 68  ? 0.1794 0.1829 0.1865 0.0172  0.0009  0.0112  74  VAL   C CG1 
1644 C CG2 . VAL   B 68  ? 0.1661 0.1693 0.1717 0.0168  -0.0034 0.0095  74  VAL   C CG2 
1645 N N   . SER   B 69  ? 0.1218 0.1284 0.1373 0.0222  -0.0061 0.0068  75  SER   C N   
1646 C CA  . SER   B 69  ? 0.1277 0.1366 0.1469 0.0234  -0.0098 0.0048  75  SER   C CA  
1647 C C   . SER   B 69  ? 0.1180 0.1291 0.1426 0.0217  -0.0102 0.0041  75  SER   C C   
1648 O O   . SER   B 69  ? 0.1255 0.1377 0.1549 0.0203  -0.0075 0.0054  75  SER   C O   
1649 C CB  . SER   B 69  ? 0.1583 0.1698 0.1848 0.0253  -0.0112 0.0039  75  SER   C CB  
1650 O OG  . SER   B 69  ? 0.2187 0.2281 0.2406 0.0271  -0.0106 0.0048  75  SER   C OG  
1651 N N   . PHE   B 70  ? 0.1160 0.1274 0.1396 0.0220  -0.0129 0.0022  76  PHE   C N   
1652 C CA  . PHE   B 70  ? 0.1129 0.1258 0.1419 0.0204  -0.0131 0.0013  76  PHE   C CA  
1653 C C   . PHE   B 70  ? 0.1158 0.1306 0.1486 0.0217  -0.0173 -0.0024 76  PHE   C C   
1654 O O   . PHE   B 70  ? 0.1309 0.1448 0.1582 0.0240  -0.0202 -0.0039 76  PHE   C O   
1655 C CB  . PHE   B 70  ? 0.1223 0.1330 0.1455 0.0187  -0.0112 0.0029  76  PHE   C CB  
1656 C CG  . PHE   B 70  ? 0.1227 0.1305 0.1367 0.0199  -0.0121 0.0027  76  PHE   C CG  
1657 C CD1 . PHE   B 70  ? 0.1296 0.1347 0.1368 0.0203  -0.0106 0.0045  76  PHE   C CD1 
1658 C CD2 . PHE   B 70  ? 0.1332 0.1407 0.1457 0.0208  -0.0140 0.0006  76  PHE   C CD2 
1659 C CE1 . PHE   B 70  ? 0.1317 0.1339 0.1317 0.0216  -0.0106 0.0048  76  PHE   C CE1 
1660 C CE2 . PHE   B 70  ? 0.1404 0.1449 0.1443 0.0222  -0.0137 0.0010  76  PHE   C CE2 
1661 C CZ  . PHE   B 70  ? 0.1371 0.1390 0.1352 0.0227  -0.0120 0.0033  76  PHE   C CZ  
1662 N N   . SER   B 71  ? 0.1071 0.1241 0.1492 0.0204  -0.0176 -0.0038 77  SER   C N   
1663 C CA  . SER   B 71  ? 0.1230 0.1420 0.1708 0.0214  -0.0220 -0.0082 77  SER   C CA  
1664 C C   . SER   B 71  ? 0.1359 0.1527 0.1761 0.0222  -0.0238 -0.0104 77  SER   C C   
1665 O O   . SER   B 71  ? 0.1560 0.1701 0.1883 0.0215  -0.0212 -0.0081 77  SER   C O   
1666 C CB  . SER   B 71  ? 0.1340 0.1561 0.1966 0.0197  -0.0214 -0.0091 77  SER   C CB  
1667 O OG  . SER   B 71  ? 0.1572 0.1784 0.2217 0.0175  -0.0180 -0.0072 77  SER   C OG  
1668 N N   . LYS   B 72  ? 0.1598 0.1779 0.2028 0.0236  -0.0284 -0.0150 78  LYS   C N   
1669 C CA  . LYS   B 72  ? 0.1625 0.1782 0.1979 0.0248  -0.0300 -0.0177 78  LYS   C CA  
1670 C C   . LYS   B 72  ? 0.1612 0.1768 0.2031 0.0222  -0.0276 -0.0180 78  LYS   C C   
1671 O O   . LYS   B 72  ? 0.1735 0.1916 0.2279 0.0202  -0.0268 -0.0181 78  LYS   C O   
1672 C CB  . LYS   B 72  ? 0.2130 0.2300 0.2490 0.0276  -0.0363 -0.0233 78  LYS   C CB  
1673 C CG  . LYS   B 72  ? 0.2524 0.2698 0.2822 0.0306  -0.0390 -0.0227 78  LYS   C CG  
1674 C CD  . LYS   B 72  ? 0.4114 0.4284 0.4339 0.0346  -0.0451 -0.0275 78  LYS   C CD  
1675 C CE  . LYS   B 72  ? 0.5291 0.5445 0.5399 0.0382  -0.0459 -0.0249 78  LYS   C CE  
1676 N NZ  . LYS   B 72  ? 0.5934 0.6068 0.5918 0.0428  -0.0501 -0.0280 78  LYS   C NZ  
1677 N N   . PRO   B 73  ? 0.1551 0.1677 0.1895 0.0223  -0.0259 -0.0178 79  PRO   C N   
1678 C CA  . PRO   B 73  ? 0.1585 0.1709 0.1997 0.0199  -0.0232 -0.0175 79  PRO   C CA  
1679 C C   . PRO   B 73  ? 0.1630 0.1774 0.2157 0.0195  -0.0262 -0.0226 79  PRO   C C   
1680 O O   . PRO   B 73  ? 0.1974 0.2116 0.2477 0.0218  -0.0309 -0.0279 79  PRO   C O   
1681 C CB  . PRO   B 73  ? 0.1881 0.1969 0.2188 0.0211  -0.0217 -0.0174 79  PRO   C CB  
1682 C CG  . PRO   B 73  ? 0.2350 0.2419 0.2537 0.0232  -0.0217 -0.0153 79  PRO   C CG  
1683 C CD  . PRO   B 73  ? 0.1850 0.1941 0.2052 0.0248  -0.0256 -0.0170 79  PRO   C CD  
1684 N N   A SER   B 74  ? 0.1537 0.1700 0.2194 0.0169  -0.0239 -0.0211 80  SER   C N   
1685 N N   B SER   B 74  ? 0.1556 0.1720 0.2214 0.0169  -0.0238 -0.0211 80  SER   C N   
1686 C CA  A SER   B 74  ? 0.1553 0.1738 0.2351 0.0162  -0.0263 -0.0256 80  SER   C CA  
1687 C CA  B SER   B 74  ? 0.1611 0.1794 0.2406 0.0162  -0.0263 -0.0257 80  SER   C CA  
1688 C C   A SER   B 74  ? 0.1487 0.1675 0.2399 0.0136  -0.0220 -0.0232 80  SER   C C   
1689 C C   B SER   B 74  ? 0.1490 0.1678 0.2405 0.0135  -0.0219 -0.0230 80  SER   C C   
1690 O O   A SER   B 74  ? 0.1475 0.1651 0.2347 0.0125  -0.0176 -0.0179 80  SER   C O   
1691 O O   B SER   B 74  ? 0.1428 0.1609 0.2313 0.0124  -0.0174 -0.0174 80  SER   C O   
1692 C CB  A SER   B 74  ? 0.1711 0.1930 0.2596 0.0164  -0.0285 -0.0262 80  SER   C CB  
1693 C CB  B SER   B 74  ? 0.1871 0.2087 0.2745 0.0168  -0.0295 -0.0274 80  SER   C CB  
1694 O OG  A SER   B 74  ? 0.1911 0.2129 0.2696 0.0190  -0.0322 -0.0275 80  SER   C OG  
1695 O OG  B SER   B 74  ? 0.2056 0.2289 0.2992 0.0152  -0.0253 -0.0220 80  SER   C OG  
1696 N N   . LEU   B 75  ? 0.1527 0.1729 0.2584 0.0126  -0.0234 -0.0271 81  LEU   C N   
1697 C CA  . LEU   B 75  ? 0.1593 0.1800 0.2784 0.0104  -0.0193 -0.0249 81  LEU   C CA  
1698 C C   . LEU   B 75  ? 0.1602 0.1838 0.2907 0.0093  -0.0168 -0.0210 81  LEU   C C   
1699 O O   . LEU   B 75  ? 0.1892 0.2152 0.3297 0.0095  -0.0199 -0.0246 81  LEU   C O   
1700 C CB  . LEU   B 75  ? 0.1797 0.1999 0.3093 0.0101  -0.0222 -0.0318 81  LEU   C CB  
1701 C CG  . LEU   B 75  ? 0.2125 0.2326 0.3567 0.0080  -0.0178 -0.0300 81  LEU   C CG  
1702 C CD1 . LEU   B 75  ? 0.2097 0.2270 0.3456 0.0077  -0.0138 -0.0260 81  LEU   C CD1 
1703 C CD2 . LEU   B 75  ? 0.2447 0.2646 0.4018 0.0076  -0.0215 -0.0379 81  LEU   C CD2 
1704 N N   . ILE   B 76  ? 0.1763 0.1997 0.3053 0.0085  -0.0114 -0.0140 82  ILE   C N   
1705 C CA  . ILE   B 76  ? 0.1938 0.2193 0.3300 0.0081  -0.0079 -0.0094 82  ILE   C CA  
1706 C C   . ILE   B 76  ? 0.1877 0.2132 0.3342 0.0068  -0.0022 -0.0045 82  ILE   C C   
1707 O O   . ILE   B 76  ? 0.1719 0.1956 0.3124 0.0065  0.0001  -0.0015 82  ILE   C O   
1708 C CB  . ILE   B 76  ? 0.2271 0.2518 0.3480 0.0091  -0.0067 -0.0052 82  ILE   C CB  
1709 C CG1 . ILE   B 76  ? 0.2760 0.3003 0.3860 0.0107  -0.0119 -0.0094 82  ILE   C CG1 
1710 C CG2 . ILE   B 76  ? 0.2556 0.2817 0.3808 0.0091  -0.0023 0.0001  82  ILE   C CG2 
1711 C CD1 . ILE   B 76  ? 0.3014 0.3280 0.4148 0.0118  -0.0139 -0.0103 82  ILE   C CD1 
1712 N N   . PHE   B 77  ? 0.1782 0.2058 0.3399 0.0063  0.0007  -0.0027 83  PHE   C N   
1713 C CA  . PHE   B 77  ? 0.1760 0.2033 0.3466 0.0057  0.0070  0.0032  83  PHE   C CA  
