data_7I30
# 
_entry.id   7I30 
# 
_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   7I30         pdb_00007i30 10.2210/pdb7i30/pdb 
WWPDB D_1001408251 ?            ?                   
# 
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                        7I30 
_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 'N-(2-methyl-2H-indazol-7-yl)-2-(1,3-oxazol-4-yl)acetamide' 256.260   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                  65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                        78.133    2   ?         ? ? ? 
5 water       nat water                                                       18.015    338 ?         ? ? ? 
# 
_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 'N-(2-methyl-2H-indazol-7-yl)-2-(1,3-oxazol-4-yl)acetamide' A1B02 
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 
A1B02 non-polymer         . 'N-(2-methyl-2H-indazol-7-yl)-2-(1,3-oxazol-4-yl)acetamide' ? 'C13 H12 N4 O2'  256.260 
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        A1B02 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B02 
_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 A1B02 1   201 201 A1B02 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 5 HOH   1   301 2   HOH   HOH A . 
H 5 HOH   2   302 48  HOH   HOH A . 
H 5 HOH   3   303 4   HOH   HOH A . 
H 5 HOH   4   304 108 HOH   HOH A . 
H 5 HOH   5   305 123 HOH   HOH A . 
H 5 HOH   6   306 215 HOH   HOH A . 
H 5 HOH   7   307 212 HOH   HOH A . 
H 5 HOH   8   308 170 HOH   HOH A . 
H 5 HOH   9   309 253 HOH   HOH A . 
H 5 HOH   10  310 171 HOH   HOH A . 
H 5 HOH   11  311 252 HOH   HOH A . 
H 5 HOH   12  312 166 HOH   HOH A . 
H 5 HOH   13  313 76  HOH   HOH A . 
H 5 HOH   14  314 227 HOH   HOH A . 
H 5 HOH   15  315 60  HOH   HOH A . 
H 5 HOH   16  316 236 HOH   HOH A . 
H 5 HOH   17  317 49  HOH   HOH A . 
H 5 HOH   18  318 187 HOH   HOH A . 
H 5 HOH   19  319 53  HOH   HOH A . 
H 5 HOH   20  320 207 HOH   HOH A . 
H 5 HOH   21  321 130 HOH   HOH A . 
H 5 HOH   22  322 317 HOH   HOH A . 
H 5 HOH   23  323 132 HOH   HOH A . 
H 5 HOH   24  324 10  HOH   HOH A . 
H 5 HOH   25  325 289 HOH   HOH A . 
H 5 HOH   26  326 21  HOH   HOH A . 
H 5 HOH   27  327 112 HOH   HOH A . 
H 5 HOH   28  328 63  HOH   HOH A . 
H 5 HOH   29  329 294 HOH   HOH A . 
H 5 HOH   30  330 133 HOH   HOH A . 
H 5 HOH   31  331 201 HOH   HOH A . 
H 5 HOH   32  332 77  HOH   HOH A . 
H 5 HOH   33  333 218 HOH   HOH A . 
H 5 HOH   34  334 244 HOH   HOH A . 
H 5 HOH   35  335 197 HOH   HOH A . 
H 5 HOH   36  336 157 HOH   HOH A . 
H 5 HOH   37  337 184 HOH   HOH A . 
H 5 HOH   38  338 75  HOH   HOH A . 
H 5 HOH   39  339 65  HOH   HOH A . 
H 5 HOH   40  340 260 HOH   HOH A . 
H 5 HOH   41  341 203 HOH   HOH A . 
H 5 HOH   42  342 83  HOH   HOH A . 
H 5 HOH   43  343 35  HOH   HOH A . 
H 5 HOH   44  344 59  HOH   HOH A . 
H 5 HOH   45  345 8   HOH   HOH A . 
H 5 HOH   46  346 84  HOH   HOH A . 
H 5 HOH   47  347 223 HOH   HOH A . 
H 5 HOH   48  348 23  HOH   HOH A . 
H 5 HOH   49  349 228 HOH   HOH A . 
H 5 HOH   50  350 15  HOH   HOH A . 
H 5 HOH   51  351 50  HOH   HOH A . 
H 5 HOH   52  352 194 HOH   HOH A . 
H 5 HOH   53  353 93  HOH   HOH A . 
H 5 HOH   54  354 14  HOH   HOH A . 
H 5 HOH   55  355 51  HOH   HOH A . 
H 5 HOH   56  356 310 HOH   HOH A . 
H 5 HOH   57  357 58  HOH   HOH A . 
H 5 HOH   58  358 274 HOH   HOH A . 
H 5 HOH   59  359 9   HOH   HOH A . 
H 5 HOH   60  360 55  HOH   HOH A . 
H 5 HOH   61  361 267 HOH   HOH A . 
H 5 HOH   62  362 306 HOH   HOH A . 
H 5 HOH   63  363 167 HOH   HOH A . 
H 5 HOH   64  364 97  HOH   HOH A . 
H 5 HOH   65  365 62  HOH   HOH A . 
H 5 HOH   66  366 25  HOH   HOH A . 
H 5 HOH   67  367 31  HOH   HOH A . 
H 5 HOH   68  368 273 HOH   HOH A . 
H 5 HOH   69  369 13  HOH   HOH A . 
H 5 HOH   70  370 7   HOH   HOH A . 
H 5 HOH   71  371 57  HOH   HOH A . 
H 5 HOH   72  372 281 HOH   HOH A . 
H 5 HOH   73  373 150 HOH   HOH A . 
H 5 HOH   74  374 104 HOH   HOH A . 
H 5 HOH   75  375 168 HOH   HOH A . 
H 5 HOH   76  376 113 HOH   HOH A . 
H 5 HOH   77  377 47  HOH   HOH A . 
H 5 HOH   78  378 28  HOH   HOH A . 
H 5 HOH   79  379 159 HOH   HOH A . 
H 5 HOH   80  380 283 HOH   HOH A . 
H 5 HOH   81  381 61  HOH   HOH A . 
H 5 HOH   82  382 99  HOH   HOH A . 
H 5 HOH   83  383 190 HOH   HOH A . 
H 5 HOH   84  384 100 HOH   HOH A . 
H 5 HOH   85  385 17  HOH   HOH A . 
H 5 HOH   86  386 87  HOH   HOH A . 
H 5 HOH   87  387 155 HOH   HOH A . 
H 5 HOH   88  388 202 HOH   HOH A . 
H 5 HOH   89  389 115 HOH   HOH A . 
H 5 HOH   90  390 278 HOH   HOH A . 
H 5 HOH   91  391 323 HOH   HOH A . 
H 5 HOH   92  392 199 HOH   HOH A . 
H 5 HOH   93  393 1   HOH   HOH A . 
H 5 HOH   94  394 211 HOH   HOH A . 
H 5 HOH   95  395 54  HOH   HOH A . 
H 5 HOH   96  396 18  HOH   HOH A . 
H 5 HOH   97  397 147 HOH   HOH A . 
H 5 HOH   98  398 149 HOH   HOH A . 
H 5 HOH   99  399 144 HOH   HOH A . 
H 5 HOH   100 400 173 HOH   HOH A . 
H 5 HOH   101 401 5   HOH   HOH A . 
H 5 HOH   102 402 119 HOH   HOH A . 
H 5 HOH   103 403 176 HOH   HOH A . 
H 5 HOH   104 404 103 HOH   HOH A . 
H 5 HOH   105 405 64  HOH   HOH A . 
H 5 HOH   106 406 256 HOH   HOH A . 
H 5 HOH   107 407 16  HOH   HOH A . 
H 5 HOH   108 408 122 HOH   HOH A . 
H 5 HOH   109 409 277 HOH   HOH A . 
H 5 HOH   110 410 250 HOH   HOH A . 
H 5 HOH   111 411 66  HOH   HOH A . 
H 5 HOH   112 412 124 HOH   HOH A . 
H 5 HOH   113 413 22  HOH   HOH A . 
H 5 HOH   114 414 247 HOH   HOH A . 
H 5 HOH   115 415 95  HOH   HOH A . 
H 5 HOH   116 416 196 HOH   HOH A . 
H 5 HOH   117 417 314 HOH   HOH A . 
H 5 HOH   118 418 222 HOH   HOH A . 
H 5 HOH   119 419 183 HOH   HOH A . 
H 5 HOH   120 420 210 HOH   HOH A . 
H 5 HOH   121 421 258 HOH   HOH A . 
H 5 HOH   122 422 266 HOH   HOH A . 
H 5 HOH   123 423 56  HOH   HOH A . 
H 5 HOH   124 424 12  HOH   HOH A . 
H 5 HOH   125 425 301 HOH   HOH A . 
H 5 HOH   126 426 160 HOH   HOH A . 
H 5 HOH   127 427 24  HOH   HOH A . 
H 5 HOH   128 428 121 HOH   HOH A . 
H 5 HOH   129 429 172 HOH   HOH A . 
H 5 HOH   130 430 92  HOH   HOH A . 
H 5 HOH   131 431 20  HOH   HOH A . 
H 5 HOH   132 432 240 HOH   HOH A . 
H 5 HOH   133 433 27  HOH   HOH A . 
H 5 HOH   134 434 243 HOH   HOH A . 
H 5 HOH   135 435 161 HOH   HOH A . 
H 5 HOH   136 436 327 HOH   HOH A . 
H 5 HOH   137 437 153 HOH   HOH A . 
H 5 HOH   138 438 189 HOH   HOH A . 
H 5 HOH   139 439 333 HOH   HOH A . 
H 5 HOH   140 440 300 HOH   HOH A . 
H 5 HOH   141 441 255 HOH   HOH A . 
H 5 HOH   142 442 268 HOH   HOH A . 
H 5 HOH   143 443 233 HOH   HOH A . 
H 5 HOH   144 444 165 HOH   HOH A . 
H 5 HOH   145 445 241 HOH   HOH A . 
H 5 HOH   146 446 338 HOH   HOH A . 
H 5 HOH   147 447 206 HOH   HOH A . 
H 5 HOH   148 448 231 HOH   HOH A . 
H 5 HOH   149 449 319 HOH   HOH A . 
H 5 HOH   150 450 269 HOH   HOH A . 
H 5 HOH   151 451 325 HOH   HOH A . 
H 5 HOH   152 452 321 HOH   HOH A . 
H 5 HOH   153 453 73  HOH   HOH A . 
H 5 HOH   154 454 305 HOH   HOH A . 
H 5 HOH   155 455 316 HOH   HOH A . 
H 5 HOH   156 456 111 HOH   HOH A . 
H 5 HOH   157 457 265 HOH   HOH A . 
H 5 HOH   158 458 74  HOH   HOH A . 
H 5 HOH   159 459 52  HOH   HOH A . 
H 5 HOH   160 460 322 HOH   HOH A . 
H 5 HOH   161 461 292 HOH   HOH A . 
H 5 HOH   162 462 331 HOH   HOH A . 
H 5 HOH   163 463 286 HOH   HOH A . 
H 5 HOH   164 464 324 HOH   HOH A . 
H 5 HOH   165 465 341 HOH   HOH A . 
H 5 HOH   166 466 169 HOH   HOH A . 
H 5 HOH   167 467 339 HOH   HOH A . 
H 5 HOH   168 468 335 HOH   HOH A . 
H 5 HOH   169 469 336 HOH   HOH A . 
I 5 HOH   1   301 205 HOH   HOH C . 
I 5 HOH   2   302 128 HOH   HOH C . 
I 5 HOH   3   303 137 HOH   HOH C . 
I 5 HOH   4   304 237 HOH   HOH C . 
I 5 HOH   5   305 280 HOH   HOH C . 
I 5 HOH   6   306 142 HOH   HOH C . 
I 5 HOH   7   307 254 HOH   HOH C . 
I 5 HOH   8   308 106 HOH   HOH C . 
I 5 HOH   9   309 220 HOH   HOH C . 
I 5 HOH   10  310 136 HOH   HOH C . 
I 5 HOH   11  311 26  HOH   HOH C . 
I 5 HOH   12  312 249 HOH   HOH C . 
I 5 HOH   13  313 311 HOH   HOH C . 
I 5 HOH   14  314 68  HOH   HOH C . 
I 5 HOH   15  315 302 HOH   HOH C . 
I 5 HOH   16  316 219 HOH   HOH C . 
I 5 HOH   17  317 264 HOH   HOH C . 
I 5 HOH   18  318 82  HOH   HOH C . 
I 5 HOH   19  319 213 HOH   HOH C . 
I 5 HOH   20  320 164 HOH   HOH C . 
I 5 HOH   21  321 337 HOH   HOH C . 
I 5 HOH   22  322 288 HOH   HOH C . 
I 5 HOH   23  323 86  HOH   HOH C . 
I 5 HOH   24  324 141 HOH   HOH C . 
I 5 HOH   25  325 297 HOH   HOH C . 
I 5 HOH   26  326 158 HOH   HOH C . 
I 5 HOH   27  327 214 HOH   HOH C . 
I 5 HOH   28  328 96  HOH   HOH C . 
I 5 HOH   29  329 94  HOH   HOH C . 
I 5 HOH   30  330 34  HOH   HOH C . 
I 5 HOH   31  331 315 HOH   HOH C . 
I 5 HOH   32  332 296 HOH   HOH C . 
I 5 HOH   33  333 79  HOH   HOH C . 
I 5 HOH   34  334 188 HOH   HOH C . 
I 5 HOH   35  335 46  HOH   HOH C . 
I 5 HOH   36  336 309 HOH   HOH C . 
I 5 HOH   37  337 105 HOH   HOH C . 
I 5 HOH   38  338 72  HOH   HOH C . 
I 5 HOH   39  339 80  HOH   HOH C . 
I 5 HOH   40  340 32  HOH   HOH C . 
I 5 HOH   41  341 307 HOH   HOH C . 
I 5 HOH   42  342 81  HOH   HOH C . 
I 5 HOH   43  343 139 HOH   HOH C . 
I 5 HOH   44  344 69  HOH   HOH C . 
I 5 HOH   45  345 198 HOH   HOH C . 
I 5 HOH   46  346 118 HOH   HOH C . 
I 5 HOH   47  347 38  HOH   HOH C . 
I 5 HOH   48  348 30  HOH   HOH C . 
I 5 HOH   49  349 42  HOH   HOH C . 
I 5 HOH   50  350 127 HOH   HOH C . 
I 5 HOH   51  351 162 HOH   HOH C . 
I 5 HOH   52  352 131 HOH   HOH C . 
I 5 HOH   53  353 238 HOH   HOH C . 
I 5 HOH   54  354 185 HOH   HOH C . 
I 5 HOH   55  355 193 HOH   HOH C . 
I 5 HOH   56  356 101 HOH   HOH C . 
I 5 HOH   57  357 208 HOH   HOH C . 
I 5 HOH   58  358 148 HOH   HOH C . 
I 5 HOH   59  359 19  HOH   HOH C . 
I 5 HOH   60  360 138 HOH   HOH C . 
I 5 HOH   61  361 180 HOH   HOH C . 
I 5 HOH   62  362 43  HOH   HOH C . 
I 5 HOH   63  363 110 HOH   HOH C . 
I 5 HOH   64  364 67  HOH   HOH C . 
I 5 HOH   65  365 116 HOH   HOH C . 
I 5 HOH   66  366 39  HOH   HOH C . 
I 5 HOH   67  367 36  HOH   HOH C . 
I 5 HOH   68  368 120 HOH   HOH C . 
I 5 HOH   69  369 151 HOH   HOH C . 
I 5 HOH   70  370 191 HOH   HOH C . 
I 5 HOH   71  371 232 HOH   HOH C . 
I 5 HOH   72  372 114 HOH   HOH C . 
I 5 HOH   73  373 209 HOH   HOH C . 
I 5 HOH   74  374 71  HOH   HOH C . 
I 5 HOH   75  375 182 HOH   HOH C . 
I 5 HOH   76  376 41  HOH   HOH C . 
I 5 HOH   77  377 229 HOH   HOH C . 
I 5 HOH   78  378 37  HOH   HOH C . 
I 5 HOH   79  379 245 HOH   HOH C . 
I 5 HOH   80  380 117 HOH   HOH C . 
I 5 HOH   81  381 11  HOH   HOH C . 
I 5 HOH   82  382 308 HOH   HOH C . 
I 5 HOH   83  383 270 HOH   HOH C . 
I 5 HOH   84  384 126 HOH   HOH C . 
I 5 HOH   85  385 145 HOH   HOH C . 
I 5 HOH   86  386 221 HOH   HOH C . 
I 5 HOH   87  387 40  HOH   HOH C . 
I 5 HOH   88  388 156 HOH   HOH C . 
I 5 HOH   89  389 29  HOH   HOH C . 
I 5 HOH   90  390 91  HOH   HOH C . 
I 5 HOH   91  391 140 HOH   HOH C . 
I 5 HOH   92  392 109 HOH   HOH C . 
I 5 HOH   93  393 226 HOH   HOH C . 
I 5 HOH   94  394 98  HOH   HOH C . 
I 5 HOH   95  395 178 HOH   HOH C . 
I 5 HOH   96  396 70  HOH   HOH C . 
I 5 HOH   97  397 78  HOH   HOH C . 
I 5 HOH   98  398 90  HOH   HOH C . 
I 5 HOH   99  399 154 HOH   HOH C . 
I 5 HOH   100 400 175 HOH   HOH C . 
I 5 HOH   101 401 200 HOH   HOH C . 
I 5 HOH   102 402 45  HOH   HOH C . 
I 5 HOH   103 403 285 HOH   HOH C . 
I 5 HOH   104 404 174 HOH   HOH C . 
I 5 HOH   105 405 89  HOH   HOH C . 
I 5 HOH   106 406 85  HOH   HOH C . 
I 5 HOH   107 407 195 HOH   HOH C . 
I 5 HOH   108 408 44  HOH   HOH C . 
I 5 HOH   109 409 318 HOH   HOH C . 
I 5 HOH   110 410 135 HOH   HOH C . 
I 5 HOH   111 411 248 HOH   HOH C . 
I 5 HOH   112 412 204 HOH   HOH C . 
I 5 HOH   113 413 134 HOH   HOH C . 
I 5 HOH   114 414 239 HOH   HOH C . 
I 5 HOH   115 415 177 HOH   HOH C . 
I 5 HOH   116 416 88  HOH   HOH C . 
I 5 HOH   117 417 192 HOH   HOH C . 
I 5 HOH   118 418 271 HOH   HOH C . 
I 5 HOH   119 419 251 HOH   HOH C . 
I 5 HOH   120 420 33  HOH   HOH C . 
I 5 HOH   121 421 217 HOH   HOH C . 
I 5 HOH   122 422 102 HOH   HOH C . 
I 5 HOH   123 423 107 HOH   HOH C . 
I 5 HOH   124 424 146 HOH   HOH C . 
I 5 HOH   125 425 320 HOH   HOH C . 
I 5 HOH   126 426 179 HOH   HOH C . 
I 5 HOH   127 427 225 HOH   HOH C . 
I 5 HOH   128 428 235 HOH   HOH C . 
I 5 HOH   129 429 143 HOH   HOH C . 
I 5 HOH   130 430 340 HOH   HOH C . 
I 5 HOH   131 431 279 HOH   HOH C . 
I 5 HOH   132 432 186 HOH   HOH C . 
I 5 HOH   133 433 328 HOH   HOH C . 
I 5 HOH   134 434 312 HOH   HOH C . 
I 5 HOH   135 435 246 HOH   HOH C . 
I 5 HOH   136 436 272 HOH   HOH C . 
I 5 HOH   137 437 276 HOH   HOH C . 
I 5 HOH   138 438 181 HOH   HOH C . 
I 5 HOH   139 439 303 HOH   HOH C . 
I 5 HOH   140 440 163 HOH   HOH C . 
I 5 HOH   141 441 329 HOH   HOH C . 
I 5 HOH   142 442 326 HOH   HOH C . 
I 5 HOH   143 443 216 HOH   HOH C . 
I 5 HOH   144 444 313 HOH   HOH C . 
I 5 HOH   145 445 298 HOH   HOH C . 
I 5 HOH   146 446 284 HOH   HOH C . 
I 5 HOH   147 447 242 HOH   HOH C . 
I 5 HOH   148 448 257 HOH   HOH C . 
I 5 HOH   149 449 290 HOH   HOH C . 
I 5 HOH   150 450 282 HOH   HOH C . 
I 5 HOH   151 451 129 HOH   HOH C . 
I 5 HOH   152 452 304 HOH   HOH C . 
I 5 HOH   153 453 275 HOH   HOH C . 
I 5 HOH   154 454 230 HOH   HOH C . 
I 5 HOH   155 455 224 HOH   HOH C . 
I 5 HOH   156 456 263 HOH   HOH C . 
I 5 HOH   157 457 234 HOH   HOH C . 
I 5 HOH   158 458 293 HOH   HOH C . 
I 5 HOH   159 459 125 HOH   HOH C . 
I 5 HOH   160 460 152 HOH   HOH C . 
I 5 HOH   161 461 330 HOH   HOH C . 
I 5 HOH   162 462 262 HOH   HOH C . 
I 5 HOH   163 463 299 HOH   HOH C . 
I 5 HOH   164 464 334 HOH   HOH C . 
I 5 HOH   165 465 261 HOH   HOH C . 
I 5 HOH   166 466 332 HOH   HOH C . 
I 5 HOH   167 467 287 HOH   HOH C . 
I 5 HOH   168 468 291 HOH   HOH C . 
I 5 HOH   169 469 259 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           7I30 
_cell.length_a           86.424 
_cell.length_b           56.899 
_cell.length_c           64.864 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.80 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I30 
_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          7I30 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.50 
_exptl_crystal.density_percent_sol   50.80 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-14 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I30 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.63 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   84292 
_reflns.percent_possible_obs         75.9 
_reflns.pdbx_Rmerge_I_obs            0.037 
_reflns.pdbx_netI_over_sigmaI        26.6 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.040 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     447095 
_reflns.pdbx_chi_squared             1.13 
_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           301 
_reflns_shell.Rmerge_I_obs                0.348 
_reflns_shell.pdbx_chi_squared            0.15 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        5.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             0.784 
_reflns_shell.pdbx_Rpim_I_all             0.348 
_reflns_shell.pdbx_CC_half                0.193 
_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                                 7I30 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     84248 
_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                             16.48 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    75.9 
_refine.ls_R_factor_obs                          0.1917 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1910 
_refine.ls_R_factor_R_free                       0.2043 
_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                  4221 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               20.79 
_refine.aniso_B[1][1]                            -1.32190 
_refine.aniso_B[2][2]                            0.72040 
_refine.aniso_B[3][3]                            0.60150 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.65450 
_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             0.045 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.045 
_refine.pdbx_overall_SU_R_Blow_DPI               0.047 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.047 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I30 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_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         29 
_refine_hist.number_atoms_solvent             339 
_refine_hist.number_atoms_total               2534 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        16.48 
# 
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               1.16  ? 2.00  3109 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  758  '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  418  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2280 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.17  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.70 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2056 '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             1615 
_refine_ls_shell.R_factor_R_work                  0.3250 
_refine_ls_shell.percent_reflns_obs               12.27 
_refine_ls_shell.R_factor_R_free                  0.3324 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.15 
_refine_ls_shell.number_reflns_R_free             70 
_refine_ls_shell.number_reflns_all                1685 
_refine_ls_shell.R_factor_all                     0.3253 
# 
_struct.entry_id                  7I30 
_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-0032079-001 (A71EV2A-x3403)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I30 
_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 5 ? 
I N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I30 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I30 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,H 
2 1 B,F,G,I   
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.188 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.189 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
# 
_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_555 117.0 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.9 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.2 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.9 ? 
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_555 100.6 ? 
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_555 110.1 ? 
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_555 109.1 ? 
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_555 118.0 ? 
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_555 100.3 ? 
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_555 115.3 ? 
# 
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 VAL A 26  ? N VAL A 32  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 THR A 120 ? N THR A 126 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                   7I30 
_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 312 ? ? O A HOH 322 ? ? 1.94 
2 1 O A HOH 405 ? ? O A HOH 461 ? ? 2.18 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CA 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_1             105 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CB 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_2             105 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.645 
_pdbx_validate_rmsd_bond.bond_target_value         1.525 
_pdbx_validate_rmsd_bond.bond_deviation            0.120 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.015 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A GLY 103 ? ? C  A GLY 103 ? ? N  A HIS 104 ? ? 100.36 117.20 -16.84 2.20 Y 
2 1 CA A HIS 104 ? ? CB A HIS 104 ? ? CG A HIS 104 ? ? 102.79 113.60 -10.81 1.70 N 
3 1 CB A GLU 106 ? ? CA A GLU 106 ? ? C  A GLU 106 ? ? 97.41  110.40 -12.99 2.00 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 87  ? A -125.19 -153.49 
2 1 SER A 87  ? B -125.43 -153.77 
3 1 SER A 125 ? ? -145.88 -42.56  
4 1 SER C 125 ? ? -133.89 -30.35  
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 SER A 87  ? A -16.38 
2 1 SER A 87  ? B -16.07 
3 1 GLY A 103 ? ? 10.81  
# 
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 14.8480 8.3617   14.5446 -0.0173 -0.0141 0.0028 0.0075 0.0015  0.0056 1.7708 1.1452 0.6466 1.2935  
-0.7116 -0.5094 0.0094  0.0559 0.1443 0.0469 0.0518 0.0548  -0.0270 -0.0628 -0.0611 
'X-RAY DIFFRACTION' 2 ? refined 25.6658 -20.1428 17.7625 -0.0200 -0.0150 0.0146 0.0095 -0.0025 0.0183 0.8663 1.1888 0.1416 -0.5145 
-0.1731 -0.0634 -0.0125 0.0073 0.1362 0.0535 0.0520 -0.0137 0.0327  0.0025  -0.0396 
# 
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 
A1B02 N1   N  N N 1   
A1B02 N3   N  Y N 2   
A1B02 C4   C  Y N 3   
A1B02 C5   C  Y N 4   
A1B02 C6   C  Y N 5   
A1B02 C7   C  N N 6   
A1B02 C8   C  N N 7   
A1B02 C10  C  Y N 8   
A1B02 O    O  N N 9   
A1B02 C9   C  Y N 10  
A1B02 N2   N  Y N 11  
A1B02 C11  C  Y N 12  
A1B02 O1   O  Y N 13  
A1B02 C3   C  Y N 14  
A1B02 C12  C  Y N 15  
A1B02 C2   C  Y N 16  
A1B02 C1   C  Y N 17  
A1B02 N    N  Y N 18  
A1B02 C    C  N N 19  
A1B02 H7   H  N N 20  
A1B02 H5   H  N N 21  
A1B02 H6   H  N N 22  
A1B02 H8   H  N N 23  
A1B02 H9   H  N N 24  
A1B02 H10  H  N N 25  
A1B02 H11  H  N N 26  
A1B02 H4   H  N N 27  
A1B02 H3   H  N N 28  
A1B02 H1   H  N N 29  
A1B02 H2   H  N N 30  
A1B02 H    H  N N 31  
ALA   N    N  N N 32  
ALA   CA   C  N S 33  
ALA   C    C  N N 34  
ALA   O    O  N N 35  
ALA   CB   C  N N 36  
ALA   OXT  O  N N 37  
ALA   H    H  N N 38  
ALA   H2   H  N N 39  
ALA   HA   H  N N 40  
ALA   HB1  H  N N 41  
ALA   HB2  H  N N 42  
ALA   HB3  H  N N 43  
ALA   HXT  H  N N 44  
ARG   N    N  N N 45  
ARG   CA   C  N S 46  
ARG   C    C  N N 47  
ARG   O    O  N N 48  
ARG   CB   C  N N 49  
ARG   CG   C  N N 50  
ARG   CD   C  N N 51  
ARG   NE   N  N N 52  
ARG   CZ   C  N N 53  
ARG   NH1  N  N N 54  
ARG   NH2  N  N N 55  
ARG   OXT  O  N N 56  
ARG   H    H  N N 57  
ARG   H2   H  N N 58  
ARG   HA   H  N N 59  
ARG   HB2  H  N N 60  
ARG   HB3  H  N N 61  
ARG   HG2  H  N N 62  
ARG   HG3  H  N N 63  
ARG   HD2  H  N N 64  
ARG   HD3  H  N N 65  
ARG   HE   H  N N 66  
ARG   HH11 H  N N 67  
ARG   HH12 H  N N 68  
ARG   HH21 H  N N 69  
ARG   HH22 H  N N 70  
ARG   HXT  H  N N 71  
ASN   N    N  N N 72  
ASN   CA   C  N S 73  
ASN   C    C  N N 74  
ASN   O    O  N N 75  
ASN   CB   C  N N 76  
ASN   CG   C  N N 77  
ASN   OD1  O  N N 78  
ASN   ND2  N  N N 79  
ASN   OXT  O  N N 80  
ASN   H    H  N N 81  
ASN   H2   H  N N 82  
ASN   HA   H  N N 83  
ASN   HB2  H  N N 84  
ASN   HB3  H  N N 85  
ASN   HD21 H  N N 86  
ASN   HD22 H  N N 87  
ASN   HXT  H  N N 88  
ASP   N    N  N N 89  
ASP   CA   C  N S 90  
ASP   C    C  N N 91  
ASP   O    O  N N 92  
ASP   CB   C  N N 93  
ASP   CG   C  N N 94  
ASP   OD1  O  N N 95  
ASP   OD2  O  N N 96  
ASP   OXT  O  N N 97  
ASP   H    H  N N 98  
ASP   H2   H  N N 99  
ASP   HA   H  N N 100 
ASP   HB2  H  N N 101 
ASP   HB3  H  N N 102 
ASP   HD2  H  N N 103 
ASP   HXT  H  N N 104 
CYS   N    N  N N 105 
CYS   CA   C  N R 106 
CYS   C    C  N N 107 
CYS   O    O  N N 108 
CYS   CB   C  N N 109 
CYS   SG   S  N N 110 
CYS   OXT  O  N N 111 
CYS   H    H  N N 112 
CYS   H2   H  N N 113 
CYS   HA   H  N N 114 
CYS   HB2  H  N N 115 
CYS   HB3  H  N N 116 
CYS   HG   H  N N 117 
CYS   HXT  H  N N 118 
DMS   S    S  N N 119 
DMS   O    O  N N 120 
DMS   C1   C  N N 121 
DMS   C2   C  N N 122 
DMS   H11  H  N N 123 
DMS   H12  H  N N 124 
DMS   H13  H  N N 125 
DMS   H21  H  N N 126 
DMS   H22  H  N N 127 
DMS   H23  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
HIS   N    N  N N 178 
HIS   CA   C  N S 179 
HIS   C    C  N N 180 
HIS   O    O  N N 181 
HIS   CB   C  N N 182 
HIS   CG   C  Y N 183 
HIS   ND1  N  Y N 184 
HIS   CD2  C  Y N 185 
HIS   CE1  C  Y N 186 
HIS   NE2  N  Y N 187 
HIS   OXT  O  N N 188 
HIS   H    H  N N 189 
HIS   H2   H  N N 190 
HIS   HA   H  N N 191 
HIS   HB2  H  N N 192 
HIS   HB3  H  N N 193 
HIS   HD1  H  N N 194 
HIS   HD2  H  N N 195 
HIS   HE1  H  N N 196 
HIS   HE2  H  N N 197 
HIS   HXT  H  N N 198 
HOH   O    O  N N 199 
HOH   H1   H  N N 200 
HOH   H2   H  N N 201 
ILE   N    N  N N 202 
ILE   CA   C  N S 203 
ILE   C    C  N N 204 
ILE   O    O  N N 205 
ILE   CB   C  N S 206 
ILE   CG1  C  N N 207 
ILE   CG2  C  N N 208 
ILE   CD1  C  N N 209 
ILE   OXT  O  N N 210 
ILE   H    H  N N 211 
ILE   H2   H  N N 212 
ILE   HA   H  N N 213 
ILE   HB   H  N N 214 
ILE   HG12 H  N N 215 
ILE   HG13 H  N N 216 
ILE   HG21 H  N N 217 
ILE   HG22 H  N N 218 
ILE   HG23 H  N N 219 
ILE   HD11 H  N N 220 
ILE   HD12 H  N N 221 
ILE   HD13 H  N N 222 
ILE   HXT  H  N N 223 
LEU   N    N  N N 224 
LEU   CA   C  N S 225 
LEU   C    C  N N 226 
LEU   O    O  N N 227 
LEU   CB   C  N N 228 
LEU   CG   C  N N 229 
LEU   CD1  C  N N 230 
LEU   CD2  C  N N 231 
LEU   OXT  O  N N 232 
LEU   H    H  N N 233 
LEU   H2   H  N N 234 
LEU   HA   H  N N 235 
LEU   HB2  H  N N 236 
LEU   HB3  H  N N 237 
LEU   HG   H  N N 238 
LEU   HD11 H  N N 239 
LEU   HD12 H  N N 240 
LEU   HD13 H  N N 241 
LEU   HD21 H  N N 242 
LEU   HD22 H  N N 243 
LEU   HD23 H  N N 244 
LEU   HXT  H  N N 245 
LYS   N    N  N N 246 
LYS   CA   C  N S 247 
LYS   C    C  N N 248 
LYS   O    O  N N 249 
LYS   CB   C  N N 250 
LYS   CG   C  N N 251 
LYS   CD   C  N N 252 
LYS   CE   C  N N 253 
LYS   NZ   N  N N 254 
LYS   OXT  O  N N 255 
LYS   H    H  N N 256 
LYS   H2   H  N N 257 
LYS   HA   H  N N 258 
LYS   HB2  H  N N 259 
LYS   HB3  H  N N 260 
LYS   HG2  H  N N 261 
LYS   HG3  H  N N 262 
LYS   HD2  H  N N 263 
LYS   HD3  H  N N 264 
LYS   HE2  H  N N 265 
LYS   HE3  H  N N 266 
LYS   HZ1  H  N N 267 
LYS   HZ2  H  N N 268 
LYS   HZ3  H  N N 269 
LYS   HXT  H  N N 270 
MET   N    N  N N 271 
MET   CA   C  N S 272 
MET   C    C  N N 273 
MET   O    O  N N 274 
MET   CB   C  N N 275 
MET   CG   C  N N 276 
MET   SD   S  N N 277 
MET   CE   C  N N 278 
MET   OXT  O  N N 279 
MET   H    H  N N 280 
MET   H2   H  N N 281 
MET   HA   H  N N 282 
MET   HB2  H  N N 283 
MET   HB3  H  N N 284 
MET   HG2  H  N N 285 
MET   HG3  H  N N 286 
MET   HE1  H  N N 287 
MET   HE2  H  N N 288 
MET   HE3  H  N N 289 
MET   HXT  H  N N 290 
PHE   N    N  N N 291 
PHE   CA   C  N S 292 
PHE   C    C  N N 293 
PHE   O    O  N N 294 
PHE   CB   C  N N 295 
PHE   CG   C  Y N 296 
PHE   CD1  C  Y N 297 
PHE   CD2  C  Y N 298 
PHE   CE1  C  Y N 299 
PHE   CE2  C  Y N 300 
PHE   CZ   C  Y N 301 
PHE   OXT  O  N N 302 
PHE   H    H  N N 303 
PHE   H2   H  N N 304 
PHE   HA   H  N N 305 
PHE   HB2  H  N N 306 
PHE   HB3  H  N N 307 
PHE   HD1  H  N N 308 
PHE   HD2  H  N N 309 
PHE   HE1  H  N N 310 
PHE   HE2  H  N N 311 
PHE   HZ   H  N N 312 
PHE   HXT  H  N N 313 
PRO   N    N  N N 314 
PRO   CA   C  N S 315 
PRO   C    C  N N 316 
PRO   O    O  N N 317 
PRO   CB   C  N N 318 
PRO   CG   C  N N 319 
PRO   CD   C  N N 320 
PRO   OXT  O  N N 321 
PRO   H    H  N N 322 
PRO   HA   H  N N 323 
PRO   HB2  H  N N 324 
PRO   HB3  H  N N 325 
PRO   HG2  H  N N 326 
PRO   HG3  H  N N 327 
PRO   HD2  H  N N 328 
PRO   HD3  H  N N 329 
PRO   HXT  H  N N 330 
SER   N    N  N N 331 
SER   CA   C  N S 332 
SER   C    C  N N 333 
SER   O    O  N N 334 
SER   CB   C  N N 335 
SER   OG   O  N N 336 
SER   OXT  O  N N 337 
SER   H    H  N N 338 
SER   H2   H  N N 339 
SER   HA   H  N N 340 
SER   HB2  H  N N 341 
SER   HB3  H  N N 342 
SER   HG   H  N N 343 
SER   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TRP   N    N  N N 362 
TRP   CA   C  N S 363 
TRP   C    C  N N 364 
TRP   O    O  N N 365 
TRP   CB   C  N N 366 
TRP   CG   C  Y N 367 
TRP   CD1  C  Y N 368 
TRP   CD2  C  Y N 369 
TRP   NE1  N  Y N 370 
TRP   CE2  C  Y N 371 
TRP   CE3  C  Y N 372 
TRP   CZ2  C  Y N 373 
TRP   CZ3  C  Y N 374 
TRP   CH2  C  Y N 375 
TRP   OXT  O  N N 376 
TRP   H    H  N N 377 
TRP   H2   H  N N 378 
TRP   HA   H  N N 379 
TRP   HB2  H  N N 380 
TRP   HB3  H  N N 381 
TRP   HD1  H  N N 382 
TRP   HE1  H  N N 383 
TRP   HE3  H  N N 384 
TRP   HZ2  H  N N 385 
TRP   HZ3  H  N N 386 
TRP   HH2  H  N N 387 
TRP   HXT  H  N N 388 
TYR   N    N  N N 389 
TYR   CA   C  N S 390 
TYR   C    C  N N 391 
TYR   O    O  N N 392 
TYR   CB   C  N N 393 
TYR   CG   C  Y N 394 
TYR   CD1  C  Y N 395 
TYR   CD2  C  Y N 396 
TYR   CE1  C  Y N 397 
TYR   CE2  C  Y N 398 
TYR   CZ   C  Y N 399 
TYR   OH   O  N N 400 
TYR   OXT  O  N N 401 