1714 C C   . PHE   B 77  ? 0.1876 0.2144 0.3463 0.0068  0.0111  0.0103  83  PHE   C C   
1715 O O   . PHE   B 77  ? 0.2181 0.2458 0.3736 0.0077  0.0115  0.0114  83  PHE   C O   
1716 C CB  . PHE   B 77  ? 0.1719 0.2014 0.3640 0.0051  0.0094  0.0030  83  PHE   C CB  
1717 C CG  . PHE   B 77  ? 0.1891 0.2178 0.3918 0.0046  0.0160  0.0089  83  PHE   C CG  
1718 C CD1 . PHE   B 77  ? 0.1995 0.2268 0.4081 0.0036  0.0161  0.0073  83  PHE   C CD1 
1719 C CD2 . PHE   B 77  ? 0.2057 0.2347 0.4104 0.0056  0.0227  0.0165  83  PHE   C CD2 
1720 C CE1 . PHE   B 77  ? 0.2255 0.2520 0.4436 0.0035  0.0225  0.0134  83  PHE   C CE1 
1721 C CE2 . PHE   B 77  ? 0.2173 0.2454 0.4306 0.0057  0.0291  0.0227  83  PHE   C CE2 
1722 C CZ  . PHE   B 77  ? 0.2165 0.2435 0.4373 0.0046  0.0289  0.0211  83  PHE   C CZ  
1723 N N   . VAL   B 78  ? 0.1510 0.1762 0.3029 0.0068  0.0140  0.0150  84  VAL   C N   
1724 C CA  . VAL   B 78  ? 0.1549 0.1793 0.2943 0.0080  0.0171  0.0212  84  VAL   C CA  
1725 C C   . VAL   B 78  ? 0.1475 0.1720 0.2956 0.0085  0.0236  0.0280  84  VAL   C C   
1726 O O   . VAL   B 78  ? 0.1512 0.1754 0.3078 0.0079  0.0251  0.0289  84  VAL   C O   
1727 C CB  . VAL   B 78  ? 0.1701 0.1929 0.2948 0.0078  0.0145  0.0210  84  VAL   C CB  
1728 C CG1 . VAL   B 78  ? 0.1737 0.1958 0.2856 0.0090  0.0167  0.0265  84  VAL   C CG1 
1729 C CG2 . VAL   B 78  ? 0.1936 0.2159 0.3105 0.0076  0.0089  0.0147  84  VAL   C CG2 
1730 N N   . GLU   B 79  ? 0.1480 0.1726 0.2927 0.0101  0.0278  0.0331  85  GLU   C N   
1731 C CA  . GLU   B 79  ? 0.1525 0.1767 0.3027 0.0114  0.0345  0.0404  85  GLU   C CA  
1732 C C   . GLU   B 79  ? 0.1492 0.1722 0.2891 0.0121  0.0349  0.0446  85  GLU   C C   
1733 O O   . GLU   B 79  ? 0.1455 0.1680 0.2726 0.0116  0.0304  0.0423  85  GLU   C O   
1734 C CB  . GLU   B 79  ? 0.1815 0.2056 0.3287 0.0135  0.0392  0.0448  85  GLU   C CB  
1735 C CG  . GLU   B 79  ? 0.2373 0.2631 0.3991 0.0131  0.0401  0.0420  85  GLU   C CG  
1736 C CD  . GLU   B 79  ? 0.2845 0.3114 0.4686 0.0120  0.0429  0.0420  85  GLU   C CD  
1737 O OE1 . GLU   B 79  ? 0.3286 0.3545 0.5182 0.0127  0.0481  0.0476  85  GLU   C OE1 
1738 O OE2 . GLU   B 79  ? 0.3315 0.3600 0.5284 0.0105  0.0398  0.0362  85  GLU   C OE2 
1739 N N   . ALA   B 80  ? 0.1608 0.1835 0.3073 0.0133  0.0403  0.0509  86  ALA   C N   
1740 C CA  . ALA   B 80  ? 0.1752 0.1971 0.3134 0.0142  0.0406  0.0554  86  ALA   C CA  
1741 C C   . ALA   B 80  ? 0.1866 0.2079 0.3048 0.0158  0.0386  0.0572  86  ALA   C C   
1742 O O   . ALA   B 80  ? 0.2109 0.2318 0.3226 0.0172  0.0403  0.0583  86  ALA   C O   
1743 C CB  . ALA   B 80  ? 0.1878 0.2094 0.3355 0.0162  0.0476  0.0632  86  ALA   C CB  
1744 N N   . SER   B 81  ? 0.1731 0.1943 0.2826 0.0153  0.0347  0.0567  87  SER   C N   
1745 C CA  . SER   B 81  ? 0.1805 0.2012 0.2728 0.0166  0.0324  0.0582  87  SER   C CA  
1746 C C   . SER   B 81  ? 0.1874 0.2082 0.2764 0.0182  0.0333  0.0641  87  SER   C C   
1747 O O   . SER   B 81  ? 0.1988 0.2200 0.2994 0.0184  0.0363  0.0673  87  SER   C O   
1748 C CB  . SER   B 81  ? 0.1728 0.1934 0.2576 0.0146  0.0262  0.0519  87  SER   C CB  
1749 O OG  . SER   B 81  ? 0.1705 0.1914 0.2598 0.0131  0.0241  0.0507  87  SER   C OG  
1750 N N   . GLU   B 82  ? 0.2029 0.2235 0.2771 0.0194  0.0302  0.0652  88  GLU   C N   
1751 C CA  . GLU   B 82  ? 0.2269 0.2481 0.2983 0.0211  0.0301  0.0707  88  GLU   C CA  
1752 C C   . GLU   B 82  ? 0.2147 0.2369 0.2940 0.0189  0.0273  0.0688  88  GLU   C C   
1753 O O   . GLU   B 82  ? 0.2280 0.2509 0.3102 0.0202  0.0282  0.0737  88  GLU   C O   
1754 C CB  . GLU   B 82  ? 0.3063 0.3272 0.3604 0.0230  0.0269  0.0719  88  GLU   C CB  
1755 C CG  . GLU   B 82  ? 0.4143 0.4357 0.4613 0.0210  0.0203  0.0669  88  GLU   C CG  
1756 C CD  . GLU   B 82  ? 0.4857 0.5070 0.5176 0.0231  0.0170  0.0685  88  GLU   C CD  
1757 O OE1 . GLU   B 82  ? 0.5026 0.5227 0.5260 0.0259  0.0195  0.0713  88  GLU   C OE1 
1758 O OE2 . GLU   B 82  ? 0.4862 0.5084 0.5149 0.0220  0.0118  0.0667  88  GLU   C OE2 
1759 N N   . TYR   B 83  ? 0.1812 0.2032 0.2642 0.0161  0.0245  0.0622  89  TYR   C N   
1760 C CA  . TYR   B 83  ? 0.1694 0.1918 0.2581 0.0143  0.0221  0.0601  89  TYR   C CA  
1761 C C   . TYR   B 83  ? 0.1846 0.2065 0.2873 0.0124  0.0237  0.0561  89  TYR   C C   
1762 O O   . TYR   B 83  ? 0.1943 0.2161 0.3025 0.0114  0.0227  0.0548  89  TYR   C O   
1763 C CB  . TYR   B 83  ? 0.1645 0.1869 0.2430 0.0130  0.0168  0.0559  89  TYR   C CB  
1764 C CG  . TYR   B 83  ? 0.1583 0.1797 0.2304 0.0121  0.0151  0.0508  89  TYR   C CG  
1765 C CD1 . TYR   B 83  ? 0.1679 0.1889 0.2292 0.0134  0.0147  0.0517  89  TYR   C CD1 
1766 C CD2 . TYR   B 83  ? 0.1554 0.1761 0.2319 0.0103  0.0141  0.0450  89  TYR   C CD2 
1767 C CE1 . TYR   B 83  ? 0.1639 0.1839 0.2201 0.0127  0.0134  0.0472  89  TYR   C CE1 
1768 C CE2 . TYR   B 83  ? 0.1637 0.1836 0.2347 0.0099  0.0125  0.0408  89  TYR   C CE2 
1769 C CZ  . TYR   B 83  ? 0.1574 0.1769 0.2188 0.0110  0.0124  0.0421  89  TYR   C CZ  
1770 O OH  . TYR   B 83  ? 0.1713 0.1900 0.2281 0.0108  0.0113  0.0384  89  TYR   C OH  
1771 N N   . TYR   B 84  ? 0.1571 0.1786 0.2663 0.0121  0.0259  0.0539  90  TYR   C N   
1772 C CA  . TYR   B 84  ? 0.1526 0.1736 0.2762 0.0105  0.0271  0.0501  90  TYR   C CA  
1773 C C   . TYR   B 84  ? 0.1513 0.1724 0.2856 0.0113  0.0318  0.0524  90  TYR   C C   
1774 O O   . TYR   B 84  ? 0.1616 0.1830 0.2904 0.0125  0.0334  0.0546  90  TYR   C O   
1775 C CB  . TYR   B 84  ? 0.1385 0.1590 0.2595 0.0088  0.0229  0.0419  90  TYR   C CB  
1776 C CG  . TYR   B 84  ? 0.1299 0.1497 0.2439 0.0079  0.0191  0.0387  90  TYR   C CG  
1777 C CD1 . TYR   B 84  ? 0.1379 0.1572 0.2584 0.0074  0.0196  0.0387  90  TYR   C CD1 
1778 C CD2 . TYR   B 84  ? 0.1304 0.1500 0.2324 0.0077  0.0156  0.0357  90  TYR   C CD2 
1779 C CE1 . TYR   B 84  ? 0.1459 0.1645 0.2606 0.0068  0.0169  0.0360  90  TYR   C CE1 
1780 C CE2 . TYR   B 84  ? 0.1345 0.1533 0.2309 0.0070  0.0129  0.0332  90  TYR   C CE2 
1781 C CZ  . TYR   B 84  ? 0.1357 0.1539 0.2386 0.0066  0.0137  0.0333  90  TYR   C CZ  
1782 O OH  . TYR   B 84  ? 0.1321 0.1493 0.2303 0.0062  0.0118  0.0309  90  TYR   C OH  
1783 N N   . PRO   B 85  ? 0.1544 0.1753 0.3051 0.0104  0.0344  0.0516  91  PRO   C N   
1784 C CA  . PRO   B 85  ? 0.1471 0.1682 0.3106 0.0107  0.0386  0.0527  91  PRO   C CA  