TYR   H    H  N N 402 
TYR   H2   H  N N 403 
TYR   HA   H  N N 404 
TYR   HB2  H  N N 405 
TYR   HB3  H  N N 406 
TYR   HD1  H  N N 407 
TYR   HD2  H  N N 408 
TYR   HE1  H  N N 409 
TYR   HE2  H  N N 410 
TYR   HH   H  N N 411 
TYR   HXT  H  N N 412 
VAL   N    N  N N 413 
VAL   CA   C  N S 414 
VAL   C    C  N N 415 
VAL   O    O  N N 416 
VAL   CB   C  N N 417 
VAL   CG1  C  N N 418 
VAL   CG2  C  N N 419 
VAL   OXT  O  N N 420 
VAL   H    H  N N 421 
VAL   H2   H  N N 422 
VAL   HA   H  N N 423 
VAL   HB   H  N N 424 
VAL   HG11 H  N N 425 
VAL   HG12 H  N N 426 
VAL   HG13 H  N N 427 
VAL   HG21 H  N N 428 
VAL   HG22 H  N N 429 
VAL   HG23 H  N N 430 
VAL   HXT  H  N N 431 
ZN    ZN   ZN N N 432 
# 
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 
A1B02 C   N    sing N N 1   
A1B02 N   C1   sing Y N 2   
A1B02 C1  C2   doub Y N 3   
A1B02 C2  C3   sing Y N 4   
A1B02 C3  C4   doub Y N 5   
A1B02 C4  C5   sing Y N 6   
A1B02 C5  C6   doub Y N 7   
A1B02 C6  N1   sing N N 8   
A1B02 N1  C7   sing N N 9   
A1B02 C7  O    doub N N 10  
A1B02 C8  C7   sing N N 11  
A1B02 C9  C8   sing N N 12  
A1B02 C9  C10  doub Y N 13  
A1B02 C10 O1   sing Y N 14  
A1B02 O1  C11  sing Y N 15  
A1B02 C11 N2   doub Y N 16  
A1B02 N2  C9   sing Y N 17  
A1B02 C12 C6   sing Y N 18  
A1B02 C2  C12  sing Y N 19  
A1B02 N3  C12  doub Y N 20  
A1B02 N   N3   sing Y N 21  
A1B02 N1  H7   sing N N 22  
A1B02 C4  H5   sing N N 23  
A1B02 C5  H6   sing N N 24  
A1B02 C8  H8   sing N N 25  
A1B02 C8  H9   sing N N 26  
A1B02 C10 H10  sing N N 27  
A1B02 C11 H11  sing N N 28  
A1B02 C3  H4   sing N N 29  
A1B02 C1  H3   sing N N 30  
A1B02 C   H1   sing N N 31  
A1B02 C   H2   sing N N 32  
A1B02 C   H    sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
DMS   S   O    doub N N 116 
DMS   S   C1   sing N N 117 
DMS   S   C2   sing N N 118 
DMS   C1  H11  sing N N 119 
DMS   C1  H12  sing N N 120 
DMS   C1  H13  sing N N 121 
DMS   C2  H21  sing N N 122 
DMS   C2  H22  sing N N 123 
DMS   C2  H23  sing N N 124 
GLN   N   CA   sing N N 125 
GLN   N   H    sing N N 126 
GLN   N   H2   sing N N 127 
GLN   CA  C    sing N N 128 
GLN   CA  CB   sing N N 129 
GLN   CA  HA   sing N N 130 
GLN   C   O    doub N N 131 
GLN   C   OXT  sing N N 132 
GLN   CB  CG   sing N N 133 
GLN   CB  HB2  sing N N 134 
GLN   CB  HB3  sing N N 135 
GLN   CG  CD   sing N N 136 
GLN   CG  HG2  sing N N 137 
GLN   CG  HG3  sing N N 138 
GLN   CD  OE1  doub N N 139 
GLN   CD  NE2  sing N N 140 
GLN   NE2 HE21 sing N N 141 
GLN   NE2 HE22 sing N N 142 
GLN   OXT HXT  sing N N 143 
GLU   N   CA   sing N N 144 
GLU   N   H    sing N N 145 
GLU   N   H2   sing N N 146 
GLU   CA  C    sing N N 147 
GLU   CA  CB   sing N N 148 
GLU   CA  HA   sing N N 149 
GLU   C   O    doub N N 150 
GLU   C   OXT  sing N N 151 
GLU   CB  CG   sing N N 152 
GLU   CB  HB2  sing N N 153 
GLU   CB  HB3  sing N N 154 
GLU   CG  CD   sing N N 155 
GLU   CG  HG2  sing N N 156 
GLU   CG  HG3  sing N N 157 
GLU   CD  OE1  doub N N 158 
GLU   CD  OE2  sing N N 159 
GLU   OE2 HE2  sing N N 160 
GLU   OXT HXT  sing N N 161 
GLY   N   CA   sing N N 162 
GLY   N   H    sing N N 163 
GLY   N   H2   sing N N 164 
GLY   CA  C    sing N N 165 
GLY   CA  HA2  sing N N 166 
GLY   CA  HA3  sing N N 167 
GLY   C   O    doub N N 168 
GLY   C   OXT  sing N N 169 
GLY   OXT HXT  sing N N 170 
HIS   N   CA   sing N N 171 
HIS   N   H    sing N N 172 
HIS   N   H2   sing N N 173 
HIS   CA  C    sing N N 174 
HIS   CA  CB   sing N N 175 
HIS   CA  HA   sing N N 176 
HIS   C   O    doub N N 177 
HIS   C   OXT  sing N N 178 
HIS   CB  CG   sing N N 179 
HIS   CB  HB2  sing N N 180 
HIS   CB  HB3  sing N N 181 
HIS   CG  ND1  sing Y N 182 
HIS   CG  CD2  doub Y N 183 
HIS   ND1 CE1  doub Y N 184 
HIS   ND1 HD1  sing N N 185 
HIS   CD2 NE2  sing Y N 186 
HIS   CD2 HD2  sing N N 187 
HIS   CE1 NE2  sing Y N 188 
HIS   CE1 HE1  sing N N 189 
HIS   NE2 HE2  sing N N 190 
HIS   OXT HXT  sing N N 191 
HOH   O   H1   sing N N 192 
HOH   O   H2   sing N N 193 
ILE   N   CA   sing N N 194 
ILE   N   H    sing N N 195 
ILE   N   H2   sing N N 196 
ILE   CA  C    sing N N 197 
ILE   CA  CB   sing N N 198 
ILE   CA  HA   sing N N 199 
ILE   C   O    doub N N 200 
ILE   C   OXT  sing N N 201 
ILE   CB  CG1  sing N N 202 
ILE   CB  CG2  sing N N 203 
ILE   CB  HB   sing N N 204 
ILE   CG1 CD1  sing N N 205 
ILE   CG1 HG12 sing N N 206 
ILE   CG1 HG13 sing N N 207 
ILE   CG2 HG21 sing N N 208 
ILE   CG2 HG22 sing N N 209 
ILE   CG2 HG23 sing N N 210 
ILE   CD1 HD11 sing N N 211 
ILE   CD1 HD12 sing N N 212 
ILE   CD1 HD13 sing N N 213 
ILE   OXT HXT  sing N N 214 
LEU   N   CA   sing N N 215 
LEU   N   H    sing N N 216 
LEU   N   H2   sing N N 217 
LEU   CA  C    sing N N 218 
LEU   CA  CB   sing N N 219 
LEU   CA  HA   sing N N 220 
LEU   C   O    doub N N 221 
LEU   C   OXT  sing N N 222 
LEU   CB  CG   sing N N 223 
LEU   CB  HB2  sing N N 224 
LEU   CB  HB3  sing N N 225 
LEU   CG  CD1  sing N N 226 
LEU   CG  CD2  sing N N 227 
LEU   CG  HG   sing N N 228 
LEU   CD1 HD11 sing N N 229 
LEU   CD1 HD12 sing N N 230 
LEU   CD1 HD13 sing N N 231 
LEU   CD2 HD21 sing N N 232 
LEU   CD2 HD22 sing N N 233 
LEU   CD2 HD23 sing N N 234 
LEU   OXT HXT  sing N N 235 
LYS   N   CA   sing N N 236 
LYS   N   H    sing N N 237 
LYS   N   H2   sing N N 238 
LYS   CA  C    sing N N 239 
LYS   CA  CB   sing N N 240 
LYS   CA  HA   sing N N 241 
LYS   C   O    doub N N 242 
LYS   C   OXT  sing N N 243 
LYS   CB  CG   sing N N 244 
LYS   CB  HB2  sing N N 245 
LYS   CB  HB3  sing N N 246 
LYS   CG  CD   sing N N 247 
LYS   CG  HG2  sing N N 248 
LYS   CG  HG3  sing N N 249 
LYS   CD  CE   sing N N 250 
LYS   CD  HD2  sing N N 251 
LYS   CD  HD3  sing N N 252 
LYS   CE  NZ   sing N N 253 
LYS   CE  HE2  sing N N 254 
LYS   CE  HE3  sing N N 255 
LYS   NZ  HZ1  sing N N 256 
LYS   NZ  HZ2  sing N N 257 
LYS   NZ  HZ3  sing N N 258 
LYS   OXT HXT  sing N N 259 
MET   N   CA   sing N N 260 
MET   N   H    sing N N 261 
MET   N   H2   sing N N 262 
MET   CA  C    sing N N 263 
MET   CA  CB   sing N N 264 
MET   CA  HA   sing N N 265 
MET   C   O    doub N N 266 
MET   C   OXT  sing N N 267 
MET   CB  CG   sing N N 268 
MET   CB  HB2  sing N N 269 
MET   CB  HB3  sing N N 270 
MET   CG  SD   sing N N 271 
MET   CG  HG2  sing N N 272 
MET   CG  HG3  sing N N 273 
MET   SD  CE   sing N N 274 
MET   CE  HE1  sing N N 275 
MET   CE  HE2  sing N N 276 
MET   CE  HE3  sing N N 277 
MET   OXT HXT  sing N N 278 
PHE   N   CA   sing N N 279 
PHE   N   H    sing N N 280 
PHE   N   H2   sing N N 281 
PHE   CA  C    sing N N 282 
PHE   CA  CB   sing N N 283 
PHE   CA  HA   sing N N 284 
PHE   C   O    doub N N 285 
PHE   C   OXT  sing N N 286 
PHE   CB  CG   sing N N 287 
PHE   CB  HB2  sing N N 288 
PHE   CB  HB3  sing N N 289 
PHE   CG  CD1  doub Y N 290 
PHE   CG  CD2  sing Y N 291 
PHE   CD1 CE1  sing Y N 292 
PHE   CD1 HD1  sing N N 293 
PHE   CD2 CE2  doub Y N 294 
PHE   CD2 HD2  sing N N 295 
PHE   CE1 CZ   doub Y N 296 
PHE   CE1 HE1  sing N N 297 
PHE   CE2 CZ   sing Y N 298 
PHE   CE2 HE2  sing N N 299 
PHE   CZ  HZ   sing N N 300 
PHE   OXT HXT  sing N N 301 
PRO   N   CA   sing N N 302 
PRO   N   CD   sing N N 303 
PRO   N   H    sing N N 304 
PRO   CA  C    sing N N 305 
PRO   CA  CB   sing N N 306 
PRO   CA  HA   sing N N 307 
PRO   C   O    doub N N 308 
PRO   C   OXT  sing N N 309 
PRO   CB  CG   sing N N 310 
PRO   CB  HB2  sing N N 311 
PRO   CB  HB3  sing N N 312 
PRO   CG  CD   sing N N 313 
PRO   CG  HG2  sing N N 314 
PRO   CG  HG3  sing N N 315 
PRO   CD  HD2  sing N N 316 
PRO   CD  HD3  sing N N 317 
PRO   OXT HXT  sing N N 318 
SER   N   CA   sing N N 319 
SER   N   H    sing N N 320 
SER   N   H2   sing N N 321 
SER   CA  C    sing N N 322 
SER   CA  CB   sing N N 323 
SER   CA  HA   sing N N 324 
SER   C   O    doub N N 325 
SER   C   OXT  sing N N 326 
SER   CB  OG   sing N N 327 
SER   CB  HB2  sing N N 328 
SER   CB  HB3  sing N N 329 
SER   OG  HG   sing N N 330 
SER   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
_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                    7I30 
_atom_sites.fract_transf_matrix[1][1]   0.011571 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000972 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017575 
_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]   0.015471 
_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   ? 17.743 7.953   24.819 1.00 17.05  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.005 8.067   24.049 1.00 16.66  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.136 6.861   23.103 1.00 16.32  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.402 5.880   23.272 1.00 16.63  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.181 8.099   25.038 1.00 19.17  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.248 6.855   25.708 1.00 22.62  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.032 6.938   22.137 1.00 14.77  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.308 5.848   21.217 1.00 13.82  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.679 6.327   19.836 1.00 11.98  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.409 7.466   19.465 1.00 13.58  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.359 5.497   19.121 1.00 11.78  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.822 5.854   17.775 1.00 12.41  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.778 4.638   16.862 1.00 12.29  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.703 3.483   17.331 1.00 13.73  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.276 6.374   17.875 1.00 14.25  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.858 4.880   15.554 1.00 12.01  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.052 3.846   14.537 1.00 11.53  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.522 3.924   14.139 1.00 12.55  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.025 5.020   13.855 1.00 12.59  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.178 4.060   13.295 1.00 11.40  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.726 4.237   13.655 1.00 13.84  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.371 2.895   12.291 1.00 13.36  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.893 4.800   12.461 1.00 13.90  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.231 2.793   14.101 1.00 12.78  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.647 2.762   13.682 1.00 14.42  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.741 1.957   12.399 1.00 14.54  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.700 0.708   12.451 1.00 15.36  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.531 2.178   14.784 1.00 15.53  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.588 3.058   16.002 1.00 14.19  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.477 4.130   16.078 1.00 15.33  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.772 2.819   17.093 1.00 16.10  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.474 5.000   17.170 1.00 16.06  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.774 3.666   18.204 1.00 16.64  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.640 4.757   18.234 1.00 17.07  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.680 5.610   19.333 1.00 19.69  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.765 2.610   11.234 1.00 14.58  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.831 1.987   9.917  1.00 15.66  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.080 2.478   9.202  1.00 16.02  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.322 3.696   9.137  1.00 15.42  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.534 2.256   9.100  1.00 17.14  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.199 3.743   8.994  1.00 16.79  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.655 1.646   7.708  1.00 18.18  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.926 1.555   8.707  1.00 17.30  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.186 1.979   8.068  1.00 18.36  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.024 2.842   8.997  1.00 17.02  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.141 2.555   10.189 1.00 17.33  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.490 3.991   8.478  1.00 15.87  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.188 4.993   9.304  1.00 15.77  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.297 6.176   9.645  1.00 15.17  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.793 7.303   9.789  1.00 15.30  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.539 5.451   8.711  1.00 18.23  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.594 4.372   8.812  1.00 22.80  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.322 4.269   9.801  1.00 24.89  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.623 3.503   7.847  1.00 21.04  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.028 5.897   9.882  1.00 13.58  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.053 6.915   10.284 1.00 13.23  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.416 6.586   11.633 1.00 12.67  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.121 5.415   11.931 1.00 13.59  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.935 7.025   9.213  1.00 14.53  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.432 7.443   7.842  1.00 14.77  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.118 8.646   7.655  1.00 15.69  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.252 6.618   6.742  1.00 17.14  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.598 9.012   6.400  1.00 16.95  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.670 7.010   5.471  1.00 17.96  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.312 8.222   5.304  1.00 18.48  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.777 8.604   4.049  1.00 22.50  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.071 7.642   12.375 1.00 12.09  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.287 7.559   13.604 1.00 11.83  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.066 8.441   13.372 1.00 11.58  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.238 9.642   13.086 1.00 12.24  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.104 8.093   14.779 1.00 13.85  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.343 8.406   16.052 1.00 14.06  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.288 8.774   17.216 1.00 16.00  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.751 9.831   18.080 1.00 15.66  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.099 9.642   19.220 1.00 16.29  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.790 8.400   19.624 1.00 17.27  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.646 10.684  19.907 1.00 16.82  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.864 7.855   13.441 1.00 10.81  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.588 8.561   13.221 1.00 10.70  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.937 8.778   14.552 1.00 11.65  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.630 7.782   15.247 1.00 12.22  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.635 7.803   12.266 1.00 11.39  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.436 8.668   11.942 1.00 12.30  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.335 7.316   10.991 1.00 12.57  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.699 10.033  14.925 1.00 10.66  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.094 10.367  16.225 0.50 10.79  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.132 10.340  16.239 0.50 12.69  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.994 11.374  16.066 1.00 11.12  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.850 12.016  15.000 1.00 12.03  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.132 10.963  17.238 0.50 10.11  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.301 10.915  17.140 0.50 15.98  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.052 9.885   17.761 0.50 12.28  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.888 11.213  18.568 0.50 16.48  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.871 12.211  16.645 0.50 7.25   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.492 9.998   17.157 0.50 18.84  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.159 11.543  17.101 1.00 11.06  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.169 12.633  17.079 1.00 11.77  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.995 13.948  17.103 1.00 12.17  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.928 14.108  17.908 1.00 12.69  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.331 12.622  18.365 1.00 12.24  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.459 11.378  18.467 1.00 12.37  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.863 10.347  19.046 1.00 12.76  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.301 11.441  17.849 1.00 13.20  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.598 14.884  16.229 1.00 12.46  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.354 16.162  16.178 1.00 11.65  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.349 16.840  17.555 1.00 14.34  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.363 17.393  17.980 1.00 14.76  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.731 17.057  15.142 1.00 13.39  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.551 18.369  14.872 1.00 13.86  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.757 19.236  13.919 1.00 15.76  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.495 20.426  13.460 1.00 16.30  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.499 21.584  14.097 1.00 17.40  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.944 21.698  15.295 1.00 18.05  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.082 22.645  13.549 1.00 18.84  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.206 16.726  18.273 1.00 13.93  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.114 17.417  19.568 1.00 15.97  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.987 16.812  20.665 1.00 15.81  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.117 17.406  21.740 1.00 18.84  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.649 17.602  20.062 1.00 17.60  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.946 16.337  20.518 1.00 16.33  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.312 15.478  19.640 1.00 15.92  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.781 15.854  21.774 1.00 16.76  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.768 14.498  20.388 1.00 16.96  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.007 14.707  21.678 1.00 17.08  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.507 15.574  20.467 1.00 15.72  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.377 14.868  21.406 1.00 15.81  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.835 14.805  20.951 1.00 16.76  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.664 14.192  21.595 1.00 17.57  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.831 13.482  21.729 1.00 15.34  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.435 13.484  22.333 1.00 15.66  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 18.007 12.027  22.591 1.00 16.34  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.442 14.256  23.688 1.00 17.99  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.163 15.461  19.797 1.00 15.54  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.537 15.434  19.290 1.00 14.83  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.527 16.098  20.256 1.00 15.96  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.193 17.100  20.904 1.00 17.28  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.573 16.159  17.932 1.00 15.15  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.703 15.476  20.379 1.00 15.34  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.745 15.990  21.289 1.00 14.55  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.665 17.008  20.566 1.00 15.69  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.603 17.154  19.326 1.00 14.55  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.611 14.820  21.789 1.00 17.26  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.300 14.286  20.658 1.00 17.65  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.777 13.707  22.435 1.00 17.97  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.589 17.642  21.284 1.00 16.49  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.562 18.513  20.652 1.00 16.54  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.423 17.707  19.676 1.00 15.66  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.682 18.175  18.563 1.00 15.48  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.487 19.167  21.706 1.00 18.60  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.748 19.787  21.079 1.00 25.46  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.708 20.989  20.357 1.00 28.95  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.002 19.253  20.927 1.00 28.80  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.949 21.234  19.956 1.00 29.15  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.763 20.185  20.208 1.00 30.76  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.789 16.449  20.040 1.00 15.97  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.595 15.663  19.117 1.00 15.64  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.803 15.372  17.819 1.00 14.51  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.367 15.397  16.723 1.00 15.55  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.027 14.331  19.746 1.00 17.55  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.999 13.619  18.822 1.00 25.15  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.171 14.047  18.652 1.00 29.44  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.555 12.514  18.191 1.00 26.32  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.462 15.117  17.946 1.00 13.68  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.663 14.965  16.723 1.00 13.61  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.734 16.209  15.817 1.00 12.78  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.935 16.097  14.618 1.00 13.86  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.207 14.666  17.075 1.00 13.42  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.966 13.299  17.655 1.00 14.58  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.614 12.329  17.189 1.00 15.51  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.134 13.207  18.592 1.00 14.44  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.524 17.383  16.398 1.00 12.75  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.547 18.635  15.620 1.00 13.46  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.962 18.925  15.052 1.00 13.45  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.024 19.482  13.956 1.00 13.94  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.099 19.819  16.525 1.00 13.99  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.611 19.895  16.672 1.00 13.30  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.873 19.559  17.776 1.00 15.06  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.667 20.334  15.679 1.00 13.94  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.526 19.830  17.552 1.00 14.42  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.377 20.287  16.255 1.00 14.16  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.806 20.813  14.366 1.00 15.32  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.227 20.667  15.529 1.00 16.81  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.681 21.128  13.638 1.00 16.13  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.432 21.147  14.227 1.00 16.56  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.014 18.497  15.760 1.00 13.32  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.384 18.717  15.278 1.00 13.90  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.805 17.721  14.188 1.00 15.25  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.832 17.876  13.540 1.00 16.86  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.335 18.652  16.460 1.00 16.16  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.023 16.646  13.993 1.00 14.93  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.291 15.607  12.971 1.00 14.66  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.034 15.444  12.112 1.00 14.07  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.632 14.315  11.774 1.00 14.23  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.704 14.267  13.643 1.00 16.22  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.034 14.454  14.329 1.00 18.25  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.073 14.396  13.679 1.00 21.22  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.041 14.742  15.621 1.00 18.07  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.366 16.533  11.799 1.00 14.65  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.061 16.503  11.127 1.00 12.96  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.114 16.076  9.692  1.00 14.22  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.947 16.536  8.899  1.00 16.04  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.483 17.926  11.218 1.00 13.80  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.078 18.089  10.619 1.00 15.10  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.057 17.296  11.462 1.00 14.37  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.659 19.579  10.566 1.00 17.38  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.177 15.205  9.295  1.00 13.05  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.023 14.801  7.897  1.00 14.03  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.757 15.497  7.340  1.00 13.58  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.783 16.054  6.225  1.00 15.48  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.879 13.260  7.792  1.00 13.80  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.489 12.850  6.349  1.00 16.12  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.184 12.576  8.251  1.00 15.13  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.632 15.486  8.082  1.00 13.59  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.364 16.027  7.571  1.00 13.55  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.406 16.252  8.724  1.00 13.81  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.434 15.452  9.681  1.00 13.00  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.746 14.997  6.554  1.00 14.95  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.328 15.271  6.106  1.00 15.94  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.926 16.113  5.105  1.00 18.08  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.126 14.673  6.625  1.00 15.19  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.548 16.094  4.995  1.00 19.27  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.037 15.186  5.881  1.00 17.12  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.862 13.757  7.647  1.00 16.01  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.704 14.771  6.112  1.00 18.27  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.569 13.304  7.816  1.00 17.29  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.499 13.851  7.095  1.00 18.09  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.575 17.281  8.678  1.00 13.71  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.578 17.464  9.717  1.00 14.22  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.354 18.094  9.104  1.00 15.48  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.452 18.918  8.141  1.00 15.95  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.123 18.304  10.884 1.00 16.48  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.713 19.671  10.510 1.00 17.31  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.740 20.837  10.321 1.00 17.87  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.083 21.810  9.589  1.00 18.49  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.653 20.832  10.947 1.00 16.84  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.194 17.817  9.698  1.00 14.72  