1785 C C   . PRO   B 85  ? 0.1537 0.1753 0.3174 0.0093  0.0353  0.0455  91  PRO   C C   
1786 O O   . PRO   B 85  ? 0.1448 0.1663 0.2995 0.0083  0.0299  0.0397  91  PRO   C O   
1787 C CB  . PRO   B 85  ? 0.1609 0.1814 0.3421 0.0097  0.0411  0.0522  91  PRO   C CB  
1788 C CG  . PRO   B 85  ? 0.1660 0.1858 0.3434 0.0081  0.0362  0.0463  91  PRO   C CG  
1789 C CD  . PRO   B 85  ? 0.1618 0.1819 0.3204 0.0090  0.0331  0.0483  91  PRO   C CD  
1790 N N   . ALA   B 86  ? 0.1401 0.1622 0.3154 0.0094  0.0385  0.0459  92  ALA   C N   
1791 C CA  . ALA   B 86  ? 0.1551 0.1781 0.3346 0.0082  0.0353  0.0391  92  ALA   C CA  
1792 C C   . ALA   B 86  ? 0.1694 0.1921 0.3568 0.0062  0.0309  0.0314  92  ALA   C C   
1793 O O   . ALA   B 86  ? 0.1917 0.2137 0.3914 0.0055  0.0330  0.0319  92  ALA   C O   
1794 C CB  . ALA   B 86  ? 0.1599 0.1838 0.3544 0.0087  0.0403  0.0415  92  ALA   C CB  
1795 N N   . ARG   B 87  ? 0.1703 0.1931 0.3488 0.0055  0.0249  0.0247  93  ARG   C N   
1796 C CA  . ARG   B 87  ? 0.1640 0.1860 0.3460 0.0042  0.0205  0.0173  93  ARG   C CA  
1797 C C   . ARG   B 87  ? 0.1595 0.1819 0.3323 0.0042  0.0145  0.0107  93  ARG   C C   
1798 O O   . ARG   B 87  ? 0.1540 0.1771 0.3163 0.0051  0.0138  0.0123  93  ARG   C O   
1799 C CB  . ARG   B 87  ? 0.1774 0.1977 0.3512 0.0043  0.0205  0.0189  93  ARG   C CB  
1800 C CG  . ARG   B 87  ? 0.1557 0.1757 0.3098 0.0050  0.0177  0.0197  93  ARG   C CG  
1801 C CD  . ARG   B 87  ? 0.1549 0.1737 0.3028 0.0052  0.0182  0.0222  93  ARG   C CD  
1802 N NE  . ARG   B 87  ? 0.1636 0.1820 0.2950 0.0055  0.0148  0.0211  93  ARG   C NE  
1803 C CZ  . ARG   B 87  ? 0.1679 0.1849 0.2927 0.0054  0.0129  0.0189  93  ARG   C CZ  
1804 N NH1 . ARG   B 87  ? 0.1851 0.2010 0.3174 0.0050  0.0138  0.0175  93  ARG   C NH1 
1805 N NH2 . ARG   B 87  ? 0.1808 0.1974 0.2922 0.0057  0.0103  0.0180  93  ARG   C NH2 
1806 N N   . TYR   B 88  ? 0.1756 0.1972 0.3511 0.0036  0.0103  0.0033  94  TYR   C N   
1807 C CA  . TYR   B 88  ? 0.1948 0.2163 0.3592 0.0042  0.0044  -0.0026 94  TYR   C CA  
1808 C C   . TYR   B 88  ? 0.1696 0.1890 0.3166 0.0048  0.0035  -0.0016 94  TYR   C C   
1809 O O   . TYR   B 88  ? 0.1836 0.2014 0.3308 0.0045  0.0048  -0.0012 94  TYR   C O   
1810 C CB  . TYR   B 88  ? 0.2174 0.2385 0.3904 0.0038  0.0000  -0.0113 94  TYR   C CB  
1811 C CG  . TYR   B 88  ? 0.2409 0.2644 0.4302 0.0032  -0.0009 -0.0138 94  TYR   C CG  
1812 C CD1 . TYR   B 88  ? 0.2466 0.2720 0.4328 0.0040  -0.0045 -0.0161 94  TYR   C CD1 
1813 C CD2 . TYR   B 88  ? 0.2451 0.2690 0.4543 0.0019  0.0024  -0.0133 94  TYR   C CD2 
1814 C CE1 . TYR   B 88  ? 0.2558 0.2838 0.4586 0.0035  -0.0051 -0.0180 94  TYR   C CE1 
1815 C CE2 . TYR   B 88  ? 0.2491 0.2754 0.4753 0.0013  0.0022  -0.0152 94  TYR   C CE2 
1816 C CZ  . TYR   B 88  ? 0.2583 0.2868 0.4816 0.0020  -0.0018 -0.0177 94  TYR   C CZ  
1817 O OH  . TYR   B 88  ? 0.2847 0.3158 0.5273 0.0013  -0.0019 -0.0194 94  TYR   C OH  
1818 N N   . GLN   B 89  ? 0.1486 0.1682 0.2817 0.0058  0.0014  -0.0012 95  GLN   C N   
1819 C CA  . GLN   B 89  ? 0.1446 0.1623 0.2623 0.0064  0.0003  -0.0007 95  GLN   C CA  
1820 C C   . GLN   B 89  ? 0.1364 0.1533 0.2462 0.0075  -0.0046 -0.0070 95  GLN   C C   
1821 O O   . GLN   B 89  ? 0.1504 0.1688 0.2610 0.0081  -0.0070 -0.0090 95  GLN   C O   
1822 C CB  . GLN   B 89  ? 0.1508 0.1689 0.2593 0.0066  0.0025  0.0054  95  GLN   C CB  
1823 C CG  . GLN   B 89  ? 0.1630 0.1795 0.2579 0.0070  0.0015  0.0062  95  GLN   C CG  
1824 C CD  . GLN   B 89  ? 0.1516 0.1683 0.2400 0.0070  0.0037  0.0122  95  GLN   C CD  
1825 O OE1 . GLN   B 89  ? 0.1535 0.1713 0.2473 0.0067  0.0067  0.0168  95  GLN   C OE1 
1826 N NE2 . GLN   B 89  ? 0.1475 0.1633 0.2243 0.0074  0.0021  0.0122  95  GLN   C NE2 
1827 N N   . SER   B 90  ? 0.1323 0.1469 0.2347 0.0082  -0.0059 -0.0097 96  SER   C N   
1828 C CA  . SER   B 90  ? 0.1306 0.1439 0.2240 0.0100  -0.0101 -0.0153 96  SER   C CA  
1829 C C   . SER   B 90  ? 0.1322 0.1444 0.2103 0.0111  -0.0103 -0.0127 96  SER   C C   
1830 O O   . SER   B 90  ? 0.1276 0.1395 0.2019 0.0104  -0.0073 -0.0075 96  SER   C O   
1831 C CB  . SER   B 90  ? 0.1567 0.1675 0.2507 0.0106  -0.0111 -0.0204 96  SER   C CB  
1832 O OG  . SER   B 90  ? 0.1703 0.1792 0.2586 0.0105  -0.0078 -0.0169 96  SER   C OG  
1833 N N   . HIS   B 91  ? 0.1329 0.1443 0.2027 0.0131  -0.0140 -0.0166 97  HIS   C N   
1834 C CA  . HIS   B 91  ? 0.1332 0.1430 0.1891 0.0146  -0.0140 -0.0145 97  HIS   C CA  
1835 C C   . HIS   B 91  ? 0.1297 0.1409 0.1844 0.0134  -0.0120 -0.0091 97  HIS   C C   
1836 O O   . HIS   B 91  ? 0.1447 0.1545 0.1911 0.0135  -0.0102 -0.0057 97  HIS   C O   
1837 C CB  . HIS   B 91  ? 0.1424 0.1491 0.1904 0.0152  -0.0118 -0.0137 97  HIS   C CB  
1838 C CG  . HIS   B 91  ? 0.1660 0.1705 0.2125 0.0169  -0.0134 -0.0193 97  HIS   C CG  
1839 N ND1 . HIS   B 91  ? 0.2037 0.2058 0.2383 0.0200  -0.0156 -0.0222 97  HIS   C ND1 
1840 C CD2 . HIS   B 91  ? 0.1809 0.1851 0.2360 0.0163  -0.0132 -0.0225 97  HIS   C CD2 
1841 C CE1 . HIS   B 91  ? 0.2120 0.2123 0.2471 0.0213  -0.0167 -0.0274 97  HIS   C CE1 
1842 N NE2 . HIS   B 91  ? 0.2062 0.2076 0.2540 0.0189  -0.0154 -0.0280 97  HIS   C NE2 
1843 N N   . LEU   B 92  ? 0.1164 0.1302 0.1795 0.0127  -0.0123 -0.0086 98  LEU   C N   
1844 C CA  . LEU   B 92  ? 0.1215 0.1364 0.1840 0.0118  -0.0099 -0.0038 98  LEU   C CA  
1845 C C   . LEU   B 92  ? 0.1225 0.1382 0.1818 0.0132  -0.0122 -0.0050 98  LEU   C C   
1846 O O   . LEU   B 92  ? 0.1258 0.1429 0.1900 0.0141  -0.0154 -0.0090 98  LEU   C O   
1847 C CB  . LEU   B 92  ? 0.1272 0.1442 0.2023 0.0103  -0.0072 -0.0013 98  LEU   C CB  
1848 C CG  . LEU   B 92  ? 0.1431 0.1609 0.2166 0.0099  -0.0041 0.0040  98  LEU   C CG  
1849 C CD1 . LEU   B 92  ? 0.1551 0.1714 0.2205 0.0094  -0.0024 0.0077  98  LEU   C CD1 
1850 C CD2 . LEU   B 92  ? 0.1796 0.1992 0.2659 0.0091  -0.0010 0.0064  98  LEU   C CD2 
1851 N N   . MET   B 93  ? 0.1210 0.1361 0.1730 0.0133  -0.0108 -0.0017 99  MET   C N   
1852 C CA  . MET   B 93  ? 0.1120 0.1274 0.1607 0.0147  -0.0122 -0.0021 99  MET   C CA  
1853 C C   . MET   B 93  ? 0.1179 0.1343 0.1694 0.0138  -0.0091 0.0017  99  MET   C C   
1854 O O   . MET   B 93  ? 0.1324 0.1479 0.1804 0.0128  -0.0064 0.0051  99  MET   C O   
1855 C CB  . MET   B 93  ? 0.1336 0.1464 0.1699 0.0160  -0.0129 -0.0017 99  MET   C CB  
1856 C CG  . MET   B 93  ? 0.1593 0.1705 0.1909 0.0175  -0.0152 -0.0049 99  MET   C CG  