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.937 18.396  9.206  1.00 14.97  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.978 18.560  10.387 1.00 14.58  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.461 17.580  10.940 1.00 15.52  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.369 17.485  8.101  1.00 16.44  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.091 17.966  7.470  1.00 20.04  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.248 18.502  8.195  1.00 22.35  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.893 17.713  6.263  1.00 24.16  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.750 19.803  10.796 1.00 15.45  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.906 20.157  11.927 0.50 15.77  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.925 20.102  11.947 0.50 16.88  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.460 19.731  11.695 1.00 16.90  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.819 19.210  12.618 1.00 17.53  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.960 21.662  12.173 0.50 16.83  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.087 21.561  12.356 0.50 20.94  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 15.050 22.024  13.200 0.50 16.72  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.771 22.404  11.267 0.50 26.86  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.971 19.868  10.462 1.00 17.85  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.585 19.469  10.169 1.00 18.33  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.327 17.981  10.371 1.00 17.25  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.194 17.579  10.651 1.00 18.46  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.167 19.861  8.756  1.00 20.45  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.713 19.038  7.747  1.00 25.23  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.375 17.152  10.303 1.00 15.18  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.300 15.687  10.491 1.00 15.03  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.764 15.234  11.863 1.00 14.52  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.684 14.028  12.169 1.00 13.92  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.139 14.965  9.404  1.00 15.25  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.612 15.169  7.996  1.00 17.70  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.485 14.507  6.953  1.00 17.36  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.383 13.046  7.058  1.00 14.85  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.539 12.208  6.046  1.00 15.64  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.803 12.670  4.817  1.00 18.07  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.380 10.893  6.230  1.00 15.76  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.351 16.117  12.661 1.00 14.09  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.985 15.766  13.914 1.00 13.29  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.124 14.751  13.742 1.00 12.58  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.335 13.914  14.624 1.00 13.14  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.992 15.296  15.004 1.00 14.28  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.628 15.050  16.368 1.00 14.21  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.477 15.869  16.813 1.00 14.63  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.231 14.076  17.058 1.00 15.72  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.909 14.881  12.666 1.00 12.75  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 18.010 13.935  12.444 1.00 12.15  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.357 14.642  12.319 1.00 11.91  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.465 15.746  11.737 1.00 12.94  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.761 13.169  11.146 1.00 12.56  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.687 12.042  11.219 1.00 14.11  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.556 11.335  9.864  1.00 15.02  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.962 11.004  12.319 1.00 14.78  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.398 13.969  12.781 1.00 11.57  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.772 14.417  12.550 1.00 11.27  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.603 13.181  12.384 1.00 11.24  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.411 12.147  13.082 1.00 11.73  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.237 15.248  13.771 1.00 11.86  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.673 15.841  13.672 1.00 12.29  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.783 17.198  14.366 1.00 14.47  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.690 14.871  14.276 1.00 12.93  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.584 13.270  11.448 1.00 11.42  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.511 12.173  11.165 1.00 11.03  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.922 12.684  11.330 1.00 11.87  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.262 13.734  10.741 1.00 12.14  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.278 11.613  9.744  1.00 11.73  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.299 10.510  9.444  1.00 13.15  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.823 11.094  9.623  1.00 12.89  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.749 11.978  12.094 1.00 11.68  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.171 12.310  12.282 1.00 11.46  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.025 11.132  11.812 1.00 12.68  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.539 10.004  11.567 1.00 13.03  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.466 12.669  13.737 1.00 13.15  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.117 11.589  14.578 1.00 13.61  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.311 11.397  11.583 1.00 13.50  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.227 10.341  11.131 1.00 15.02  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.854 9.619   12.325 1.00 17.55  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.046 10.204  13.416 1.00 19.33  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.303 10.966  10.244 1.00 17.23  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.019 11.918  11.019 1.00 20.09  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.179 8.315   12.133 1.00 17.82  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.773 7.507   13.185 1.00 19.87  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.125 6.940   12.727 1.00 21.58  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.325 6.694   11.536 1.00 20.45  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.847 6.310   13.539 1.00 20.15  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.699 5.442   12.430 1.00 21.02  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.464 6.746   14.000 1.00 20.82  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.989 6.639   13.700 1.00 22.64  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.267 6.014   13.396 1.00 25.22  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.032 4.510   13.183 1.00 25.59  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.560 3.950   12.210 1.00 28.35  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.293 6.356   14.508 1.00 29.67  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.799 5.876   15.749 1.00 34.33  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.516 7.826   14.632 1.00 30.66  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.238 3.864   14.053 1.00 26.05  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.952 2.433   13.881 1.00 26.74  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.717 2.147   12.987 1.00 25.02  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.759 2.922   13.004 1.00 24.27  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.721 1.776   15.221 1.00 29.36  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.687 1.003   12.292 1.00 23.56  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.530 0.626   11.448 1.00 23.72  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.427 0.006   12.300 1.00 23.30  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.709 -0.739  13.235 1.00 23.74  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 32.943 -0.363  10.354 1.00 25.98  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.843 0.283   9.293  1.00 32.42  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.127 -0.712  8.227  1.00 41.32  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 34.921 -1.649  8.433  1.00 43.09  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.447 -0.554  7.094  1.00 42.54  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.173 0.368   12.014 1.00 19.23  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.004 -0.128  12.756 1.00 19.56  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.374 -1.394  12.190 1.00 19.05  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.640 -1.772  11.032 1.00 19.70  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.444 -1.977  12.963 1.00 17.57  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.819 -3.257  12.605 1.00 18.62  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.395 -3.176  12.147 1.00 17.04  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.851 -4.217  11.788 1.00 18.09  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 26.944 -4.263  13.748 1.00 20.38  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.644 -4.645  14.183 1.00 24.34  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.746 -2.035  12.300 1.00 15.77  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.365 -1.931  11.866 1.00 15.73  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.285 -1.883  10.352 1.00 16.92  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.155 -1.292  9.683  1.00 18.71  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.731 -0.683  12.476 1.00 14.55  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.618 -0.730  13.985 1.00 15.08  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.263 -1.837  14.541 1.00 16.22  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.865 0.300   14.632 1.00 16.19  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.242 -2.423  9.808  1.00 17.80  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 21.904 -2.402  8.369  1.00 19.60  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.597 -1.582  8.212  1.00 17.65  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.694 -1.735  9.039  1.00 17.69  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.695 -3.831  7.861  1.00 26.39  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 22.987 -4.486  7.864  1.00 30.64  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.010 -3.892  6.497  1.00 30.01  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.474 -0.762  7.176  1.00 16.70  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.272 0.021   6.949  1.00 15.36  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.286 -0.722  6.078  1.00 16.19  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.648 -1.258  5.014  1.00 17.19  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.583 1.406   6.344  1.00 15.26  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.697 2.150   7.125  1.00 16.30  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.315 2.289   6.203  1.00 14.94  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.337 2.441   8.659  1.00 16.34  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.033 -0.756  6.458  1.00 15.21  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 15.955 -1.329  5.659  1.00 15.51  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.689 -0.461  4.425  1.00 15.61  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.700 0.784   4.486  1.00 15.81  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.667 -1.352  6.498  1.00 15.74  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.452 -1.135  3.263  1.00 17.64  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.101 -0.423  2.023  1.00 19.14  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.795 -1.057  1.544  1.00 21.21  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.830 -2.058  0.806  1.00 22.82  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.247 -0.518  0.974  1.00 20.87  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.588 0.007   1.480  1.00 20.35  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.664 1.503   1.837  1.00 19.09  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 18.994 1.936   2.317  1.00 18.32  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.202 3.083   2.960  1.00 18.96  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.214 3.955   3.124  1.00 17.21  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.419 3.386   3.432  1.00 20.80  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.633 -0.455  1.975  1.00 20.61  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.264 -1.035  1.872  1.00 19.81  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.159 -0.020  2.197  1.00 20.37  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.384 1.093   2.641  1.00 22.88  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.208 -2.181  2.857  1.00 20.10  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.135 -1.615  4.567  1.00 19.58  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 8.837  -0.510  2.109  1.00 22.75  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.683  0.294   2.525  1.00 25.87  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 6.922  -0.477  3.617  1.00 25.10  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.696  -0.341  3.727  1.00 25.70  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.740  0.649   1.343  1.00 31.06  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.126  -0.542  0.668  1.00 38.25  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.467  -1.699  1.057  1.00 39.39  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.312  -0.339  -0.283 1.00 43.15  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.640  -1.266  4.499  1.00 21.22  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 6.957  -1.963  5.627  1.00 19.33  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.218  -0.943  6.483  1.00 19.73  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.688  0.200   6.682  1.00 19.37  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 7.965  -2.700  6.500  1.00 20.38  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.653  -4.211  5.782  1.00 22.03  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.117  -1.390  7.041  1.00 17.35  ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.335  -0.639  7.994  1.00 17.32  ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.129  -1.460  9.245  1.00 15.08  ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.319  -1.085  10.039 1.00 15.91  ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 2.979  -0.166  7.437  1.00 21.35  ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.061  1.018   6.476  1.00 23.33  ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.649  1.518   6.132  1.00 29.14  ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.133  1.299   5.031  1.00 30.89  ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 0.965  2.189   7.054  1.00 26.06  ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.897  -2.559  9.438  1.00 14.41  ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.905  -3.289  10.702 1.00 14.66  ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.346  -3.581  11.096 1.00 13.72  ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.204  -3.771  10.225 1.00 15.52  ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.114  -4.574  10.690 1.00 17.80  ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.733  -5.480  9.827  1.00 24.73  ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.678  -4.391  10.277 1.00 17.46  ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.616  -3.525  12.376 1.00 12.60  ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 7.982  -3.744  12.843 1.00 12.68  ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.001  -3.761  14.351 1.00 10.89  ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 6.981  -4.023  14.975 1.00 11.51  ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.172  -3.550  14.955 1.00 10.62  ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.341  -3.632  16.406 1.00 9.86   ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.215 -2.461  16.835 1.00 9.75   ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.197 -2.160  16.157 1.00 10.92  ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.056 -4.989  16.744 1.00 11.94  ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.449 -5.088  18.180 1.00 14.07  ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.171  -6.176  16.372 1.00 12.74  ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.861  -1.811  17.941 1.00 9.91   ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.728 -0.731  18.445 1.00 10.10  ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.176 -0.934  19.883 1.00 10.52  ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.492 -1.620  20.656 1.00 11.42  ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.058 0.692   18.300 1.00 10.49  ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.084  1.089   19.402 1.00 10.42  ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.794  0.549   19.456 1.00 11.06  ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.454  1.977   20.411 1.00 11.06  ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.908  0.893   20.478 1.00 12.11  ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.547  2.346   21.416 1.00 12.05  ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.280  1.821   21.413 1.00 12.90  ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.366  2.141   22.410 1.00 15.18  ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.304 -0.337  20.251 1.00 10.15  ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.783 -0.427  21.629 1.00 10.44  ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.330 0.806   22.424 1.00 10.78  ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.563 1.954   22.034 1.00 10.89  ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.332 -0.486  21.646 1.00 11.91  ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.828 -0.647  23.065 1.00 12.47  ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.485 -1.755  23.812 1.00 13.02  ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.577 0.360   23.693 1.00 12.87  ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.893 -1.881  25.138 1.00 14.35  ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.966 0.244   25.027 1.00 14.38  ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.650 -0.890  25.725 1.00 14.37  ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.021 -1.030  27.066 1.00 17.75  ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.738 0.504   23.588 1.00 11.20  ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.216 1.491   24.545 1.00 11.13  ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.039 1.444   25.831 1.00 12.14  ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.842 0.523   26.663 1.00 12.68  ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.753  1.187   24.826 1.00 11.19  ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 9.026  2.320   26.049 1.00 13.27  ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.944 2.391   26.006 1.00 12.20  ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.830 2.373   27.173 1.00 13.51  ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.101 2.546   28.494 1.00 13.34  ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.530 1.973   29.505 1.00 15.55  ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.965 3.384   27.038 1.00 15.22  ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.544 4.734   27.167 1.00 17.80  ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.984 3.300   28.488 1.00 12.76  ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.204 3.509   29.702 1.00 13.66  ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.383 2.310   30.115 1.00 13.98  ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.785  2.319   31.177 1.00 14.69  ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.339 4.748   29.580 1.00 14.52  ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.333  4.560   28.617 1.00 14.22  ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.454 1.203   29.343 1.00 13.90  ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.868  -0.080  29.724 1.00 13.58  ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.889 -1.222  29.662 1.00 15.39  ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.516 -2.363  29.922 1.00 15.35  ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.693  -0.363  28.782 1.00 14.01  ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.508  0.596   28.934 1.00 15.18  ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.716  0.303   30.203 1.00 15.41  ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.598  1.240   30.359 1.00 17.15  ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.656  2.395   31.012 1.00 16.72  ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.811  2.810   31.574 1.00 18.27  ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.554  3.137   31.164 1.00 19.15  ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.127 -0.978  29.217 1.00 16.12  ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.102 -2.062  28.927 1.00 16.23  ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.473 -3.164  28.056 1.00 18.42  ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.640 -4.378  28.331 1.00 20.96  ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.718 -2.700  30.195 1.00 18.96  ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.660 -1.769  30.811 1.00 19.48  ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.452 -2.566  31.845 1.00 22.54  ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.224 -1.629  32.653 1.00 25.76  ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.910 -1.250  33.894 1.00 24.18  ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.819 -1.730  34.489 1.00 22.96  ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.661 -0.369  34.533 1.00 24.80  ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.754 -2.766  27.026 1.00 15.03  ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.041 -3.750  26.225 1.00 15.73  ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.027 -3.325  24.789 1.00 14.83  ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.950 -2.130  24.457 1.00 14.18  ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.577  -3.817  26.740 1.00 18.78  ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.424  -4.728  27.975 1.00 28.23  ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 7.990  -5.175  28.178 1.00 37.09  ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.854  -5.977  29.457 1.00 44.11  ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.263  -5.196  30.662 1.00 48.70  ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 10.990 -4.329  23.912 1.00 13.07  ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.746 -4.163  22.496 1.00 12.18  ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.284  -4.501  22.216 1.00 13.44  ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.783  -5.571  22.648 1.00 16.76  ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.627 -5.126  21.669 1.00 11.81  ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.101 -4.805  21.756 1.00 13.38  ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.800 -4.135  20.782 1.00 16.96  ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.963 -5.118  22.762 1.00 13.30  ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.087 -4.086  21.211 1.00 14.22  ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.190 -4.653  22.389 1.00 16.31  ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.578  -3.639  21.486 1.00 12.15  ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.154  -3.837  21.215 1.00 11.52  ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.918  -3.940  19.728 1.00 11.52  ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.396  -3.089  18.968 1.00 11.35  ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.341  -2.577  21.688 1.00 12.13  ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.262  -2.398  23.197 1.00 13.87  ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.431  -3.206  23.967 1.00 15.45  ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.027  -1.443  23.845 1.00 13.86  ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.338  -3.046  25.355 1.00 15.76  ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.945  -1.267  25.237 1.00 14.91  ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.094  -2.074  25.981 1.00 15.58  ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.001  -1.873  27.362 1.00 18.22  ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.081  -4.893  19.305 1.00 11.62  ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.648  -4.937  17.908 1.00 11.56  ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.612  -3.842  17.637 1.00 12.66  ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.678  -3.692  18.445 1.00 14.37  ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.054  -6.368  17.727 1.00 14.14  ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.634  -6.745  19.122 1.00 15.74  ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.536  -6.013  20.114 1.00 12.62  ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.739  -3.185  16.519 1.00 11.03  ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.807  -2.063  16.179 1.00 12.34  ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.499  -2.044  14.713 1.00 12.37  ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.296  -2.398  13.878 1.00 12.84  ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.402  -0.683  16.574 1.00 14.46  ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.374  -0.494  18.088 1.00 16.06  ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.787  -0.486  16.015 1.00 15.77  ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.308  -1.500  14.385 1.00 12.81  ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.932  -1.037  13.060 1.00 13.48  ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.180  0.483   13.026 1.00 12.56  ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.871  1.160   14.004 1.00 13.76  ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.450  -1.268  12.838 1.00 16.96  ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.239  -2.658  12.838 1.00 24.62  ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.746  1.006   11.955 1.00 13.31  ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.075  2.425   11.898 1.00 13.68  ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.688  3.007   10.565 1.00 14.04  ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.616  2.315   9.552  1.00 15.61  ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.598  2.654   12.249 1.00 13.89  ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.599  1.860   11.432 1.00 13.53  ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.014  0.599   11.836 1.00 13.37  ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.184  2.406   10.291 1.00 13.19  ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.929  -0.119  11.090 1.00 14.01  ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.114  1.672   9.548  1.00 14.74  ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.461  0.421   9.944  1.00 14.22  ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.446  4.306   10.547 1.00 14.36  ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 2.037  5.001   9.328  1.00 15.89  ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.202  5.243   8.384  1.00 16.71  ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.377  5.114   8.765  1.00 15.86  ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.314  6.310   9.691  1.00 18.44  ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.181  7.202   10.379 1.00 19.04  ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.904  5.560   7.127  1.00 17.05  ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.973  