1857 S SD  . MET   B 93  ? 0.1739 0.1815 0.1919 0.0191  -0.0144 -0.0033 99  MET   C SD  
1858 C CE  . MET   B 93  ? 0.1757 0.1822 0.1936 0.0164  -0.0104 0.0010  99  MET   C CE  
1859 N N   . LEU   B 94  ? 0.1112 0.1295 0.1683 0.0145  -0.0093 0.0014  100 LEU   C N   
1860 C CA  . LEU   B 94  ? 0.1193 0.1381 0.1783 0.0142  -0.0056 0.0050  100 LEU   C CA  
1861 C C   . LEU   B 94  ? 0.1122 0.1299 0.1641 0.0155  -0.0058 0.0054  100 LEU   C C   
1862 O O   . LEU   B 94  ? 0.1245 0.1424 0.1751 0.0169  -0.0090 0.0028  100 LEU   C O   
1863 C CB  . LEU   B 94  ? 0.1300 0.1515 0.2033 0.0140  -0.0043 0.0049  100 LEU   C CB  
1864 C CG  . LEU   B 94  ? 0.1495 0.1722 0.2330 0.0127  -0.0034 0.0048  100 LEU   C CG  
1865 C CD1 . LEU   B 94  ? 0.1842 0.2097 0.2833 0.0126  -0.0014 0.0051  100 LEU   C CD1 
1866 C CD2 . LEU   B 94  ? 0.1611 0.1824 0.2402 0.0117  0.0001  0.0089  100 LEU   C CD2 
1867 N N   . ALA   B 95  ? 0.1235 0.1400 0.1714 0.0153  -0.0024 0.0087  101 ALA   C N   
1868 C CA  . ALA   B 95  ? 0.1212 0.1366 0.1643 0.0165  -0.0015 0.0093  101 ALA   C CA  
1869 C C   . ALA   B 95  ? 0.1160 0.1317 0.1621 0.0166  0.0031  0.0124  101 ALA   C C   
1870 O O   . ALA   B 95  ? 0.1147 0.1308 0.1631 0.0158  0.0055  0.0147  101 ALA   C O   
1871 C CB  . ALA   B 95  ? 0.1297 0.1419 0.1606 0.0164  -0.0019 0.0097  101 ALA   C CB  
1872 N N   . VAL   B 96  ? 0.1185 0.1337 0.1638 0.0180  0.0046  0.0127  102 VAL   C N   
1873 C CA  . VAL   B 96  ? 0.1314 0.1460 0.1768 0.0187  0.0095  0.0157  102 VAL   C CA  
1874 C C   . VAL   B 96  ? 0.1353 0.1465 0.1674 0.0185  0.0105  0.0169  102 VAL   C C   
1875 O O   . VAL   B 96  ? 0.1595 0.1685 0.1841 0.0188  0.0088  0.0153  102 VAL   C O   
1876 C CB  . VAL   B 96  ? 0.1459 0.1611 0.1963 0.0204  0.0109  0.0153  102 VAL   C CB  
1877 C CG1 . VAL   B 96  ? 0.1708 0.1847 0.2198 0.0216  0.0168  0.0184  102 VAL   C CG1 
1878 C CG2 . VAL   B 96  ? 0.1514 0.1703 0.2162 0.0204  0.0090  0.0136  102 VAL   C CG2 
1879 N N   . GLY   B 97  ? 0.1520 0.1629 0.1818 0.0181  0.0127  0.0195  103 GLY   C N   
1880 C CA  . GLY   B 97  ? 0.1696 0.1777 0.1874 0.0181  0.0127  0.0202  103 GLY   C CA  
1881 C C   . GLY   B 97  ? 0.1634 0.1719 0.1798 0.0179  0.0144  0.0232  103 GLY   C C   
1882 O O   . GLY   B 97  ? 0.1870 0.1978 0.2121 0.0177  0.0158  0.0251  103 GLY   C O   
1883 N N   . HIS   B 98  ? 0.1689 0.1752 0.1747 0.0182  0.0141  0.0238  104 HIS   C N   
1884 C CA  . HIS   B 98  ? 0.1674 0.1740 0.1701 0.0186  0.0152  0.0270  104 HIS   C CA  
1885 C C   . HIS   B 98  ? 0.1595 0.1673 0.1634 0.0167  0.0117  0.0270  104 HIS   C C   
1886 O O   . HIS   B 98  ? 0.1613 0.1684 0.1623 0.0153  0.0080  0.0244  104 HIS   C O   
1887 C CB  . HIS   B 98  ? 0.2028 0.2064 0.1930 0.0201  0.0158  0.0271  104 HIS   C CB  
1888 C CG  . HIS   B 98  ? 0.2154 0.2192 0.2009 0.0214  0.0170  0.0307  104 HIS   C CG  
1889 N ND1 . HIS   B 98  ? 0.2557 0.2605 0.2453 0.0233  0.0221  0.0350  104 HIS   C ND1 
1890 C CD2 . HIS   B 98  ? 0.2477 0.2512 0.2261 0.0210  0.0137  0.0310  104 HIS   C CD2 
1891 C CE1 . HIS   B 98  ? 0.2754 0.2802 0.2591 0.0243  0.0217  0.0379  104 HIS   C CE1 
1892 N NE2 . HIS   B 98  ? 0.2803 0.2845 0.2571 0.0230  0.0164  0.0354  104 HIS   C NE2 
1893 N N   . SER   B 99  ? 0.1574 0.1670 0.1660 0.0169  0.0133  0.0303  105 SER   C N   
1894 C CA  . SER   B 99  ? 0.1657 0.1765 0.1763 0.0154  0.0106  0.0310  105 SER   C CA  
1895 C C   . SER   B 99  ? 0.1778 0.1897 0.1897 0.0167  0.0132  0.0358  105 SER   C C   
1896 O O   . SER   B 99  ? 0.2025 0.2154 0.2226 0.0175  0.0171  0.0382  105 SER   C O   
1897 C CB  . SER   B 99  ? 0.1808 0.1932 0.2018 0.0139  0.0096  0.0290  105 SER   C CB  
1898 O OG  . SER   B 99  ? 0.1912 0.2046 0.2151 0.0127  0.0079  0.0297  105 SER   C OG  
1899 N N   . GLU   B 100 ? 0.1798 0.1915 0.1851 0.0170  0.0111  0.0373  106 GLU   C N   
1900 C CA  . GLU   B 100 ? 0.1939 0.2067 0.1996 0.0184  0.0129  0.0422  106 GLU   C CA  
1901 C C   . GLU   B 100 ? 0.1731 0.1874 0.1838 0.0167  0.0098  0.0423  106 GLU   C C   
1902 O O   . GLU   B 100 ? 0.1635 0.1778 0.1748 0.0146  0.0063  0.0387  106 GLU   C O   
1903 C CB  . GLU   B 100 ? 0.2450 0.2562 0.2371 0.0206  0.0117  0.0434  106 GLU   C CB  
1904 C CG  . GLU   B 100 ? 0.3366 0.3458 0.3223 0.0230  0.0156  0.0440  106 GLU   C CG  
1905 C CD  . GLU   B 100 ? 0.3588 0.3660 0.3296 0.0252  0.0137  0.0439  106 GLU   C CD  
1906 O OE1 . GLU   B 100 ? 0.4536 0.4615 0.4195 0.0257  0.0103  0.0453  106 GLU   C OE1 
1907 O OE2 . GLU   B 100 ? 0.3701 0.3748 0.3342 0.0266  0.0156  0.0422  106 GLU   C OE2 
1908 N N   . PRO   B 101 ? 0.1819 0.1977 0.1966 0.0176  0.0113  0.0469  107 PRO   C N   
1909 C CA  . PRO   B 101 ? 0.1742 0.1916 0.1950 0.0160  0.0087  0.0470  107 PRO   C CA  
1910 C C   . PRO   B 101 ? 0.1767 0.1939 0.1912 0.0147  0.0035  0.0444  107 PRO   C C   
1911 O O   . PRO   B 101 ? 0.1743 0.1919 0.1944 0.0127  0.0017  0.0421  107 PRO   C O   
1912 C CB  . PRO   B 101 ? 0.1910 0.2095 0.2143 0.0180  0.0113  0.0532  107 PRO   C CB  
1913 C CG  . PRO   B 101 ? 0.2319 0.2497 0.2572 0.0198  0.0165  0.0555  107 PRO   C CG  
1914 C CD  . PRO   B 101 ? 0.2099 0.2259 0.2262 0.0202  0.0163  0.0523  107 PRO   C CD  
1915 N N   . GLY   B 102 ? 0.1695 0.1858 0.1730 0.0161  0.0013  0.0445  108 GLY   C N   
1916 C CA  . GLY   B 102 ? 0.1757 0.1921 0.1751 0.0148  -0.0040 0.0419  108 GLY   C CA  
1917 C C   . GLY   B 102 ? 0.1579 0.1727 0.1577 0.0126  -0.0054 0.0367  108 GLY   C C   
1918 O O   . GLY   B 102 ? 0.1765 0.1911 0.1759 0.0111  -0.0090 0.0344  108 GLY   C O   
1919 N N   . ASP   B 103 ? 0.1461 0.1597 0.1473 0.0125  -0.0024 0.0349  109 ASP   C N   
1920 C CA  . ASP   B 103 ? 0.1366 0.1485 0.1380 0.0109  -0.0034 0.0306  109 ASP   C CA  
1921 C C   . ASP   B 103 ? 0.1376 0.1503 0.1473 0.0093  -0.0036 0.0296  109 ASP   C C   
1922 O O   . ASP   B 103 ? 0.1319 0.1433 0.1415 0.0083  -0.0045 0.0266  109 ASP   C O   
1923 C CB  . ASP   B 103 ? 0.1515 0.1621 0.1514 0.0119  -0.0006 0.0294  109 ASP   C CB  
1924 C CG  . ASP   B 103 ? 0.1720 0.1809 0.1621 0.0136  -0.0004 0.0294  109 ASP   C CG  
1925 O OD1 . ASP   B 103 ? 0.1820 0.1899 0.1659 0.0133  -0.0036 0.0280  109 ASP   C OD1 
1926 O OD2 . ASP   B 103 ? 0.1894 0.1979 0.1785 0.0154  0.0032  0.0309  109 ASP   C OD2 
1927 N N   . CYS   B 104 ? 0.1255 0.1400 0.1426 0.0093  -0.0022 0.0320  110 CYS   C N   
1928 C CA  . CYS   B 104 ? 0.1212 0.1361 0.1455 0.0080  -0.0021 0.0307  110 CYS   C CA  
1929 C C   . CYS   B 104 ? 0.1219 0.1360 0.1448 0.0068  -0.0047 0.0292  110 CYS   C C   
1930 O O   . CYS   B 104 ? 0.1414 0.1562 0.1621 0.0066  -0.0068 0.0306  110 CYS   C O   
1931 C CB  . CYS   B 104 ? 0.1229 0.1395 0.1552 0.0082  -0.0004 0.0337  110 CYS   C CB  
1932 S SG  . CYS   B 104 ? 0.1513 0.1685 0.1899 0.0092  0.0035  0.0347  110 CYS   C SG  
1933 N N   . GLY   B 105 ? 0.1098 0.1227 0.1342 0.0061  -0.0044 0.0265  111 GLY   C N   
1934 C CA  . GLY   B 105 ? 0.1221 0.1339 0.1464 0.0052  -0.0058 0.0254  111 GLY   C CA  
1935 C C   . GLY   B 105 ? 0.1185 0.1281 0.1369 0.0050  -0.0067 0.0230  111 GLY   C C   
1936 O O   . GLY   B 105 ? 0.1379 0.1461 0.1568 0.0044  -0.0070 0.0221  111 GLY   C O   
1937 N N   . GLY   B 106 ? 0.1266 0.1356 0.1398 0.0058  -0.0067 0.0223  112 GLY   C N   
1938 C CA  . GLY   B 106 ? 0.1360 0.1425 0.1441 0.0058  -0.0072 0.0200  112 GLY   C CA  
1939 C C   . GLY   B 106 ? 0.1230 0.1280 0.1320 0.0062  -0.0059 0.0183  112 GLY   C C   
1940 O O   . GLY   B 106 ? 0.1193 0.1251 0.1308 0.0070  -0.0048 0.0180  112 GLY   C O   
1941 N N   . ILE   B 107 ? 0.1184 0.1211 0.1253 0.0060  -0.0061 0.0172  113 ILE   C N   
1942 C CA  . ILE   B 107 ? 0.1191 0.1200 0.1256 0.0070  -0.0048 0.0161  113 ILE   C CA  
1943 C C   . ILE   B 107 ? 0.1158 0.1158 0.1187 0.0084  -0.0045 0.0147  113 ILE   C C   
1944 O O   . ILE   B 107 ? 0.1156 0.1147 0.1154 0.0084  -0.0048 0.0142  113 ILE   C O   
1945 C CB  . ILE   B 107 ? 0.1473 0.1459 0.1542 0.0064  -0.0043 0.0162  113 ILE   C CB  
1946 C CG1 . ILE   B 107 ? 0.1938 0.1936 0.2063 0.0056  -0.0037 0.0177  113 ILE   C CG1 
1947 C CG2 . ILE   B 107 ? 0.1541 0.1499 0.1579 0.0080  -0.0027 0.0155  113 ILE   C CG2 
1948 C CD1 . ILE   B 107 ? 0.2527 0.2509 0.2685 0.0048  -0.0028 0.0186  113 ILE   C CD1 
1949 N N   . LEU   B 108 ? 0.1078 0.1079 0.1111 0.0097  -0.0040 0.0138  114 LEU   C N   
1950 C CA  . LEU   B 108 ? 0.1076 0.1067 0.1080 0.0115  -0.0040 0.0124  114 LEU   C CA  
1951 C C   . LEU   B 108 ? 0.1136 0.1100 0.1110 0.0128  -0.0033 0.0123  114 LEU   C C   
1952 O O   . LEU   B 108 ? 0.1149 0.1110 0.1130 0.0132  -0.0026 0.0124  114 LEU   C O   
1953 C CB  . LEU   B 108 ? 0.1149 0.1163 0.1186 0.0125  -0.0047 0.0112  114 LEU   C CB  
1954 C CG  . LEU   B 108 ? 0.1227 0.1238 0.1246 0.0146  -0.0056 0.0095  114 LEU   C CG  
1955 C CD1 . LEU   B 108 ? 0.1316 0.1324 0.1324 0.0148  -0.0052 0.0098  114 LEU   C CD1 
1956 C CD2 . LEU   B 108 ? 0.1370 0.1405 0.1437 0.0152  -0.0069 0.0077  114 LEU   C CD2 
1957 N N   . ARG   B 109 ? 0.1133 0.1074 0.1073 0.0136  -0.0028 0.0123  115 ARG   C N   
1958 C CA  . ARG   B 109 ? 0.1208 0.1119 0.1119 0.0152  -0.0013 0.0130  115 ARG   C CA  
1959 C C   . ARG   B 109 ? 0.1322 0.1221 0.1196 0.0177  -0.0016 0.0125  115 ARG   C C   
1960 O O   . ARG   B 109 ? 0.1403 0.1308 0.1280 0.0177  -0.0023 0.0119  115 ARG   C O   
1961 C CB  . ARG   B 109 ? 0.1639 0.1526 0.1563 0.0136  0.0000  0.0143  115 ARG   C CB  
1962 C CG  . ARG   B 109 ? 0.2062 0.1940 0.1980 0.0128  -0.0005 0.0136  115 ARG   C CG  
1963 C CD  . ARG   B 109 ? 0.2578 0.2434 0.2522 0.0110  0.0002  0.0140  115 ARG   C CD  
1964 N NE  . ARG   B 109 ? 0.3182 0.3060 0.3159 0.0087  -0.0014 0.0139  115 ARG   C NE  
1965 C CZ  . ARG   B 109 ? 0.4220 0.4097 0.4243 0.0074  -0.0010 0.0148  115 ARG   C CZ  
1966 N NH1 . ARG   B 109 ? 0.4674 0.4525 0.4712 0.0081  0.0016  0.0162  115 ARG   C NH1 
1967 N NH2 . ARG   B 109 ? 0.4505 0.4406 0.4559 0.0055  -0.0031 0.0148  115 ARG   C NH2 
1968 N N   . CYS   B 110 ? 0.1368 0.1247 0.1206 0.0203  -0.0007 0.0131  116 CYS   C N   
1969 C CA  . CYS   B 110 ? 0.1482 0.1347 0.1278 0.0233  -0.0010 0.0132  116 CYS   C CA  
1970 C C   . CYS   B 110 ? 0.1681 0.1504 0.1449 0.0247  0.0022  0.0158  116 CYS   C C   
1971 O O   . CYS   B 110 ? 0.1669 0.1476 0.1461 0.0229  0.0044  0.0171  116 CYS   C O   
1972 C CB  . CYS   B 110 ? 0.1467 0.1349 0.1238 0.0260  -0.0033 0.0116  116 CYS   C CB  
1973 S SG  . CYS   B 110 ? 0.1539 0.1402 0.1265 0.0279  -0.0018 0.0121  116 CYS   C SG  
1974 N N   . GLN   B 111 ? 0.1785 0.1588 0.1507 0.0281  0.0026  0.0169  117 GLN   C N   
1975 C CA  . GLN   B 111 ? 0.2019 0.1778 0.1717 0.0298  0.0063  0.0199  117 GLN   C CA  
1976 C C   . GLN   B 111 ? 0.2037 0.1780 0.1713 0.0309  0.0088  0.0214  117 GLN   C C   
1977 O O   . GLN   B 111 ? 0.2301 0.2009 0.1983 0.0313  0.0129  0.0243  117 GLN   C O   
1978 C CB  . GLN   B 111 ? 0.2199 0.1939 0.1845 0.0341  0.0065  0.0215  117 GLN   C CB  
1979 C CG  . GLN   B 111 ? 0.2414 0.2168 0.1995 0.0379  0.0039  0.0206  117 GLN   C CG  
1980 C CD  . GLN   B 111 ? 0.3794 0.3531 0.3323 0.0424  0.0035  0.0223  117 GLN   C CD  
1981 O OE1 . GLN   B 111 ? 0.4175 0.3938 0.3716 0.0431  0.0001  0.0207  117 GLN   C OE1 
1982 N NE2 . GLN   B 111 ? 0.3908 0.3604 0.3384 0.0456  0.0072  0.0260  117 GLN   C NE2 
1983 N N   . HIS   B 112 ? 0.1783 0.1549 0.1440 0.0313  0.0068  0.0194  118 HIS   C N   
1984 C CA  . HIS   B 112 ? 0.1821 0.1569 0.1449 0.0327  0.0095  0.0205  118 HIS   C CA  
1985 C C   . HIS   B 112 ? 0.1901 0.1661 0.1599 0.0290  0.0108  0.0205  118 HIS   C C   
1986 O O   . HIS   B 112 ? 0.2086 0.1829 0.1775 0.0300  0.0138  0.0218  118 HIS   C O   
1987 C CB  . HIS   B 112 ? 0.1961 0.1723 0.1527 0.0357  0.0066  0.0180  118 HIS   C CB  
1988 C CG  . HIS   B 112 ? 0.1876 0.1634 0.1376 0.0398  0.0044  0.0178  118 HIS   C CG  
1989 N ND1 . HIS   B 112 ? 0.1727 0.1521 0.1244 0.0396  -0.0005 0.0149  118 HIS   C ND1 
1990 C CD2 . HIS   B 112 ? 0.2278 0.1999 0.1695 0.0445  0.0065  0.0206  118 HIS   C CD2 
1991 C CE1 . HIS   B 112 ? 0.2068 0.1850 0.1520 0.0439  -0.0017 0.0158  118 HIS   C CE1 
1992 N NE2 . HIS   B 112 ? 0.2424 0.2162 0.1810 0.0470  0.0024  0.0193  118 HIS   C NE2 
1993 N N   . GLY   B 113 ? 0.1714 0.1503 0.1477 0.0251  0.0085  0.0190  119 GLY   C N   
1994 C CA  . GLY   B 113 ? 0.1704 0.1509 0.1534 0.0218  0.0090  0.0191  119 GLY   C CA  
1995 C C   . GLY   B 113 ? 0.1478 0.1323 0.1341 0.0195  0.0054  0.0167  119 GLY   C C   
1996 O O   . GLY   B 113 ? 0.1505 0.1367 0.1360 0.0195  0.0029  0.0151  119 GLY   C O   
1997 N N   . VAL   B 114 ? 0.1471 0.1332 0.1380 0.0177  0.0057  0.0167  120 VAL   C N   
1998 C CA  . VAL   B 114 ? 0.1393 0.1291 0.1342 0.0156  0.0031  0.0152  120 VAL   C CA  