5.901   6.172  1.00 17.32  ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.589  7.258   6.520  1.00 18.04  ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.890  8.121   7.060  1.00 19.47  ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.400  5.917   4.751  1.00 19.28  ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.907  4.556   4.339  1.00 22.31  ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.560  4.466   2.855  1.00 27.97  ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.183  3.047   2.508  1.00 33.80  ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.253  2.808   1.032  1.00 39.07  ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.850  7.523   6.166  1.00 17.08  ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.476  8.802   6.517  1.00 17.43  ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.675  9.978   5.952  1.00 18.91  ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.332  10.001  4.752  1.00 21.39  ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.888  8.685   5.928  1.00 19.34  ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.137  7.261   5.765  1.00 21.93  ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.796  6.594   5.512  1.00 18.88  ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.403  10.941  6.819  1.00 19.02  ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.518  12.050  6.477  1.00 21.20  ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.959  13.326  7.203  1.00 19.59  ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.780  13.308  8.126  1.00 18.23  ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.048  11.742  6.874  1.00 26.48  ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.633  10.434  6.528  1.00 35.93  ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.242  14.442  6.867  1.00 21.26  ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.446  15.738  7.480  1.00 23.47  ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.339  15.842  8.545  1.00 24.54  ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.137  15.894  8.208  1.00 27.18  ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.270  16.836  6.389  1.00 25.36  ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.588  18.233  6.818  1.00 28.88  ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.062  18.417  7.045  1.00 29.28  ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.120  19.248  5.739  1.00 29.97  ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.714  15.814  9.807  1.00 23.03  ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.800  15.790  10.960 1.00 24.01  ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.049  16.945  11.904 1.00 25.23  ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.204  17.271  12.210 1.00 23.27  ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.070  14.477  11.724 1.00 26.57  ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.881  13.221  10.842 1.00 30.47  ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.290  14.383  13.054 1.00 27.69  ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 1.408  12.749  10.656 1.00 35.23  ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.982  17.569  12.415 1.00 25.45  ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.092  18.598  13.410 1.00 26.23  ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.367  17.968  14.747 1.00 27.66  ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.692  17.017  15.156 1.00 29.82  ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.772  19.400  13.519 1.00 27.53  ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.012  20.684  14.251 1.00 31.30  ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.746  21.698  13.671 1.00 33.64  ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.557  20.850  15.547 1.00 35.13  ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 1.974  22.884  14.351 1.00 36.34  ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.768  22.037  16.217 1.00 36.34  ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.463  23.054  15.610 1.00 36.94  ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.479  18.380  15.365 1.00 25.88  ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 3.916  17.846  16.639 1.00 24.28  ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 3.846  18.977  17.641 1.00 23.98  ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.356  20.074  17.370 1.00 24.41  ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.380  17.290  16.525 1.00 22.07  ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 5.857  16.763  17.896 1.00 22.11  ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.454  16.180  15.454 1.00 22.45  ? 84  VAL   A CG2 1 
ATOM   625  N  N   A GLU   A 1 79  ? 3.502  18.677  18.893 0.50 23.91  ? 85  GLU   A N   1 
ATOM   626  N  N   B GLU   A 1 79  ? 3.503  18.676  18.894 0.50 24.38  ? 85  GLU   A N   1 
ATOM   627  C  CA  A GLU   A 1 79  ? 3.334  19.752  19.926 0.50 25.18  ? 85  GLU   A CA  1 
ATOM   628  C  CA  B GLU   A 1 79  ? 3.334  19.754  19.926 0.50 25.99  ? 85  GLU   A CA  1 
ATOM   629  C  C   A GLU   A 1 79  ? 4.665  20.278  20.443 0.50 25.55  ? 85  GLU   A C   1 
ATOM   630  C  C   B GLU   A 1 79  ? 4.665  20.276  20.446 0.50 25.98  ? 85  GLU   A C   1 
ATOM   631  O  O   A GLU   A 1 79  ? 5.619  19.530  20.461 0.50 25.06  ? 85  GLU   A O   1 
ATOM   632  O  O   B GLU   A 1 79  ? 5.623  19.532  20.454 0.50 25.56  ? 85  GLU   A O   1 
ATOM   633  C  CB  A GLU   A 1 79  ? 2.549  19.292  21.160 0.50 27.23  ? 85  GLU   A CB  1 
ATOM   634  C  CB  B GLU   A 1 79  ? 2.527  19.333  21.163 0.50 29.48  ? 85  GLU   A CB  1 
ATOM   635  C  CG  A GLU   A 1 79  ? 1.061  19.155  20.863 0.50 29.11  ? 85  GLU   A CG  1 
ATOM   636  C  CG  B GLU   A 1 79  ? 3.244  18.439  22.141 0.50 34.84  ? 85  GLU   A CG  1 
ATOM   637  C  CD  A GLU   A 1 79  ? 0.482  20.322  20.076 0.50 34.90  ? 85  GLU   A CD  1 
ATOM   638  C  CD  B GLU   A 1 79  ? 2.687  17.029  22.150 0.50 37.70  ? 85  GLU   A CD  1 
ATOM   639  O  OE1 A GLU   A 1 79  ? 0.299  21.398  20.662 0.50 36.53  ? 85  GLU   A OE1 1 
ATOM   640  O  OE1 B GLU   A 1 79  ? 1.985  16.688  23.109 0.50 41.22  ? 85  GLU   A OE1 1 
ATOM   641  O  OE2 A GLU   A 1 79  ? 0.225  20.161  18.876 0.50 37.06  ? 85  GLU   A OE2 1 
ATOM   642  O  OE2 B GLU   A 1 79  ? 2.937  16.287  21.178 0.50 34.11  ? 85  GLU   A OE2 1 
ATOM   643  N  N   . ALA   A 1 80  ? 4.626  21.476  21.034 1.00 26.87  ? 86  ALA   A N   1 
ATOM   644  C  CA  . ALA   A 1 80  ? 5.843  22.070  21.584 1.00 28.27  ? 86  ALA   A CA  1 
ATOM   645  C  C   . ALA   A 1 80  ? 6.409  21.264  22.721 1.00 29.77  ? 86  ALA   A C   1 
ATOM   646  O  O   . ALA   A 1 80  ? 5.624  20.594  23.398 1.00 30.55  ? 86  ALA   A O   1 
ATOM   647  C  CB  . ALA   A 1 80  ? 5.481  23.448  22.093 1.00 30.29  ? 86  ALA   A CB  1 
ATOM   648  N  N   A SER   A 1 81  ? 7.726  21.060  22.720 0.50 28.38  ? 87  SER   A N   1 
ATOM   649  N  N   B SER   A 1 81  ? 7.726  21.061  22.719 0.50 30.07  ? 87  SER   A N   1 
ATOM   650  C  CA  A SER   A 1 81  ? 8.379  20.365  23.845 0.50 27.49  ? 87  SER   A CA  1 
ATOM   651  C  CA  B SER   A 1 81  ? 8.378  20.363  23.844 0.50 30.89  ? 87  SER   A CA  1 
ATOM   652  C  C   A SER   A 1 81  ? 9.464  21.324  24.310 0.50 28.51  ? 87  SER   A C   1 
ATOM   653  C  C   B SER   A 1 81  ? 9.466  21.321  24.306 0.50 30.26  ? 87  SER   A C   1 
ATOM   654  O  O   A SER   A 1 81  ? 9.563  22.364  23.637 0.50 28.83  ? 87  SER   A O   1 
ATOM   655  O  O   B SER   A 1 81  ? 9.564  22.364  23.636 0.50 30.74  ? 87  SER   A O   1 
ATOM   656  C  CB  A SER   A 1 81  ? 9.045  19.051  23.489 0.50 25.53  ? 87  SER   A CB  1 
ATOM   657  C  CB  B SER   A 1 81  ? 8.995  19.010  23.490 0.50 33.79  ? 87  SER   A CB  1 
ATOM   658  O  OG  A SER   A 1 81  ? 9.930  19.284  22.393 0.50 20.05  ? 87  SER   A OG  1 
ATOM   659  O  OG  B SER   A 1 81  ? 9.446  18.295  24.622 0.50 37.49  ? 87  SER   A OG  1 
ATOM   660  N  N   . GLU   A 1 82  ? 10.509 20.757  24.905 1.00 29.57  ? 88  GLU   A N   1 
ATOM   661  C  CA  . GLU   A 1 82  ? 11.648 21.617  25.321 1.00 29.25  ? 88  GLU   A CA  1 
ATOM   662  C  C   . GLU   A 1 82  ? 12.532 21.726  24.109 1.00 26.28  ? 88  GLU   A C   1 
ATOM   663  O  O   . GLU   A 1 82  ? 13.389 22.486  24.151 1.00 27.89  ? 88  GLU   A O   1 
ATOM   664  C  CB  . GLU   A 1 82  ? 12.407 21.216  26.622 1.00 34.13  ? 88  GLU   A CB  1 
ATOM   665  C  CG  . GLU   A 1 82  ? 12.872 19.766  26.724 1.00 42.38  ? 88  GLU   A CG  1 
ATOM   666  C  CD  . GLU   A 1 82  ? 13.631 19.403  27.986 1.00 53.04  ? 88  GLU   A CD  1 
ATOM   667  O  OE1 . GLU   A 1 82  ? 14.748 19.922  28.197 1.00 55.65  ? 88  GLU   A OE1 1 
ATOM   668  O  OE2 . GLU   A 1 82  ? 13.086 18.627  28.773 1.00 53.94  ? 88  GLU   A OE2 1 
ATOM   669  N  N   . TYR   A 1 83  ? 12.411 20.815  23.148 1.00 23.85  ? 89  TYR   A N   1 
ATOM   670  C  CA  . TYR   A 1 83  ? 13.395 20.802  22.008 1.00 21.81  ? 89  TYR   A CA  1 
ATOM   671  C  C   . TYR   A 1 83  ? 12.974 21.532  20.730 1.00 22.53  ? 89  TYR   A C   1 
ATOM   672  O  O   . TYR   A 1 83  ? 13.823 21.978  20.022 1.00 22.79  ? 89  TYR   A O   1 
ATOM   673  C  CB  . TYR   A 1 83  ? 13.786 19.360  21.679 1.00 21.76  ? 89  TYR   A CB  1 
ATOM   674  C  CG  . TYR   A 1 83  ? 14.378 18.668  22.884 1.00 22.64  ? 89  TYR   A CG  1 
ATOM   675  C  CD1 . TYR   A 1 83  ? 15.590 19.086  23.394 1.00 24.85  ? 89  TYR   A CD1 1 
ATOM   676  C  CD2 . TYR   A 1 83  ? 13.711 17.667  23.576 1.00 24.69  ? 89  TYR   A CD2 1 
ATOM   677  C  CE1 . TYR   A 1 83  ? 16.157 18.495  24.506 1.00 28.03  ? 89  TYR   A CE1 1 
ATOM   678  C  CE2 . TYR   A 1 83  ? 14.255 17.070  24.704 1.00 27.22  ? 89  TYR   A CE2 1 
ATOM   679  C  CZ  . TYR   A 1 83  ? 15.496 17.477  25.160 1.00 29.42  ? 89  TYR   A CZ  1 
ATOM   680  O  OH  . TYR   A 1 83  ? 16.070 16.907  26.261 1.00 32.58  ? 89  TYR   A OH  1 
ATOM   681  N  N   . TYR   A 1 84  ? 11.661 21.538  20.444 1.00 23.63  ? 90  TYR   A N   1 
ATOM   682  C  CA  . TYR   A 1 84  ? 11.134 22.236  19.260 1.00 22.49  ? 90  TYR   A CA  1 
ATOM   683  C  C   . TYR   A 1 84  ? 9.841  23.000  19.535 1.00 24.27  ? 90  TYR   A C   1 
ATOM   684  O  O   . TYR   A 1 84  ? 9.091  22.499  20.363 1.00 24.29  ? 90  TYR   A O   1 
ATOM   685  C  CB  . TYR   A 1 84  ? 10.783 21.202  18.197 1.00 21.40  ? 90  TYR   A CB  1 
ATOM   686  C  CG  . TYR   A 1 84  ? 11.994 20.453  17.662 1.00 19.59  ? 90  TYR   A CG  1 
ATOM   687  C  CD1 . TYR   A 1 84  ? 12.838 20.991  16.702 1.00 19.67  ? 90  TYR   A CD1 1 
ATOM   688  C  CD2 . TYR   A 1 84  ? 12.350 19.214  18.179 1.00 18.19  ? 90  TYR   A CD2 1 
ATOM   689  C  CE1 . TYR   A 1 84  ? 13.968 20.319  16.247 1.00 18.48  ? 90  TYR   A CE1 1 
ATOM   690  C  CE2 . TYR   A 1 84  ? 13.453 18.507  17.710 1.00 17.39  ? 90  TYR   A CE2 1 
ATOM   691  C  CZ  . TYR   A 1 84  ? 14.278 19.061  16.740 1.00 17.32  ? 90  TYR   A CZ  1 
ATOM   692  O  OH  . TYR   A 1 84  ? 15.375 18.390  16.233 1.00 17.34  ? 90  TYR   A OH  1 
ATOM   693  N  N   . PRO   A 1 85  ? 9.573  24.092  18.811 1.00 25.46  ? 91  PRO   A N   1 
ATOM   694  C  CA  . PRO   A 1 85  ? 8.281  24.777  18.917 1.00 26.43  ? 91  PRO   A CA  1 
ATOM   695  C  C   . PRO   A 1 85  ? 7.256  23.873  18.224 1.00 26.69  ? 91  PRO   A C   1 
ATOM   696  O  O   . PRO   A 1 85  ? 7.709  22.978  17.545 1.00 26.14  ? 91  PRO   A O   1 
ATOM   697  C  CB  . PRO   A 1 85  ? 8.585  26.124  18.222 1.00 28.31  ? 91  PRO   A CB  1 
ATOM   698  C  CG  . PRO   A 1 85  ? 9.549  25.726  17.140 1.00 29.28  ? 91  PRO   A CG  1 
ATOM   699  C  CD  . PRO   A 1 85  ? 10.455 24.724  17.825 1.00 26.20  ? 91  PRO   A CD  1 
ATOM   700  N  N   . ALA   A 1 86  ? 6.000  23.924  18.686 1.00 27.99  ? 92  ALA   A N   1 
ATOM   701  C  CA  . ALA   A 1 86  ? 4.931  23.170  17.957 1.00 28.54  ? 92  ALA   A CA  1 
ATOM   702  C  C   . ALA   A 1 86  ? 5.190  23.529  16.504 1.00 29.86  ? 92  ALA   A C   1 
ATOM   703  O  O   . ALA   A 1 86  ? 5.402  24.699  16.186 1.00 31.86  ? 92  ALA   A O   1 
ATOM   704  C  CB  . ALA   A 1 86  ? 3.559  23.616  18.364 1.00 28.73  ? 92  ALA   A CB  1 
ATOM   705  N  N   . ARG   A 1 87  ? 5.314  22.525  15.670 1.00 29.47  ? 93  ARG   A N   1 
ATOM   706  C  CA  . ARG   A 1 87  ? 5.707  22.705  14.291 1.00 28.80  ? 93  ARG   A CA  1 
ATOM   707  C  C   . ARG   A 1 87  ? 5.357  21.441  13.522 1.00 28.00  ? 93  ARG   A C   1 
ATOM   708  O  O   . ARG   A 1 87  ? 4.990  20.396  14.104 1.00 28.16  ? 93  ARG   A O   1 
ATOM   709  C  CB  . ARG   A 1 87  ? 7.237  22.910  14.256 1.00 28.33  ? 93  ARG   A CB  1 
ATOM   710  C  CG  . ARG   A 1 87  ? 7.984  21.569  14.497 1.00 28.68  ? 93  ARG   A CG  1 
ATOM   711  C  CD  . ARG   A 1 87  ? 9.350  21.732  14.994 1.00 29.13  ? 93  ARG   A CD  1 
ATOM   712  N  NE  . ARG   A 1 87  ? 10.232 20.667  14.501 1.00 26.62  ? 93  ARG   A NE  1 
ATOM   713  C  CZ  . ARG   A 1 87  ? 10.315 19.410  14.886 1.00 30.31  ? 93  ARG   A CZ  1 
ATOM   714  N  NH1 . ARG   A 1 87  ? 9.396  18.889  15.724 1.00 29.63  ? 93  ARG   A NH1 1 
ATOM   715  N  NH2 . ARG   A 1 87  ? 11.275 18.628  14.387 1.00 24.88  ? 93  ARG   A NH2 1 
ATOM   716  N  N   . TYR   A 1 88  ? 5.553  21.516  12.218 1.00 27.70  ? 94  TYR   A N   1 
ATOM   717  C  CA  . TYR   A 1 88  ? 5.421  20.372  11.374 1.00 27.51  ? 94  TYR   A CA  1 
ATOM   718  C  C   . TYR   A 1 88  ? 6.773  19.688  11.310 1.00 25.09  ? 94  TYR   A C   1 
ATOM   719  O  O   . TYR   A 1 88  ? 7.781  20.338  11.011 1.00 25.94  ? 94  TYR   A O   1 
ATOM   720  C  CB  . TYR   A 1 88  ? 4.982  20.780  9.985  1.00 28.67  ? 94  TYR   A CB  1 
ATOM   721  C  CG  . TYR   A 1 88  ? 3.498  21.081  9.924  1.00 29.91  ? 94  TYR   A CG  1 
ATOM   722  C  CD1 . TYR   A 1 88  ? 2.566  20.057  9.832  1.00 31.51  ? 94  TYR   A CD1 1 
ATOM   723  C  CD2 . TYR   A 1 88  ? 3.019  22.377  10.067 1.00 31.15  ? 94  TYR   A CD2 1 
ATOM   724  C  CE1 . TYR   A 1 88  ? 1.204  20.313  9.809  1.00 33.92  ? 94  TYR   A CE1 1 
ATOM   725  C  CE2 . TYR   A 1 88  ? 1.655  22.641  10.080 1.00 32.88  ? 94  TYR   A CE2 1 
ATOM   726  C  CZ  . TYR   A 1 88  ? 0.749  21.604  9.951  1.00 34.21  ? 94  TYR   A CZ  1 
ATOM   727  O  OH  . TYR   A 1 88  ? -0.602 21.835  9.946  1.00 37.70  ? 94  TYR   A OH  1 
ATOM   728  N  N   . GLN   A 1 89  ? 6.780  18.353  11.561 1.00 21.74  ? 95  GLN   A N   1 
ATOM   729  C  CA  . GLN   A 1 89  ? 7.989  17.508  11.460 1.00 19.59  ? 95  GLN   A CA  1 
ATOM   730  C  C   . GLN   A 1 89  ? 7.792  16.628  10.221 1.00 18.81  ? 95  GLN   A C   1 
ATOM   731  O  O   . GLN   A 1 89  ? 6.706  16.045  10.008 1.00 19.70  ? 95  GLN   A O   1 
ATOM   732  C  CB  . GLN   A 1 89  ? 8.188  16.664  12.727 1.00 19.58  ? 95  GLN   A CB  1 
ATOM   733  C  CG  . GLN   A 1 89  ? 9.421  15.797  12.633 1.00 19.76  ? 95  GLN   A CG  1 
ATOM   734  C  CD  . GLN   A 1 89  ? 9.984  15.362  13.984 1.00 18.92  ? 95  GLN   A CD  1 
ATOM   735  O  OE1 . GLN   A 1 89  ? 9.988  16.082  15.016 1.00 19.18  ? 95  GLN   A OE1 1 
ATOM   736  N  NE2 . GLN   A 1 89  ? 10.556 14.181  13.979 1.00 16.42  ? 95  GLN   A NE2 1 
ATOM   737  N  N   . SER   A 1 90  ? 8.805  16.566  9.347  1.00 17.31  ? 96  SER   A N   1 
ATOM   738  C  CA  . SER   A 1 90  ? 8.689  15.812  8.120  1.00 17.39  ? 96  SER   A CA  1 
ATOM   739  C  C   . SER   A 1 90  ? 9.296  14.386  8.296  1.00 16.29  ? 96  SER   A C   1 
ATOM   740  O  O   . SER   A 1 90  ? 10.050 14.112  9.245  1.00 15.85  ? 96  SER   A O   1 
ATOM   741  C  CB  . SER   A 1 90  ? 9.410  16.557  6.993  1.00 19.79  ? 96  SER   A CB  1 
ATOM   742  O  OG  . SER   A 1 90  ? 10.781 16.615  7.326  1.00 23.00  ? 96  SER   A OG  1 
ATOM   743  N  N   . HIS   A 1 91  ? 8.891  13.499  7.384  1.00 16.98  ? 97  HIS   A N   1 
ATOM   744  C  CA  . HIS   A 1 91  ? 9.384  12.128  7.315  1.00 15.97  ? 97  HIS   A CA  1 
ATOM   745  C  C   . HIS   A 1 91  ? 9.116  11.396  8.656  1.00 14.85  ? 97  HIS   A C   1 
ATOM   746  O  O   . HIS   A 1 91  ? 9.943  10.564  9.065  1.00 15.33  ? 97  HIS   A O   1 
ATOM   747  C  CB  . HIS   A 1 91  ? 10.902 12.107  6.937  1.00 17.32  ? 97  HIS   A CB  1 
ATOM   748  C  CG  . HIS   A 1 91  ? 11.181 12.687  5.574  1.00 18.52  ? 97  HIS   A CG  1 
ATOM   749  N  ND1 . HIS   A 1 91  ? 11.294 11.871  4.458  1.00 19.99  ? 97  HIS   A ND1 1 
ATOM   750  C  CD2 . HIS   A 1 91  ? 11.342 13.979  5.199  1.00 21.04  ? 97  HIS   A CD2 1 
ATOM   751  C  CE1 . HIS   A 1 91  ? 11.530 12.702  3.432  1.00 21.03  ? 97  HIS   A CE1 1 
ATOM   752  N  NE2 . HIS   A 1 91  ? 11.558 13.969  3.835  1.00 22.16  ? 97  HIS   A NE2 1 
ATOM   753  N  N   . LEU   A 1 92  ? 7.991  11.621  9.268  1.00 13.94  ? 98  LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 92  ? 7.655  11.084  10.600 1.00 14.30  ? 98  LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 92  ? 6.581  10.009  10.433 1.00 14.42  ? 98  LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 92  ? 5.650  10.182  9.633  1.00 15.14  ? 98  LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 92  ? 7.119  12.222  11.501 1.00 15.87  ? 98  LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 92  ? 6.823  11.807  12.974 1.00 17.62  ? 98  LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 92  ? 8.082  11.504  13.736 1.00 16.77  ? 98  LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 92  ? 6.093  12.931  13.735 1.00 20.42  ? 98  LEU   A CD2 1 
ATOM   761  N  N   . MET   A 1 93  ? 6.711  8.916   11.195 1.00 14.16  ? 99  MET   A N   1 
ATOM   762  C  CA  . MET   A 1 93  ? 5.751  7.789   11.163 1.00 14.17  ? 99  MET   A CA  1 
ATOM   763  C  C   . MET   A 1 93  ? 5.175  7.645   12.560 1.00 14.01  ? 99  MET   A C   1 
ATOM   764  O  O   . MET   A 1 93  ? 5.937  7.715   13.536 1.00 14.53  ? 99  MET   A O   1 
ATOM   765  C  CB  . MET   A 1 93  ? 6.518  6.507   10.825 1.00 14.26  ? 99  MET   A CB  1 
ATOM   766  C  CG  . MET   A 1 93  ? 7.128  6.593   9.445  1.00 15.28  ? 99  MET   A CG  1 
ATOM   767  S  SD  . MET   A 1 93  ? 8.237  5.234   8.985  1.00 18.43  ? 99  MET   A SD  1 
ATOM   768  C  CE  . MET   A 1 93  ? 9.588  5.497   10.241 1.00 20.69  ? 99  MET   A CE  1 
ATOM   769  N  N   . LEU   A 1 94  ? 3.860  7.412   12.700 1.00 13.38  ? 100 LEU   A N   1 
ATOM   770  C  CA  . LEU   A 1 94  ? 3.283  7.281   14.026 1.00 14.21  ? 100 LEU   A CA  1 
ATOM   771  C  C   . LEU   A 1 94  ? 2.778  5.857   14.296 1.00 13.42  ? 100 LEU   A C   1 
ATOM   772  O  O   . LEU   A 1 94  ? 2.339  5.141   13.360 1.00 15.24  ? 100 LEU   A O   1 
ATOM   773  C  CB  . LEU   A 1 94  ? 2.050  8.232   14.210 1.00 16.14  ? 100 LEU   A CB  1 
ATOM   774  C  CG  . LEU   A 1 94  ? 2.317  9.707   14.209 1.00 20.39  ? 100 LEU   A CG  1 
ATOM   775  C  CD1 . LEU   A 1 94  ? 1.013  10.505  14.549 1.00 22.94  ? 100 LEU   A CD1 1 
ATOM   776  C  CD2 . LEU   A 1 94  ? 3.335  10.115  15.267 1.00 22.97  ? 100 LEU   A CD2 1 
ATOM   777  N  N   . ALA   A 1 95  ? 2.850  5.465   15.544 1.00 13.40  ? 101 ALA   A N   1 
ATOM   778  C  CA  . ALA   A 1 95  ? 2.293  4.161   15.999 1.00 12.19  ? 101 ALA   A CA  1 
ATOM   779  C  C   . ALA   A 1 95  ? 1.669  4.366   17.386 1.00 13.08  ? 101 ALA   A C   1 
ATOM   780  O  O   . ALA   A 1 95  ? 1.957  5.365   18.081 1.00 13.55  ? 101 ALA   A O   1 
ATOM   781  C  CB  . ALA   A 1 95  ? 3.392  3.088   16.118 1.00 13.74  ? 101 ALA   A CB  1 
ATOM   782  N  N   . VAL   A 1 96  ? 0.837  3.406   17.813 1.00 12.30  ? 102 VAL   A N   1 
ATOM   783  C  CA  . VAL   A 1 96  ? 0.321  3.416   19.154 1.00 12.14  ? 102 VAL   A CA  1 
ATOM   784  C  C   . VAL   A 1 96  ? 1.329  2.673   20.054 1.00 13.10  ? 102 VAL   A C   1 
ATOM   785  O  O   . VAL   A 1 96  ? 1.652  1.508   19.826 1.00 15.38  ? 102 VAL   A O   1 
ATOM   786  C  CB  . VAL   A 1 96  ? -1.049 2.727   19.174 1.00 12.27  ? 102 VAL   A CB  1 
ATOM   787  C  CG1 . VAL   A 1 96  ? -1.546 2.574   20.633 1.00 14.18  ? 102 VAL   A CG1 1 
ATOM   788  C  CG2 . VAL   A 1 96  ? -2.029 3.519   18.315 1.00 13.16  ? 102 VAL   A CG2 1 
ATOM   789  N  N   . GLY   A 1 97  ? 1.824  3.406   21.051 1.00 13.76  ? 103 GLY   A N   1 
ATOM   790  C  CA  . GLY   A 1 97  ? 2.809  2.830   21.970 1.00 15.15  ? 103 GLY   A CA  1 
ATOM   791  C  C   . GLY   A 1 97  ? 3.280  3.866   22.958 1.00 16.12  ? 103 GLY   A C   1 
ATOM   792  O  O   . GLY   A 1 97  ? 3.019  5.044   22.848 1.00 17.96  ? 103 GLY   A O   1 
ATOM   793  N  N   . HIS   A 1 98  ? 3.493  3.070   24.071 1.00 18.14  ? 104 HIS   A N   1 
ATOM   794  C  CA  . HIS   A 1 98  ? 4.027  3.779   25.223 1.00 18.82  ? 104 HIS   A CA  1 
ATOM   795  C  C   . HIS   A 1 98  ? 5.342  4.544   24.857 1.00 17.88  ? 104 HIS   A C   1 
ATOM   796  O  O   . HIS   A 1 98  ? 6.251  3.858   24.319 1.00 17.40  ? 104 HIS   A O   1 
ATOM   797  C  CB  . HIS   A 1 98  ? 4.201  2.829   26.416 1.00 20.08  ? 104 HIS   A CB  1 
ATOM   798  C  CG  . HIS   A 1 98  ? 4.844  3.699   27.439 1.00 20.27  ? 104 HIS   A CG  1 
ATOM   799  N  ND1 . HIS   A 1 98  ? 4.176  4.800   27.959 1.00 20.96  ? 104 HIS   A ND1 1 
ATOM   800  C  CD2 . HIS   A 1 98  ? 6.116  3.803   27.873 1.00 21.75  ? 104 HIS   A CD2 1 
ATOM   801  C  CE1 . HIS   A 1 98  ? 4.982  5.495   28.732 1.00 21.03  ? 104 HIS   A CE1 1 
ATOM   802  N  NE2 . HIS   A 1 98  ? 6.186  4.901   28.689 1.00 21.56  ? 104 HIS   A NE2 1 
ATOM   803  N  N   . SER   A 1 99  ? 5.421  5.871   24.973 1.00 18.09  ? 105 SER   A N   1 
ATOM   804  C  CA  . SER   A 1 99  ? 6.628  6.758   24.812 1.00 19.89  ? 105 SER   A CA  1 
ATOM   805  C  C   . SER   A 1 99  ? 6.804  7.847   25.907 1.00 21.80  ? 105 SER   A C   1 
ATOM   806  O  O   . SER   A 1 99  ? 5.784  8.372   26.269 1.00 24.77  ? 105 SER   A O   1 
ATOM   807  C  CB  . SER   A 1 99  ? 6.725  7.455   23.325 1.00 21.76  ? 105 SER   A CB  1 
ATOM   808  O  OG  . SER   A 1 99  ? 5.824  8.479   23.080 1.00 29.57  ? 105 SER   A OG  1 
ATOM   809  N  N   . GLU   A 1 100 ? 8.066  8.253   26.240 1.00 17.31  ? 106 GLU   A N   1 
ATOM   810  C  CA  . GLU   A 1 100 ? 8.478  9.399   27.099 1.00 18.21  ? 106 GLU   A CA  1 
ATOM   811  C  C   . GLU   A 1 100 ? 9.753  9.932   26.473 1.00 19.02  ? 106 GLU   A C   1 
ATOM   812  O  O   . GLU   A 1 100 ? 10.429 9.265   25.680 1.00 17.55  ? 106 GLU   A O   1 
ATOM   813  C  CB  . GLU   A 1 100 ? 9.041  9.141   28.507 1.00 19.81  ? 106 GLU   A CB  1 
ATOM   814  C  CG  . GLU   A 1 100 ? 7.878  8.890   29.432 1.00 23.01  ? 106 GLU   A CG  1 
ATOM   815  C  CD  . GLU   A 1 100 ? 8.127  7.971   30.612 1.00 25.52  ? 106 GLU   A CD  1 
ATOM   816  O  OE1 . GLU   A 1 100 ? 8.952  8.344   31.413 1.00 29.86  ? 106 GLU   A OE1 1 
ATOM   817  O  OE2 . GLU   A 1 100 ? 7.492  6.891   30.700 1.00 23.00  ? 106 GLU   A OE2 1 
ATOM   818  N  N   . PRO   A 1 101 ? 10.230 11.089  26.892 1.00 20.00  ? 107 PRO   A N   1 
ATOM   819  C  CA  . PRO   A 1 101 ? 11.279 11.780  26.112 1.00 19.11  ? 107 PRO   A CA  1 
ATOM   820  C  C   . PRO   A 1 101 ? 12.549 11.022  25.888 1.00 17.70  ? 107 PRO   A C   1 
ATOM   821  O  O   . PRO   A 1 101 ? 12.956 10.919  24.815 1.00 17.79  ? 107 PRO   A O   1 
ATOM   822  C  CB  . PRO   A 1 101 ? 11.733 12.949  27.005 1.00 20.78  ? 107 PRO   A CB  1 
ATOM   823  C  CG  . PRO   A 1 101 ? 10.442 13.291  27.763 1.00 22.65  ? 107 PRO   A CG  1 
ATOM   824  C  CD  . PRO   A 1 101 ? 9.729  11.963  27.976 1.00 20.97  ? 107 PRO   A CD  1 
ATOM   825  N  N   . GLY   A 1 102 ? 13.203 10.729  26.990 1.00 16.96  ? 108 GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 102 ? 14.422 9.908   26.974 1.00 16.85  ? 108 GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 102 ? 14.377 8.613   26.208 1.00 14.46  ? 108 GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 102 ? 15.370 8.039   25.996 1.00 15.14  ? 108 GLY   A O   1 
ATOM   829  N  N   . ASP   A 1 103 ? 13.220 8.199   25.777 1.00 13.81  ? 109 ASP   A N   1 
ATOM   830  C  CA  . ASP   A 1 103 ? 13.155 7.066   24.808 1.00 13.19  ? 109 ASP   A CA  1 
ATOM   831  C  C   . ASP   A 1 103 ? 13.677 7.491   23.419 1.00 12.58  ? 109 ASP   A C   1 
ATOM   832  O  O   . ASP   A 1 103 ? 13.938 6.596   22.629 1.00 12.25  ? 109 ASP   A O   1 
ATOM   833  C  CB  . ASP   A 1 103 ? 11.727 6.540   24.687 1.00 12.90  ? 109 ASP   A CB  1 
ATOM   834  C  CG  . ASP   A 1 103 ? 11.271 5.738   25.884 1.00 14.13  ? 109 ASP   A CG  1 
ATOM   835  O  OD1 . ASP   A 1 103 ? 12.135 5.065   26.484 1.00 14.46  ? 109 ASP   A OD1 1 
ATOM   836  O  OD2 . ASP   A 1 103 ? 10.062 5.820   26.205 1.00 14.68  ? 109 ASP   A OD2 1 
ATOM   837  N  N   . CYS   A 1 104 ? 13.772 8.791   23.122 1.00 12.12  ? 110 CYS   A N   1 
ATOM   838  C  CA  . CYS   A 1 104 ? 14.194 9.128   21.735 1.00 12.78  ? 110 CYS   A CA  1 
ATOM   839  C  C   . CYS   A 1 104 ? 15.526 8.393   21.525 1.00 12.30  ? 110 CYS   A C   1 
ATOM   840  O  O   . CYS   A 1 104 ? 16.319 8.310   22.477 1.00 13.07  ? 110 CYS   A O   1 
ATOM   841  C  CB  . CYS   A 1 104 ? 14.288 10.635  21.552 1.00 12.76  ? 110 CYS   A CB  1 
ATOM   842  S  SG  . CYS   A 1 104 ? 12.665 11.448  21.517 1.00 15.63  ? 110 CYS   A SG  1 
ATOM   843  N  N   . GLY   A 1 105 ? 15.695 7.895   20.324 1.00 10.72  ? 111 GLY   A N   1 
ATOM   844  C  CA  . GLY   A 1 105 ? 16.938 7.181   19.988 1.00 11.63  ? 111 GLY   A CA  1 
ATOM   845  C  C   . GLY   A 1 105 ? 16.734 5.673   19.864 1.00 11.71  ? 111 GLY   A C   1 
ATOM   846  O  O   . GLY   A 1 105 ? 17.586 5.020   19.325 1.00 11.81  ? 111 GLY   A O   1 
ATOM   847  N  N   . GLY   A 1 106 ? 15.634 5.163   20.429 1.00 10.96  ? 112 GLY   A N   1 
ATOM   848  C  CA  . GLY   A 1 106 ? 15.347 3.738   20.310 1.00 11.55  ? 112 GLY   A CA  1 
ATOM   849  C  C   . GLY   A 1 106 ? 15.079 3.337   18.864 1.00 9.97   ? 112 GLY   A C   1 
ATOM   850  O  O   . GLY   A 1 106 ? 14.406 4.091   18.131 1.00 10.78  ? 112 GLY   A O   1 
ATOM   851  N  N   . ILE   A 1 107 ? 15.571 2.191   18.438 1.00 10.32  ? 113 ILE   A N   1 
ATOM   852  C  CA  . ILE   A 1 107 ? 15.396 1.798   17.033 1.00 10.08  ? 113 ILE   A CA  1 
ATOM   853  C  C   . ILE   A 1 107 ? 14.054 1.147   16.752 1.00 9.47   ? 113 ILE   A C   1 
ATOM   854  O  O   . ILE   A 1 107 ? 13.601 0.304   17.564 1.00 10.15  ? 113 ILE   A O   1 
ATOM   855  C  CB  . ILE   A 1 107 ? 16.553 0.812   16.686 1.00 10.79  ? 113 ILE   A CB  1 
ATOM   856  C  CG1 . ILE   A 1 107 ? 17.853 1.669   16.429 1.00 12.71  ? 113 ILE   A CG1 1 
ATOM   857  C  CG2 . ILE   A 1 107 ? 16.255 -0.045  15.456 1.00 12.37  ? 113 ILE   A CG2 1 
ATOM   858  C  CD1 . ILE   A 1 107 ? 19.131 0.819   16.245 1.00 15.74  ? 113 ILE   A CD1 1 
ATOM   859  N  N   . LEU   A 1 108 ? 13.481 1.494   15.617 1.00 9.29   ? 114 LEU   A N   1 
ATOM   860  C  CA  . LEU   A 1 108 ? 12.378 0.770   14.992 1.00 9.55   ? 114 LEU   A CA  1 
ATOM   861  C  C   . LEU   A 1 108 ? 12.981 -0.068  13.858 1.00 9.24   ? 114 LEU   A C   1 
ATOM   862  O  O   . LEU   A 1 108 ? 13.747 0.481   13.028 1.00 10.60  ? 114 LEU   A O   1 
ATOM   863  C  CB  . LEU   A 1 108 ? 11.397 1.793   14.394 1.00 9.90   ? 114 LEU   A CB  1 
ATOM   864  C  CG  . LEU   A 1 108 ? 10.258 1.194   13.523 1.00 10.68  ? 114 LEU   A CG  1 
ATOM   865  C  CD1 . LEU   A 1 108 ? 9.270  0.397   14.379 1.00 12.05  ? 114 LEU   A CD1 1 
ATOM   866  C  CD2 . LEU   A 1 108 ? 9.488  2.326   12.780 1.00 12.77  ? 114 LEU   A CD2 1 
ATOM   867  N  N   . ARG   A 1 109 ? 12.650 -1.342  13.803 1.00 9.88   ? 115 ARG   A N   1 
ATOM   868  C  CA  . ARG   A 1 109 ? 13.212 -2.251  12.764 1.00 10.39  ? 115 ARG   A CA  1 
ATOM   869  C  C   . ARG   A 1 109 ? 12.112 -3.120  12.208 1.00 11.36  ? 115 ARG   A C   1 
ATOM   870  O  O   . ARG   A 1 109 ? 11.121 -3.447  12.869 1.00 11.47  ? 115 ARG   A O   1 
ATOM   871  C  CB  . ARG   A 1 109 ? 14.366 -3.095  13.354 1.00 11.96  ? 115 ARG   A CB  1 
ATOM   872  C  CG  . ARG   A 1 109 ? 13.891 -4.076  14.456 1.00 12.54  ? 115 ARG   A CG  1 
ATOM   873  C  CD  . ARG   A 1 109 ? 15.113 -4.799  15.025 1.00 14.07  ? 115 ARG   A CD  1 
ATOM   874  N  NE  . ARG   A 1 109 ? 15.933 -3.921  15.858 1.00 15.36  ? 115 ARG   A NE  1 
ATOM   875  C  CZ  . ARG   A 1 109 ? 17.237 -3.744  15.734 1.00 15.20  ? 115 ARG   A CZ  1 
ATOM   876  N  NH1 . ARG   A 1 109 ? 17.886 -4.196  14.650 1.00 16.35  ? 115 ARG   A NH1 1 
ATOM   877  N  NH2 . ARG   A 1 109 ? 17.901 -3.036  16.636 1.00 16.76  ? 115 ARG   A NH2 1 
ATOM   878  N  N   . CYS   A 1 110 ? 12.328 -3.593  10.977 1.00 14.07  ? 116 CYS   A N   1 
ATOM   879  C  CA  . CYS   A 1 110 ? 11.376 -4.507  10.261 1.00 17.30  ? 116 CYS   A CA  1 
ATOM   880  C  C   . CYS   A 1 110 ? 12.192 -5.666  9.805  1.00 20.28  ? 116 CYS   A C   1 
ATOM   881  O  O   . CYS   A 1 110 ? 13.374 -5.841  10.185 1.00 20.14  ? 116 CYS   A O   1 