1999 C C   . VAL   B 114 ? 0.1360 0.1271 0.1287 0.0173  0.0015  0.0129  120 VAL   C C   
2000 O O   . VAL   B 114 ? 0.1459 0.1358 0.1364 0.0191  0.0027  0.0123  120 VAL   C O   
2001 C CB  . VAL   B 114 ? 0.1415 0.1324 0.1426 0.0133  0.0040  0.0165  120 VAL   C CB  
2002 C CG1 . VAL   B 114 ? 0.1599 0.1544 0.1650 0.0117  0.0017  0.0156  120 VAL   C CG1 
2003 C CG2 . VAL   B 114 ? 0.1622 0.1523 0.1669 0.0114  0.0045  0.0181  120 VAL   C CG2 
2004 N N   . VAL   B 115 ? 0.1232 0.1168 0.1171 0.0169  -0.0010 0.0114  121 VAL   C N   
2005 C CA  . VAL   B 115 ? 0.1335 0.1288 0.1276 0.0182  -0.0031 0.0087  121 VAL   C CA  
2006 C C   . VAL   B 115 ? 0.1343 0.1320 0.1350 0.0163  -0.0035 0.0081  121 VAL   C C   
2007 O O   . VAL   B 115 ? 0.1382 0.1364 0.1401 0.0172  -0.0042 0.0058  121 VAL   C O   
2008 C CB  . VAL   B 115 ? 0.1296 0.1263 0.1235 0.0188  -0.0053 0.0076  121 VAL   C CB  
2009 C CG1 . VAL   B 115 ? 0.1511 0.1501 0.1479 0.0197  -0.0079 0.0047  121 VAL   C CG1 
2010 C CG2 . VAL   B 115 ? 0.1534 0.1474 0.1410 0.0210  -0.0049 0.0084  121 VAL   C CG2 
2011 N N   . GLY   B 116 ? 0.1219 0.1212 0.1269 0.0138  -0.0031 0.0099  122 GLY   C N   
2012 C CA  . GLY   B 116 ? 0.1366 0.1383 0.1482 0.0122  -0.0031 0.0102  122 GLY   C CA  
2013 C C   . GLY   B 116 ? 0.1137 0.1168 0.1276 0.0103  -0.0031 0.0127  122 GLY   C C   
2014 O O   . GLY   B 116 ? 0.1208 0.1228 0.1314 0.0099  -0.0031 0.0137  122 GLY   C O   
2015 N N   . ILE   B 117 ? 0.1075 0.1129 0.1271 0.0092  -0.0030 0.0136  123 ILE   C N   
2016 C CA  . ILE   B 117 ? 0.1121 0.1189 0.1328 0.0079  -0.0031 0.0162  123 ILE   C CA  
2017 C C   . ILE   B 117 ? 0.1104 0.1192 0.1345 0.0080  -0.0028 0.0167  123 ILE   C C   
2018 O O   . ILE   B 117 ? 0.1161 0.1259 0.1453 0.0084  -0.0025 0.0155  123 ILE   C O   
2019 C CB  . ILE   B 117 ? 0.1202 0.1277 0.1447 0.0068  -0.0026 0.0184  123 ILE   C CB  
2020 C CG1 . ILE   B 117 ? 0.1386 0.1468 0.1691 0.0070  -0.0015 0.0179  123 ILE   C CG1 
2021 C CG2 . ILE   B 117 ? 0.1449 0.1505 0.1671 0.0064  -0.0026 0.0186  123 ILE   C CG2 
2022 C CD1 . ILE   B 117 ? 0.1401 0.1495 0.1760 0.0060  -0.0009 0.0208  123 ILE   C CD1 
2023 N N   . VAL   B 118 ? 0.1040 0.1134 0.1257 0.0078  -0.0029 0.0185  124 VAL   C N   
2024 C CA  . VAL   B 118 ? 0.1037 0.1148 0.1285 0.0082  -0.0016 0.0199  124 VAL   C CA  
2025 C C   . VAL   B 118 ? 0.1109 0.1236 0.1430 0.0078  -0.0005 0.0218  124 VAL   C C   
2026 O O   . VAL   B 118 ? 0.1092 0.1223 0.1420 0.0072  -0.0009 0.0236  124 VAL   C O   
2027 C CB  . VAL   B 118 ? 0.1104 0.1213 0.1297 0.0084  -0.0016 0.0219  124 VAL   C CB  
2028 C CG1 . VAL   B 118 ? 0.1234 0.1357 0.1453 0.0093  0.0007  0.0243  124 VAL   C CG1 
2029 C CG2 . VAL   B 118 ? 0.1268 0.1357 0.1397 0.0089  -0.0022 0.0199  124 VAL   C CG2 
2030 N N   . SER   B 119 ? 0.1065 0.1204 0.1451 0.0082  0.0008  0.0215  125 SER   C N   
2031 C CA  . SER   B 119 ? 0.1090 0.1243 0.1563 0.0079  0.0024  0.0233  125 SER   C CA  
2032 C C   . SER   B 119 ? 0.1248 0.1414 0.1777 0.0085  0.0050  0.0257  125 SER   C C   
2033 O O   . SER   B 119 ? 0.1213 0.1388 0.1802 0.0086  0.0070  0.0288  125 SER   C O   
2034 C CB  . SER   B 119 ? 0.1214 0.1361 0.1738 0.0076  0.0017  0.0196  125 SER   C CB  
2035 O OG  . SER   B 119 ? 0.1333 0.1490 0.1953 0.0073  0.0034  0.0206  125 SER   C OG  
2036 N N   . THR   B 120 ? 0.1195 0.1362 0.1725 0.0092  0.0056  0.0245  126 THR   C N   
2037 C CA  . THR   B 120 ? 0.1161 0.1339 0.1760 0.0099  0.0089  0.0271  126 THR   C CA  
2038 C C   . THR   B 120 ? 0.1115 0.1287 0.1645 0.0112  0.0102  0.0284  126 THR   C C   
2039 O O   . THR   B 120 ? 0.1173 0.1333 0.1621 0.0112  0.0080  0.0261  126 THR   C O   
2040 C CB  . THR   B 120 ? 0.1201 0.1389 0.1916 0.0096  0.0089  0.0239  126 THR   C CB  
2041 O OG1 . THR   B 120 ? 0.1241 0.1428 0.1932 0.0099  0.0068  0.0201  126 THR   C OG1 
2042 C CG2 . THR   B 120 ? 0.1362 0.1551 0.2139 0.0086  0.0075  0.0215  126 THR   C CG2 
2043 N N   . GLY   B 121 ? 0.1261 0.1439 0.1830 0.0123  0.0140  0.0319  127 GLY   C N   
2044 C CA  . GLY   B 121 ? 0.1582 0.1752 0.2097 0.0139  0.0162  0.0332  127 GLY   C CA  
2045 C C   . GLY   B 121 ? 0.1744 0.1924 0.2350 0.0151  0.0215  0.0369  127 GLY   C C   
2046 O O   . GLY   B 121 ? 0.2156 0.2341 0.2815 0.0154  0.0240  0.0406  127 GLY   C O   
2047 N N   . GLY   B 122 ? 0.2123 0.2302 0.2752 0.0161  0.0237  0.0365  128 GLY   C N   
2048 C CA  . GLY   B 122 ? 0.2343 0.2529 0.3072 0.0175  0.0295  0.0403  128 GLY   C CA  
2049 C C   . GLY   B 122 ? 0.2413 0.2604 0.3193 0.0179  0.0305  0.0380  128 GLY   C C   
2050 O O   . GLY   B 122 ? 0.2406 0.2604 0.3201 0.0167  0.0261  0.0331  128 GLY   C O   
2051 N N   . ASN   B 123 ? 0.2219 0.2408 0.3039 0.0199  0.0365  0.0419  129 ASN   C N   
2052 C CA  . ASN   B 123 ? 0.2219 0.2417 0.3120 0.0206  0.0385  0.0406  129 ASN   C CA  
2053 C C   . ASN   B 123 ? 0.2055 0.2242 0.2852 0.0206  0.0346  0.0366  129 ASN   C C   
2054 O O   . ASN   B 123 ? 0.2467 0.2669 0.3345 0.0203  0.0332  0.0335  129 ASN   C O   
2055 C CB  . ASN   B 123 ? 0.2502 0.2730 0.3605 0.0189  0.0373  0.0380  129 ASN   C CB  
2056 C CG  . ASN   B 123 ? 0.3221 0.3459 0.4480 0.0196  0.0439  0.0425  129 ASN   C CG  
2057 O OD1 . ASN   B 123 ? 0.3450 0.3674 0.4687 0.0220  0.0507  0.0478  129 ASN   C OD1 
2058 N ND2 . ASN   B 123 ? 0.3435 0.3695 0.4859 0.0178  0.0426  0.0405  129 ASN   C ND2 
2059 N N   . GLY   B 124 ? 0.1991 0.2153 0.2622 0.0210  0.0329  0.0365  130 GLY   C N   
2060 C CA  . GLY   B 124 ? 0.1877 0.2025 0.2418 0.0211  0.0297  0.0328  130 GLY   C CA  
2061 C C   . GLY   B 124 ? 0.1563 0.1721 0.2114 0.0191  0.0232  0.0280  130 GLY   C C   
2062 O O   . GLY   B 124 ? 0.1614 0.1765 0.2129 0.0193  0.0209  0.0251  130 GLY   C O   
2063 N N   . LEU   B 125 ? 0.1341 0.1513 0.1942 0.0175  0.0208  0.0273  131 LEU   C N   
2064 C CA  . LEU   B 125 ? 0.1330 0.1508 0.1934 0.0160  0.0152  0.0230  131 LEU   C CA  
2065 C C   . LEU   B 125 ? 0.1432 0.1598 0.1949 0.0149  0.0130  0.0233  131 LEU   C C   
2066 O O   . LEU   B 125 ? 0.1794 0.1959 0.2306 0.0149  0.0152  0.0268  131 LEU   C O   
2067 C CB  . LEU   B 125 ? 0.1588 0.1793 0.2341 0.0151  0.0139  0.0209  131 LEU   C CB  
2068 C CG  . LEU   B 125 ? 0.1853 0.2078 0.2721 0.0160  0.0153  0.0202  131 LEU   C CG  
2069 C CD1 . LEU   B 125 ? 0.2280 0.2532 0.3322 0.0151  0.0155  0.0193  131 LEU   C CD1 