ATOM   882  C  CB  . CYS   A 1 110 ? 10.702 -3.790  9.093  1.00 16.39  ? 116 CYS   A CB  1 
ATOM   883  S  SG  . CYS   A 1 110 ? 11.841 -3.391  7.744  1.00 17.27  ? 116 CYS   A SG  1 
ATOM   884  N  N   . GLN   A 1 111 ? 11.534 -6.564  8.999  1.00 21.32  ? 117 GLN   A N   1 
ATOM   885  C  CA  . GLN   A 1 111 ? 12.250 -7.711  8.485  1.00 24.14  ? 117 GLN   A CA  1 
ATOM   886  C  C   . GLN   A 1 111 ? 13.484 -7.367  7.632  1.00 25.55  ? 117 GLN   A C   1 
ATOM   887  O  O   . GLN   A 1 111 ? 14.387 -8.196  7.504  1.00 29.08  ? 117 GLN   A O   1 
ATOM   888  C  CB  . GLN   A 1 111 ? 11.291 -8.653  7.702  1.00 28.18  ? 117 GLN   A CB  1 
ATOM   889  C  CG  . GLN   A 1 111 ? 10.860 -8.061  6.375  1.00 30.78  ? 117 GLN   A CG  1 
ATOM   890  C  CD  . GLN   A 1 111 ? 9.925  -8.979  5.624  1.00 36.65  ? 117 GLN   A CD  1 
ATOM   891  O  OE1 . GLN   A 1 111 ? 8.696  -8.876  5.741  1.00 39.76  ? 117 GLN   A OE1 1 
ATOM   892  N  NE2 . GLN   A 1 111 ? 10.503 -9.883  4.839  1.00 35.29  ? 117 GLN   A NE2 1 
ATOM   893  N  N   . HIS   A 1 112 ? 13.564 -6.162  7.083  1.00 20.96  ? 118 HIS   A N   1 
ATOM   894  C  CA  . HIS   A 1 112 ? 14.684 -5.757  6.188  1.00 21.04  ? 118 HIS   A CA  1 
ATOM   895  C  C   . HIS   A 1 112 ? 15.862 -5.058  6.917  1.00 21.76  ? 118 HIS   A C   1 
ATOM   896  O  O   . HIS   A 1 112 ? 16.905 -4.784  6.305  1.00 24.25  ? 118 HIS   A O   1 
ATOM   897  C  CB  . HIS   A 1 112 ? 14.093 -4.840  5.112  1.00 21.73  ? 118 HIS   A CB  1 
ATOM   898  C  CG  . HIS   A 1 112 ? 12.960 -5.489  4.337  1.00 24.35  ? 118 HIS   A CG  1 
ATOM   899  N  ND1 . HIS   A 1 112 ? 11.623 -5.082  4.458  1.00 20.70  ? 118 HIS   A ND1 1 
ATOM   900  C  CD2 . HIS   A 1 112 ? 13.022 -6.405  3.336  1.00 26.74  ? 118 HIS   A CD2 1 
ATOM   901  C  CE1 . HIS   A 1 112 ? 10.921 -5.868  3.644  1.00 26.06  ? 118 HIS   A CE1 1 
ATOM   902  N  NE2 . HIS   A 1 112 ? 11.721 -6.689  2.968  1.00 29.41  ? 118 HIS   A NE2 1 
ATOM   903  N  N   . GLY   A 1 113 ? 15.678 -4.626  8.190  1.00 19.24  ? 119 GLY   A N   1 
ATOM   904  C  CA  . GLY   A 1 113 ? 16.725 -3.888  8.896  1.00 18.00  ? 119 GLY   A CA  1 
ATOM   905  C  C   . GLY   A 1 113 ? 16.153 -2.701  9.669  1.00 14.79  ? 119 GLY   A C   1 
ATOM   906  O  O   . GLY   A 1 113 ? 14.966 -2.670  10.006 1.00 14.41  ? 119 GLY   A O   1 
ATOM   907  N  N   . VAL   A 1 114 ? 17.018 -1.696  9.939  1.00 13.15  ? 120 VAL   A N   1 
ATOM   908  C  CA  . VAL   A 1 114 ? 16.585 -0.504  10.715 1.00 12.77  ? 120 VAL   A CA  1 
ATOM   909  C  C   . VAL   A 1 114 ? 15.745 0.418   9.872  1.00 11.43  ? 120 VAL   A C   1 
ATOM   910  O  O   . VAL   A 1 114 ? 16.131 0.756   8.728  1.00 12.41  ? 120 VAL   A O   1 
ATOM   911  C  CB  . VAL   A 1 114 ? 17.809 0.251   11.291 1.00 12.44  ? 120 VAL   A CB  1 
ATOM   912  C  CG1 . VAL   A 1 114 ? 17.397 1.574   11.937 1.00 13.79  ? 120 VAL   A CG1 1 
ATOM   913  C  CG2 . VAL   A 1 114 ? 18.593 -0.628  12.259 1.00 14.55  ? 120 VAL   A CG2 1 
ATOM   914  N  N   . VAL   A 1 115 ? 14.601 0.816   10.385 1.00 10.61  ? 121 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 115 ? 13.667 1.694   9.730  1.00 10.62  ? 121 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 115 ? 13.811 3.133   10.142 1.00 10.57  ? 121 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 115 ? 13.665 4.067   9.350  1.00 11.97  ? 121 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 115 ? 12.209 1.212   9.984  1.00 12.52  ? 121 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 115 ? 11.139 2.205   9.467  1.00 15.04  ? 121 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 115 ? 11.966 -0.187  9.453  1.00 14.30  ? 121 VAL   A CG2 1 
ATOM   921  N  N   . GLY   A 1 116 ? 14.011 3.365   11.440 1.00 10.87  ? 122 GLY   A N   1 
ATOM   922  C  CA  . GLY   A 1 116 ? 14.110 4.732   11.963 1.00 11.78  ? 122 GLY   A CA  1 
ATOM   923  C  C   . GLY   A 1 116 ? 14.361 4.745   13.463 1.00 10.25  ? 122 GLY   A C   1 
ATOM   924  O  O   . GLY   A 1 116 ? 14.665 3.675   14.039 1.00 10.56  ? 122 GLY   A O   1 
ATOM   925  N  N   . ILE   A 1 117 ? 14.192 5.943   14.083 1.00 10.14  ? 123 ILE   A N   1 
ATOM   926  C  CA  . ILE   A 1 117 ? 14.511 6.078   15.541 1.00 10.25  ? 123 ILE   A CA  1 
ATOM   927  C  C   . ILE   A 1 117 ? 13.406 6.889   16.191 1.00 10.80  ? 123 ILE   A C   1 
ATOM   928  O  O   . ILE   A 1 117 ? 12.857 7.837   15.518 1.00 11.38  ? 123 ILE   A O   1 
ATOM   929  C  CB  . ILE   A 1 117 ? 15.859 6.803   15.807 1.00 11.22  ? 123 ILE   A CB  1 
ATOM   930  C  CG1 . ILE   A 1 117 ? 16.012 8.119   15.040 1.00 13.18  ? 123 ILE   A CG1 1 
ATOM   931  C  CG2 . ILE   A 1 117 ? 17.004 5.844   15.544 1.00 12.98  ? 123 ILE   A CG2 1 
ATOM   932  C  CD1 . ILE   A 1 117 ? 17.223 8.904   15.481 1.00 14.06  ? 123 ILE   A CD1 1 
ATOM   933  N  N   . VAL   A 1 118 ? 13.238 6.613   17.470 1.00 10.58  ? 124 VAL   A N   1 
ATOM   934  C  CA  . VAL   A 1 118 ? 12.183 7.331   18.221 1.00 10.95  ? 124 VAL   A CA  1 
ATOM   935  C  C   . VAL   A 1 118 ? 12.494 8.844   18.281 1.00 11.78  ? 124 VAL   A C   1 
ATOM   936  O  O   . VAL   A 1 118 ? 13.624 9.171   18.446 1.00 10.92  ? 124 VAL   A O   1 
ATOM   937  C  CB  . VAL   A 1 118 ? 12.047 6.724   19.597 1.00 10.91  ? 124 VAL   A CB  1 
ATOM   938  C  CG1 . VAL   A 1 118 ? 11.227 7.612   20.524 1.00 11.34  ? 124 VAL   A CG1 1 
ATOM   939  C  CG2 . VAL   A 1 118 ? 11.479 5.305   19.597 1.00 11.38  ? 124 VAL   A CG2 1 
ATOM   940  N  N   . SER   A 1 119 ? 11.487 9.686   18.183 1.00 11.59  ? 125 SER   A N   1 
ATOM   941  C  CA  . SER   A 1 119 ? 11.618 11.163  18.050 1.00 12.92  ? 125 SER   A CA  1 
ATOM   942  C  C   . SER   A 1 119 ? 10.482 11.877  18.759 1.00 14.09  ? 125 SER   A C   1 
ATOM   943  O  O   . SER   A 1 119 ? 10.832 12.906  19.381 1.00 15.60  ? 125 SER   A O   1 
ATOM   944  C  CB  . SER   A 1 119 ? 11.659 11.448  16.552 1.00 13.21  ? 125 SER   A CB  1 
ATOM   945  O  OG  . SER   A 1 119 ? 11.807 12.857  16.242 1.00 15.76  ? 125 SER   A OG  1 
ATOM   946  N  N   . THR   A 1 120 ? 9.211  11.425  18.657 1.00 14.49  ? 126 THR   A N   1 
ATOM   947  C  CA  . THR   A 1 120 ? 7.988  12.136  19.232 1.00 15.78  ? 126 THR   A CA  1 
ATOM   948  C  C   . THR   A 1 120 ? 6.979  11.130  19.828 1.00 17.75  ? 126 THR   A C   1 
ATOM   949  O  O   . THR   A 1 120 ? 7.289  9.953   19.764 1.00 15.92  ? 126 THR   A O   1 
ATOM   950  C  CB  . THR   A 1 120 ? 7.162  12.827  18.129 1.00 17.17  ? 126 THR   A CB  1 
ATOM   951  O  OG1 . THR   A 1 120 ? 6.521  11.876  17.288 1.00 18.01  ? 126 THR   A OG1 1 
ATOM   952  C  CG2 . THR   A 1 120 ? 8.007  13.716  17.239 1.00 17.33  ? 126 THR   A CG2 1 
ATOM   953  N  N   . GLY   A 1 121 ? 5.889  11.593  20.480 1.00 20.00  ? 127 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 121 ? 4.951  10.654  21.139 1.00 22.18  ? 127 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 121 ? 4.262  11.222  22.365 1.00 25.78  ? 127 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 121 ? 4.024  12.415  22.473 1.00 28.54  ? 127 GLY   A O   1 
ATOM   957  N  N   . GLY   A 1 122 ? 3.827  10.306  23.225 1.00 26.83  ? 128 GLY   A N   1 
ATOM   958  C  CA  . GLY   A 1 122 ? 3.007  10.781  24.379 1.00 27.85  ? 128 GLY   A CA  1 
ATOM   959  C  C   . GLY   A 1 122 ? 1.535  10.403  24.160 1.00 30.31  ? 128 GLY   A C   1 
ATOM   960  O  O   . GLY   A 1 122 ? 1.179  10.172  23.035 1.00 31.23  ? 128 GLY   A O   1 
ATOM   961  N  N   . ASN   A 1 123 ? 0.760  10.411  25.213 1.00 29.07  ? 129 ASN   A N   1 
ATOM   962  C  CA  . ASN   A 1 123 ? -0.651 9.888   25.158 1.00 30.62  ? 129 ASN   A CA  1 
ATOM   963  C  C   . ASN   A 1 123 ? -0.788 8.544   24.365 1.00 28.88  ? 129 ASN   A C   1 
ATOM   964  O  O   . ASN   A 1 123 ? -1.925 8.388   23.757 1.00 28.92  ? 129 ASN   A O   1 
ATOM   965  C  CB  . ASN   A 1 123 ? -1.705 10.986  24.862 1.00 33.28  ? 129 ASN   A CB  1 
ATOM   966  C  CG  . ASN   A 1 123 ? -1.563 12.271  25.628 1.00 37.30  ? 129 ASN   A CG  1 
ATOM   967  O  OD1 . ASN   A 1 123 ? -1.908 12.312  26.807 1.00 40.27  ? 129 ASN   A OD1 1 
ATOM   968  N  ND2 . ASN   A 1 123 ? -1.186 13.330  24.921 1.00 36.22  ? 129 ASN   A ND2 1 
ATOM   969  N  N   . GLY   A 1 124 ? 0.189  7.615   24.413 1.00 25.46  ? 130 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 124 ? 0.145  6.308   23.721 1.00 23.60  ? 130 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 124 ? 0.451  6.569   22.257 1.00 18.34  ? 130 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 124 ? 0.025  5.749   21.489 1.00 18.95  ? 130 GLY   A O   1 
ATOM   973  N  N   . LEU   A 1 125 ? 1.109  7.743   21.979 1.00 17.76  ? 131 LEU   A N   1 
ATOM   974  C  CA  . LEU   A 1 125 ? 1.680  7.891   20.569 1.00 16.90  ? 131 LEU   A CA  1 
ATOM   975  C  C   . LEU   A 1 125 ? 3.217  7.764   20.613 1.00 17.91  ? 131 LEU   A C   1 
ATOM   976  O  O   . LEU   A 1 125 ? 3.843  7.934   21.721 1.00 21.32  ? 131 LEU   A O   1 
ATOM   977  C  CB  . LEU   A 1 125 ? 1.211  9.071   19.745 1.00 17.93  ? 131 LEU   A CB  1 
ATOM   978  C  CG  . LEU   A 1 125 ? -0.305 9.021   19.496 1.00 18.71  ? 131 LEU   A CG  1 
ATOM   979  C  CD1 . LEU   A 1 125 ? -0.877 10.391  19.244 1.00 22.15  ? 131 LEU   A CD1 1 
ATOM   980  C  CD2 . LEU   A 1 125 ? -0.745 8.040   18.395 1.00 18.82  ? 131 LEU   A CD2 1 
ATOM   981  N  N   . VAL   A 1 126 ? 3.832  7.328   19.549 1.00 13.67  ? 132 VAL   A N   1 
ATOM   982  C  CA  . VAL   A 1 126 ? 5.329  7.276   19.466 1.00 13.61  ? 132 VAL   A CA  1 
ATOM   983  C  C   . VAL   A 1 126 ? 5.586  7.573   18.000 1.00 13.53  ? 132 VAL   A C   1 
ATOM   984  O  O   . VAL   A 1 126 ? 4.869  6.956   17.193 1.00 14.15  ? 132 VAL   A O   1 
ATOM   985  C  CB  . VAL   A 1 126 ? 5.940  5.914   19.855 1.00 13.56  ? 132 VAL   A CB  1 
ATOM   986  C  CG1 . VAL   A 1 126 ? 5.302  4.681   19.236 1.00 15.62  ? 132 VAL   A CG1 1 
ATOM   987  C  CG2 . VAL   A 1 126 ? 7.440  5.936   19.747 1.00 13.14  ? 132 VAL   A CG2 1 
ATOM   988  N  N   . GLY   A 1 127 ? 6.420  8.577   17.770 1.00 13.02  ? 133 GLY   A N   1 
ATOM   989  C  CA  . GLY   A 1 127 ? 6.695  9.042   16.390 1.00 12.72  ? 133 GLY   A CA  1 
ATOM   990  C  C   . GLY   A 1 127 ? 8.128  8.632   16.126 1.00 12.47  ? 133 GLY   A C   1 
ATOM   991  O  O   . GLY   A 1 127 ? 8.982  8.887   17.026 1.00 13.74  ? 133 GLY   A O   1 
ATOM   992  N  N   . PHE   A 1 128 ? 8.334  7.972   14.998 1.00 11.79  ? 134 PHE   A N   1 
ATOM   993  C  CA  . PHE   A 1 128 ? 9.685  7.583   14.526 1.00 11.68  ? 134 PHE   A CA  1 
ATOM   994  C  C   . PHE   A 1 128 ? 10.136 8.433   13.331 1.00 11.66  ? 134 PHE   A C   1 
ATOM   995  O  O   . PHE   A 1 128 ? 9.363  8.472   12.344 1.00 12.64  ? 134 PHE   A O   1 
ATOM   996  C  CB  . PHE   A 1 128 ? 9.633  6.100   14.109 1.00 11.58  ? 134 PHE   A CB  1 
ATOM   997  C  CG  . PHE   A 1 128 ? 9.036  5.193   15.174 1.00 10.80  ? 134 PHE   A CG  1 
ATOM   998  C  CD1 . PHE   A 1 128 ? 9.778  4.714   16.248 1.00 10.97  ? 134 PHE   A CD1 1 
ATOM   999  C  CD2 . PHE   A 1 128 ? 7.710  4.798   15.110 1.00 12.64  ? 134 PHE   A CD2 1 
ATOM   1000 C  CE1 . PHE   A 1 128 ? 9.204  3.899   17.221 1.00 10.97  ? 134 PHE   A CE1 1 
ATOM   1001 C  CE2 . PHE   A 1 128 ? 7.157  3.953   16.064 1.00 12.98  ? 134 PHE   A CE2 1 
ATOM   1002 C  CZ  . PHE   A 1 128 ? 7.891  3.518   17.137 1.00 12.17  ? 134 PHE   A CZ  1 
ATOM   1003 N  N   . ALA   A 1 129 ? 11.347 9.017   13.362 1.00 11.20  ? 135 ALA   A N   1 
ATOM   1004 C  CA  . ALA   A 1 129 ? 12.025 9.671   12.215 1.00 12.18  ? 135 ALA   A CA  1 
ATOM   1005 C  C   . ALA   A 1 129 ? 12.518 8.585   11.236 1.00 11.52  ? 135 ALA   A C   1 
ATOM   1006 O  O   . ALA   A 1 129 ? 13.404 7.830   11.651 1.00 11.96  ? 135 ALA   A O   1 
ATOM   1007 C  CB  . ALA   A 1 129 ? 13.167 10.452  12.833 1.00 11.49  ? 135 ALA   A CB  1 
ATOM   1008 N  N   . ASP   A 1 130 ? 11.931 8.492   10.049 1.00 12.07  ? 136 ASP   A N   1 
ATOM   1009 C  CA  . ASP   A 1 130 ? 12.340 7.495   9.049  1.00 13.09  ? 136 ASP   A CA  1 
ATOM   1010 C  C   . ASP   A 1 130 ? 13.740 7.781   8.532  1.00 12.32  ? 136 ASP   A C   1 
ATOM   1011 O  O   . ASP   A 1 130 ? 14.163 8.945   8.419  1.00 13.39  ? 136 ASP   A O   1 
ATOM   1012 C  CB  . ASP   A 1 130 ? 11.384 7.615   7.830  1.00 15.22  ? 136 ASP   A CB  1 
ATOM   1013 C  CG  . ASP   A 1 130 ? 11.637 6.604   6.764  1.00 17.89  ? 136 ASP   A CG  1 
ATOM   1014 O  OD1 . ASP   A 1 130 ? 11.701 5.389   7.076  1.00 18.02  ? 136 ASP   A OD1 1 
ATOM   1015 O  OD2 . ASP   A 1 130 ? 11.885 7.043   5.605  1.00 21.57  ? 136 ASP   A OD2 1 
ATOM   1016 N  N   . VAL   A 1 131 ? 14.476 6.718   8.237  1.00 12.11  ? 137 VAL   A N   1 
ATOM   1017 C  CA  . VAL   A 1 131 ? 15.816 6.833   7.581  1.00 12.55  ? 137 VAL   A CA  1 
ATOM   1018 C  C   . VAL   A 1 131 ? 15.898 6.026   6.285  1.00 13.16  ? 137 VAL   A C   1 
ATOM   1019 O  O   . VAL   A 1 131 ? 16.960 6.018   5.644  1.00 12.90  ? 137 VAL   A O   1 
ATOM   1020 C  CB  . VAL   A 1 131 ? 16.990 6.458   8.537  1.00 12.38  ? 137 VAL   A CB  1 
ATOM   1021 C  CG1 . VAL   A 1 131 ? 17.000 7.361   9.774  1.00 13.27  ? 137 VAL   A CG1 1 
ATOM   1022 C  CG2 . VAL   A 1 131 ? 16.997 4.982   8.941  1.00 12.78  ? 137 VAL   A CG2 1 
ATOM   1023 N  N   . ARG   A 1 132 ? 14.809 5.338   5.885  1.00 13.49  ? 138 ARG   A N   1 
ATOM   1024 C  CA  . ARG   A 1 132 ? 14.885 4.433   4.732  1.00 13.56  ? 138 ARG   A CA  1 
ATOM   1025 C  C   . ARG   A 1 132 ? 15.145 5.148   3.396  1.00 15.15  ? 138 ARG   A C   1 
ATOM   1026 O  O   . ARG   A 1 132 ? 15.593 4.486   2.421  1.00 16.25  ? 138 ARG   A O   1 
ATOM   1027 C  CB  . ARG   A 1 132 ? 13.604 3.591   4.639  1.00 14.90  ? 138 ARG   A CB  1 
ATOM   1028 C  CG  . ARG   A 1 132 ? 13.486 2.626   5.845  1.00 13.11  ? 138 ARG   A CG  1 
ATOM   1029 C  CD  . ARG   A 1 132 ? 12.172 1.858   5.725  1.00 15.30  ? 138 ARG   A CD  1 
ATOM   1030 N  NE  . ARG   A 1 132 ? 11.059 2.802   5.944  1.00 14.68  ? 138 ARG   A NE  1 
ATOM   1031 C  CZ  . ARG   A 1 132 ? 9.770  2.446   6.025  1.00 17.55  ? 138 ARG   A CZ  1 
ATOM   1032 N  NH1 . ARG   A 1 132 ? 9.405  1.217   5.727  1.00 17.49  ? 138 ARG   A NH1 1 
ATOM   1033 N  NH2 . ARG   A 1 132 ? 8.852  3.340   6.386  1.00 18.18  ? 138 ARG   A NH2 1 
ATOM   1034 N  N   . ASP   A 1 133 ? 14.846 6.475   3.292  1.00 14.24  ? 139 ASP   A N   1 
ATOM   1035 C  CA  . ASP   A 1 133 ? 15.119 7.189   2.053  1.00 15.83  ? 139 ASP   A CA  1 
ATOM   1036 C  C   . ASP   A 1 133 ? 16.551 7.685   1.960  1.00 15.72  ? 139 ASP   A C   1 
ATOM   1037 O  O   . ASP   A 1 133 ? 16.925 8.211   0.908  1.00 17.77  ? 139 ASP   A O   1 
ATOM   1038 C  CB  . ASP   A 1 133 ? 14.155 8.404   1.945  1.00 18.13  ? 139 ASP   A CB  1 
ATOM   1039 C  CG  . ASP   A 1 133 ? 14.375 9.433   3.038  1.00 19.97  ? 139 ASP   A CG  1 
ATOM   1040 O  OD1 . ASP   A 1 133 ? 14.532 9.045   4.211  1.00 18.83  ? 139 ASP   A OD1 1 
ATOM   1041 O  OD2 . ASP   A 1 133 ? 14.362 10.649  2.741  1.00 22.83  ? 139 ASP   A OD2 1 
ATOM   1042 N  N   . LEU   A 1 134 ? 17.357 7.583   3.030  1.00 14.18  ? 140 LEU   A N   1 
ATOM   1043 C  CA  . LEU   A 1 134 ? 18.735 8.124   3.059  1.00 13.80  ? 140 LEU   A CA  1 
ATOM   1044 C  C   . LEU   A 1 134 ? 19.674 7.078   2.493  1.00 14.68  ? 140 LEU   A C   1 
ATOM   1045 O  O   . LEU   A 1 134 ? 20.380 6.366   3.235  1.00 14.99  ? 140 LEU   A O   1 
ATOM   1046 C  CB  . LEU   A 1 134 ? 19.088 8.506   4.497  1.00 13.99  ? 140 LEU   A CB  1 
ATOM   1047 C  CG  . LEU   A 1 134 ? 18.150 9.560   5.180  1.00 15.05  ? 140 LEU   A CG  1 
ATOM   1048 C  CD1 . LEU   A 1 134 ? 18.555 9.772   6.626  1.00 15.92  ? 140 LEU   A CD1 1 
ATOM   1049 C  CD2 . LEU   A 1 134 ? 18.134 10.899  4.430  1.00 17.52  ? 140 LEU   A CD2 1 
ATOM   1050 N  N   . LEU   A 1 135 ? 19.650 6.931   1.155  1.00 14.60  ? 141 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 135 ? 20.383 5.818   0.531  1.00 15.93  ? 141 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 135 ? 21.883 5.908   0.679  1.00 16.18  ? 141 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 135 ? 22.605 4.899   0.715  1.00 17.74  ? 141 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 135 ? 20.016 5.696   -0.982 1.00 17.81  ? 141 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 135 ? 18.497 5.710   -1.282 1.00 19.06  ? 141 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 135 ? 18.293 5.372   -2.778 1.00 22.21  ? 141 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 135 ? 17.702 4.698   -0.456 1.00 21.08  ? 141 LEU   A CD2 1 
ATOM   1058 N  N   . TRP   A 1 136 ? 22.373 7.140   0.828  1.00 15.09  ? 142 TRP   A N   1 
ATOM   1059 C  CA  . TRP   A 1 136 ? 23.792 7.408   1.000  1.00 15.47  ? 142 TRP   A CA  1 
ATOM   1060 C  C   . TRP   A 1 136 ? 24.358 6.823   2.295  1.00 15.64  ? 142 TRP   A C   1 
ATOM   1061 O  O   . TRP   A 1 136 ? 25.577 6.667   2.403  1.00 17.27  ? 142 TRP   A O   1 
ATOM   1062 C  CB  . TRP   A 1 136 ? 24.089 8.924   0.881  1.00 16.07  ? 142 TRP   A CB  1 
ATOM   1063 C  CG  . TRP   A 1 136 ? 23.287 9.752   1.854  1.00 14.54  ? 142 TRP   A CG  1 
ATOM   1064 C  CD1 . TRP   A 1 136 ? 22.152 10.451  1.574  1.00 15.44  ? 142 TRP   A CD1 1 
ATOM   1065 C  CD2 . TRP   A 1 136 ? 23.652 10.088  3.199  1.00 14.69  ? 142 TRP   A CD2 1 
ATOM   1066 N  NE1 . TRP   A 1 136 ? 21.717 11.125  2.709  1.00 16.34  ? 142 TRP   A NE1 1 
ATOM   1067 C  CE2 . TRP   A 1 136 ? 22.639 10.934  3.710  1.00 15.45  ? 142 TRP   A CE2 1 
ATOM   1068 C  CE3 . TRP   A 1 136 ? 24.728 9.752   4.028  1.00 15.09  ? 142 TRP   A CE3 1 
ATOM   1069 C  CZ2 . TRP   A 1 136 ? 22.697 11.462  5.024  1.00 16.03  ? 142 TRP   A CZ2 1 
ATOM   1070 C  CZ3 . TRP   A 1 136 ? 24.785 10.276  5.313  1.00 16.35  ? 142 TRP   A CZ3 1 
ATOM   1071 C  CH2 . TRP   A 1 136 ? 23.789 11.139  5.776  1.00 15.86  ? 142 TRP   A CH2 1 
ATOM   1072 N  N   . LEU   A 1 137 ? 23.517 6.487   3.299  1.00 14.49  ? 143 LEU   A N   1 
ATOM   1073 C  CA  . LEU   A 1 137 ? 24.034 5.828   4.505  1.00 15.69  ? 143 LEU   A CA  1 
ATOM   1074 C  C   . LEU   A 1 137 ? 24.715 4.512   4.179  1.00 17.97  ? 143 LEU   A C   1 
ATOM   1075 O  O   . LEU   A 1 137 ? 25.569 4.073   4.963  1.00 19.23  ? 143 LEU   A O   1 
ATOM   1076 C  CB  . LEU   A 1 137 ? 22.898 5.570   5.503  1.00 15.45  ? 143 LEU   A CB  1 
ATOM   1077 C  CG  . LEU   A 1 137 ? 22.364 6.813   6.209  1.00 14.96  ? 143 LEU   A CG  1 
ATOM   1078 C  CD1 . LEU   A 1 137 ? 21.121 6.447   6.969  1.00 16.52  ? 143 LEU   A CD1 1 
ATOM   1079 C  CD2 . LEU   A 1 137 ? 23.443 7.432   7.155  1.00 16.16  ? 143 LEU   A CD2 1 
ATOM   1080 N  N   . ASP   A 1 138 ? 24.374 3.884   3.008  1.00 19.80  ? 144 ASP   A N   1 
ATOM   1081 C  CA  . ASP   A 1 138 ? 24.943 2.573   2.624  1.00 22.11  ? 144 ASP   A CA  1 
ATOM   1082 C  C   . ASP   A 1 138 ? 26.269 2.645   1.910  1.00 26.54  ? 144 ASP   A C   1 
ATOM   1083 O  O   . ASP   A 1 138 ? 26.789 1.596   1.516  1.00 29.04  ? 144 ASP   A O   1 
ATOM   1084 C  CB  . ASP   A 1 138 ? 23.970 1.791   1.686  1.00 23.73  ? 144 ASP   A CB  1 
ATOM   1085 C  CG  . ASP   A 1 138 ? 22.613 1.499   2.258  1.00 24.93  ? 144 ASP   A CG  1 
ATOM   1086 O  OD1 . ASP   A 1 138 ? 22.458 1.588   3.502  1.00 26.23  ? 144 ASP   A OD1 1 
ATOM   1087 O  OD2 . ASP   A 1 138 ? 21.686 1.170   1.479  1.00 31.87  ? 144 ASP   A OD2 1 
ATOM   1088 N  N   . GLU   A 1 139 ? 26.815 3.837   1.679  1.00 27.35  ? 145 GLU   A N   1 
ATOM   1089 C  CA  . GLU   A 1 139 ? 28.059 3.975   0.897  1.00 31.83  ? 145 GLU   A CA  1 
ATOM   1090 C  C   . GLU   A 1 139 ? 29.038 4.980   1.492  1.00 35.41  ? 145 GLU   A C   1 
ATOM   1091 O  O   . GLU   A 1 139 ? 28.698 5.668   2.456  1.00 35.41  ? 145 GLU   A O   1 
ATOM   1092 C  CB  . GLU   A 1 139 ? 27.662 4.400   -0.523 1.00 36.05  ? 145 GLU   A CB  1 
ATOM   1093 C  CG  . GLU   A 1 139 ? 26.937 5.733   -0.527 1.00 43.96  ? 145 GLU   A CG  1 
ATOM   1094 C  CD  . GLU   A 1 139 ? 26.170 6.110   -1.781 1.00 51.96  ? 145 GLU   A CD  1 
ATOM   1095 O  OE1 . GLU   A 1 139 ? 26.079 7.328   -2.067 1.00 52.78  ? 145 GLU   A OE1 1 
ATOM   1096 O  OE2 . GLU   A 1 139 ? 25.646 5.200   -2.464 1.00 55.24  ? 145 GLU   A OE2 1 
ATOM   1097 N  N   . GLU   A 1 140 ? 30.241 5.098   0.880  1.00 38.73  ? 146 GLU   A N   1 
ATOM   1098 C  CA  . GLU   A 1 140 ? 31.335 6.035   1.190  1.00 42.41  ? 146 GLU   A CA  1 
ATOM   1099 C  C   . GLU   A 1 140 ? 32.135 5.603   2.412  1.00 44.87  ? 146 GLU   A C   1 
ATOM   1100 O  O   . GLU   A 1 140 ? 33.368 5.577   2.331  1.00 46.40  ? 146 GLU   A O   1 
ATOM   1101 C  CB  . GLU   A 1 140 ? 30.846 7.493   1.284  1.00 46.48  ? 146 GLU   A CB  1 
ATOM   1102 C  CG  . GLU   A 1 140 ? 31.781 8.477   1.980  1.00 53.91  ? 146 GLU   A CG  1 
ATOM   1103 C  CD  . GLU   A 1 140 ? 32.659 9.301   1.057  1.00 63.31  ? 146 GLU   A CD  1 
ATOM   1104 O  OE1 . GLU   A 1 140 ? 32.351 10.499  0.867  1.00 65.51  ? 146 GLU   A OE1 1 
ATOM   1105 O  OE2 . GLU   A 1 140 ? 33.652 8.752   0.524  1.00 66.02  ? 146 GLU   A OE2 1 
ATOM   1106 N  N   . SER   B 1 1   ? 21.830 -21.262 7.610  1.00 18.31  ? 7   SER   C N   1 
ATOM   1107 C  CA  . SER   B 1 1   ? 20.681 -21.039 8.536  1.00 17.47  ? 7   SER   C CA  1 
ATOM   1108 C  C   . SER   B 1 1   ? 20.647 -22.166 9.597  1.00 17.62  ? 7   SER   C C   1 
ATOM   1109 O  O   . SER   B 1 1   ? 21.338 -23.195 9.447  1.00 19.27  ? 7   SER   C O   1 
ATOM   1110 C  CB  . SER   B 1 1   ? 19.382 -21.080 7.731  1.00 20.79  ? 7   SER   C CB  1 
ATOM   1111 O  OG  . SER   B 1 1   ? 19.271 -22.356 7.125  1.00 25.95  ? 7   SER   C OG  1 
ATOM   1112 N  N   . GLY   B 1 2   ? 19.882 -21.944 10.671 1.00 16.50  ? 8   GLY   C N   1 
ATOM   1113 C  CA  . GLY   B 1 2   ? 19.686 -22.951 11.709 1.00 16.32  ? 8   GLY   C CA  1 
ATOM   1114 C  C   . GLY   B 1 2   ? 19.410 -22.345 13.059 1.00 15.17  ? 8   GLY   C C   1 
ATOM   1115 O  O   . GLY   B 1 2   ? 19.791 -21.200 13.325 1.00 15.33  ? 8   GLY   C O   1 
ATOM   1116 N  N   . ALA   B 1 3   ? 18.764 -23.086 13.929 1.00 14.34  ? 9   ALA   C N   1 
ATOM   1117 C  CA  . ALA   B 1 3   ? 18.440 -22.597 15.270 1.00 14.52  ? 9   ALA   C CA  1 
ATOM   1118 C  C   . ALA   B 1 3   ? 18.549 -23.715 16.301 1.00 13.43  ? 9   ALA   C C   1 
ATOM   1119 O  O   . ALA   B 1 3   ? 18.622 -24.901 15.927 1.00 14.79  ? 9   ALA   C O   1 
ATOM   1120 C  CB  . ALA   B 1 3   ? 16.998 -22.056 15.255 1.00 16.08  ? 9   ALA   C CB  1 
ATOM   1121 N  N   . ILE   B 1 4   ? 18.570 -23.353 17.569 1.00 12.98  ? 10  ILE   C N   1 
ATOM   1122 C  CA  . ILE   B 1 4   ? 18.469 -24.290 18.686 1.00 13.87  ? 10  ILE   C CA  1 
ATOM   1123 C  C   . ILE   B 1 4   ? 17.056 -24.096 19.277 1.00 13.65  ? 10  ILE   C C   1 
ATOM   1124 O  O   . ILE   B 1 4   ? 16.611 -22.950 19.478 1.00 14.54  ? 10  ILE   C O   1 
ATOM   1125 C  CB  . ILE   B 1 4   ? 19.495 -23.966 19.769 1.00 13.64  ? 10  ILE   C CB  1 
ATOM   1126 C  CG1 . ILE   B 1 4   ? 20.925 -23.835 19.205 1.00 15.81  ? 10  ILE   C CG1 1 
ATOM   1127 C  CG2 . ILE   B 1 4   ? 19.438 -25.043 20.876 1.00 15.74  ? 10  ILE   C CG2 1 
ATOM   1128 C  CD1 . ILE   B 1 4   ? 21.889 -23.224 20.233 1.00 14.84  ? 10  ILE   C CD1 1 
ATOM   1129 N  N   . TYR   B 1 5   ? 16.347 -25.185 19.594 1.00 13.69  ? 11  TYR   C N   1 
ATOM   1130 C  CA  . TYR   B 1 5   ? 15.010 -25.141 20.165 1.00 14.80  ? 11  TYR   C CA  1 
ATOM   1131 C  C   . TYR   B 1 5   ? 15.072 -25.816 21.532 1.00 15.41  ? 11  TYR   C C   1 
ATOM   1132 O  O   . TYR   B 1 5   ? 15.183 -27.057 21.608 1.00 16.70  ? 11  TYR   C O   1 
ATOM   1133 C  CB  . TYR   B 1 5   ? 13.958 -25.857 19.253 1.00 15.61  ? 11  TYR   C CB  1 
ATOM   1134 C  CG  . TYR   B 1 5   ? 13.780 -25.100 17.946 1.00 15.60  ? 11  TYR   C CG  1 
ATOM   1135 C  CD1 . TYR   B 1 5   ? 12.939 -23.988 17.864 1.00 15.65  ? 11  TYR   C CD1 1 
ATOM   1136 C  CD2 . TYR   B 1 5   ? 14.490 -25.455 16.812 1.00 15.84  ? 11  TYR   C CD2 1 
ATOM   1137 C  CE1 . TYR   B 1 5   ? 12.832 -23.258 16.679 1.00 17.30  ? 11  TYR   C CE1 1 
ATOM   1138 C  CE2 . TYR   B 1 5   ? 14.398 -24.735 15.630 1.00 17.45  ? 11  TYR   C CE2 1 
ATOM   1139 C  CZ  . TYR   B 1 5   ? 13.540 -23.651 15.561 1.00 17.38  ? 11  TYR   C CZ  1 
ATOM   1140 O  OH  . TYR   B 1 5   ? 13.458 -22.909 14.406 1.00 20.43  ? 11  TYR   C OH  1 
ATOM   1141 N  N   . VAL   B 1 6   ? 15.102 -25.077 22.619 1.00 16.74  ? 12  VAL   C N   1 
ATOM   1142 C  CA  . VAL   B 1 6   ? 15.190 -25.602 24.005 1.00 17.42  ? 12  VAL   C CA  1 
ATOM   1143 C  C   . VAL   B 1 6   ? 14.042 -24.997 24.816 1.00 18.63  ? 12  VAL   C C   1 
ATOM   1144 O  O   . VAL   B 1 6   ? 13.856 -23.777 24.816 1.00 17.24  ? 12  VAL   C O   1 
ATOM   1145 C  CB  . VAL   B 1 6   ? 16.600 -25.311 24.606 1.00 19.00  ? 12  VAL   C CB  1 
ATOM   1146 C  CG1 . VAL   B 1 6   ? 16.962 -23.823 24.531 1.00 19.44  ? 12  VAL   C CG1 1 
ATOM   1147 C  CG2 . VAL   B 1 6   ? 16.660 -25.798 26.041 1.00 20.31  ? 12  VAL   C CG2 1 
ATOM   1148 N  N   . GLY   B 1 7   ? 13.211 -25.834 25.476 1.00 18.92  ? 13  GLY   C N   1 
ATOM   1149 C  CA  . GLY   B 1 7   ? 12.091 -25.321 26.238 1.00 19.40  ? 13  GLY   C CA  1 
ATOM   1150 C  C   . GLY   B 1 7   ? 11.170 -24.487 25.359 1.00 19.57  ? 13  GLY   C C   1 
ATOM   1151 O  O   . GLY   B 1 7   ? 10.904 -24.872 24.217 1.00 20.51  ? 13  GLY   C O   1 
ATOM   1152 N  N   . ASN   B 1 8   ? 10.823 -23.289 25.811 1.00 19.02  ? 14  ASN   C N   1 
ATOM   1153 C  CA  . ASN   B 1 8   ? 10.025 -22.362 24.983 1.00 19.16  ? 14  ASN   C CA  1 
ATOM   1154 C  C   . ASN   B 1 8   ? 10.897 -21.248 24.404 1.00 18.05  ? 14  ASN   C C   1 
ATOM   1155 O  O   . ASN   B 1 8   ? 10.420 -20.117 24.211 1.00 17.74  ? 14  ASN   C O   1 
ATOM   1156 C  CB  . ASN   B 1 8   ? 8.799  -21.782 25.721 1.00 22.68  ? 14  ASN   C CB  1 
ATOM   1157 C  CG  . ASN   B 1 8   ? 7.732  -22.846 25.852 1.00 29.45  ? 14  ASN   C CG  1 
ATOM   1158 O  OD1 . ASN   B 1 8   ? 6.884  -23.007 24.980 1.00 31.69  ? 14  ASN   C OD1 1 
ATOM   1159 N  ND2 . ASN   B 1 8   ? 7.826  -23.639 26.897 1.00 33.13  ? 14  ASN   C ND2 1 
ATOM   1160 N  N   . TYR   B 1 9   ? 12.123 -21.613 24.013 1.00 15.38  ? 15  TYR   C N   1 
ATOM   1161 C  CA  . TYR   B 1 9   ? 13.075 -20.667 23.411 1.00 15.05  ? 15  TYR   C CA  1 
ATOM   1162 C  C   . TYR   B 1 9   ? 13.557 -21.137 22.048 1.00 14.81  ? 15  TYR   C C   1 
ATOM   1163 O  O   . TYR   B 1 9   ? 13.749 -22.343 21.835 1.00 15.93  ? 15  TYR   C O   1 
ATOM   1164 C  CB  . TYR   B 1 9   ? 14.310 -20.476 24.332 1.00 16.30  ? 15  TYR   C CB  1 
ATOM   1165 C  CG  . TYR   B 1 9   ? 13.971 -19.946 25.721 1.00 16.67  ? 15  TYR   C CG  1 
ATOM   1166 C  CD1 . TYR   B 1 9   ? 13.381 -18.703 25.887 1.00 19.13  ? 15  TYR   C CD1 1 
ATOM   1167 C  CD2 . TYR   B 1 9   ? 14.276 -20.685 26.862 1.00 19.84  ? 15  TYR   C CD2 1 
ATOM   1168 C  CE1 . TYR   B 1 9   ? 13.065 -18.222 27.161 1.00 22.71  ? 15  TYR   C CE1 1 
ATOM   1169 C  CE2 . TYR   B 1 9   ? 14.012 -20.187 28.142 1.00 22.64  ? 15  TYR   C CE2 1 
ATOM   1170 C  CZ  . TYR   B 1 9   ? 13.418 -18.953 28.276 1.00 25.37  ? 15  TYR   C CZ  1 
ATOM   1171 O  OH  . TYR   B 1 9   ? 13.090 -18.423 29.513 1.00 30.72  ? 15  TYR   C OH  1 
ATOM   1172 N  N   . ARG   B 1 10  ? 13.810 -20.171 21.158 1.00 13.99  ? 16  ARG   C N   1 
ATOM   1173 C  CA  . ARG   B 1 10  ? 14.450 -20.402 19.851 1.00 13.76  ? 16  ARG   C CA  1 
ATOM   1174 C  C   . ARG   B 1 10  ? 15.706 -19.537 19.858 1.00 13.28  ? 16  ARG   C C   1 
ATOM   1175 O  O   . ARG   B 1 10  ? 15.596 -18.315 20.054 1.00 14.24  ? 16  ARG   C O   1 
ATOM   1176 C  CB  . ARG   B 1 10  ? 13.498 -19.973 18.713 1.00 14.42  ? 16  ARG   C CB  1 
ATOM   1177 C  CG  . ARG   B 1 10  ? 14.134 -19.803 17.334 1.00 15.26  ? 16  ARG   C CG  1 
ATOM   1178 C  CD  . ARG   B 1 10  ? 13.062 -19.522 16.283 1.00 16.14  ? 16  ARG   C CD  1 
ATOM   1179 N  NE  . ARG   B 1 10  ? 13.480 -18.567 15.238 1.00 16.68  ? 16  ARG   C NE  1 
ATOM   1180 C  CZ  . ARG   B 1 10  ? 14.006 -18.870 14.047 1.00 17.24  ? 16  ARG   C CZ  1 
ATOM   1181 N  NH1 . ARG   B 1 10  ? 14.286 -20.147 13.731 1.00 19.14  ? 16  ARG   C NH1 1 
ATOM   1182 N  NH2 . ARG   B 1 10  ? 14.381 -17.901 13.212 1.00 18.25  ? 16  ARG   C NH2 1 
ATOM   1183 N  N   . VAL   B 1 11  ? 16.873 -20.117 19.606 1.00 12.49  ? 17  VAL   C N   1 
ATOM   1184 C  CA  . VAL   B 1 11  ? 18.163 -19.408 19.602 1.00 12.19  ? 17  VAL   C CA  1 
ATOM   1185 C  C   . VAL   B 1 11  ? 18.639 -19.344 18.202 1.00 12.69  ? 17  VAL   C C   1 
ATOM   1186 O  O   . VAL   B 1 11  ? 18.846 -20.416 17.565 1.00 13.45  ? 17  VAL   C O   1 
ATOM   1187 C  CB  . VAL   B 1 11  ? 19.233 -20.131 20.476 1.00 13.39  ? 17  VAL   C CB  1 
ATOM   1188 C  CG1 . VAL   B 1 11  ? 20.466 -19.252 20.588 1.00 15.20  ? 17  VAL   C CG1 1 
ATOM   1189 C  CG2 . VAL   B 1 11  ? 18.685 -20.481 21.877 1.00 15.59  ? 17  VAL   C CG2 1 
ATOM   1190 N  N   . VAL   B 1 12  ? 18.887 -18.140 17.671 1.00 11.99  ? 18  VAL   C N   1 
ATOM   1191 C  CA  A VAL   B 1 12  ? 19.344 -17.960 16.284 0.50 11.67  ? 18  VAL   C CA  1 
ATOM   1192 C  CA  B VAL   B 1 12  ? 19.305 -17.991 16.280 0.50 13.66  ? 18  VAL   C CA  1 
ATOM   1193 C  C   . VAL   B 1 12  ? 20.483 -16.952 16.229 1.00 12.83  ? 18  VAL   C C   1 
ATOM   1194 O  O   . VAL   B 1 12  ? 20.738 -16.200 17.196 1.00 13.14  ? 18  VAL   C O   1 
ATOM   1195 C  CB  A VAL   B 1 12  ? 18.195 -17.435 15.353 0.50 11.15  ? 18  VAL   C CB  1 
ATOM   1196 C  CB  B VAL   B 1 12  ? 18.037 -17.477 15.486 0.50 17.62  ? 18  VAL   C CB  1 
ATOM   1197 C  CG1 A VAL   B 1 12  ? 17.236 -18.575 15.061 0.50 12.29  ? 18  VAL   C CG1 1 
ATOM   1198 C  CG1 B VAL   B 1 12  ? 18.303 -17.322 14.007 0.50 18.66  ? 18  VAL   C CG1 1 
ATOM   1199 C  CG2 A VAL   B 1 12  ? 17.536 -16.139 15.916 0.50 7.90   ? 18  VAL   C CG2 1 
ATOM   1200 C  CG2 B VAL   B 1 12  ? 16.862 -18.415 15.688 0.50 21.05  ? 18  VAL   C CG2 1 
ATOM   1201 N  N   . ASN   B 1 13  ? 21.196 -16.893 15.094 1.00 12.19  ? 19  ASN   C N   1 
ATOM   1202 C  CA  . ASN   B 1 13  ? 22.184 -15.827 14.896 1.00 12.15  ? 19  ASN   C CA  1 
ATOM   1203 C  C   . ASN   B 1 13  ? 21.348 -14.491 14.828 1.00 12.72  ? 19  ASN   C C   1 
ATOM   1204 O  O   . ASN   B 1 13  ? 20.353 -14.409 14.116 1.00 12.49  ? 19  ASN   C O   1 
ATOM   1205 C  CB  . ASN   B 1 13  ? 22.883 -15.968 13.514 1.00 12.73  ? 19  ASN   C CB  1 
ATOM   1206 C  CG  . ASN   B 1 13  ? 23.751 -17.236 13.449 1.00 13.04  ? 19  ASN   C CG  1 
ATOM   1207 O  OD1 . ASN   B 1 13  ? 23.295 -18.302 13.037 1.00 13.57  ? 19  ASN   C OD1 1 
ATOM   1208 N  ND2 . ASN   B 1 13  ? 24.970 -17.127 13.929 1.00 13.73  ? 19  ASN   C ND2 1 
ATOM   1209 N  N   . ARG   B 1 14  ? 21.868 -13.468 15.515 1.00 12.50  ? 20  ARG   C N   1 
ATOM   1210 C  CA  . ARG   B 1 14  ? 21.123 -12.183 15.548 1.00 12.67  ? 20  ARG   C CA  1 
ATOM   1211 C  C   . ARG   B 1 14  ? 20.972 -11.646 14.102 1.00 14.49  ? 20  ARG   C C   1 
ATOM   1212 O  O   . ARG   B 1 14  ? 19.913 -11.107 13.742 1.00 14.41  ? 20  ARG   C O   1 
ATOM   1213 C  CB  . ARG   B 1 14  ? 21.870 -11.186 16.408 1.00 13.94  ? 20  ARG   C CB  1 
ATOM   1214 C  CG  . ARG   B 1 14  ? 21.061 -9.840  16.613 1.00 13.57  ? 20  ARG   C CG  1 
ATOM   1215 C  CD  . ARG   B 1 14  ? 21.940 -8.909  17.412 1.00 13.92  ? 20  ARG   C CD  1 
ATOM   1216 N  NE  . ARG   B 1 14  ? 21.256 -7.646  17.844 1.00 14.50  ? 20  ARG   C NE  1 
ATOM   1217 C  CZ  . ARG   B 1 14  ? 21.165 -6.547  17.111 1.00 14.48  ? 20  ARG   C CZ  1 
ATOM   1218 N  NH1 . ARG   B 1 14  ? 21.577 -6.544  15.853 1.00 16.33  ? 20  ARG   C NH1 1 
ATOM   1219 N  NH2 . ARG   B 1 14  ? 20.665 -5.429  17.636 1.00 15.55  ? 20  ARG   C NH2 1 
ATOM   1220 N  N   . HIS   B 1 15  ? 22.010 -11.844 13.261 1.00 13.57  ? 21  HIS   C N   1 
ATOM   1221 C  CA  . HIS   B 1 15  ? 21.934 -11.308 11.888 1.00 14.42  ? 21  HIS   C CA  1 
ATOM   1222 C  C   . HIS   B 1 15  ? 20.922 -12.035 10.984 1.00 14.93  ? 21  HIS   C C   1 
ATOM   1223 O  O   . HIS   B 1 15  ? 20.642 -11.535 9.897  1.00 16.91  ? 21  HIS   C O   1 
ATOM   1224 C  CB  . HIS   B 1 15  ? 23.315 -11.191 11.207 1.00 15.52  ? 21  HIS   C CB  1 
ATOM   1225 C  CG  . HIS   B 1 15  ? 23.932 -12.513 10.801 1.00 14.10  ? 21  HIS   C CG  1 
ATOM   1226 N  ND1 . HIS   B 1 15  ? 24.661 -13.315 11.697 1.00 14.61  ? 21  HIS   C ND1 1 
ATOM   1227 C  CD2 . HIS   B 1 15  ? 23.974 -13.085 9.567  1.00 15.48  ? 21  HIS   C CD2 1 
ATOM   1228 C  CE1 . HIS   B 1 15  ? 25.083 -14.367 10.978 1.00 15.67  ? 21  HIS   C CE1 1 
ATOM   1229 N  NE2 . HIS   B 1 15  ? 24.699 -14.252 9.691  1.00 15.09  ? 21  HIS   C NE2 1 
ATOM   1230 N  N   . LEU   B 1 16  ? 20.408 -13.181 11.406 1.00 13.24  ? 22  LEU   C N   1 
ATOM   1231 C  CA  . LEU   B 1 16  ? 19.404 -13.968 10.657 1.00 14.22  ? 22  LEU   C CA  1 
ATOM   1232 C  C   . LEU   B 1 16  ? 18.014 -13.910 11.311 1.00 15.09  ? 22  LEU   C C   1 
ATOM   1233 O  O   . LEU   B 1 16  ? 17.095 -14.629 10.875 1.00 15.74  ? 22  LEU   C O   1 
ATOM   1234 C  CB  . LEU   B 1 16  ? 19.896 -15.419 10.473 1.00 14.48  ? 22  LEU   C CB  1 
ATOM   1235 C  CG  . LEU   B 1 16  ? 21.214 -15.540 9.690  1.00 15.26  ? 22  LEU   C CG  1 
ATOM   1236 C  CD1 . LEU   B 1 16  ? 21.631 -17.015 9.609  1.00 15.76  ? 22  LEU   C CD1 1 
ATOM   1237 C  CD2 . LEU   B 1 16  ? 21.078 -14.960 8.292  1.00 16.46  ? 22  LEU   C CD2 1 
ATOM   1238 N  N   . ALA   B 1 17  ? 17.850 -13.152 12.437 1.00 14.95  ? 23  ALA   C N   1 
ATOM   1239 C  CA  . ALA   B 1 17  ? 16.559 -13.088 13.137 1.00 14.50  ? 23  ALA   C CA  1 
ATOM   1240 C  C   . ALA   B 1 17  ? 15.462 -12.520 12.252 1.00 15.82  ? 23  ALA   C C   1 
ATOM   1241 O  O   . ALA   B 1 17  ? 15.702 -11.593 11.446 1.00 17.35  ? 23  ALA   C O   1 
ATOM   1242 C  CB  . ALA   B 1 17  ? 16.707 -12.243 14.408 1.00 16.74  ? 23  ALA   C CB  1 
ATOM   1243 N  N   . THR   B 1 18  ? 14.263 -13.088 12.384 1.00 16.53  ? 24  THR   C N   1 
ATOM   1244 C  CA  . THR   B 1 18  ? 13.128 -12.661 11.580 1.00 17.12  ? 24  THR   C CA  1 
ATOM   1245 C  C   . THR   B 1 18  ? 12.298 -11.614 12.361 1.00 16.23  ? 24  THR   C C   1 
ATOM   1246 O  O   . THR   B 1 18  ? 12.519 -11.322 13.530 1.00 17.02  ? 24  THR   C O   1 
ATOM   1247 C  CB  . THR   B 1 18  ? 12.218 -13.900 11.296 1.00 18.00  ? 24  THR   C CB  1 
ATOM   1248 O  OG1 . THR   B 1 18  ? 11.683 -14.333 12.539 1.00 18.54  ? 24  THR   C OG1 1 
ATOM   1249 C  CG2 . THR   B 1 18  ? 12.971 -15.088 10.640 1.00 19.19  ? 24  THR   C CG2 1 
ATOM   1250 N  N   . HIS   B 1 19  ? 11.292 -11.007 11.668 1.00 18.84  ? 25  HIS   C N   1 
ATOM   1251 C  CA  . HIS   B 1 19  ? 10.364 -10.093 12.351 1.00 19.66  ? 25  HIS   C CA  1 
ATOM   1252 C  C   . HIS   B 1 19  ? 9.646  -10.839 13.465 1.00 16.57  ? 25  HIS   C C   1 
ATOM   1253 O  O   . HIS   B 1 19  ? 9.580  -10.278 14.570 1.00 18.62  ? 25  HIS   C O   1 
ATOM   1254 C  CB  . HIS   B 1 19  ? 9.280  -9.558  11.395 1.00 20.88  ? 25  HIS   C CB  1 
ATOM   1255 C  CG  . HIS   B 1 19  ? 8.138  -8.856  12.118 1.00 20.71  ? 25  HIS   C CG  1 
ATOM   1256 N  ND1 . HIS   B 1 19  ? 8.300  -7.604  12.680 1.00 23.62  ? 25  HIS   C ND1 1 
ATOM   1257 C  CD2 . HIS   B 1 19  ? 6.934  -9.345  12.486 1.00 22.63  ? 25  HIS   C CD2 1 
ATOM   1258 C  CE1 . HIS   B 1 19  ? 7.131  -7.296  13.234 1.00 24.06  ? 25  HIS   C CE1 1 
ATOM   1259 N  NE2 . HIS   B 1 19  ? 6.284  -8.333  13.180 1.00 23.48  ? 25  HIS   C NE2 1 
ATOM   1260 N  N   . ASN   B 1 20  ? 9.230  -12.101 13.246 1.00 17.32  ? 26  ASN   C N   1 
ATOM   1261 C  CA  . ASN   B 1 20  ? 8.594  -12.830 14.330 1.00 18.68  ? 26  ASN   C CA  1 
ATOM   1262 C  C   . ASN   B 1 20  ? 9.503  -13.023 15.535 1.00 17.17  ? 26  ASN   C C   1 
ATOM   1263 O  O   . ASN   B 1 20  ? 9.083  -12.924 16.676 1.00 16.84  ? 26  ASN   C O   1 
ATOM   1264 C  CB  . ASN   B 1 20  ? 8.066  -14.188 13.871 1.00 19.99  ? 26  ASN   C CB  1 
ATOM   1265 C  CG  . ASN   B 1 20  ? 7.227  -14.876 14.948 1.00 26.84  ? 26  ASN   C CG  1 
ATOM   1266 O  OD1 . ASN   B 1 20  ? 6.090  -14.454 15.252 1.00 29.55  ? 26  ASN   C OD1 1 
ATOM   1267 N  ND2 . ASN   B 1 20  ? 7.749  -15.920 15.570 1.00 27.74  ? 26  ASN   C ND2 1 
ATOM   1268 N  N   . ASP   B 1 21  ? 10.833 -13.258 15.279 1.00 15.80  ? 27  ASP   C N   1 
ATOM   1269 C  CA  . ASP   B 1 21  ? 11.758 -13.322 16.387 1.00 15.83  ? 27  ASP   C CA  1 
ATOM   1270 C  C   . ASP   B 1 21  ? 11.796 -12.020 17.199 1.00 14.56  ? 27  ASP   C C   1 
ATOM   1271 O  O   . ASP   B 1 21  ? 11.736 -12.043 18.413 1.00 15.54  ? 27  ASP   C O   1 
ATOM   1272 C  CB  . ASP   B 1 21  ? 13.181 -13.658 15.893 1.00 15.29  ? 27  ASP   C CB  1 
ATOM   1273 C  CG  . ASP   B 1 21  ? 13.393 -15.077 15.411 1.00 15.79  ? 27  ASP   C CG  1 
ATOM   1274 O  OD1 . ASP   B 1 21  ? 12.797 -16.004 16.021 1.00 17.26  ? 27  ASP   C OD1 1 
ATOM   1275 O  OD2 . ASP   B 1 21  ? 14.088 -15.250 14.370 1.00 16.20  ? 27  ASP   C OD2 1 
ATOM   1276 N  N   . TRP   B 1 22  ? 11.906 -10.866 16.508 1.00 15.11  ? 28  TRP   C N   1 
ATOM   1277 C  CA  . TRP   B 1 22  ? 11.947 -9.574  17.196 1.00 15.08  ? 28  TRP   C CA  1 
ATOM   1278 C  C   . TRP   B 1 22  ? 10.600 -9.234  17.894 1.00 15.31  ? 28  TRP   C C   1 
ATOM   1279 O  O   . TRP   B 1 22  ? 10.623 -8.654  18.980 1.00 17.17  ? 28  TRP   C O   1 
ATOM   1280 C  CB  . TRP   B 1 22  ? 12.358 -8.451  16.239 1.00 16.27  ? 28  TRP   C CB  1 
ATOM   1281 C  CG  . TRP   B 1 22  ? 13.834 -8.413  15.976 1.00 15.73  ? 28  TRP   C CG  1 
ATOM   1282 C  CD1 . TRP   B 1 22  ? 14.488 -8.904  14.888 1.00 17.57  ? 28  TRP   C CD1 1 
ATOM   1283 C  CD2 . TRP   B 1 22  ? 14.837 -7.842  16.833 1.00 14.80  ? 28  TRP   C CD2 1 
ATOM   1284 N  NE1 . TRP   B 1 22  ? 15.848 -8.626  14.992 1.00 16.85  ? 28  TRP   C NE1 1 
ATOM   1285 C  CE2 . TRP   B 1 22  ? 16.079 -7.968  16.173 1.00 16.40  ? 28  TRP   C CE2 1 
ATOM   1286 C  CE3 . TRP   B 1 22  ? 14.797 -7.154  18.053 1.00 17.78  ? 28  TRP   C CE3 1 
ATOM   1287 C  CZ2 . TRP   B 1 22  ? 17.256 -7.464  16.697 1.00 16.09  ? 28  TRP   C CZ2 1 
ATOM   1288 C  CZ3 . TRP   B 1 22  ? 15.983 -6.648  18.566 1.00 18.07  ? 28  TRP   C CZ3 1 
ATOM   1289 C  CH2 . TRP   B 1 22  ? 17.192 -6.812  17.881 1.00 17.27  ? 28  TRP   C CH2 1 
ATOM   1290 N  N   . ALA   B 1 23  ? 9.513  -9.717  17.325 1.00 16.09  ? 29  ALA   C N   1 
ATOM   1291 C  CA  . ALA   B 1 23  ? 8.185  -9.471  17.910 1.00 16.28  ? 29  ALA   C CA  1 
ATOM   1292 C  C   . ALA   B 1 23  ? 7.901  -10.348 19.141 1.00 18.30  ? 29  ALA   C C   1 
ATOM   1293 O  O   . ALA   B 1 23  ? 6.923  -10.136 19.867 1.00 19.17  ? 29  ALA   C O   1 
ATOM   1294 C  CB  . ALA   B 1 23  ? 7.105  -9.731  16.868 1.00 17.90  ? 29  ALA   C CB  1 
ATOM   1295 N  N   . ASN   B 1 24  ? 8.729  -11.390 19.370 1.00 18.13  ? 30  ASN   C N   1 
ATOM   1296 C  CA  . ASN   B 1 24  ? 8.624  -12.315 20.512 1.00 17.16  ? 30  ASN   C CA  1 
ATOM   1297 C  C   . ASN   B 1 24  ? 10.001 -12.368 21.217 1.00 17.07  ? 30  ASN   C C   1 
ATOM   1298 O  O   . ASN   B 1 24  ? 10.445 -13.445 21.643 1.00 16.40  ? 30  ASN   C O   1 
ATOM   1299 C  CB  . ASN   B 1 24  ? 8.174  -13.703 19.999 1.00 18.58  ? 30  ASN   C CB  1 
ATOM   1300 C  CG  . ASN   B 1 24  ? 6.774  -13.640 19.490 1.00 20.28  ? 30  ASN   C CG  1 
ATOM   1301 O  OD1 . ASN   B 1 24  ? 5.806  -13.662 20.299 1.00 22.51  ? 30  ASN   C OD1 1 
ATOM   1302 N  ND2 . ASN   B 1 24  ? 6.602  -13.507 18.200 1.00 21.53  ? 30  ASN   C ND2 1 
ATOM   1303 N  N   . LEU   B 1 25  ? 10.708 -11.240 21.277 1.00 17.59  ? 31  LEU   C N   1 
ATOM   1304 C  CA  . LEU   B 1 25  ? 12.079 -11.219 21.826 1.00 16.59  ? 31  LEU   C CA  1 
ATOM   1305 C  C   . LEU   B 1 25  ? 12.195 -11.540 23.297 1.00 18.13  ? 31  LEU   C C   1 
ATOM   1306 O  O   . LEU   B 1 25  ? 11.432 -11.020 24.127 1.00 19.05  ? 31  LEU   C O   1 
ATOM   1307 C  CB  . LEU   B 1 25  ? 12.626 -9.816  21.556 1.00 17.42  ? 31  LEU   C CB  1 
ATOM   1308 C  CG  . LEU   B 1 25  ? 14.086 -9.642  21.940 1.00 17.31  ? 31  LEU   C CG  1 
ATOM   1309 C  CD1 . LEU   B 1 25  ? 15.019 -10.514 21.041 1.00 17.24  ? 31  LEU   C CD1 1 
ATOM   1310 C  CD2 . LEU   B 1 25  ? 14.513 -8.192  21.832 1.00 19.06  ? 31  LEU   C CD2 1 
ATOM   1311 N  N   . VAL   B 1 26  ? 13.192 -12.350 23.648 1.00 16.20  ? 32  VAL   C N   1 
ATOM   1312 C  CA  . VAL   B 1 26  ? 13.528 -12.634 25.039 1.00 17.12  ? 32  VAL   C CA  1 
ATOM   1313 C  C   . VAL   B 1 26  ? 14.837 -11.919 25.369 1.00 17.69  ? 32  VAL   C C   1 
ATOM   1314 O  O   . VAL   B 1 26  ? 14.956 -11.257 26.423 1.00 19.63  ? 32  VAL   C O   1 
ATOM   1315 C  CB  . VAL   B 1 26  ? 13.665 -14.153 25.264 1.00 18.41  ? 32  VAL   C CB  1 
ATOM   1316 C  CG1 . VAL   B 1 26  ? 14.220 -14.461 26.659 1.00 20.40  ? 32  VAL   C CG1 1 
ATOM   1317 C  CG2 . VAL   B 1 26  ? 12.328 -14.842 25.049 1.00 18.72  ? 32  VAL   C CG2 1 
ATOM   1318 N  N   . TRP   B 1 27  ? 15.861 -12.045 24.476 1.00 16.17  ? 33  TRP   C N   1 
ATOM   1319 C  CA  . TRP   B 1 27  ? 17.182 -11.478 24.784 1.00 16.17  ? 33  TRP   C CA  1 
ATOM   1320 C  C   . TRP   B 1 27  ? 17.982 -11.399 23.483 1.00 15.79  ? 33  TRP   C C   1 
ATOM   1321 O  O   . TRP   B 1 27  ? 17.825 -12.293 22.625 1.00 15.63  ? 33  TRP   C O   1 
ATOM   1322 C  CB  . TRP   B 1 27  ? 17.917 -12.385 25.831 1.00 18.48  ? 33  TRP   C CB  1 
ATOM   1323 C  CG  . TRP   B 1 27  ? 19.383 -12.115 26.046 1.00 18.85  ? 33  TRP   C CG  1 
ATOM   1324 C  CD1 . TRP   B 1 27  ? 19.941 -11.166 26.852 1.00 21.22  ? 33  TRP   C CD1 1 
ATOM   1325 C  CD2 . TRP   B 1 27  ? 20.483 -12.791 25.406 1.00 17.40  ? 33  TRP   C CD2 1 
ATOM   1326 N  NE1 . TRP   B 1 27  ? 21.328 -11.258 26.810 1.00 22.05  ? 33  TRP   C NE1 1 
ATOM   1327 C  CE2 . TRP   B 1 27  ? 21.679 -12.252 25.930 1.00 19.36  ? 33  TRP   C CE2 1 
ATOM   1328 C  CE3 . TRP   B 1 27  ? 20.571 -13.812 24.447 1.00 16.94  ? 33  TRP   C CE3 1 
ATOM   1329 C  CZ2 . TRP   B 1 27  ? 22.950 -12.714 25.541 1.00 18.98  ? 33  TRP   C CZ2 1 
ATOM   1330 C  CZ3 . TRP   B 1 27  ? 21.829 -14.312 24.121 1.00 18.47  ? 33  TRP   C CZ3 1 
ATOM   1331 C  CH2 . TRP   B 1 27  ? 22.990 -13.711 24.613 1.00 19.14  ? 33  TRP   C CH2 1 
ATOM   1332 N  N   . GLU   B 1 28  ? 18.844 -10.408 23.346 1.00 15.11  ? 34  GLU   C N   1 
ATOM   1333 C  CA  . GLU   B 1 28  ? 19.697 -10.326 22.171 1.00 16.20  ? 34  GLU   C CA  1 
ATOM   1334 C  C   . GLU   B 1 28  ? 20.989 -9.646  22.540 1.00 15.69  ? 34  GLU   C C   1 
ATOM   1335 O  O   . GLU   B 1 28  ? 21.003 -8.750  23.444 1.00 16.21  ? 34  GLU   C O   1 
ATOM   1336 C  CB  . GLU   B 1 28  ? 19.018 -9.653  20.972 1.00 16.80  ? 34  GLU   C CB  1 
ATOM   1337 C  CG  . GLU   B 1 28  ? 18.447 -8.263  21.241 1.00 17.85  ? 34  GLU   C CG  1 
ATOM   1338 C  CD  . GLU   B 1 28  ? 19.440 -7.118  21.199 1.00 18.77  ? 34  GLU   C CD  1 
ATOM   1339 O  OE1 . GLU   B 1 28  ? 19.153 -6.069  21.824 1.00 21.25  ? 34  GLU   C OE1 1 
ATOM   1340 O  OE2 . GLU   B 1 28  ? 20.441 -7.192  20.450 1.00 18.56  ? 34  GLU   C OE2 1 
ATOM   1341 N  N   . ASP   B 1 29  ? 22.076 -9.988  21.819 1.00 14.66  ? 35  ASP   C N   1 
ATOM   1342 C  CA  . ASP   B 1 29  ? 23.360 -9.346  22.066 1.00 15.54  ? 35  ASP   C CA  1 
ATOM   1343 C  C   . ASP   B 1 29  ? 24.144 -9.301  20.748 1.00 15.95  ? 35  ASP   C C   1 
ATOM   1344 O  O   . ASP   B 1 29  ? 24.598 -10.340 20.250 1.00 15.25  ? 35  ASP   C O   1 
ATOM   1345 C  CB  . ASP   B 1 29  ? 24.064 -10.111 23.196 1.00 17.05  ? 35  ASP   C CB  1 
ATOM   1346 C  CG  . ASP   B 1 29  ? 25.406 -9.579  23.599 1.00 21.05  ? 35  ASP   C CG  1 
ATOM   1347 O  OD1 . ASP   B 1 29  ? 26.151 -9.107  22.716 1.00 21.56  ? 35  ASP   C OD1 1 
ATOM   1348 O  OD2 . ASP   B 1 29  ? 25.775 -9.734  24.790 1.00 24.77  ? 35  ASP   C OD2 1 
ATOM   1349 N  N   . SER   B 1 30  ? 24.322 -8.090  20.180 1.00 15.57  ? 36  SER   C N   1 
ATOM   1350 C  CA  A SER   B 1 30  ? 25.025 -7.914  18.916 0.50 16.25  ? 36  SER   C CA  1 
ATOM   1351 C  CA  B SER   B 1 30  ? 25.001 -7.968  18.907 0.50 16.64  ? 36  SER   C CA  1 
ATOM   1352 C  C   . SER   B 1 30  ? 26.493 -8.349  19.017 1.00 16.65  ? 36  SER   C C   1 
ATOM   1353 O  O   . SER   B 1 30  ? 27.018 -8.976  18.072 1.00 16.81  ? 36  SER   C O   1 
ATOM   1354 C  CB  A SER   B 1 30  ? 24.989 -6.453  18.487 0.50 17.37  ? 36  SER   C CB  1 
ATOM   1355 C  CB  B SER   B 1 30  ? 24.828 -6.568  18.344 0.50 19.21  ? 36  SER   C CB  1 
ATOM   1356 O  OG  A SER   B 1 30  ? 25.853 -6.228  17.379 0.50 17.80  ? 36  SER   C OG  1 
ATOM   1357 O  OG  B SER   B 1 30  ? 25.279 -5.601  19.275 0.50 20.86  ? 36  SER   C OG  1 
ATOM   1358 N  N   . SER   B 1 31  ? 27.136 -8.088  20.178 1.00 16.71  ? 37  SER   C N   1 
ATOM   1359 C  CA  . SER   B 1 31  ? 28.543 -8.478  20.302 1.00 17.52  ? 37  SER   C CA  1 
ATOM   1360 C  C   . SER   B 1 31  ? 28.734 -9.988  20.234 1.00 16.69  ? 37  SER   C C   1 
ATOM   1361 O  O   . SER   B 1 31  ? 29.828 -10.445 19.879 1.00 17.17  ? 37  SER   C O   1 
ATOM   1362 C  CB  . SER   B 1 31  ? 29.156 -7.941  21.581 1.00 21.42  ? 37  SER   C CB  1 
ATOM   1363 O  OG  . SER   B 1 31  ? 28.721 -8.640  22.731 1.00 26.55  ? 37  SER   C OG  1 
ATOM   1364 N  N   . ARG   B 1 32  ? 27.683 -10.785 20.566 1.00 15.64  ? 38  ARG   C N   1 
ATOM   1365 C  CA  . ARG   B 1 32  ? 27.770 -12.253 20.505 1.00 14.91  ? 38  ARG   C CA  1 
ATOM   1366 C  C   . ARG   B 1 32  ? 27.143 -12.814 19.224 1.00 13.62  ? 38  ARG   C C   1 
ATOM   1367 O  O   . ARG   B 1 32  ? 27.195 -14.035 19.009 1.00 13.63  ? 38  ARG   C O   1 
ATOM   1368 C  CB  . ARG   B 1 32  ? 27.026 -12.853 21.728 1.00 16.83  ? 38  ARG   C CB  1 
ATOM   1369 C  CG  . ARG   B 1 32  ? 27.691 -12.506 23.045 1.00 18.47  ? 38  ARG   C CG  1 
ATOM   1370 C  CD  . ARG   B 1 32  ? 26.936 -13.063 24.253 1.00 15.88  ? 38  ARG   C CD  1 
ATOM   1371 N  NE  . ARG   B 1 32  ? 26.989 -14.530 24.278 1.00 15.69  ? 38  ARG   C NE  1 
ATOM   1372 C  CZ  . ARG   B 1 32  ? 26.956 -15.280 25.386 1.00 15.49  ? 38  ARG   C CZ  1 
ATOM   1373 N  NH1 . ARG   B 1 32  ? 26.828 -14.720 26.574 1.00 17.55  ? 38  ARG   C NH1 1 
ATOM   1374 N  NH2 . ARG   B 1 32  ? 27.092 -16.603 25.303 1.00 15.72  ? 38  ARG   C NH2 1 
ATOM   1375 N  N   . ASP   B 1 33  ? 26.484 -11.983 18.413 1.00 13.04  ? 39  ASP   C N   1 
ATOM   1376 C  CA  . ASP   B 1 33  ? 25.706 -12.445 17.270 1.00 12.84  ? 39  ASP   C CA  1 
ATOM   1377 C  C   . ASP   B 1 33  ? 24.600 -13.416 17.706 1.00 12.95  ? 39  ASP   C C   1 
ATOM   1378 O  O   . ASP   B 1 33  ? 24.313 -14.364 16.939 1.00 13.05  ? 39  ASP   C O   1 
ATOM   1379 C  CB  . ASP   B 1 33  ? 26.577 -13.061 16.162 1.00 12.97  ? 39  ASP   C CB  1 
ATOM   1380 C  CG  . ASP   B 1 33  ? 25.790 -13.390 14.875 1.00 13.99  ? 39  ASP   C CG  1 
ATOM   1381 O  OD1 . ASP   B 1 33  ? 24.896 -12.606 14.487 1.00 15.05  ? 39  ASP   C OD1 1 
ATOM   1382 O  OD2 . ASP   B 1 33  ? 26.113 -14.411 14.223 1.00 14.20  ? 39  ASP   C OD2 1 
ATOM   1383 N  N   . LEU   B 1 34  ? 23.929 -13.200 18.859 1.00 12.33  ? 40  LEU   C N   1 
ATOM   1384 C  CA  . LEU   B 1 34  ? 22.841 -14.117 19.263 1.00 12.77  ? 40  LEU   C CA  1 
ATOM   1385 C  C   . LEU   B 1 34  ? 21.544 -13.359 19.512 1.00 13.09  ? 40  LEU   C C   1 
ATOM   1386 O  O   . LEU   B 1 34  ? 21.553 -12.201 19.988 1.00 13.12  ? 40  LEU   C O   1 
ATOM   1387 C  CB  . LEU   B 1 34  ? 23.242 -14.780 20.574 1.00 13.50  ? 40  LEU   C CB  1 
ATOM   1388 C  CG  . LEU   B 1 34  ? 24.333 -15.913 20.474 1.00 13.99  ? 40  LEU   C CG  1 
ATOM   1389 C  CD1 . LEU   B 1 34  ? 24.580 -16.492 21.916 1.00 16.02  ? 40  LEU   C CD1 1 
ATOM   1390 C  CD2 . LEU   B 1 34  ? 23.889 -17.047 19.537 1.00 14.06  ? 40  LEU   C CD2 1 
ATOM   1391 N  N   . LEU   B 1 35  ? 20.450 -14.058 19.270 1.00 12.25  ? 41  LEU   C N   1 
ATOM   1392 C  CA  . LEU   B 1 35  ? 19.118 -13.565 19.629 1.00 13.57  ? 41  LEU   C CA  1 
ATOM   1393 C  C   . LEU   B 1 35  ? 18.282 -14.778 20.020 1.00 12.60  ? 41  LEU   C C   1 
ATOM   1394 O  O   . LEU   B 1 35  ? 18.391 -15.849 19.387 1.00 13.42  ? 41  LEU   C O   1 
ATOM   1395 C  CB  . LEU   B 1 35  ? 18.485 -12.842 18.397 1.00 13.68  ? 41  LEU   C CB  1 
ATOM   1396 C  CG  . LEU   B 1 35  ? 17.090 -12.230 18.644 1.00 13.94  ? 41  LEU   C CG  1 
ATOM   1397 C  CD1 . LEU   B 1 35  ? 16.889 -10.938 17.855 1.00 16.56  ? 41  LEU   C CD1 1 
ATOM   1398 C  CD2 . LEU   B 1 35  ? 16.009 -13.277 18.285 1.00 14.76  ? 41  LEU   C CD2 1 
ATOM   1399 N  N   . VAL   B 1 36  ? 17.488 -14.593 21.073 1.00 12.97  ? 42  VAL   C N   1 
ATOM   1400 C  CA  . VAL   B 1 36  ? 16.577 -15.627 21.576 1.00 13.37  ? 42  VAL   C CA  1 
ATOM   1401 C  C   . VAL   B 1 36  ? 15.162 -15.093 21.559 1.00 13.86  ? 42  VAL   C C   1 
ATOM   1402 O  O   . VAL   B 1 36  ? 14.914 -13.967 22.050 1.00 14.98  ? 42  VAL   C O   1 
ATOM   1403 C  CB  . VAL   B 1 36  ? 16.960 -16.046 22.997 1.00 13.96  ? 42  VAL   C CB  1 
ATOM   1404 C  CG1 . VAL   B 1 36  ? 15.986 -17.094 23.536 1.00 16.12  ? 42  VAL   C CG1 1 
ATOM   1405 C  CG2 . VAL   B 1 36  ? 18.398 -16.625 23.012 1.00 14.73  ? 42  VAL   C CG2 1 
ATOM   1406 N  N   . SER   B 1 37  ? 14.244 -15.848 20.981 1.00 13.73  ? 43  SER   C N   1 
ATOM   1407 C  CA  . SER   B 1 37  ? 12.807 -15.514 20.948 1.00 14.05  ? 43  SER   C CA  1 
ATOM   1408 C  C   . SER   B 1 37  ? 12.006 -16.600 21.632 1.00 14.23  ? 43  SER   C C   1 
ATOM   1409 O  O   . SER   B 1 37  ? 12.510 -17.701 21.891 1.00 15.22  ? 43  SER   C O   1 
ATOM   1410 C  CB  . SER   B 1 37  ? 12.342 -15.301 19.514 1.00 13.88  ? 43  SER   C CB  1 
ATOM   1411 O  OG  . SER   B 1 37  ? 12.526 -16.468 18.726 1.00 15.97  ? 43  SER   C OG  1 
ATOM   1412 N  N   . SER   B 1 38  ? 10.781 -16.278 22.029 1.00 15.84  ? 44  SER   C N   1 
ATOM   1413 C  CA  . SER   B 1 38  ? 9.916  -17.263 22.667 1.00 17.14  ? 44  SER   C CA  1 
ATOM   1414 C  C   . SER   B 1 38  ? 9.106  -18.071 21.630 1.00 19.99  ? 44  SER   C C   1 
ATOM   1415 O  O   . SER   B 1 38  ? 8.792  -17.599 20.545 1.00 21.16  ? 44  SER   C O   1 
ATOM   1416 C  CB  . SER   B 1 38  ? 8.996  -16.558 23.658 1.00 19.13  ? 44  SER   C CB  1 
ATOM   1417 O  OG  . SER   B 1 38  ? 8.159  -15.667 22.957 1.00 23.46  ? 44  SER   C OG  1 
ATOM   1418 N  N   . THR   B 1 39  ? 8.747  -19.300 21.982 1.00 19.17  ? 45  THR   C N   1 
ATOM   1419 C  CA  . THR   B 1 39  ? 8.016  -20.203 21.090 1.00 20.92  ? 45  THR   C CA  1 
ATOM   1420 C  C   . THR   B 1 39  ? 6.711  -20.658 21.773 1.00 23.60  ? 45  THR   C C   1 
ATOM   1421 O  O   . THR   B 1 39  ? 6.644  -20.747 22.997 1.00 22.25  ? 45  THR   C O   1 
ATOM   1422 C  CB  . THR   B 1 39  ? 8.868  -21.472 20.751 1.00 21.06  ? 45  THR   C CB  1 
ATOM   1423 O  OG1 . THR   B 1 39  ? 9.122  -22.210 21.939 1.00 21.97  ? 45  THR   C OG1 1 
ATOM   1424 C  CG2 . THR   B 1 39  ? 10.234 -21.148 20.081 1.00 20.86  ? 45  THR   C CG2 1 
ATOM   1425 N  N   . THR   B 1 40  ? 5.729  -21.048 20.958 1.00 25.38  ? 46  THR   C N   1 
ATOM   1426 C  CA  . THR   B 1 40  ? 4.477  -21.593 21.507 1.00 27.60  ? 46  THR   C CA  1 
ATOM   1427 C  C   . THR   B 1 40  ? 4.694  -23.061 21.867 1.00 28.26  ? 46  THR   C C   1 
ATOM   1428 O  O   . THR   B 1 40  ? 4.293  -23.511 22.951 1.00 30.55  ? 46  THR   C O   1 
ATOM   1429 C  CB  . THR   B 1 40  ? 3.326  -21.342 20.523 1.00 32.36  ? 46  THR   C CB  1 
ATOM   1430 O  OG1 . THR   B 1 40  ? 3.660  -21.975 19.294 1.00 36.14  ? 46  THR   C OG1 1 
ATOM   1431 C  CG2 . THR   B 1 40  ? 3.143  -19.871 20.240 1.00 32.41  ? 46  THR   C CG2 1 
ATOM   1432 N  N   . ALA   B 1 41  ? 5.372  -23.818 20.981 1.00 26.30  ? 47  ALA   C N   1 
ATOM   1433 C  CA  . ALA   B 1 41  ? 5.659  -25.226 21.235 1.00 27.30  ? 47  ALA   C CA  1 
ATOM   1434 C  C   . ALA   B 1 41  ? 6.969  -25.463 21.996 1.00 26.54  ? 47  ALA   C C   1 
ATOM   1435 O  O   . ALA   B 1 41  ? 7.924  -24.721 21.782 1.00 25.87  ? 47  ALA   C O   1 
ATOM   1436 C  CB  . ALA   B 1 41  ? 5.715  -25.980 19.917 1.00 29.05  ? 47  ALA   C CB  1 
ATOM   1437 N  N   . GLN   B 1 42  ? 7.070  -26.525 22.791 1.00 26.27  ? 48  GLN   C N   1 
ATOM   1438 C  CA  . GLN   B 1 42  ? 8.296  -26.855 23.496 1.00 25.86  ? 48  GLN   C CA  1 
ATOM   1439 C  C   . GLN   B 1 42  ? 9.269  -27.522 22.551 1.00 24.17  ? 48  GLN   C C   1 
ATOM   1440 O  O   . GLN   B 1 42  ? 8.885  -28.335 21.712 1.00 26.24  ? 48  GLN   C O   1 
ATOM   1441 C  CB  . GLN   B 1 42  ? 8.019  -27.760 24.710 1.00 30.87  ? 48  GLN   C CB  1 
ATOM   1442 C  CG  . GLN   B 1 42  ? 7.343  -26.998 25.840 1.00 39.80  ? 48  GLN   C CG  1 
ATOM   1443 C  CD  . GLN   B 1 42  ? 7.307  -27.899 27.039 1.00 50.54  ? 48  GLN   C CD  1 
ATOM   1444 O  OE1 . GLN   B 1 42  ? 6.585  -28.908 27.073 1.00 53.65  ? 48  GLN   C OE1 1 
ATOM   1445 N  NE2 . GLN   B 1 42  ? 8.115  -27.587 28.041 1.00 53.14  ? 48  GLN   C NE2 1 
ATOM   1446 N  N   . GLY   B 1 43  ? 10.538 -27.140 22.686 1.00 20.76  ? 49  GLY   C N   1 
ATOM   1447 C  CA  . GLY   B 1 43  ? 11.640 -27.714 21.939 1.00 20.05  ? 49  GLY   C CA  1 
ATOM   1448 C  C   . GLY   B 1 43  ? 12.331 -28.787 22.750 1.00 19.92  ? 49  GLY   C C   1 
ATOM   1449 O  O   . GLY   B 1 43  ? 12.089 -28.920 23.968 1.00 22.72  ? 49  GLY   C O   1 
ATOM   1450 N  N   . CYS   B 1 44  ? 13.161 -29.561 22.073 1.00 18.79  ? 50  CYS   C N   1 
ATOM   1451 C  CA  . CYS   B 1 44  ? 13.779 -30.761 22.634 1.00 20.01  ? 50  CYS   C CA  1 
ATOM   1452 C  C   . CYS   B 1 44  ? 15.256 -30.795 22.638 1.00 19.78  ? 50  CYS   C C   1 
ATOM   1453 O  O   . CYS   B 1 44  ? 15.832 -31.858 22.979 1.00 21.69  ? 50  CYS   C O   1 
ATOM   1454 C  CB  . CYS   B 1 44  ? 13.256 -31.975 21.887 1.00 20.40  ? 50  CYS   C CB  1 
ATOM   1455 S  SG  . CYS   B 1 44  ? 11.471 -32.155 21.998 1.00 26.42  ? 50  CYS   C SG  1 
ATOM   1456 N  N   . ASP   B 1 45  ? 15.930 -29.745 22.187 1.00 17.12  ? 51  ASP   C N   1 
ATOM   1457 C  CA  . ASP   B 1 45  ? 17.385 -29.737 22.217 1.00 16.95  ? 51  ASP   C CA  1 
ATOM   1458 C  C   . ASP   B 1 45  ? 17.812 -29.558 23.672 1.00 17.84  ? 51  ASP   C C   1 
ATOM   1459 O  O   . ASP   B 1 45  ? 17.122 -28.875 24.472 1.00 19.33  ? 51  ASP   C O   1 
ATOM   1460 C  CB  . ASP   B 1 45  ? 17.973 -28.607 21.368 1.00 16.39  ? 51  ASP   C CB  1 
ATOM   1461 C  CG  . ASP   B 1 45  ? 17.792 -28.781 19.880 1.00 21.78  ? 51  ASP   C CG  1 
ATOM   1462 O  OD1 . ASP   B 1 45  ? 17.880 -29.921 19.411 1.00 24.94  ? 51  ASP   C OD1 1 
ATOM   1463 O  OD2 . ASP   B 1 45  ? 17.638 -27.748 19.155 1.00 19.15  ? 51  ASP   C OD2 1 
ATOM   1464 N  N   . THR   B 1 46  ? 18.909 -30.201 24.024 1.00 16.13  ? 52  THR   C N   1 
ATOM   1465 C  CA  . THR   B 1 46  ? 19.501 -30.051 25.343 1.00 16.64  ? 52  THR   C CA  1 
ATOM   1466 C  C   . THR   B 1 46  ? 20.758 -29.166 25.166 1.00 15.59  ? 52  THR   C C   1 
ATOM   1467 O  O   . THR   B 1 46  ? 21.598 -29.492 24.288 1.00 16.01  ? 52  THR   C O   1 
ATOM   1468 C  CB  . THR   B 1 46  ? 19.910 -31.412 25.899 1.00 19.15  ? 52  THR   C CB  1 
ATOM   1469 O  OG1 . THR   B 1 46  ? 18.691 -32.192 26.083 1.00 21.53  ? 52  THR   C OG1 1 
ATOM   1470 C  CG2 . THR   B 1 46  ? 20.644 -31.260 27.246 1.00 21.78  ? 52  THR   C CG2 1 
ATOM   1471 N  N   . ILE   B 1 47  ? 20.940 -28.151 26.004 1.00 16.47  ? 53  ILE   C N   1 
ATOM   1472 C  CA  . ILE   B 1 47  ? 22.137 -27.324 25.965 1.00 15.80  ? 53  ILE   C CA  1 
ATOM   1473 C  C   . ILE   B 1 47  ? 23.219 -28.000 26.803 1.00 15.79  ? 53  ILE   C C   1 
ATOM   1474 O  O   . ILE   B 1 47  ? 22.974 -28.453 27.937 1.00 17.38  ? 53  ILE   C O   1 
ATOM   1475 C  CB  . ILE   B 1 47  ? 21.866 -25.945 26.560 1.00 16.32  ? 53  ILE   C CB  1 
ATOM   1476 C  CG1 . ILE   B 1 47  ? 20.658 -25.253 25.893 1.00 17.40  ? 53  ILE   C CG1 1 
ATOM   1477 C  CG2 . ILE   B 1 47  ? 23.130 -25.074 26.483 1.00 17.16  ? 53  ILE   C CG2 1 
ATOM   1478 C  CD1 . ILE   B 1 47  ? 20.885 -25.113 24.329 1.00 18.97  ? 53  ILE   C CD1 1 
ATOM   1479 N  N   . ALA   B 1 48  ? 24.433 -28.072 26.282 1.00 14.48  ? 54  ALA   C N   1 
ATOM   1480 C  CA  . ALA   B 1 48  ? 25.549 -28.642 27.022 1.00 14.18  ? 54  ALA   C CA  1 
ATOM   1481 C  C   . ALA   B 1 48  ? 25.883 -27.695 28.204 1.00 14.51  ? 54  ALA   C C   1 
ATOM   1482 O  O   . ALA   B 1 48  ? 25.857 -26.450 28.056 1.00 14.58  ? 54  ALA   C O   1 
ATOM   1483 C  CB  . ALA   B 1 48  ? 26.765 -28.703 26.095 1.00 13.69  ? 54  ALA   C CB  1 
ATOM   1484 N  N   . ARG   B 1 49  ? 26.226 -28.308 29.364 1.00 14.42  ? 55  ARG   C N   1 
ATOM   1485 C  CA  . ARG   B 1 49  ? 26.679 -27.547 30.540 1.00 15.03  ? 55  ARG   C CA  1 
ATOM   1486 C  C   . ARG   B 1 49  ? 27.991 -28.186 30.926 1.00 14.77  ? 55  ARG   C C   1 
ATOM   1487 O  O   . ARG   B 1 49  ? 28.026 -29.212 31.630 1.00 16.47  ? 55  ARG   C O   1 
ATOM   1488 C  CB  . ARG   B 1 49  ? 25.666 -27.587 31.691 1.00 15.86  ? 55  ARG   C CB  1 
ATOM   1489 C  CG  . ARG   B 1 49  ? 24.314 -27.014 31.260 1.00 15.71  ? 55  ARG   C CG  1 
ATOM   1490 C  CD  . ARG   B 1 49  ? 24.289 -25.543 30.836 1.00 16.98  ? 55  ARG   C CD  1 
ATOM   1491 N  NE  . ARG   B 1 49  ? 22.937 -25.105 30.467 1.00 17.00  ? 55  ARG   C NE  1 
ATOM   1492 C  CZ  . ARG   B 1 49  ? 22.679 -24.002 29.755 1.00 16.20  ? 55  ARG   C CZ  1 
ATOM   1493 N  NH1 . ARG   B 1 49  ? 23.651 -23.157 29.455 1.00 15.63  ? 55  ARG   C NH1 1 
ATOM   1494 N  NH2 . ARG   B 1 49  ? 21.422 -23.707 29.383 1.00 17.77  ? 55  ARG   C NH2 1 
ATOM   1495 N  N   . CYS   B 1 50  ? 29.103 -27.614 30.412 1.00 14.15  ? 56  CYS   C N   1 
ATOM   1496 C  CA  . CYS   B 1 50  ? 30.452 -28.227 30.441 1.00 14.49  ? 56  CYS   C CA  1 
ATOM   1497 C  C   . CYS   B 1 50  ? 31.513 -27.254 29.930 1.00 14.58  ? 56  CYS   C C   1 
ATOM   1498 O  O   . CYS   B 1 50  ? 31.191 -26.141 29.495 1.00 15.36  ? 56  CYS   C O   1 
ATOM   1499 C  CB  . CYS   B 1 50  ? 30.416 -29.447 29.518 1.00 14.21  ? 56  CYS   C CB  1 