2070 C CD2 . LEU   B 125 ? 0.1983 0.2209 0.2818 0.0166  0.0114  0.0166  131 LEU   C CD2 
2071 N N   . VAL   B 126 ? 0.1198 0.1354 0.1654 0.0142  0.0090  0.0203  132 VAL   C N   
2072 C CA  . VAL   B 126 ? 0.1129 0.1275 0.1525 0.0131  0.0068  0.0202  132 VAL   C CA  
2073 C C   . VAL   B 126 ? 0.1036 0.1190 0.1481 0.0123  0.0037  0.0169  132 VAL   C C   
2074 O O   . VAL   B 126 ? 0.1188 0.1344 0.1642 0.0129  0.0015  0.0139  132 VAL   C O   
2075 C CB  . VAL   B 126 ? 0.1191 0.1313 0.1467 0.0132  0.0054  0.0197  132 VAL   C CB  
2076 C CG1 . VAL   B 126 ? 0.1510 0.1621 0.1758 0.0139  0.0039  0.0170  132 VAL   C CG1 
2077 C CG2 . VAL   B 126 ? 0.1371 0.1486 0.1608 0.0120  0.0031  0.0196  132 VAL   C CG2 
2078 N N   . GLY   B 127 ? 0.1042 0.1200 0.1514 0.0113  0.0034  0.0175  133 GLY   C N   
2079 C CA  . GLY   B 127 ? 0.1046 0.1207 0.1552 0.0108  0.0007  0.0141  133 GLY   C CA  
2080 C C   . GLY   B 127 ? 0.1030 0.1174 0.1463 0.0102  -0.0007 0.0140  133 GLY   C C   
2081 O O   . GLY   B 127 ? 0.1116 0.1256 0.1520 0.0096  0.0004  0.0170  133 GLY   C O   
2082 N N   . PHE   B 128 ? 0.1016 0.1149 0.1419 0.0107  -0.0031 0.0108  134 PHE   C N   
2083 C CA  . PHE   B 128 ? 0.1059 0.1173 0.1399 0.0105  -0.0039 0.0105  134 PHE   C CA  
2084 C C   . PHE   B 128 ? 0.1017 0.1129 0.1392 0.0106  -0.0047 0.0080  134 PHE   C C   
2085 O O   . PHE   B 128 ? 0.1129 0.1245 0.1531 0.0116  -0.0065 0.0046  134 PHE   C O   
2086 C CB  . PHE   B 128 ? 0.1147 0.1241 0.1405 0.0116  -0.0051 0.0093  134 PHE   C CB  
2087 C CG  . PHE   B 128 ? 0.1109 0.1201 0.1334 0.0117  -0.0044 0.0108  134 PHE   C CG  
2088 C CD1 . PHE   B 128 ? 0.1158 0.1239 0.1336 0.0109  -0.0035 0.0130  134 PHE   C CD1 
2089 C CD2 . PHE   B 128 ? 0.1242 0.1342 0.1484 0.0128  -0.0048 0.0096  134 PHE   C CD2 
2090 C CE1 . PHE   B 128 ? 0.1237 0.1310 0.1376 0.0112  -0.0029 0.0137  134 PHE   C CE1 
2091 C CE2 . PHE   B 128 ? 0.1314 0.1408 0.1524 0.0132  -0.0036 0.0109  134 PHE   C CE2 
2092 C CZ  . PHE   B 128 ? 0.1292 0.1370 0.1446 0.0124  -0.0026 0.0127  134 PHE   C CZ  
2093 N N   . ALA   B 129 ? 0.1087 0.1192 0.1463 0.0098  -0.0037 0.0094  135 ALA   C N   
2094 C CA  . ALA   B 129 ? 0.1139 0.1235 0.1535 0.0102  -0.0039 0.0070  135 ALA   C CA  
2095 C C   . ALA   B 129 ? 0.1127 0.1197 0.1433 0.0117  -0.0048 0.0053  135 ALA   C C   
2096 O O   . ALA   B 129 ? 0.1241 0.1297 0.1495 0.0115  -0.0038 0.0075  135 ALA   C O   
2097 C CB  . ALA   B 129 ? 0.1222 0.1319 0.1654 0.0090  -0.0019 0.0098  135 ALA   C CB  
2098 N N   . ASP   B 130 ? 0.1144 0.1207 0.1434 0.0135  -0.0067 0.0013  136 ASP   C N   
2099 C CA  . ASP   B 130 ? 0.1243 0.1279 0.1439 0.0156  -0.0072 0.0000  136 ASP   C CA  
2100 C C   . ASP   B 130 ? 0.1322 0.1336 0.1497 0.0159  -0.0049 0.0007  136 ASP   C C   
2101 O O   . ASP   B 130 ? 0.1370 0.1387 0.1601 0.0152  -0.0041 -0.0003 136 ASP   C O   
2102 C CB  . ASP   B 130 ? 0.1436 0.1472 0.1620 0.0179  -0.0104 -0.0046 136 ASP   C CB  
2103 C CG  . ASP   B 130 ? 0.1711 0.1720 0.1787 0.0209  -0.0112 -0.0057 136 ASP   C CG  
2104 O OD1 . ASP   B 130 ? 0.1740 0.1738 0.1761 0.0214  -0.0103 -0.0030 136 ASP   C OD1 
2105 O OD2 . ASP   B 130 ? 0.2232 0.2225 0.2273 0.0230  -0.0123 -0.0090 136 ASP   C OD2 
2106 N N   . VAL   B 131 ? 0.1332 0.1320 0.1430 0.0171  -0.0035 0.0022  137 VAL   C N   
2107 C CA  . VAL   B 131 ? 0.1363 0.1325 0.1436 0.0180  -0.0007 0.0029  137 VAL   C CA  
2108 C C   . VAL   B 131 ? 0.1557 0.1486 0.1530 0.0215  -0.0004 0.0014  137 VAL   C C   
2109 O O   . VAL   B 131 ? 0.1606 0.1507 0.1546 0.0229  0.0027  0.0021  137 VAL   C O   
2110 C CB  . VAL   B 131 ? 0.1438 0.1397 0.1534 0.0161  0.0020  0.0071  137 VAL   C CB  
2111 C CG1 . VAL   B 131 ? 0.1474 0.1465 0.1659 0.0133  0.0015  0.0087  137 VAL   C CG1 
2112 C CG2 . VAL   B 131 ? 0.1565 0.1516 0.1618 0.0161  0.0020  0.0092  137 VAL   C CG2 
2113 N N   . ARG   B 132 ? 0.1499 0.1429 0.1421 0.0234  -0.0032 -0.0004 138 ARG   C N   
2114 C CA  . ARG   B 132 ? 0.1536 0.1433 0.1351 0.0272  -0.0029 -0.0008 138 ARG   C CA  
2115 C C   . ARG   B 132 ? 0.1616 0.1493 0.1382 0.0302  -0.0033 -0.0045 138 ARG   C C   
2116 O O   . ARG   B 132 ? 0.1941 0.1783 0.1606 0.0338  -0.0015 -0.0041 138 ARG   C O   
2117 C CB  . ARG   B 132 ? 0.1526 0.1434 0.1310 0.0286  -0.0062 -0.0016 138 ARG   C CB  
2118 C CG  . ARG   B 132 ? 0.1532 0.1449 0.1344 0.0263  -0.0051 0.0021  138 ARG   C CG  
2119 C CD  . ARG   B 132 ? 0.1525 0.1452 0.1313 0.0279  -0.0082 0.0011  138 ARG   C CD  
2120 N NE  . ARG   B 132 ? 0.1523 0.1487 0.1382 0.0268  -0.0118 -0.0020 138 ARG   C NE  
2121 C CZ  . ARG   B 132 ? 0.1562 0.1546 0.1436 0.0275  -0.0148 -0.0032 138 ARG   C CZ  
2122 N NH1 . ARG   B 132 ? 0.1635 0.1605 0.1449 0.0298  -0.0150 -0.0017 138 ARG   C NH1 
2123 N NH2 . ARG   B 132 ? 0.1547 0.1566 0.1508 0.0261  -0.0172 -0.0056 138 ARG   C NH2 
2124 N N   . ASP   B 133 ? 0.1568 0.1462 0.1396 0.0291  -0.0052 -0.0082 139 ASP   C N   
2125 C CA  . ASP   B 133 ? 0.1775 0.1647 0.1560 0.0318  -0.0058 -0.0126 139 ASP   C CA  
2126 C C   . ASP   B 133 ? 0.1868 0.1713 0.1659 0.0316  -0.0006 -0.0110 139 ASP   C C   
2127 O O   . ASP   B 133 ? 0.2093 0.1910 0.1831 0.0343  -0.0001 -0.0145 139 ASP   C O   
2128 C CB  . ASP   B 133 ? 0.1991 0.1891 0.1858 0.0305  -0.0101 -0.0178 139 ASP   C CB  
2129 C CG  . ASP   B 133 ? 0.2005 0.1930 0.2004 0.0263  -0.0084 -0.0162 139 ASP   C CG  
2130 O OD1 . ASP   B 133 ? 0.2016 0.1956 0.2054 0.0238  -0.0064 -0.0114 139 ASP   C OD1 
2131 O OD2 . ASP   B 133 ? 0.2355 0.2281 0.2418 0.0258  -0.0090 -0.0199 139 ASP   C OD2 
2132 N N   . LEU   B 134 ? 0.1736 0.1589 0.1591 0.0286  0.0029  -0.0062 140 LEU   C N   
2133 C CA  . LEU   B 134 ? 0.1797 0.1633 0.1685 0.0280  0.0076  -0.0043 140 LEU   C CA  
2134 C C   . LEU   B 134 ? 0.1816 0.1613 0.1617 0.0308  0.0120  -0.0012 140 LEU   C C   
2135 O O   . LEU   B 134 ? 0.1805 0.1602 0.1637 0.0293  0.0149  0.0034  140 LEU   C O   
2136 C CB  . LEU   B 134 ? 0.1692 0.1560 0.1698 0.0237  0.0085  -0.0007 140 LEU   C CB  
2137 C CG  . LEU   B 134 ? 0.1674 0.1580 0.1771 0.0212  0.0051  -0.0027 140 LEU   C CG  
2138 C CD1 . LEU   B 134 ? 0.1742 0.1677 0.1931 0.0176  0.0060  0.0019  140 LEU   C CD1 
2139 C CD2 . LEU   B 134 ? 0.1869 0.1766 0.1999 0.0220  0.0049  -0.0072 140 LEU   C CD2 
2140 N N   . LEU   B 135 ? 0.1972 0.1732 0.1658 0.0353  0.0124  -0.0039 141 LEU   C N   