ATOM   1500 S  SG  . CYS   B 1 50  ? 30.283 -29.014 27.751 1.00 14.44  ? 56  CYS   C SG  1 
ATOM   1501 N  N   . ASP   B 1 51  ? 32.825 -27.703 29.983 1.00 15.92  ? 57  ASP   C N   1 
ATOM   1502 C  CA  . ASP   B 1 51  ? 33.928 -26.948 29.404 1.00 17.45  ? 57  ASP   C CA  1 
ATOM   1503 C  C   . ASP   B 1 51  ? 34.596 -27.826 28.303 1.00 15.90  ? 57  ASP   C C   1 
ATOM   1504 O  O   . ASP   B 1 51  ? 35.801 -27.681 28.062 1.00 17.85  ? 57  ASP   C O   1 
ATOM   1505 C  CB  . ASP   B 1 51  ? 34.942 -26.507 30.476 1.00 20.42  ? 57  ASP   C CB  1 
ATOM   1506 C  CG  . ASP   B 1 51  ? 35.635 -27.627 31.181 1.00 24.13  ? 57  ASP   C CG  1 
ATOM   1507 O  OD1 . ASP   B 1 51  ? 35.324 -28.802 30.901 1.00 23.35  ? 57  ASP   C OD1 1 
ATOM   1508 O  OD2 . ASP   B 1 51  ? 36.567 -27.331 31.996 1.00 29.43  ? 57  ASP   C OD2 1 
ATOM   1509 N  N   . CYS   B 1 52  ? 33.809 -28.704 27.603 1.00 14.79  ? 58  CYS   C N   1 
ATOM   1510 C  CA  . CYS   B 1 52  ? 34.401 -29.479 26.471 1.00 14.52  ? 58  CYS   C CA  1 
ATOM   1511 C  C   . CYS   B 1 52  ? 35.058 -28.564 25.450 1.00 13.75  ? 58  CYS   C C   1 
ATOM   1512 O  O   . CYS   B 1 52  ? 34.604 -27.429 25.224 1.00 14.55  ? 58  CYS   C O   1 
ATOM   1513 C  CB  . CYS   B 1 52  ? 33.323 -30.305 25.753 1.00 14.59  ? 58  CYS   C CB  1 
ATOM   1514 S  SG  . CYS   B 1 52  ? 32.718 -31.720 26.678 1.00 15.33  ? 58  CYS   C SG  1 
ATOM   1515 N  N   . GLN   B 1 53  ? 36.104 -29.066 24.841 1.00 13.44  ? 59  GLN   C N   1 
ATOM   1516 C  CA  . GLN   B 1 53  ? 36.793 -28.421 23.731 1.00 14.43  ? 59  GLN   C CA  1 
ATOM   1517 C  C   . GLN   B 1 53  ? 36.879 -29.365 22.571 1.00 12.57  ? 59  GLN   C C   1 
ATOM   1518 O  O   . GLN   B 1 53  ? 37.653 -29.117 21.639 1.00 13.34  ? 59  GLN   C O   1 
ATOM   1519 C  CB  . GLN   B 1 53  ? 38.209 -27.940 24.141 1.00 15.40  ? 59  GLN   C CB  1 
ATOM   1520 C  CG  . GLN   B 1 53  ? 38.203 -26.649 24.987 1.00 20.52  ? 59  GLN   C CG  1 
ATOM   1521 C  CD  . GLN   B 1 53  ? 39.589 -26.114 25.197 1.00 21.64  ? 59  GLN   C CD  1 
ATOM   1522 O  OE1 . GLN   B 1 53  ? 40.123 -26.218 26.311 1.00 23.79  ? 59  GLN   C OE1 1 
ATOM   1523 N  NE2 . GLN   B 1 53  ? 40.227 -25.584 24.135 1.00 20.28  ? 59  GLN   C NE2 1 
ATOM   1524 N  N   . THR   B 1 54  ? 36.088 -30.475 22.544 1.00 12.15  ? 60  THR   C N   1 
ATOM   1525 C  CA  . THR   B 1 54  ? 36.009 -31.294 21.340 1.00 12.74  ? 60  THR   C CA  1 
ATOM   1526 C  C   . THR   B 1 54  ? 34.535 -31.597 21.081 1.00 13.08  ? 60  THR   C C   1 
ATOM   1527 O  O   . THR   B 1 54  ? 33.746 -31.731 22.026 1.00 13.98  ? 60  THR   C O   1 
ATOM   1528 C  CB  . THR   B 1 54  ? 36.770 -32.587 21.406 1.00 16.02  ? 60  THR   C CB  1 
ATOM   1529 O  OG1 . THR   B 1 54  ? 36.214 -33.391 22.381 1.00 19.80  ? 60  THR   C OG1 1 
ATOM   1530 C  CG2 . THR   B 1 54  ? 38.234 -32.384 21.723 1.00 16.04  ? 60  THR   C CG2 1 
ATOM   1531 N  N   . GLY   B 1 55  ? 34.162 -31.665 19.815 1.00 11.80  ? 61  GLY   C N   1 
ATOM   1532 C  CA  . GLY   B 1 55  ? 32.765 -31.934 19.470 1.00 12.03  ? 61  GLY   C CA  1 
ATOM   1533 C  C   . GLY   B 1 55  ? 32.640 -32.071 17.968 1.00 10.86  ? 61  GLY   C C   1 
ATOM   1534 O  O   . GLY   B 1 55  ? 33.622 -32.396 17.283 1.00 11.92  ? 61  GLY   C O   1 
ATOM   1535 N  N   . VAL   B 1 56  ? 31.422 -31.977 17.473 1.00 11.16  ? 62  VAL   C N   1 
ATOM   1536 C  CA  . VAL   B 1 56  ? 31.157 -32.164 16.028 1.00 9.77   ? 62  VAL   C CA  1 
ATOM   1537 C  C   . VAL   B 1 56  ? 30.242 -31.021 15.589 1.00 10.28  ? 62  VAL   C C   1 
ATOM   1538 O  O   . VAL   B 1 56  ? 29.305 -30.715 16.287 1.00 10.75  ? 62  VAL   C O   1 
ATOM   1539 C  CB  . VAL   B 1 56  ? 30.421 -33.527 15.848 1.00 10.73  ? 62  VAL   C CB  1 
ATOM   1540 C  CG1 . VAL   B 1 56  ? 29.950 -33.703 14.415 1.00 12.98  ? 62  VAL   C CG1 1 
ATOM   1541 C  CG2 . VAL   B 1 56  ? 31.346 -34.709 16.269 1.00 12.31  ? 62  VAL   C CG2 1 
ATOM   1542 N  N   . TYR   B 1 57  ? 30.511 -30.429 14.408 1.00 10.66  ? 63  TYR   C N   1 
ATOM   1543 C  CA  . TYR   B 1 57  ? 29.616 -29.370 13.910 1.00 9.75   ? 63  TYR   C CA  1 
ATOM   1544 C  C   . TYR   B 1 57  ? 29.075 -29.713 12.525 1.00 10.92  ? 63  TYR   C C   1 
ATOM   1545 O  O   . TYR   B 1 57  ? 29.738 -30.433 11.777 1.00 11.58  ? 63  TYR   C O   1 
ATOM   1546 C  CB  . TYR   B 1 57  ? 30.288 -27.949 13.905 1.00 10.67  ? 63  TYR   C CB  1 
ATOM   1547 C  CG  . TYR   B 1 57  ? 31.171 -27.636 12.695 1.00 10.47  ? 63  TYR   C CG  1 
ATOM   1548 C  CD1 . TYR   B 1 57  ? 32.456 -28.161 12.585 1.00 11.40  ? 63  TYR   C CD1 1 
ATOM   1549 C  CD2 . TYR   B 1 57  ? 30.710 -26.814 11.668 1.00 10.56  ? 63  TYR   C CD2 1 
ATOM   1550 C  CE1 . TYR   B 1 57  ? 33.276 -27.861 11.503 1.00 11.51  ? 63  TYR   C CE1 1 
ATOM   1551 C  CE2 . TYR   B 1 57  ? 31.538 -26.482 10.583 1.00 11.35  ? 63  TYR   C CE2 1 
ATOM   1552 C  CZ  . TYR   B 1 57  ? 32.816 -27.001 10.519 1.00 11.55  ? 63  TYR   C CZ  1 
ATOM   1553 O  OH  . TYR   B 1 57  ? 33.661 -26.720 9.451  1.00 14.00  ? 63  TYR   C OH  1 
ATOM   1554 N  N   . TYR   B 1 58  ? 27.891 -29.173 12.230 1.00 10.46  ? 64  TYR   C N   1 
ATOM   1555 C  CA  . TYR   B 1 58  ? 27.281 -29.333 10.892 1.00 10.95  ? 64  TYR   C CA  1 
ATOM   1556 C  C   . TYR   B 1 58  ? 27.675 -28.174 9.985  1.00 11.94  ? 64  TYR   C C   1 
ATOM   1557 O  O   . TYR   B 1 58  ? 27.448 -26.996 10.316 1.00 11.64  ? 64  TYR   C O   1 
ATOM   1558 C  CB  . TYR   B 1 58  ? 25.763 -29.430 10.988 1.00 11.62  ? 64  TYR   C CB  1 
ATOM   1559 C  CG  . TYR   B 1 58  ? 25.177 -29.707 9.618  1.00 12.62  ? 64  TYR   C CG  1 
ATOM   1560 C  CD1 . TYR   B 1 58  ? 25.522 -30.853 8.916  1.00 12.89  ? 64  TYR   C CD1 1 
ATOM   1561 C  CD2 . TYR   B 1 58  ? 24.325 -28.802 9.004  1.00 13.13  ? 64  TYR   C CD2 1 
ATOM   1562 C  CE1 . TYR   B 1 58  ? 25.004 -31.118 7.629  1.00 13.75  ? 64  TYR   C CE1 1 
ATOM   1563 C  CE2 . TYR   B 1 58  ? 23.792 -29.066 7.714  1.00 13.49  ? 64  TYR   C CE2 1 
ATOM   1564 C  CZ  . TYR   B 1 58  ? 24.155 -30.221 7.059  1.00 14.02  ? 64  TYR   C CZ  1 
ATOM   1565 O  OH  . TYR   B 1 58  ? 23.725 -30.485 5.759  1.00 17.10  ? 64  TYR   C OH  1 
ATOM   1566 N  N   . CYS   B 1 59  ? 28.191 -28.540 8.793  1.00 11.24  ? 65  CYS   C N   1 
ATOM   1567 C  CA  . CYS   B 1 59  ? 28.614 -27.608 7.741  1.00 11.89  ? 65  CYS   C CA  1 
ATOM   1568 C  C   . CYS   B 1 59  ? 27.686 -27.786 6.526  1.00 11.86  ? 65  CYS   C C   1 
ATOM   1569 O  O   . CYS   B 1 59  ? 27.849 -28.731 5.735  1.00 13.39  ? 65  CYS   C O   1 
ATOM   1570 C  CB  . CYS   B 1 59  ? 30.045 -27.887 7.376  1.00 11.15  ? 65  CYS   C CB  1 
ATOM   1571 S  SG  . CYS   B 1 59  ? 30.652 -26.821 6.044  1.00 14.11  ? 65  CYS   C SG  1 
ATOM   1572 N  N   . SER   B 1 60  ? 26.678 -26.933 6.419  1.00 13.42  ? 66  SER   C N   1 
ATOM   1573 C  CA  . SER   B 1 60  ? 25.695 -27.069 5.344  1.00 14.23  ? 66  SER   C CA  1 
ATOM   1574 C  C   . SER   B 1 60  ? 26.331 -26.967 3.927  1.00 14.36  ? 66  SER   C C   1 
ATOM   1575 O  O   . SER   B 1 60  ? 25.913 -27.730 3.059  1.00 15.98  ? 66  SER   C O   1 
ATOM   1576 C  CB  . SER   B 1 60  ? 24.565 -26.066 5.510  1.00 18.33  ? 66  SER   C CB  1 
ATOM   1577 O  OG  . SER   B 1 60  ? 25.013 -24.737 5.404  1.00 27.38  ? 66  SER   C OG  1 
ATOM   1578 N  N   . SER   B 1 61  ? 27.364 -26.101 3.768  1.00 14.20  ? 67  SER   C N   1 
ATOM   1579 C  CA  . SER   B 1 61  ? 28.047 -25.944 2.463  1.00 14.84  ? 67  SER   C CA  1 
ATOM   1580 C  C   . SER   B 1 61  ? 28.891 -27.134 2.084  1.00 15.66  ? 67  SER   C C   1 
ATOM   1581 O  O   . SER   B 1 61  ? 29.380 -27.145 0.949  1.00 18.39  ? 67  SER   C O   1 
ATOM   1582 C  CB  . SER   B 1 61  ? 28.874 -24.677 2.442  1.00 15.38  ? 67  SER   C CB  1 
ATOM   1583 O  OG  . SER   B 1 61  ? 29.981 -24.782 3.320  1.00 16.71  ? 67  SER   C OG  1 
ATOM   1584 N  N   . ARG   B 1 62  ? 28.994 -28.171 2.920  1.00 14.09  ? 68  ARG   C N   1 
ATOM   1585 C  CA  . ARG   B 1 62  ? 29.620 -29.435 2.551  1.00 14.20  ? 68  ARG   C CA  1 
ATOM   1586 C  C   . ARG   B 1 62  ? 28.684 -30.627 2.751  1.00 14.84  ? 68  ARG   C C   1 
ATOM   1587 O  O   . ARG   B 1 62  ? 29.089 -31.760 2.554  1.00 16.15  ? 68  ARG   C O   1 
ATOM   1588 C  CB  . ARG   B 1 62  ? 30.888 -29.641 3.376  1.00 14.22  ? 68  ARG   C CB  1 
ATOM   1589 C  CG  . ARG   B 1 62  ? 31.951 -28.572 3.168  1.00 18.48  ? 68  ARG   C CG  1 
ATOM   1590 C  CD  . ARG   B 1 62  ? 32.655 -28.810 1.842  1.00 18.28  ? 68  ARG   C CD  1 
ATOM   1591 N  NE  . ARG   B 1 62  ? 33.712 -27.812 1.581  1.00 21.09  ? 68  ARG   C NE  1 
ATOM   1592 C  CZ  . ARG   B 1 62  ? 33.519 -26.649 0.984  1.00 24.47  ? 68  ARG   C CZ  1 
ATOM   1593 N  NH1 . ARG   B 1 62  ? 32.331 -26.344 0.473  1.00 24.05  ? 68  ARG   C NH1 1 
ATOM   1594 N  NH2 . ARG   B 1 62  ? 34.555 -25.837 0.738  1.00 27.84  ? 68  ARG   C NH2 1 
ATOM   1595 N  N   . ARG   B 1 63  ? 27.462 -30.381 3.265  1.00 14.46  ? 69  ARG   C N   1 
ATOM   1596 C  CA  . ARG   B 1 63  ? 26.541 -31.472 3.695  1.00 16.25  ? 69  ARG   C CA  1 
ATOM   1597 C  C   . ARG   B 1 63  ? 27.248 -32.511 4.567  1.00 17.15  ? 69  ARG   C C   1 
ATOM   1598 O  O   . ARG   B 1 63  ? 27.103 -33.726 4.365  1.00 19.66  ? 69  ARG   C O   1 
ATOM   1599 C  CB  . ARG   B 1 63  ? 25.874 -32.143 2.478  1.00 18.25  ? 69  ARG   C CB  1 
ATOM   1600 C  CG  . ARG   B 1 63  ? 24.942 -31.203 1.761  1.00 24.31  ? 69  ARG   C CG  1 
ATOM   1601 C  CD  . ARG   B 1 63  ? 23.634 -31.896 1.530  1.00 36.34  ? 69  ARG   C CD  1 
ATOM   1602 N  NE  . ARG   B 1 63  ? 22.625 -30.958 1.053  1.00 42.46  ? 69  ARG   C NE  1 
ATOM   1603 C  CZ  . ARG   B 1 63  ? 22.300 -30.796 -0.222 1.00 49.05  ? 69  ARG   C CZ  1 
ATOM   1604 N  NH1 . ARG   B 1 63  ? 22.935 -31.481 -1.173 1.00 51.20  ? 69  ARG   C NH1 1 
ATOM   1605 N  NH2 . ARG   B 1 63  ? 21.353 -29.933 -0.564 1.00 49.41  ? 69  ARG   C NH2 1 
ATOM   1606 N  N   . LYS   B 1 64  ? 28.048 -32.017 5.540  1.00 14.99  ? 70  LYS   C N   1 
ATOM   1607 C  CA  . LYS   B 1 64  ? 28.838 -32.922 6.343  1.00 15.05  ? 70  LYS   C CA  1 
ATOM   1608 C  C   . LYS   B 1 64  ? 28.926 -32.427 7.772  1.00 13.92  ? 70  LYS   C C   1 
ATOM   1609 O  O   . LYS   B 1 64  ? 28.957 -31.208 8.011  1.00 14.64  ? 70  LYS   C O   1 
ATOM   1610 C  CB  . LYS   B 1 64  ? 30.261 -32.952 5.754  1.00 19.14  ? 70  LYS   C CB  1 
ATOM   1611 C  CG  . LYS   B 1 64  ? 30.387 -33.933 4.587  1.00 29.04  ? 70  LYS   C CG  1 
ATOM   1612 C  CD  . LYS   B 1 64  ? 31.839 -34.334 4.331  1.00 36.70  ? 70  LYS   C CD  1 
ATOM   1613 C  CE  . LYS   B 1 64  ? 31.940 -35.203 3.098  1.00 42.02  ? 70  LYS   C CE  1 
ATOM   1614 N  NZ  . LYS   B 1 64  ? 31.461 -34.505 1.873  1.00 46.77  ? 70  LYS   C NZ  1 
ATOM   1615 N  N   . HIS   B 1 65  ? 29.020 -33.380 8.678  1.00 12.75  ? 71  HIS   C N   1 
ATOM   1616 C  CA  . HIS   B 1 65  ? 29.345 -33.118 10.079 1.00 12.73  ? 71  HIS   C CA  1 
ATOM   1617 C  C   . HIS   B 1 65  ? 30.819 -33.394 10.291 1.00 14.71  ? 71  HIS   C C   1 
ATOM   1618 O  O   . HIS   B 1 65  ? 31.309 -34.485 9.953  1.00 18.39  ? 71  HIS   C O   1 
ATOM   1619 C  CB  . HIS   B 1 65  ? 28.529 -34.009 11.006 1.00 12.50  ? 71  HIS   C CB  1 
ATOM   1620 C  CG  . HIS   B 1 65  ? 27.053 -33.751 10.993 1.00 12.26  ? 71  HIS   C CG  1 
ATOM   1621 N  ND1 . HIS   B 1 65  ? 26.392 -32.967 11.937 1.00 15.45  ? 71  HIS   C ND1 1 
ATOM   1622 C  CD2 . HIS   B 1 65  ? 26.144 -34.170 10.072 1.00 11.96  ? 71  HIS   C CD2 1 
ATOM   1623 C  CE1 . HIS   B 1 65  ? 25.098 -32.983 11.591 1.00 13.67  ? 71  HIS   C CE1 1 
ATOM   1624 N  NE2 . HIS   B 1 65  ? 24.903 -33.692 10.487 1.00 15.39  ? 71  HIS   C NE2 1 
ATOM   1625 N  N   . TYR   B 1 66  ? 31.570 -32.445 10.878 1.00 12.62  ? 72  TYR   C N   1 
ATOM   1626 C  CA  . TYR   B 1 66  ? 33.016 -32.601 11.056 1.00 11.89  ? 72  TYR   C CA  1 
ATOM   1627 C  C   . TYR   B 1 66  ? 33.369 -32.633 12.544 1.00 11.99  ? 72  TYR   C C   1 
ATOM   1628 O  O   . TYR   B 1 66  ? 32.929 -31.764 13.299 1.00 11.51  ? 72  TYR   C O   1 
ATOM   1629 C  CB  . TYR   B 1 66  ? 33.767 -31.369 10.494 1.00 12.74  ? 72  TYR   C CB  1 
ATOM   1630 C  CG  . TYR   B 1 66  ? 33.738 -31.266 8.968  1.00 13.87  ? 72  TYR   C CG  1 
ATOM   1631 C  CD1 . TYR   B 1 66  ? 34.578 -32.037 8.189  1.00 16.55  ? 72  TYR   C CD1 1 
ATOM   1632 C  CD2 . TYR   B 1 66  ? 32.908 -30.358 8.315  1.00 14.87  ? 72  TYR   C CD2 1 
ATOM   1633 C  CE1 . TYR   B 1 66  ? 34.591 -31.936 6.806  1.00 16.82  ? 72  TYR   C CE1 1 
ATOM   1634 C  CE2 . TYR   B 1 66  ? 32.902 -30.252 6.922  1.00 15.56  ? 72  TYR   C CE2 1 
ATOM   1635 C  CZ  . TYR   B 1 66  ? 33.738 -31.051 6.182  1.00 15.12  ? 72  TYR   C CZ  1 
ATOM   1636 O  OH  . TYR   B 1 66  ? 33.715 -30.884 4.799  1.00 18.72  ? 72  TYR   C OH  1 
ATOM   1637 N  N   . PRO   B 1 67  ? 34.185 -33.596 12.965 1.00 11.79  ? 73  PRO   C N   1 
ATOM   1638 C  CA  . PRO   B 1 67  ? 34.705 -33.575 14.339 1.00 12.12  ? 73  PRO   C CA  1 
ATOM   1639 C  C   . PRO   B 1 67  ? 35.804 -32.487 14.466 1.00 12.58  ? 73  PRO   C C   1 
ATOM   1640 O  O   . PRO   B 1 67  ? 36.682 -32.421 13.577 1.00 15.70  ? 73  PRO   C O   1 
ATOM   1641 C  CB  . PRO   B 1 67  ? 35.316 -34.989 14.529 1.00 13.99  ? 73  PRO   C CB  1 
ATOM   1642 C  CG  . PRO   B 1 67  ? 35.595 -35.458 13.169 1.00 16.10  ? 73  PRO   C CG  1 
ATOM   1643 C  CD  . PRO   B 1 67  ? 34.692 -34.757 12.178 1.00 12.83  ? 73  PRO   C CD  1 
ATOM   1644 N  N   . VAL   B 1 68  ? 35.769 -31.724 15.516 1.00 11.23  ? 74  VAL   C N   1 
ATOM   1645 C  CA  . VAL   B 1 68  ? 36.727 -30.617 15.674 1.00 12.14  ? 74  VAL   C CA  1 
ATOM   1646 C  C   . VAL   B 1 68  ? 37.104 -30.435 17.098 1.00 12.69  ? 74  VAL   C C   1 
ATOM   1647 O  O   . VAL   B 1 68  ? 36.355 -30.724 18.030 1.00 12.82  ? 74  VAL   C O   1 
ATOM   1648 C  CB  . VAL   B 1 68  ? 36.129 -29.235 15.191 1.00 14.64  ? 74  VAL   C CB  1 
ATOM   1649 C  CG1 . VAL   B 1 68  ? 36.050 -29.153 13.654 1.00 17.59  ? 74  VAL   C CG1 1 
ATOM   1650 C  CG2 . VAL   B 1 68  ? 34.772 -28.959 15.845 1.00 14.81  ? 74  VAL   C CG2 1 
ATOM   1651 N  N   . SER   B 1 69  ? 38.328 -29.899 17.308 1.00 11.56  ? 75  SER   C N   1 
ATOM   1652 C  CA  . SER   B 1 69  ? 38.743 -29.255 18.561 1.00 12.62  ? 75  SER   C CA  1 
ATOM   1653 C  C   . SER   B 1 69  ? 38.455 -27.763 18.460 1.00 11.40  ? 75  SER   C C   1 
ATOM   1654 O  O   . SER   B 1 69  ? 38.603 -27.167 17.368 1.00 13.01  ? 75  SER   C O   1 
ATOM   1655 C  CB  . SER   B 1 69  ? 40.246 -29.427 18.749 1.00 15.18  ? 75  SER   C CB  1 
ATOM   1656 O  OG  . SER   B 1 69  ? 40.506 -30.810 18.864 1.00 21.08  ? 75  SER   C OG  1 
ATOM   1657 N  N   . PHE   B 1 70  ? 37.975 -27.161 19.529 1.00 11.62  ? 76  PHE   C N   1 
ATOM   1658 C  CA  . PHE   B 1 70  ? 37.615 -25.739 19.494 1.00 12.05  ? 76  PHE   C CA  1 
ATOM   1659 C  C   . PHE   B 1 70  ? 38.079 -25.021 20.739 1.00 12.26  ? 76  PHE   C C   1 
ATOM   1660 O  O   . PHE   B 1 70  ? 38.243 -25.627 21.803 1.00 13.18  ? 76  PHE   C O   1 
ATOM   1661 C  CB  . PHE   B 1 70  ? 36.093 -25.521 19.224 1.00 12.59  ? 76  PHE   C CB  1 
ATOM   1662 C  CG  . PHE   B 1 70  ? 35.176 -26.229 20.215 1.00 12.06  ? 76  PHE   C CG  1 
ATOM   1663 C  CD1 . PHE   B 1 70  ? 34.748 -27.534 19.989 1.00 12.54  ? 76  PHE   C CD1 1 
ATOM   1664 C  CD2 . PHE   B 1 70  ? 34.731 -25.578 21.363 1.00 12.55  ? 76  PHE   C CD2 1 
ATOM   1665 C  CE1 . PHE   B 1 70  ? 33.923 -28.181 20.924 1.00 11.70  ? 76  PHE   C CE1 1 
ATOM   1666 C  CE2 . PHE   B 1 70  ? 33.868 -26.232 22.257 1.00 12.38  ? 76  PHE   C CE2 1 
ATOM   1667 C  CZ  . PHE   B 1 70  ? 33.489 -27.522 22.042 1.00 12.21  ? 76  PHE   C CZ  1 
ATOM   1668 N  N   . SER   B 1 71  ? 38.364 -23.733 20.603 1.00 12.28  ? 77  SER   C N   1 
ATOM   1669 C  CA  . SER   B 1 71  ? 38.933 -22.958 21.690 1.00 13.48  ? 77  SER   C CA  1 
ATOM   1670 C  C   . SER   B 1 71  ? 37.905 -22.577 22.736 1.00 14.91  ? 77  SER   C C   1 
ATOM   1671 O  O   . SER   B 1 71  ? 36.710 -22.764 22.579 1.00 15.70  ? 77  SER   C O   1 
ATOM   1672 C  CB  . SER   B 1 71  ? 39.655 -21.724 21.128 1.00 14.81  ? 77  SER   C CB  1 
ATOM   1673 O  OG  . SER   B 1 71  ? 38.745 -20.858 20.453 1.00 16.76  ? 77  SER   C OG  1 
ATOM   1674 N  N   . LYS   B 1 72  ? 38.358 -22.037 23.862 1.00 17.19  ? 78  LYS   C N   1 
ATOM   1675 C  CA  . LYS   B 1 72  ? 37.444 -21.600 24.929 1.00 16.52  ? 78  LYS   C CA  1 
ATOM   1676 C  C   . LYS   B 1 72  ? 36.776 -20.256 24.517 1.00 16.66  ? 78  LYS   C C   1 
ATOM   1677 O  O   . LYS   B 1 72  ? 37.399 -19.444 23.815 1.00 18.30  ? 78  LYS   C O   1 
ATOM   1678 C  CB  . LYS   B 1 72  ? 38.254 -21.373 26.226 1.00 21.41  ? 78  LYS   C CB  1 
ATOM   1679 C  CG  . LYS   B 1 72  ? 39.096 -22.559 26.624 1.00 25.13  ? 78  LYS   C CG  1 
ATOM   1680 C  CD  . LYS   B 1 72  ? 39.265 -22.658 28.184 1.00 36.76  ? 78  LYS   C CD  1 
ATOM   1681 C  CE  . LYS   B 1 72  ? 39.329 -24.117 28.657 1.00 44.16  ? 78  LYS   C CE  1 
ATOM   1682 N  NZ  . LYS   B 1 72  ? 39.362 -24.246 30.144 1.00 48.04  ? 78  LYS   C NZ  1 
ATOM   1683 N  N   . PRO   B 1 73  ? 35.532 -19.990 24.956 1.00 16.03  ? 79  PRO   C N   1 
ATOM   1684 C  CA  . PRO   B 1 73  ? 34.829 -18.750 24.528 1.00 16.31  ? 79  PRO   C CA  1 
ATOM   1685 C  C   . PRO   B 1 73  ? 35.597 -17.490 24.907 1.00 17.01  ? 79  PRO   C C   1 
ATOM   1686 O  O   . PRO   B 1 73  ? 36.046 -17.366 26.063 1.00 19.92  ? 79  PRO   C O   1 
ATOM   1687 C  CB  . PRO   B 1 73  ? 33.501 -18.805 25.279 1.00 17.60  ? 79  PRO   C CB  1 
ATOM   1688 C  CG  . PRO   B 1 73  ? 33.316 -20.214 25.684 1.00 21.20  ? 79  PRO   C CG  1 
ATOM   1689 C  CD  . PRO   B 1 73  ? 34.689 -20.845 25.821 1.00 17.66  ? 79  PRO   C CD  1 
ATOM   1690 N  N   . SER   B 1 74  ? 35.860 -16.621 23.911 1.00 15.66  ? 80  SER   C N   1 
ATOM   1691 C  CA  . SER   B 1 74  ? 36.740 -15.462 24.116 1.00 17.17  ? 80  SER   C CA  1 
ATOM   1692 C  C   . SER   B 1 74  ? 36.301 -14.291 23.242 1.00 17.16  ? 80  SER   C C   1 
ATOM   1693 O  O   . SER   B 1 74  ? 35.427 -14.436 22.381 1.00 17.53  ? 80  SER   C O   1 
ATOM   1694 C  CB  . SER   B 1 74  ? 38.179 -15.811 23.702 1.00 19.82  ? 80  SER   C CB  1 
ATOM   1695 O  OG  . SER   B 1 74  ? 38.629 -17.025 24.282 1.00 28.68  ? 80  SER   C OG  1 
ATOM   1696 N  N   . LEU   B 1 75  ? 36.964 -13.132 23.421 1.00 18.39  ? 81  LEU   C N   1 
ATOM   1697 C  CA  . LEU   B 1 75  ? 36.757 -11.916 22.628 1.00 19.39  ? 81  LEU   C CA  1 
ATOM   1698 C  C   . LEU   B 1 75  ? 37.797 -11.954 21.494 1.00 20.79  ? 81  LEU   C C   1 
ATOM   1699 O  O   . LEU   B 1 75  ? 39.026 -11.885 21.767 1.00 23.12  ? 81  LEU   C O   1 
ATOM   1700 C  CB  . LEU   B 1 75  ? 36.986 -10.663 23.512 1.00 21.07  ? 81  LEU   C CB  1 
ATOM   1701 C  CG  . LEU   B 1 75  ? 36.687 -9.310  22.888 1.00 23.48  ? 81  LEU   C CG  1 
ATOM   1702 C  CD1 . LEU   B 1 75  ? 35.218 -9.129  22.698 1.00 23.74  ? 81  LEU   C CD1 1 
ATOM   1703 C  CD2 . LEU   B 1 75  ? 37.257 -8.157  23.758 1.00 26.05  ? 81  LEU   C CD2 1 
ATOM   1704 N  N   . ILE   B 1 76  ? 37.346 -12.130 20.265 1.00 21.16  ? 82  ILE   C N   1 
ATOM   1705 C  CA  . ILE   B 1 76  ? 38.198 -12.341 19.098 1.00 23.48  ? 82  ILE   C CA  1 
ATOM   1706 C  C   . ILE   B 1 76  ? 37.927 -11.301 18.034 1.00 23.32  ? 82  ILE   C C   1 
ATOM   1707 O  O   . ILE   B 1 76  ? 36.761 -10.995 17.761 1.00 21.72  ? 82  ILE   C O   1 
ATOM   1708 C  CB  . ILE   B 1 76  ? 37.840 -13.739 18.516 1.00 25.97  ? 82  ILE   C CB  1 
ATOM   1709 C  CG1 . ILE   B 1 76  ? 38.072 -14.891 19.534 1.00 29.11  ? 82  ILE   C CG1 1 
ATOM   1710 C  CG2 . ILE   B 1 76  ? 38.536 -14.020 17.173 1.00 28.61  ? 82  ILE   C CG2 1 
ATOM   1711 C  CD1 . ILE   B 1 76  ? 39.550 -15.385 19.690 1.00 30.34  ? 82  ILE   C CD1 1 
ATOM   1712 N  N   . PHE   B 1 77  ? 38.991 -10.780 17.386 1.00 23.17  ? 83  PHE   C N   1 
ATOM   1713 C  CA  . PHE   B 1 77  ? 38.806 -9.877  16.253 1.00 23.23  ? 83  PHE   C CA  1 
ATOM   1714 C  C   . PHE   B 1 77  ? 38.463 -10.750 15.024 1.00 23.72  ? 83  PHE   C C   1 
ATOM   1715 O  O   . PHE   B 1 77  ? 39.180 -11.712 14.699 1.00 25.78  ? 83  PHE   C O   1 
ATOM   1716 C  CB  . PHE   B 1 77  ? 40.107 -9.098  15.969 1.00 23.98  ? 83  PHE   C CB  1 
ATOM   1717 C  CG  . PHE   B 1 77  ? 39.825 -7.960  15.015 1.00 24.79  ? 83  PHE   C CG  1 
ATOM   1718 C  CD1 . PHE   B 1 77  ? 39.095 -6.864  15.423 1.00 25.69  ? 83  PHE   C CD1 1 
ATOM   1719 C  CD2 . PHE   B 1 77  ? 40.213 -8.035  13.676 1.00 26.55  ? 83  PHE   C CD2 1 
ATOM   1720 C  CE1 . PHE   B 1 77  ? 38.778 -5.832  14.526 1.00 27.02  ? 83  PHE   C CE1 1 
ATOM   1721 C  CE2 . PHE   B 1 77  ? 39.904 -7.005  12.786 1.00 26.96  ? 83  PHE   C CE2 1 
ATOM   1722 C  CZ  . PHE   B 1 77  ? 39.224 -5.899  13.223 1.00 26.97  ? 83  PHE   C CZ  1 
ATOM   1723 N  N   . VAL   B 1 78  ? 37.333 -10.441 14.387 1.00 20.60  ? 84  VAL   C N   1 
ATOM   1724 C  CA  . VAL   B 1 78  ? 36.832 -11.183 13.246 1.00 20.20  ? 84  VAL   C CA  1 
ATOM   1725 C  C   . VAL   B 1 78  ? 36.926 -10.245 12.018 1.00 19.86  ? 84  VAL   C C   1 
ATOM   1726 O  O   . VAL   B 1 78  ? 36.436 -9.118  12.087 1.00 19.94  ? 84  VAL   C O   1 
ATOM   1727 C  CB  . VAL   B 1 78  ? 35.349 -11.620 13.524 1.00 20.76  ? 84  VAL   C CB  1 
ATOM   1728 C  CG1 . VAL   B 1 78  ? 34.809 -12.405 12.336 1.00 20.69  ? 84  VAL   C CG1 1 
ATOM   1729 C  CG2 . VAL   B 1 78  ? 35.253 -12.466 14.804 1.00 21.44  ? 84  VAL   C CG2 1 
ATOM   1730 N  N   . GLU   B 1 79  ? 37.447 -10.722 10.877 1.00 19.33  ? 85  GLU   C N   1 
ATOM   1731 C  CA  . GLU   B 1 79  ? 37.479 -9.925  9.648  1.00 19.92  ? 85  GLU   C CA  1 
ATOM   1732 C  C   . GLU   B 1 79  ? 36.082 -9.680  9.104  1.00 19.19  ? 85  GLU   C C   1 
ATOM   1733 O  O   . GLU   B 1 79  ? 35.121 -10.377 9.468  1.00 18.00  ? 85  GLU   C O   1 
ATOM   1734 C  CB  . GLU   B 1 79  ? 38.414 -10.532 8.569  1.00 22.75  ? 85  GLU   C CB  1 
ATOM   1735 C  CG  . GLU   B 1 79  ? 39.883 -10.564 8.982  1.00 27.14  ? 85  GLU   C CG  1 
ATOM   1736 C  CD  . GLU   B 1 79  ? 40.487 -9.184  9.220  1.00 32.55  ? 85  GLU   C CD  1 
ATOM   1737 O  OE1 . GLU   B 1 79  ? 40.042 -8.186  8.596  1.00 36.22  ? 85  GLU   C OE1 1 
ATOM   1738 O  OE2 . GLU   B 1 79  ? 41.412 -9.095  10.060 1.00 36.33  ? 85  GLU   C OE2 1 
ATOM   1739 N  N   . ALA   B 1 80  ? 35.957 -8.689  8.219  1.00 20.20  ? 86  ALA   C N   1 
ATOM   1740 C  CA  . ALA   B 1 80  ? 34.671 -8.364  7.640  1.00 21.45  ? 86  ALA   C CA  1 
ATOM   1741 C  C   . ALA   B 1 80  ? 34.066 -9.577  6.907  1.00 21.32  ? 86  ALA   C C   1 
ATOM   1742 O  O   . ALA   B 1 80  ? 34.791 -10.398 6.330  1.00 23.13  ? 86  ALA   C O   1 
ATOM   1743 C  CB  . ALA   B 1 80  ? 34.849 -7.210  6.657  1.00 22.97  ? 86  ALA   C CB  1 
ATOM   1744 N  N   . SER   B 1 81  ? 32.788 -9.748  7.074  1.00 20.03  ? 87  SER   C N   1 
ATOM   1745 C  CA  . SER   B 1 81  ? 32.067 -10.773 6.387  1.00 20.88  ? 87  SER   C CA  1 
ATOM   1746 C  C   . SER   B 1 81  ? 30.962 -10.112 5.558  1.00 22.02  ? 87  SER   C C   1 
ATOM   1747 O  O   . SER   B 1 81  ? 30.793 -8.854  5.564  1.00 22.93  ? 87  SER   C O   1 
ATOM   1748 C  CB  . SER   B 1 81  ? 31.471 -11.757 7.393  1.00 18.47  ? 87  SER   C CB  1 
ATOM   1749 O  OG  . SER   B 1 81  ? 30.395 -11.102 8.075  1.00 18.58  ? 87  SER   C OG  1 
ATOM   1750 N  N   . GLU   B 1 82  ? 30.148 -10.939 4.890  1.00 22.25  ? 88  GLU   C N   1 
ATOM   1751 C  CA  . GLU   B 1 82  ? 29.052 -10.308 4.130  1.00 23.88  ? 88  GLU   C CA  1 
ATOM   1752 C  C   . GLU   B 1 82  ? 27.959 -9.669  5.054  1.00 23.19  ? 88  GLU   C C   1 
ATOM   1753 O  O   . GLU   B 1 82  ? 27.191 -8.805  4.602  1.00 24.29  ? 88  GLU   C O   1 
ATOM   1754 C  CB  . GLU   B 1 82  ? 28.467 -11.290 3.113  1.00 29.32  ? 88  GLU   C CB  1 
ATOM   1755 C  CG  . GLU   B 1 82  ? 27.502 -12.300 3.670  1.00 38.89  ? 88  GLU   C CG  1 
ATOM   1756 C  CD  . GLU   B 1 82  ? 26.862 -13.145 2.583  1.00 45.24  ? 88  GLU   C CD  1 
ATOM   1757 O  OE1 . GLU   B 1 82  ? 27.514 -13.363 1.532  1.00 45.33  ? 88  GLU   C OE1 1 
ATOM   1758 O  OE2 . GLU   B 1 82  ? 25.708 -13.589 2.788  1.00 47.31  ? 88  GLU   C OE2 1 
ATOM   1759 N  N   . TYR   B 1 83  ? 27.966 -10.006 6.353  1.00 20.54  ? 89  TYR   C N   1 
ATOM   1760 C  CA  . TYR   B 1 83  ? 26.926 -9.520  7.259  1.00 19.48  ? 89  TYR   C CA  1 
ATOM   1761 C  C   . TYR   B 1 83  ? 27.429 -8.668  8.459  1.00 21.09  ? 89  TYR   C C   1 
ATOM   1762 O  O   . TYR   B 1 83  ? 26.585 -8.085  9.147  1.00 21.68  ? 89  TYR   C O   1 
ATOM   1763 C  CB  . TYR   B 1 83  ? 26.073 -10.726 7.740  1.00 18.49  ? 89  TYR   C CB  1 
ATOM   1764 C  CG  . TYR   B 1 83  ? 26.908 -11.915 8.230  1.00 17.27  ? 89  TYR   C CG  1 
ATOM   1765 C  CD1 . TYR   B 1 83  ? 27.359 -12.899 7.346  1.00 17.43  ? 89  TYR   C CD1 1 
ATOM   1766 C  CD2 . TYR   B 1 83  ? 27.252 -12.053 9.568  1.00 17.42  ? 89  TYR   C CD2 1 
ATOM   1767 C  CE1 . TYR   B 1 83  ? 28.096 -14.012 7.794  1.00 17.50  ? 89  TYR   C CE1 1 
ATOM   1768 C  CE2 . TYR   B 1 83  ? 28.024 -13.125 10.018 1.00 17.93  ? 89  TYR   C CE2 1 
ATOM   1769 C  CZ  . TYR   B 1 83  ? 28.461 -14.107 9.129  1.00 17.25  ? 89  TYR   C CZ  1 
ATOM   1770 O  OH  . TYR   B 1 83  ? 29.309 -15.134 9.520  1.00 17.75  ? 89  TYR   C OH  1 
ATOM   1771 N  N   . TYR   B 1 84  ? 28.738 -8.568  8.745  1.00 18.64  ? 90  TYR   C N   1 
ATOM   1772 C  CA  . TYR   B 1 84  ? 29.249 -7.645  9.775  1.00 18.91  ? 90  TYR   C CA  1 
ATOM   1773 C  C   . TYR   B 1 84  ? 30.585 -7.023  9.260  1.00 18.72  ? 90  TYR   C C   1 
ATOM   1774 O  O   . TYR   B 1 84  ? 31.308 -7.650  8.490  1.00 19.23  ? 90  TYR   C O   1 
ATOM   1775 C  CB  . TYR   B 1 84  ? 29.611 -8.412  11.077 1.00 17.16  ? 90  TYR   C CB  1 
ATOM   1776 C  CG  . TYR   B 1 84  ? 28.437 -8.833  11.939 1.00 15.86  ? 90  TYR   C CG  1 
ATOM   1777 C  CD1 . TYR   B 1 84  ? 27.495 -7.903  12.397 1.00 16.71  ? 90  TYR   C CD1 1 
ATOM   1778 C  CD2 . TYR   B 1 84  ? 28.254 -10.146 12.268 1.00 16.06  ? 90  TYR   C CD2 1 
ATOM   1779 C  CE1 . TYR   B 1 84  ? 26.402 -8.297  13.181 1.00 17.06  ? 90  TYR   C CE1 1 
ATOM   1780 C  CE2 . TYR   B 1 84  ? 27.169 -10.550 13.046 1.00 15.39  ? 90  TYR   C CE2 1 
ATOM   1781 C  CZ  . TYR   B 1 84  ? 26.288 -9.619  13.571 1.00 16.08  ? 90  TYR   C CZ  1 
ATOM   1782 O  OH  . TYR   B 1 84  ? 25.195 -9.998  14.340 1.00 15.48  ? 90  TYR   C OH  1 
ATOM   1783 N  N   . PRO   B 1 85  ? 30.940 -5.812  9.703  1.00 19.02  ? 91  PRO   C N   1 
ATOM   1784 C  CA  . PRO   B 1 85  ? 32.288 -5.291  9.416  1.00 19.38  ? 91  PRO   C CA  1 
ATOM   1785 C  C   . PRO   B 1 85  ? 33.309 -6.085  10.249 1.00 20.04  ? 91  PRO   C C   1 
ATOM   1786 O  O   . PRO   B 1 85  ? 32.952 -6.888  11.146 1.00 18.99  ? 91  PRO   C O   1 
ATOM   1787 C  CB  . PRO   B 1 85  ? 32.178 -3.835  9.901  1.00 20.85  ? 91  PRO   C CB  1 
ATOM   1788 C  CG  . PRO   B 1 85  ? 31.281 -3.935  11.047 1.00 20.16  ? 91  PRO   C CG  1 
ATOM   1789 C  CD  . PRO   B 1 85  ? 30.199 -4.969  10.671 1.00 19.47  ? 91  PRO   C CD  1 
ATOM   1790 N  N   . ALA   B 1 86  ? 34.609 -5.813  10.027 1.00 19.89  ? 92  ALA   C N   1 
ATOM   1791 C  CA  . ALA   B 1 86  ? 35.666 -6.329  10.880 1.00 21.36  ? 92  ALA   C CA  1 
ATOM   1792 C  C   . ALA   B 1 86  ? 35.443 -5.745  12.298 1.00 22.77  ? 92  ALA   C C   1 
ATOM   1793 O  O   . ALA   B 1 86  ? 35.130 -4.549  12.433 1.00 23.87  ? 92  ALA   C O   1 
ATOM   1794 C  CB  . ALA   B 1 86  ? 37.036 -5.906  10.346 1.00 21.86  ? 92  ALA   C CB  1 
ATOM   1795 N  N   . ARG   B 1 87  ? 35.452 -6.621  13.324 1.00 22.79  ? 93  ARG   C N   1 
ATOM   1796 C  CA  . ARG   B 1 87  ? 35.109 -6.156  14.670 1.00 22.43  ? 93  ARG   C CA  1 
ATOM   1797 C  C   . ARG   B 1 87  ? 35.497 -7.206  15.696 1.00 21.58  ? 93  ARG   C C   1 
ATOM   1798 O  O   . ARG   B 1 87  ? 35.744 -8.359  15.333 1.00 20.46  ? 93  ARG   C O   1 
ATOM   1799 C  CB  . ARG   B 1 87  ? 33.587 -5.913  14.779 1.00 22.66  ? 93  ARG   C CB  1 
ATOM   1800 C  CG  . ARG   B 1 87  ? 32.783 -7.231  14.692 1.00 20.55  ? 93  ARG   C CG  1 
ATOM   1801 C  CD  . ARG   B 1 87  ? 31.304 -6.969  14.840 1.00 20.31  ? 93  ARG   C CD  1 
ATOM   1802 N  NE  . ARG   B 1 87  ? 30.614 -8.242  15.089 1.00 19.08  ? 93  ARG   C NE  1 
ATOM   1803 C  CZ  . ARG   B 1 87  ? 29.526 -8.405  15.817 1.00 19.92  ? 93  ARG   C CZ  1 
ATOM   1804 N  NH1 . ARG   B 1 87  ? 28.892 -7.352  16.327 1.00 19.97  ? 93  ARG   C NH1 1 
ATOM   1805 N  NH2 . ARG   B 1 87  ? 29.034 -9.623  16.008 1.00 20.50  ? 93  ARG   C NH2 1 
ATOM   1806 N  N   . TYR   B 1 88  ? 35.381 -6.844  17.001 1.00 22.85  ? 94  TYR   C N   1 
ATOM   1807 C  CA  . TYR   B 1 88  ? 35.544 -7.841  18.055 1.00 23.84  ? 94  TYR   C CA  1 
ATOM   1808 C  C   . TYR   B 1 88  ? 34.174 -8.488  18.321 1.00 21.32  ? 94  TYR   C C   1 
ATOM   1809 O  O   . TYR   B 1 88  ? 33.162 -7.820  18.451 1.00 22.45  ? 94  TYR   C O   1 