2141 C CA  . LEU   B 135 ? 0.2083 0.1802 0.1672 0.0388  0.0169  -0.0005 141 LEU   C CA  
2142 C C   . LEU   B 135 ? 0.2101 0.1798 0.1730 0.0384  0.0236  0.0033  141 LEU   C C   
2143 O O   . LEU   B 135 ? 0.2276 0.1949 0.1880 0.0396  0.0280  0.0079  141 LEU   C O   
2144 C CB  . LEU   B 135 ? 0.2177 0.1860 0.1620 0.0445  0.0158  -0.0042 141 LEU   C CB  
2145 C CG  . LEU   B 135 ? 0.2224 0.1932 0.1633 0.0453  0.0084  -0.0088 141 LEU   C CG  
2146 C CD1 . LEU   B 135 ? 0.2556 0.2226 0.1807 0.0516  0.0067  -0.0124 141 LEU   C CD1 
2147 C CD2 . LEU   B 135 ? 0.2296 0.2030 0.1730 0.0435  0.0062  -0.0056 141 LEU   C CD2 
2148 N N   . TRP   B 136 ? 0.1994 0.1698 0.1699 0.0368  0.0247  0.0017  142 TRP   C N   
2149 C CA  . TRP   B 136 ? 0.2125 0.1811 0.1886 0.0364  0.0310  0.0051  142 TRP   C CA  
2150 C C   . TRP   B 136 ? 0.2183 0.1897 0.2051 0.0324  0.0321  0.0104  142 TRP   C C   
2151 O O   . TRP   B 136 ? 0.2338 0.2040 0.2258 0.0322  0.0374  0.0141  142 TRP   C O   
2152 C CB  . TRP   B 136 ? 0.2126 0.1817 0.1953 0.0354  0.0312  0.0018  142 TRP   C CB  
2153 C CG  . TRP   B 136 ? 0.2044 0.1784 0.1972 0.0314  0.0259  -0.0001 142 TRP   C CG  
2154 C CD1 . TRP   B 136 ? 0.2126 0.1878 0.2044 0.0314  0.0209  -0.0054 142 TRP   C CD1 
2155 C CD2 . TRP   B 136 ? 0.1932 0.1712 0.1993 0.0270  0.0256  0.0034  142 TRP   C CD2 
2156 N NE1 . TRP   B 136 ? 0.2166 0.1962 0.2204 0.0274  0.0181  -0.0049 142 TRP   C NE1 
2157 C CE2 . TRP   B 136 ? 0.2014 0.1827 0.2132 0.0248  0.0209  0.0005  142 TRP   C CE2 
2158 C CE3 . TRP   B 136 ? 0.1910 0.1703 0.2050 0.0249  0.0287  0.0086  142 TRP   C CE3 
2159 C CZ2 . TRP   B 136 ? 0.2004 0.1858 0.2238 0.0210  0.0196  0.0033  142 TRP   C CZ2 
2160 C CZ3 . TRP   B 136 ? 0.1993 0.1829 0.2249 0.0212  0.0266  0.0107  142 TRP   C CZ3 
2161 C CH2 . TRP   B 136 ? 0.2005 0.1869 0.2297 0.0194  0.0223  0.0083  142 TRP   C CH2 
2162 N N   . LEU   B 137 ? 0.1998 0.1751 0.1907 0.0293  0.0273  0.0108  143 LEU   C N   
2163 C CA  . LEU   B 137 ? 0.2022 0.1799 0.2019 0.0260  0.0279  0.0153  143 LEU   C CA  
2164 C C   . LEU   B 137 ? 0.2404 0.2146 0.2360 0.0280  0.0324  0.0190  143 LEU   C C   
2165 O O   . LEU   B 137 ? 0.2593 0.2345 0.2634 0.0257  0.0343  0.0226  143 LEU   C O   
2166 C CB  . LEU   B 137 ? 0.1858 0.1673 0.1878 0.0232  0.0222  0.0146  143 LEU   C CB  
2167 C CG  . LEU   B 137 ? 0.1707 0.1560 0.1799 0.0206  0.0187  0.0125  143 LEU   C CG  
2168 C CD1 . LEU   B 137 ? 0.1936 0.1819 0.2027 0.0188  0.0139  0.0117  143 LEU   C CD1 
2169 C CD2 . LEU   B 137 ? 0.1944 0.1820 0.2151 0.0178  0.0201  0.0155  143 LEU   C CD2 
2170 N N   . ASP   B 138 ? 0.2239 0.1943 0.2069 0.0323  0.0338  0.0181  144 ASP   C N   
2171 C CA  . ASP   B 138 ? 0.2579 0.2246 0.2362 0.0348  0.0384  0.0220  144 ASP   C CA  
2172 C C   . ASP   B 138 ? 0.2933 0.2560 0.2718 0.0374  0.0461  0.0249  144 ASP   C C   
2173 O O   . ASP   B 138 ? 0.3204 0.2796 0.2957 0.0398  0.0511  0.0288  144 ASP   C O   
2174 C CB  . ASP   B 138 ? 0.2738 0.2380 0.2379 0.0390  0.0368  0.0206  144 ASP   C CB  
2175 C CG  . ASP   B 138 ? 0.2756 0.2433 0.2397 0.0370  0.0302  0.0187  144 ASP   C CG  
2176 O OD1 . ASP   B 138 ? 0.2744 0.2458 0.2485 0.0325  0.0275  0.0190  144 ASP   C OD1 
2177 O OD2 . ASP   B 138 ? 0.3217 0.2882 0.2753 0.0403  0.0276  0.0168  144 ASP   C OD2 
2178 N N   . GLU   B 139 ? 0.2952 0.2580 0.2774 0.0373  0.0478  0.0234  145 GLU   C N   
2179 C CA  . GLU   B 139 ? 0.3594 0.3181 0.3416 0.0401  0.0557  0.0259  145 GLU   C CA  
2180 C C   . GLU   B 139 ? 0.4155 0.3765 0.4116 0.0371  0.0574  0.0266  145 GLU   C C   
2181 O O   . GLU   B 139 ? 0.4216 0.3872 0.4258 0.0332  0.0522  0.0247  145 GLU   C O   
2182 C CB  . GLU   B 139 ? 0.4314 0.3856 0.3976 0.0458  0.0572  0.0225  145 GLU   C CB  
2183 C CG  . GLU   B 139 ? 0.5360 0.4922 0.5012 0.0449  0.0519  0.0164  145 GLU   C CG  
2184 C CD  . GLU   B 139 ? 0.6632 0.6163 0.6122 0.0497  0.0494  0.0113  145 GLU   C CD  
2185 O OE1 . GLU   B 139 ? 0.6878 0.6421 0.6371 0.0493  0.0457  0.0058  145 GLU   C OE1 
2186 O OE2 . GLU   B 139 ? 0.7059 0.6556 0.6425 0.0541  0.0512  0.0128  145 GLU   C OE2 
2187 N N   . GLU   B 140 ? 0.4602 0.4179 0.4591 0.0392  0.0652  0.0295  146 GLU   C N   
2188 C CA  . GLU   B 140 ? 0.5023 0.4612 0.5138 0.0376  0.0686  0.0307  146 GLU   C CA  
2189 C C   . GLU   B 140 ? 0.5211 0.4860 0.5450 0.0326  0.0625  0.0293  146 GLU   C C   
2190 O O   . GLU   B 140 ? 0.5282 0.4940 0.5604 0.0318  0.0643  0.0291  146 GLU   C O   
2191 C CB  . GLU   B 140 ? 0.5642 0.5185 0.5669 0.0421  0.0730  0.0278  146 GLU   C CB  
2192 C CG  . GLU   B 140 ? 0.6587 0.6137 0.6527 0.0426  0.0668  0.0212  146 GLU   C CG  
2193 C CD  . GLU   B 140 ? 0.7800 0.7361 0.7818 0.0412  0.0666  0.0183  146 GLU   C CD  
2194 O OE1 . GLU   B 140 ? 0.8139 0.7694 0.8088 0.0424  0.0629  0.0126  146 GLU   C OE1 
2195 O OE2 . GLU   B 140 ? 0.8023 0.7601 0.8180 0.0391  0.0701  0.0218  146 GLU   C OE2 
2196 N N1  . A1B05 C .   ? 0.3043 0.2873 0.3283 0.0000  0.0349  -0.0211 201 A1B05 A N1  
2197 N N3  . A1B05 C .   ? 0.2990 0.2697 0.3793 0.0127  0.0461  -0.0091 201 A1B05 A N3  
2198 C C4  . A1B05 C .   ? 0.3020 0.2744 0.3456 0.0033  0.0372  -0.0197 201 A1B05 A C4  
2199 C C5  . A1B05 C .   ? 0.3046 0.2800 0.3561 0.0077  0.0330  -0.0123 201 A1B05 A C5  
2200 C C6  . A1B05 C .   ? 0.3076 0.2841 0.3757 0.0123  0.0366  -0.0064 201 A1B05 A C6  
2201 C C7  . A1B05 C .   ? 0.3205 0.3038 0.3955 0.0159  0.0320  0.0024  201 A1B05 A C7  
2202 C C8  . A1B05 C .   ? 0.2987 0.2734 0.3939 0.0174  0.0462  -0.0008 201 A1B05 A C8  
2203 O O   . A1B05 C .   ? 0.3264 0.2945 0.3694 -0.0012 0.0493  -0.0288 201 A1B05 A O   
2204 C C3  . A1B05 C .   ? 0.3016 0.2757 0.3415 0.0018  0.0408  -0.0226 201 A1B05 A C3  
2205 C C2  . A1B05 C .   ? 0.2796 0.2582 0.3126 0.0017  0.0369  -0.0210 201 A1B05 A C2  
2206 C C1  . A1B05 C .   ? 0.2904 0.2686 0.3223 -0.0001 0.0411  -0.0241 201 A1B05 A C1  
2207 N N4  . A1B05 C .   ? 0.2993 0.2829 0.3254 0.0028  0.0285  -0.0167 201 A1B05 A N4  
2208 N N   . A1B05 C .   ? 0.3059 0.2916 0.3270 0.0017  0.0278  -0.0170 201 A1B05 A N   
2209 C C   . A1B05 C .   ? 0.3157 0.3056 0.3289 0.0019  0.0208  -0.0137 201 A1B05 A C   
2210 N N2  . A1B05 C .   ? 0.2901 0.2666 0.3314 0.0044  0.0352  -0.0177 201 A1B05 A N2  
2211 O O1  . A1B05 C .   ? 0.3178 0.3010 0.4102 0.0191  0.0374  0.0069  201 A1B05 A O1  
# 