ATOM   1810 C  CB  . TYR   B 1 88  ? 36.011 -7.192  19.367 1.00 26.43  ? 94  TYR   C CB  1 
ATOM   1811 C  CG  . TYR   B 1 88  ? 37.477 -6.860  19.319 1.00 29.18  ? 94  TYR   C CG  1 
ATOM   1812 C  CD1 . TYR   B 1 88  ? 38.436 -7.836  19.544 1.00 29.83  ? 94  TYR   C CD1 1 
ATOM   1813 C  CD2 . TYR   B 1 88  ? 37.910 -5.593  18.929 1.00 30.59  ? 94  TYR   C CD2 1 
ATOM   1814 C  CE1 . TYR   B 1 88  ? 39.798 -7.548  19.442 1.00 31.64  ? 94  TYR   C CE1 1 
ATOM   1815 C  CE2 . TYR   B 1 88  ? 39.255 -5.300  18.803 1.00 31.73  ? 94  TYR   C CE2 1 
ATOM   1816 C  CZ  . TYR   B 1 88  ? 40.198 -6.269  19.081 1.00 32.75  ? 94  TYR   C CZ  1 
ATOM   1817 O  OH  . TYR   B 1 88  ? 41.532 -5.930  18.967 1.00 35.42  ? 94  TYR   C OH  1 
ATOM   1818 N  N   . GLN   B 1 89  ? 34.171 -9.831  18.385 1.00 18.79  ? 95  GLN   C N   1 
ATOM   1819 C  CA  . GLN   B 1 89  ? 32.975 -10.606 18.738 1.00 17.46  ? 95  GLN   C CA  1 
ATOM   1820 C  C   . GLN   B 1 89  ? 33.271 -11.344 20.049 1.00 16.17  ? 95  GLN   C C   1 
ATOM   1821 O  O   . GLN   B 1 89  ? 34.365 -11.921 20.205 1.00 17.56  ? 95  GLN   C O   1 
ATOM   1822 C  CB  . GLN   B 1 89  ? 32.634 -11.576 17.597 1.00 18.26  ? 95  GLN   C CB  1 
ATOM   1823 C  CG  . GLN   B 1 89  ? 31.387 -12.389 17.891 1.00 18.84  ? 95  GLN   C CG  1 
ATOM   1824 C  CD  . GLN   B 1 89  ? 30.686 -12.934 16.677 1.00 16.41  ? 95  GLN   C CD  1 
ATOM   1825 O  OE1 . GLN   B 1 89  ? 30.648 -12.342 15.587 1.00 18.01  ? 95  GLN   C OE1 1 
ATOM   1826 N  NE2 . GLN   B 1 89  ? 30.093 -14.099 16.883 1.00 14.92  ? 95  GLN   C NE2 1 
ATOM   1827 N  N   . SER   B 1 90  ? 32.355 -11.299 20.984 1.00 15.77  ? 96  SER   C N   1 
ATOM   1828 C  CA  . SER   B 1 90  ? 32.515 -11.920 22.288 1.00 15.60  ? 96  SER   C CA  1 
ATOM   1829 C  C   . SER   B 1 90  ? 31.931 -13.344 22.355 1.00 14.60  ? 96  SER   C C   1 
ATOM   1830 O  O   . SER   B 1 90  ? 31.098 -13.715 21.530 1.00 14.49  ? 96  SER   C O   1 
ATOM   1831 C  CB  . SER   B 1 90  ? 31.952 -11.031 23.404 1.00 17.13  ? 96  SER   C CB  1 
ATOM   1832 O  OG  . SER   B 1 90  ? 30.558 -11.038 23.277 1.00 17.95  ? 96  SER   C OG  1 
ATOM   1833 N  N   . HIS   B 1 91  ? 32.404 -14.120 23.335 1.00 15.48  ? 97  HIS   C N   1 
ATOM   1834 C  CA  . HIS   B 1 91  ? 31.897 -15.475 23.609 1.00 14.52  ? 97  HIS   C CA  1 
ATOM   1835 C  C   . HIS   B 1 91  ? 32.029 -16.352 22.338 1.00 13.75  ? 97  HIS   C C   1 
ATOM   1836 O  O   . HIS   B 1 91  ? 31.135 -17.173 22.071 1.00 14.34  ? 97  HIS   C O   1 
ATOM   1837 C  CB  . HIS   B 1 91  ? 30.453 -15.436 24.153 1.00 15.66  ? 97  HIS   C CB  1 
ATOM   1838 C  CG  . HIS   B 1 91  ? 30.324 -14.694 25.464 1.00 17.24  ? 97  HIS   C CG  1 
ATOM   1839 N  ND1 . HIS   B 1 91  ? 30.302 -15.362 26.675 1.00 19.48  ? 97  HIS   C ND1 1 
ATOM   1840 C  CD2 . HIS   B 1 91  ? 30.201 -13.366 25.698 1.00 17.49  ? 97  HIS   C CD2 1 
ATOM   1841 C  CE1 . HIS   B 1 91  ? 30.159 -14.437 27.612 1.00 19.78  ? 97  HIS   C CE1 1 
ATOM   1842 N  NE2 . HIS   B 1 91  ? 30.105 -13.216 27.081 1.00 19.65  ? 97  HIS   C NE2 1 
ATOM   1843 N  N   . LEU   B 1 92  ? 33.136 -16.209 21.617 1.00 13.27  ? 98  LEU   C N   1 
ATOM   1844 C  CA  . LEU   B 1 92  ? 33.305 -16.906 20.349 1.00 13.45  ? 98  LEU   C CA  1 
ATOM   1845 C  C   . LEU   B 1 92  ? 34.401 -17.972 20.523 1.00 13.69  ? 98  LEU   C C   1 
ATOM   1846 O  O   . LEU   B 1 92  ? 35.376 -17.755 21.234 1.00 14.21  ? 98  LEU   C O   1 
ATOM   1847 C  CB  . LEU   B 1 92  ? 33.774 -15.881 19.265 1.00 14.68  ? 98  LEU   C CB  1 
ATOM   1848 C  CG  . LEU   B 1 92  ? 33.901 -16.450 17.846 1.00 15.81  ? 98  LEU   C CG  1 
ATOM   1849 C  CD1 . LEU   B 1 92  ? 32.567 -16.826 17.261 1.00 16.20  ? 98  LEU   C CD1 1 
ATOM   1850 C  CD2 . LEU   B 1 92  ? 34.611 -15.439 16.920 1.00 17.75  ? 98  LEU   C CD2 1 
ATOM   1851 N  N   . MET   B 1 93  ? 34.217 -19.122 19.894 1.00 12.89  ? 99  MET   C N   1 
ATOM   1852 C  CA  . MET   B 1 93  ? 35.159 -20.244 19.947 1.00 12.79  ? 99  MET   C CA  1 
ATOM   1853 C  C   . MET   B 1 93  ? 35.583 -20.555 18.521 1.00 13.79  ? 99  MET   C C   1 
ATOM   1854 O  O   . MET   B 1 93  ? 34.726 -20.593 17.632 1.00 13.73  ? 99  MET   C O   1 
ATOM   1855 C  CB  . MET   B 1 93  ? 34.407 -21.467 20.510 1.00 14.33  ? 99  MET   C CB  1 
ATOM   1856 C  CG  . MET   B 1 93  ? 33.946 -21.228 21.934 1.00 15.36  ? 99  MET   C CG  1 
ATOM   1857 S  SD  . MET   B 1 93  ? 32.920 -22.541 22.580 1.00 16.26  ? 99  MET   C SD  1 
ATOM   1858 C  CE  . MET   B 1 93  ? 31.405 -22.420 21.442 1.00 15.85  ? 99  MET   C CE  1 
ATOM   1859 N  N   . LEU   B 1 94  ? 36.874 -20.835 18.271 1.00 12.70  ? 100 LEU   C N   1 
ATOM   1860 C  CA  . LEU   B 1 94  ? 37.329 -21.113 16.916 1.00 13.67  ? 100 LEU   C CA  1 
ATOM   1861 C  C   . LEU   B 1 94  ? 37.786 -22.560 16.784 1.00 12.53  ? 100 LEU   C C   1 
ATOM   1862 O  O   . LEU   B 1 94  ? 38.305 -23.162 17.732 1.00 13.71  ? 100 LEU   C O   1 
ATOM   1863 C  CB  . LEU   B 1 94  ? 38.557 -20.229 16.524 1.00 14.96  ? 100 LEU   C CB  1 
ATOM   1864 C  CG  . LEU   B 1 94  ? 38.384 -18.744 16.436 1.00 16.88  ? 100 LEU   C CG  1 
ATOM   1865 C  CD1 . LEU   B 1 94  ? 39.721 -18.066 16.003 1.00 20.63  ? 100 LEU   C CD1 1 
ATOM   1866 C  CD2 . LEU   B 1 94  ? 37.242 -18.349 15.498 1.00 16.53  ? 100 LEU   C CD2 1 
ATOM   1867 N  N   . ALA   B 1 95  ? 37.631 -23.052 15.575 1.00 12.94  ? 101 ALA   C N   1 
ATOM   1868 C  CA  . ALA   B 1 95  ? 38.201 -24.340 15.168 1.00 12.75  ? 101 ALA   C CA  1 
ATOM   1869 C  C   . ALA   B 1 95  ? 38.772 -24.211 13.748 1.00 12.83  ? 101 ALA   C C   1 
ATOM   1870 O  O   . ALA   B 1 95  ? 38.391 -23.303 13.004 1.00 12.91  ? 101 ALA   C O   1 
ATOM   1871 C  CB  . ALA   B 1 95  ? 37.099 -25.444 15.184 1.00 13.52  ? 101 ALA   C CB  1 
ATOM   1872 N  N   . VAL   B 1 96  ? 39.634 -25.167 13.362 1.00 12.68  ? 102 VAL   C N   1 
ATOM   1873 C  CA  . VAL   B 1 96  ? 40.111 -25.212 11.988 1.00 13.81  ? 102 VAL   C CA  1 
ATOM   1874 C  C   . VAL   B 1 96  ? 39.059 -25.961 11.152 1.00 13.34  ? 102 VAL   C C   1 
ATOM   1875 O  O   . VAL   B 1 96  ? 38.724 -27.149 11.450 1.00 14.75  ? 102 VAL   C O   1 
ATOM   1876 C  CB  . VAL   B 1 96  ? 41.498 -25.924 11.978 1.00 14.67  ? 102 VAL   C CB  1 
ATOM   1877 C  CG1 . VAL   B 1 96  ? 41.972 -26.063 10.531 1.00 16.77  ? 102 VAL   C CG1 1 
ATOM   1878 C  CG2 . VAL   B 1 96  ? 42.496 -25.128 12.807 1.00 15.52  ? 102 VAL   C CG2 1 
ATOM   1879 N  N   . GLY   B 1 97  ? 38.485 -25.280 10.202 1.00 14.68  ? 103 GLY   C N   1 
ATOM   1880 C  CA  . GLY   B 1 97  ? 37.450 -25.904 9.380  1.00 16.24  ? 103 GLY   C CA  1 
ATOM   1881 C  C   . GLY   B 1 97  ? 36.765 -24.942 8.464  1.00 16.00  ? 103 GLY   C C   1 
ATOM   1882 O  O   . GLY   B 1 97  ? 37.050 -23.734 8.479  1.00 17.83  ? 103 GLY   C O   1 
ATOM   1883 N  N   . HIS   B 1 98  ? 35.890 -25.468 7.606  1.00 15.25  ? 104 HIS   C N   1 
ATOM   1884 C  CA  . HIS   B 1 98  ? 35.198 -24.682 6.627  1.00 15.39  ? 104 HIS   C CA  1 
ATOM   1885 C  C   . HIS   B 1 98  ? 33.919 -24.009 7.136  1.00 14.77  ? 104 HIS   C C   1 
ATOM   1886 O  O   . HIS   B 1 98  ? 33.105 -24.672 7.804  1.00 14.61  ? 104 HIS   C O   1 
ATOM   1887 C  CB  . HIS   B 1 98  ? 34.914 -25.573 5.426  1.00 18.07  ? 104 HIS   C CB  1 
ATOM   1888 C  CG  . HIS   B 1 98  ? 34.374 -24.789 4.296  1.00 20.65  ? 104 HIS   C CG  1 
ATOM   1889 N  ND1 . HIS   B 1 98  ? 35.159 -23.834 3.632  1.00 22.20  ? 104 HIS   C ND1 1 
ATOM   1890 C  CD2 . HIS   B 1 98  ? 33.102 -24.738 3.824  1.00 22.91  ? 104 HIS   C CD2 1 
ATOM   1891 C  CE1 . HIS   B 1 98  ? 34.341 -23.277 2.754  1.00 24.82  ? 104 HIS   C CE1 1 
ATOM   1892 N  NE2 . HIS   B 1 98  ? 33.099 -23.806 2.816  1.00 25.21  ? 104 HIS   C NE2 1 
ATOM   1893 N  N   . SER   B 1 99  ? 33.701 -22.748 6.802  1.00 15.14  ? 105 SER   C N   1 
ATOM   1894 C  CA  . SER   B 1 99  ? 32.456 -22.036 7.180  1.00 15.87  ? 105 SER   C CA  1 
ATOM   1895 C  C   . SER   B 1 99  ? 32.243 -20.842 6.199  1.00 17.50  ? 105 SER   C C   1 
ATOM   1896 O  O   . SER   B 1 99  ? 33.138 -19.969 6.077  1.00 20.23  ? 105 SER   C O   1 
ATOM   1897 C  CB  . SER   B 1 99  ? 32.654 -21.473 8.570  1.00 17.03  ? 105 SER   C CB  1 
ATOM   1898 O  OG  . SER   B 1 99  ? 31.573 -20.597 8.891  1.00 16.56  ? 105 SER   C OG  1 
ATOM   1899 N  N   . GLU   B 1 100 ? 31.161 -20.871 5.499  1.00 17.41  ? 106 GLU   C N   1 
ATOM   1900 C  CA  . GLU   B 1 100 ? 30.704 -19.802 4.598  1.00 18.78  ? 106 GLU   C CA  1 
ATOM   1901 C  C   . GLU   B 1 100 ? 29.506 -19.132 5.207  1.00 16.42  ? 106 GLU   C C   1 
ATOM   1902 O  O   . GLU   B 1 100 ? 28.925 -19.674 6.146  1.00 15.32  ? 106 GLU   C O   1 
ATOM   1903 C  CB  . GLU   B 1 100 ? 30.215 -20.449 3.292  1.00 22.30  ? 106 GLU   C CB  1 
ATOM   1904 C  CG  . GLU   B 1 100 ? 31.367 -20.995 2.520  1.00 30.19  ? 106 GLU   C CG  1 
ATOM   1905 C  CD  . GLU   B 1 100 ? 30.932 -21.737 1.289  1.00 32.54  ? 106 GLU   C CD  1 
ATOM   1906 O  OE1 . GLU   B 1 100 ? 29.862 -21.436 0.709  1.00 39.65  ? 106 GLU   C OE1 1 
ATOM   1907 O  OE2 . GLU   B 1 100 ? 31.691 -22.641 0.904  1.00 31.84  ? 106 GLU   C OE2 1 
ATOM   1908 N  N   . PRO   B 1 101 ? 29.076 -17.952 4.718  1.00 16.92  ? 107 PRO   C N   1 
ATOM   1909 C  CA  . PRO   B 1 101 ? 27.953 -17.285 5.383  1.00 16.13  ? 107 PRO   C CA  1 
ATOM   1910 C  C   . PRO   B 1 101 ? 26.701 -18.155 5.521  1.00 16.38  ? 107 PRO   C C   1 
ATOM   1911 O  O   . PRO   B 1 101 ? 26.083 -18.091 6.573  1.00 16.75  ? 107 PRO   C O   1 
ATOM   1912 C  CB  . PRO   B 1 101 ? 27.690 -16.063 4.461  1.00 18.39  ? 107 PRO   C CB  1 
ATOM   1913 C  CG  . PRO   B 1 101 ? 28.993 -15.795 3.884  1.00 21.79  ? 107 PRO   C CG  1 
ATOM   1914 C  CD  . PRO   B 1 101 ? 29.726 -17.078 3.706  1.00 19.11  ? 107 PRO   C CD  1 
ATOM   1915 N  N   . GLY   B 1 102 ? 26.387 -18.984 4.532  1.00 16.32  ? 108 GLY   C N   1 
ATOM   1916 C  CA  . GLY   B 1 102 ? 25.184 -19.825 4.603  1.00 16.64  ? 108 GLY   C CA  1 
ATOM   1917 C  C   . GLY   B 1 102 ? 25.265 -20.900 5.681  1.00 15.57  ? 108 GLY   C C   1 
ATOM   1918 O  O   . GLY   B 1 102 ? 24.269 -21.578 5.986  1.00 16.32  ? 108 GLY   C O   1 
ATOM   1919 N  N   . ASP   B 1 103 ? 26.477 -21.169 6.215  1.00 14.07  ? 109 ASP   C N   1 
ATOM   1920 C  CA  . ASP   B 1 103 ? 26.647 -22.170 7.271  1.00 13.56  ? 109 ASP   C CA  1 
ATOM   1921 C  C   . ASP   B 1 103 ? 26.268 -21.697 8.645  1.00 13.25  ? 109 ASP   C C   1 
ATOM   1922 O  O   . ASP   B 1 103 ? 26.134 -22.494 9.575  1.00 12.81  ? 109 ASP   C O   1 
ATOM   1923 C  CB  . ASP   B 1 103 ? 28.112 -22.631 7.313  1.00 14.72  ? 109 ASP   C CB  1 
ATOM   1924 C  CG  . ASP   B 1 103 ? 28.465 -23.412 6.079  1.00 16.18  ? 109 ASP   C CG  1 
ATOM   1925 O  OD1 . ASP   B 1 103 ? 27.632 -24.184 5.627  1.00 15.81  ? 109 ASP   C OD1 1 
ATOM   1926 O  OD2 . ASP   B 1 103 ? 29.614 -23.237 5.566  1.00 17.28  ? 109 ASP   C OD2 1 
ATOM   1927 N  N   . CYS   B 1 104 ? 26.061 -20.360 8.836  1.00 12.45  ? 110 CYS   C N   1 
ATOM   1928 C  CA  . CYS   B 1 104 ? 25.642 -19.830 10.125 1.00 12.37  ? 110 CYS   C CA  1 
ATOM   1929 C  C   . CYS   B 1 104 ? 24.387 -20.544 10.603 1.00 12.50  ? 110 CYS   C C   1 
ATOM   1930 O  O   . CYS   B 1 104 ? 23.447 -20.751 9.822  1.00 13.61  ? 110 CYS   C O   1 
ATOM   1931 C  CB  . CYS   B 1 104 ? 25.416 -18.319 10.066 1.00 12.51  ? 110 CYS   C CB  1 
ATOM   1932 S  SG  . CYS   B 1 104 ? 26.947 -17.345 9.928  1.00 14.91  ? 110 CYS   C SG  1 
ATOM   1933 N  N   . GLY   B 1 105 ? 24.383 -20.877 11.866 1.00 11.02  ? 111 GLY   C N   1 
ATOM   1934 C  CA  . GLY   B 1 105 ? 23.253 -21.554 12.491 1.00 12.05  ? 111 GLY   C CA  1 
ATOM   1935 C  C   . GLY   B 1 105 ? 23.465 -23.059 12.646 1.00 11.66  ? 111 GLY   C C   1 
ATOM   1936 O  O   . GLY   B 1 105 ? 22.700 -23.719 13.362 1.00 12.67  ? 111 GLY   C O   1 
ATOM   1937 N  N   . GLY   B 1 106 ? 24.487 -23.629 11.989 1.00 11.87  ? 112 GLY   C N   1 
ATOM   1938 C  CA  . GLY   B 1 106 ? 24.791 -25.071 12.145 1.00 12.80  ? 112 GLY   C CA  1 
ATOM   1939 C  C   . GLY   B 1 106 ? 25.197 -25.364 13.584 1.00 11.38  ? 112 GLY   C C   1 
ATOM   1940 O  O   . GLY   B 1 106 ? 25.902 -24.555 14.207 1.00 11.59  ? 112 GLY   C O   1 
ATOM   1941 N  N   . ILE   B 1 107 ? 24.747 -26.481 14.113 1.00 10.98  ? 113 ILE   C N   1 
ATOM   1942 C  CA  . ILE   B 1 107 ? 25.007 -26.805 15.517 1.00 10.84  ? 113 ILE   C CA  1 
ATOM   1943 C  C   . ILE   B 1 107 ? 26.373 -27.428 15.711 1.00 10.55  ? 113 ILE   C C   1 
ATOM   1944 O  O   . ILE   B 1 107 ? 26.809 -28.276 14.930 1.00 10.86  ? 113 ILE   C O   1 
ATOM   1945 C  CB  . ILE   B 1 107 ? 23.894 -27.791 16.012 1.00 13.20  ? 113 ILE   C CB  1 
ATOM   1946 C  CG1 . ILE   B 1 107 ? 22.633 -26.860 16.410 1.00 17.99  ? 113 ILE   C CG1 1 
ATOM   1947 C  CG2 . ILE   B 1 107 ? 24.300 -28.630 17.225 1.00 13.89  ? 113 ILE   C CG2 1 
ATOM   1948 C  CD1 . ILE   B 1 107 ? 21.280 -27.594 16.791 1.00 22.04  ? 113 ILE   C CD1 1 
ATOM   1949 N  N   . LEU   B 1 108 ? 27.028 -26.982 16.803 1.00 10.12  ? 114 LEU   C N   1 
ATOM   1950 C  CA  . LEU   B 1 108 ? 28.203 -27.643 17.364 1.00 9.90   ? 114 LEU   C CA  1 
ATOM   1951 C  C   . LEU   B 1 108 ? 27.688 -28.423 18.605 1.00 10.28  ? 114 LEU   C C   1 
ATOM   1952 O  O   . LEU   B 1 108 ? 27.050 -27.820 19.476 1.00 10.58  ? 114 LEU   C O   1 
ATOM   1953 C  CB  . LEU   B 1 108 ? 29.220 -26.572 17.806 1.00 10.38  ? 114 LEU   C CB  1 
ATOM   1954 C  CG  . LEU   B 1 108 ? 30.446 -27.101 18.605 1.00 10.96  ? 114 LEU   C CG  1 
ATOM   1955 C  CD1 . LEU   B 1 108 ? 31.349 -27.985 17.739 1.00 12.00  ? 114 LEU   C CD1 1 
ATOM   1956 C  CD2 . LEU   B 1 108 ? 31.276 -25.916 19.133 1.00 12.76  ? 114 LEU   C CD2 1 
ATOM   1957 N  N   . ARG   B 1 109 ? 27.994 -29.729 18.683 1.00 9.92   ? 115 ARG   C N   1 
ATOM   1958 C  CA  . ARG   B 1 109 ? 27.514 -30.537 19.820 1.00 10.58  ? 115 ARG   C CA  1 
ATOM   1959 C  C   . ARG   B 1 109 ? 28.684 -31.355 20.391 1.00 10.97  ? 115 ARG   C C   1 
ATOM   1960 O  O   . ARG   B 1 109 ? 29.606 -31.761 19.681 1.00 11.89  ? 115 ARG   C O   1 
ATOM   1961 C  CB  . ARG   B 1 109 ? 26.391 -31.479 19.361 1.00 13.70  ? 115 ARG   C CB  1 
ATOM   1962 C  CG  . ARG   B 1 109 ? 26.841 -32.469 18.285 1.00 16.07  ? 115 ARG   C CG  1 
ATOM   1963 C  CD  . ARG   B 1 109 ? 25.675 -33.370 17.824 1.00 19.18  ? 115 ARG   C CD  1 
ATOM   1964 N  NE  . ARG   B 1 109 ? 24.816 -32.624 16.905 1.00 24.20  ? 115 ARG   C NE  1 
ATOM   1965 C  CZ  . ARG   B 1 109 ? 23.500 -32.523 17.032 1.00 33.46  ? 115 ARG   C CZ  1 
ATOM   1966 N  NH1 . ARG   B 1 109 ? 22.883 -33.092 18.055 1.00 37.45  ? 115 ARG   C NH1 1 
ATOM   1967 N  NH2 . ARG   B 1 109 ? 22.791 -31.837 16.145 1.00 35.56  ? 115 ARG   C NH2 1 
ATOM   1968 N  N   . CYS   B 1 110 ? 28.586 -31.630 21.703 1.00 11.51  ? 116 CYS   C N   1 
ATOM   1969 C  CA  . CYS   B 1 110 ? 29.564 -32.504 22.426 1.00 12.57  ? 116 CYS   C CA  1 
ATOM   1970 C  C   . CYS   B 1 110 ? 28.702 -33.588 23.092 1.00 13.84  ? 116 CYS   C C   1 
ATOM   1971 O  O   . CYS   B 1 110 ? 27.470 -33.699 22.879 1.00 14.35  ? 116 CYS   C O   1 
ATOM   1972 C  CB  . CYS   B 1 110 ? 30.341 -31.709 23.473 1.00 12.61  ? 116 CYS   C CB  1 
ATOM   1973 S  SG  . CYS   B 1 110 ? 29.300 -31.068 24.813 1.00 13.29  ? 116 CYS   C SG  1 
ATOM   1974 N  N   . GLN   B 1 111 ? 29.345 -34.441 23.934 1.00 14.45  ? 117 GLN   C N   1 
ATOM   1975 C  CA  . GLN   B 1 111 ? 28.589 -35.480 24.630 1.00 16.23  ? 117 GLN   C CA  1 
ATOM   1976 C  C   . GLN   B 1 111 ? 27.510 -34.959 25.544 1.00 16.85  ? 117 GLN   C C   1 
ATOM   1977 O  O   . GLN   B 1 111 ? 26.565 -35.696 25.882 1.00 19.33  ? 117 GLN   C O   1 
ATOM   1978 C  CB  . GLN   B 1 111 ? 29.533 -36.412 25.447 1.00 17.93  ? 117 GLN   C CB  1 
ATOM   1979 C  CG  . GLN   B 1 111 ? 30.179 -35.712 26.624 1.00 19.87  ? 117 GLN   C CG  1 
ATOM   1980 C  CD  . GLN   B 1 111 ? 31.115 -36.604 27.407 1.00 31.41  ? 117 GLN   C CD  1 
ATOM   1981 O  OE1 . GLN   B 1 111 ? 32.322 -36.621 27.156 1.00 35.80  ? 117 GLN   C OE1 1 
ATOM   1982 N  NE2 . GLN   B 1 111 ? 30.565 -37.320 28.375 1.00 32.70  ? 117 GLN   C NE2 1 
ATOM   1983 N  N   . HIS   B 1 112 ? 27.582 -33.669 25.954 1.00 14.59  ? 118 HIS   C N   1 
ATOM   1984 C  CA  . HIS   B 1 112 ? 26.574 -33.130 26.878 1.00 16.24  ? 118 HIS   C CA  1 
ATOM   1985 C  C   . HIS   B 1 112 ? 25.387 -32.436 26.208 1.00 16.84  ? 118 HIS   C C   1 
ATOM   1986 O  O   . HIS   B 1 112 ? 24.452 -32.012 26.887 1.00 17.90  ? 118 HIS   C O   1 
ATOM   1987 C  CB  . HIS   B 1 112 ? 27.279 -32.157 27.813 1.00 17.15  ? 118 HIS   C CB  1 
ATOM   1988 C  CG  . HIS   B 1 112 ? 28.455 -32.762 28.547 1.00 14.60  ? 118 HIS   C CG  1 
ATOM   1989 N  ND1 . HIS   B 1 112 ? 29.781 -32.483 28.183 1.00 13.82  ? 118 HIS   C ND1 1 
ATOM   1990 C  CD2 . HIS   B 1 112 ? 28.467 -33.551 29.660 1.00 18.26  ? 118 HIS   C CD2 1 
ATOM   1991 C  CE1 . HIS   B 1 112 ? 30.537 -33.183 29.018 1.00 16.95  ? 118 HIS   C CE1 1 
ATOM   1992 N  NE2 . HIS   B 1 112 ? 29.786 -33.846 29.911 1.00 19.84  ? 118 HIS   C NE2 1 
ATOM   1993 N  N   . GLY   B 1 113 ? 25.468 -32.174 24.894 1.00 14.85  ? 119 GLY   C N   1 
ATOM   1994 C  CA  . GLY   B 1 113 ? 24.393 -31.488 24.176 1.00 14.74  ? 119 GLY   C CA  1 
ATOM   1995 C  C   . GLY   B 1 113 ? 24.933 -30.418 23.247 1.00 13.41  ? 119 GLY   C C   1 
ATOM   1996 O  O   . GLY   B 1 113 ? 26.077 -30.481 22.751 1.00 13.04  ? 119 GLY   C O   1 
ATOM   1997 N  N   . VAL   B 1 114 ? 24.086 -29.412 22.989 1.00 12.84  ? 120 VAL   C N   1 
ATOM   1998 C  CA  . VAL   B 1 114 ? 24.436 -28.354 22.042 1.00 12.15  ? 120 VAL   C CA  1 
ATOM   1999 C  C   . VAL   B 1 114 ? 25.352 -27.365 22.725 1.00 12.34  ? 120 VAL   C C   1 
ATOM   2000 O  O   . VAL   B 1 114 ? 25.046 -26.807 23.801 1.00 13.06  ? 120 VAL   C O   1 
ATOM   2001 C  CB  . VAL   B 1 114 ? 23.150 -27.655 21.543 1.00 12.94  ? 120 VAL   C CB  1 
ATOM   2002 C  CG1 . VAL   B 1 114 ? 23.489 -26.428 20.698 1.00 14.83  ? 120 VAL   C CG1 1 
ATOM   2003 C  CG2 . VAL   B 1 114 ? 22.250 -28.621 20.779 1.00 14.88  ? 120 VAL   C CG2 1 
ATOM   2004 N  N   . VAL   B 1 115 ? 26.501 -27.086 22.110 1.00 10.75  ? 121 VAL   C N   1 
ATOM   2005 C  CA  . VAL   B 1 115 ? 27.488 -26.133 22.609 1.00 10.99  ? 121 VAL   C CA  1 
ATOM   2006 C  C   . VAL   B 1 115 ? 27.250 -24.720 22.111 1.00 11.78  ? 121 VAL   C C   1 
ATOM   2007 O  O   . VAL   B 1 115 ? 27.485 -23.735 22.828 1.00 12.43  ? 121 VAL   C O   1 
ATOM   2008 C  CB  . VAL   B 1 115 ? 28.903 -26.646 22.250 1.00 11.32  ? 121 VAL   C CB  1 
ATOM   2009 C  CG1 . VAL   B 1 115 ? 29.975 -25.651 22.649 1.00 12.99  ? 121 VAL   C CG1 1 
ATOM   2010 C  CG2 . VAL   B 1 115 ? 29.173 -28.044 22.831 1.00 13.91  ? 121 VAL   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 116 ? 26.893 -24.621 20.827 1.00 11.05  ? 122 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 116 ? 26.720 -23.306 20.213 1.00 12.59  ? 122 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 116 ? 26.381 -23.469 18.740 1.00 10.58  ? 122 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 116 ? 26.070 -24.591 18.287 1.00 11.39  ? 122 GLY   C O   1 
ATOM   2015 N  N   . ILE   B 1 117 ? 26.390 -22.324 17.990 1.00 10.36  ? 123 ILE   C N   1 
ATOM   2016 C  CA  . ILE   B 1 117 ? 26.037 -22.348 16.571 1.00 10.76  ? 123 ILE   C CA  1 
ATOM   2017 C  C   . ILE   B 1 117 ? 27.099 -21.628 15.786 1.00 10.86  ? 123 ILE   C C   1 
ATOM   2018 O  O   . ILE   B 1 117 ? 27.725 -20.665 16.265 1.00 11.44  ? 123 ILE   C O   1 
ATOM   2019 C  CB  . ILE   B 1 117 ? 24.620 -21.730 16.298 1.00 11.99  ? 123 ILE   C CB  1 
ATOM   2020 C  CG1 . ILE   B 1 117 ? 24.514 -20.348 16.945 1.00 13.15  ? 123 ILE   C CG1 1 
ATOM   2021 C  CG2 . ILE   B 1 117 ? 23.517 -22.708 16.705 1.00 14.17  ? 123 ILE   C CG2 1 
ATOM   2022 C  CD1 . ILE   B 1 117 ? 23.187 -19.556 16.520 1.00 13.76  ? 123 ILE   C CD1 1 
ATOM   2023 N  N   . VAL   B 1 118 ? 27.287 -22.034 14.524 1.00 10.38  ? 124 VAL   C N   1 
ATOM   2024 C  CA  . VAL   B 1 118 ? 28.232 -21.362 13.636 1.00 10.92  ? 124 VAL   C CA  1 
ATOM   2025 C  C   . VAL   B 1 118 ? 27.826 -19.898 13.507 1.00 11.57  ? 124 VAL   C C   1 
ATOM   2026 O  O   . VAL   B 1 118 ? 26.637 -19.551 13.281 1.00 11.40  ? 124 VAL   C O   1 
ATOM   2027 C  CB  . VAL   B 1 118 ? 28.217 -22.022 12.248 1.00 10.84  ? 124 VAL   C CB  1 
ATOM   2028 C  CG1 . VAL   B 1 118 ? 29.077 -21.267 11.244 1.00 11.71  ? 124 VAL   C CG1 1 
ATOM   2029 C  CG2 . VAL   B 1 118 ? 28.676 -23.497 12.289 1.00 11.84  ? 124 VAL   C CG2 1 
ATOM   2030 N  N   . SER   B 1 119 ? 28.847 -19.031 13.611 1.00 11.45  ? 125 SER   C N   1 
ATOM   2031 C  CA  . SER   B 1 119 ? 28.633 -17.560 13.495 1.00 11.85  ? 125 SER   C CA  1 
ATOM   2032 C  C   . SER   B 1 119 ? 29.645 -16.869 12.586 1.00 13.50  ? 125 SER   C C   1 
ATOM   2033 O  O   . SER   B 1 119 ? 29.316 -15.789 12.044 1.00 13.31  ? 125 SER   C O   1 
ATOM   2034 C  CB  . SER   B 1 119 ? 28.670 -16.970 14.904 1.00 13.16  ? 125 SER   C CB  1 
ATOM   2035 O  OG  . SER   B 1 119 ? 28.547 -15.540 14.862 1.00 14.63  ? 125 SER   C OG  1 
ATOM   2036 N  N   . THR   B 1 120 ? 30.914 -17.399 12.493 1.00 12.87  ? 126 THR   C N   1 
ATOM   2037 C  CA  . THR   B 1 120 ? 31.942 -16.707 11.690 1.00 12.76  ? 126 THR   C CA  1 
ATOM   2038 C  C   . THR   B 1 120 ? 32.649 -17.709 10.786 1.00 12.06  ? 126 THR   C C   1 
ATOM   2039 O  O   . THR   B 1 120 ? 32.580 -18.945 11.021 1.00 12.56  ? 126 THR   C O   1 
ATOM   2040 C  CB  . THR   B 1 120 ? 33.009 -15.990 12.588 1.00 13.70  ? 126 THR   C CB  1 
ATOM   2041 O  OG1 . THR   B 1 120 ? 33.837 -16.933 13.240 1.00 14.58  ? 126 THR   C OG1 1 
ATOM   2042 C  CG2 . THR   B 1 120 ? 32.381 -15.037 13.577 1.00 16.23  ? 126 THR   C CG2 1 
ATOM   2043 N  N   . GLY   B 1 121 ? 33.352 -17.203 9.787  1.00 13.52  ? 127 GLY   C N   1 
ATOM   2044 C  CA  . GLY   B 1 121 ? 34.151 -18.043 8.901  1.00 15.62  ? 127 GLY   C CA  1 
ATOM   2045 C  C   . GLY   B 1 121 ? 35.162 -17.216 8.157  1.00 17.93  ? 127 GLY   C C   1 
ATOM   2046 O  O   . GLY   B 1 121 ? 34.924 -16.064 7.822  1.00 21.43  ? 127 GLY   C O   1 
ATOM   2047 N  N   . GLY   B 1 122 ? 36.204 -17.844 7.710  1.00 21.23  ? 128 GLY   C N   1 
ATOM   2048 C  CA  . GLY   B 1 122 ? 37.268 -17.137 6.969  1.00 23.49  ? 128 GLY   C CA  1 
ATOM   2049 C  C   . GLY   B 1 122 ? 38.631 -17.654 7.366  1.00 23.41  ? 128 GLY   C C   1 
ATOM   2050 O  O   . GLY   B 1 122 ? 38.849 -18.111 8.479  1.00 22.97  ? 128 GLY   C O   1 
ATOM   2051 N  N   . ASN   B 1 123 ? 39.602 -17.521 6.458  1.00 22.49  ? 129 ASN   C N   1 
ATOM   2052 C  CA  . ASN   B 1 123 ? 40.995 -17.925 6.662  1.00 23.39  ? 129 ASN   C CA  1 
ATOM   2053 C  C   . ASN   B 1 123 ? 41.098 -19.365 7.135  1.00 21.33  ? 129 ASN   C C   1 
ATOM   2054 O  O   . ASN   B 1 123 ? 42.036 -19.683 7.873  1.00 24.06  ? 129 ASN   C O   1 
ATOM   2055 C  CB  . ASN   B 1 123 ? 41.743 -16.972 7.666  1.00 26.97  ? 129 ASN   C CB  1 
ATOM   2056 C  CG  . ASN   B 1 123 ? 42.553 -15.861 7.042  1.00 34.75  ? 129 ASN   C CG  1 
ATOM   2057 O  OD1 . ASN   B 1 123 ? 42.945 -15.906 5.871  1.00 36.87  ? 129 ASN   C OD1 1 
ATOM   2058 N  ND2 . ASN   B 1 123 ? 42.838 -14.807 7.800  1.00 37.19  ? 129 ASN   C ND2 1 
ATOM   2059 N  N   . GLY   B 1 124 ? 40.187 -20.248 6.711  1.00 19.95  ? 130 GLY   C N   1 
ATOM   2060 C  CA  . GLY   B 1 124 ? 40.244 -21.660 7.144  1.00 18.32  ? 130 GLY   C CA  1 
ATOM   2061 C  C   . GLY   B 1 124 ? 39.823 -21.931 8.573  1.00 16.45  ? 130 GLY   C C   1 
ATOM   2062 O  O   . GLY   B 1 124 ? 40.108 -23.013 9.087  1.00 16.52  ? 130 GLY   C O   1 
ATOM   2063 N  N   . LEU   B 1 125 ? 39.174 -20.962 9.187  1.00 14.54  ? 131 LEU   C N   1 
ATOM   2064 C  CA  . LEU   B 1 125 ? 38.698 -21.102 10.564 1.00 15.26  ? 131 LEU   C CA  1 
ATOM   2065 C  C   . LEU   B 1 125 ? 37.156 -21.004 10.575 1.00 15.13  ? 131 LEU   C C   1 
ATOM   2066 O  O   . LEU   B 1 125 ? 36.541 -20.302 9.743  1.00 17.74  ? 131 LEU   C O   1 
ATOM   2067 C  CB  . LEU   B 1 125 ? 39.294 -20.012 11.492 1.00 17.67  ? 131 LEU   C CB  1 
ATOM   2068 C  CG  . LEU   B 1 125 ? 40.837 -20.031 11.566 1.00 21.00  ? 131 LEU   C CG  1 
ATOM   2069 C  CD1 . LEU   B 1 125 ? 41.412 -18.671 11.981 1.00 25.13  ? 131 LEU   C CD1 1 
ATOM   2070 C  CD2 . LEU   B 1 125 ? 41.331 -21.166 12.371 1.00 21.00  ? 131 LEU   C CD2 1 
ATOM   2071 N  N   . VAL   B 1 126 ? 36.552 -21.680 11.497 1.00 12.67  ? 132 VAL   C N   1 
ATOM   2072 C  CA  . VAL   B 1 126 ? 35.100 -21.568 11.742 1.00 12.40  ? 132 VAL   C CA  1 
ATOM   2073 C  C   . VAL   B 1 126 ? 34.940 -21.106 13.181 1.00 11.14  ? 132 VAL   C C   1 
ATOM   2074 O  O   . VAL   B 1 126 ? 35.602 -21.634 14.076 1.00 12.23  ? 132 VAL   C O   1 
ATOM   2075 C  CB  . VAL   B 1 126 ? 34.381 -22.916 11.521 1.00 12.01  ? 132 VAL   C CB  1 
ATOM   2076 C  CG1 . VAL   B 1 126 ? 35.013 -24.101 12.189 1.00 13.84  ? 132 VAL   C CG1 1 
ATOM   2077 C  CG2 . VAL   B 1 126 ? 32.881 -22.833 11.841 1.00 13.42  ? 132 VAL   C CG2 1 
ATOM   2078 N  N   . GLY   B 1 127 ? 34.051 -20.132 13.382 1.00 11.71  ? 133 GLY   C N   1 
ATOM   2079 C  CA  . GLY   B 1 127 ? 33.785 -19.620 14.734 1.00 11.51  ? 133 GLY   C CA  1 
ATOM   2080 C  C   . GLY   B 1 127 ? 32.345 -19.956 15.163 1.00 11.92  ? 133 GLY   C C   1 
ATOM   2081 O  O   . GLY   B 1 127 ? 31.406 -19.849 14.346 1.00 11.74  ? 133 GLY   C O   1 
ATOM   2082 N  N   . PHE   B 1 128 ? 32.212 -20.332 16.423 1.00 10.89  ? 134 PHE   C N   1 
ATOM   2083 C  CA  . PHE   B 1 128 ? 30.918 -20.712 17.041 1.00 10.86  ? 134 PHE   C CA  1 
ATOM   2084 C  C   . PHE   B 1 128 ? 30.563 -19.789 18.169 1.00 11.07  ? 134 PHE   C C   1 
ATOM   2085 O  O   . PHE   B 1 128 ? 31.418 -19.511 19.023 1.00 12.07  ? 134 PHE   C O   1 
ATOM   2086 C  CB  . PHE   B 1 128 ? 30.982 -22.151 17.606 1.00 11.41  ? 134 PHE   C CB  1 
ATOM   2087 C  CG  . PHE   B 1 128 ? 31.540 -23.155 16.613 1.00 10.93  ? 134 PHE   C CG  1 
ATOM   2088 C  CD1 . PHE   B 1 128 ? 30.710 -23.753 15.666 1.00 11.04  ? 134 PHE   C CD1 1 
ATOM   2089 C  CD2 . PHE   B 1 128 ? 32.878 -23.520 16.652 1.00 11.83  ? 134 PHE   C CD2 1 
ATOM   2090 C  CE1 . PHE   B 1 128 ? 31.207 -24.699 14.786 1.00 11.49  ? 134 PHE   C CE1 1 
ATOM   2091 C  CE2 . PHE   B 1 128 ? 33.395 -24.463 15.746 1.00 12.34  ? 134 PHE   C CE2 1 
ATOM   2092 C  CZ  . PHE   B 1 128 ? 32.552 -25.071 14.843 1.00 11.11  ? 134 PHE   C CZ  1 
ATOM   2093 N  N   . ALA   B 1 129 ? 29.317 -19.309 18.169 1.00 11.37  ? 135 ALA   C N   1 
ATOM   2094 C  CA  . ALA   B 1 129 ? 28.800 -18.502 19.274 1.00 11.88  ? 135 ALA   C CA  1 
ATOM   2095 C  C   . ALA   B 1 129 ? 28.410 -19.479 20.404 1.00 11.98  ? 135 ALA   C C   1 
ATOM   2096 O  O   . ALA   B 1 129 ? 27.505 -20.325 20.242 1.00 12.08  ? 135 ALA   C O   1 
ATOM   2097 C  CB  . ALA   B 1 129 ? 27.575 -17.713 18.817 1.00 12.16  ? 135 ALA   C CB  1 
ATOM   2098 N  N   . ASP   B 1 130 ? 29.106 -19.387 21.558 1.00 11.85  ? 136 ASP   C N   1 
ATOM   2099 C  CA  . ASP   B 1 130 ? 28.797 -20.276 22.694 1.00 12.45  ? 136 ASP   C CA  1 
ATOM   2100 C  C   . ASP   B 1 130 ? 27.445 -19.938 23.270 1.00 13.48  ? 136 ASP   C C   1 
ATOM   2101 O  O   . ASP   B 1 130 ? 27.076 -18.748 23.353 1.00 13.83  ? 136 ASP   C O   1 
ATOM   2102 C  CB  . ASP   B 1 130 ? 29.871 -20.035 23.788 1.00 13.57  ? 136 ASP   C CB  1 
ATOM   2103 C  CG  . ASP   B 1 130 ? 29.749 -20.964 24.982 1.00 16.63  ? 136 ASP   C CG  1 
ATOM   2104 O  OD1 . ASP   B 1 130 ? 29.607 -22.182 24.789 1.00 16.18  ? 136 ASP   C OD1 1 
ATOM   2105 O  OD2 . ASP   B 1 130 ? 29.662 -20.445 26.120 1.00 20.48  ? 136 ASP   C OD2 1 
ATOM   2106 N  N   . VAL   B 1 131 ? 26.738 -20.963 23.756 1.00 12.96  ? 137 VAL   C N   1 
ATOM   2107 C  CA  . VAL   B 1 131 ? 25.481 -20.794 24.522 1.00 13.52  ? 137 VAL   C CA  1 
ATOM   2108 C  C   . VAL   B 1 131 ? 25.547 -21.455 25.899 1.00 14.52  ? 137 VAL   C C   1 
ATOM   2109 O  O   . VAL   B 1 131 ? 24.568 -21.401 26.649 1.00 14.64  ? 137 VAL   C O   1 
ATOM   2110 C  CB  . VAL   B 1 131 ? 24.215 -21.255 23.750 1.00 13.80  ? 137 VAL   C CB  1 
ATOM   2111 C  CG1 . VAL   B 1 131 ? 24.071 -20.450 22.441 1.00 13.96  ? 137 VAL   C CG1 1 
ATOM   2112 C  CG2 . VAL   B 1 131 ? 24.221 -22.751 23.468 1.00 13.78  ? 137 VAL   C CG2 1 
ATOM   2113 N  N   . ARG   B 1 132 ? 26.674 -22.106 26.257 1.00 13.63  ? 138 ARG   C N   1 
ATOM   2114 C  CA  . ARG   B 1 132 ? 26.737 -22.881 27.512 1.00 13.64  ? 138 ARG   C CA  1 
ATOM   2115 C  C   . ARG   B 1 132 ? 26.657 -22.046 28.778 1.00 14.71  ? 138 ARG   C C   1 
ATOM   2116 O  O   . ARG   B 1 132 ? 26.313 -22.614 29.837 1.00 16.19  ? 138 ARG   C O   1 
ATOM   2117 C  CB  . ARG   B 1 132 ? 27.980 -23.734 27.513 1.00 13.38  ? 138 ARG   C CB  1 
ATOM   2118 C  CG  . ARG   B 1 132 ? 27.977 -24.804 26.377 1.00 13.14  ? 138 ARG   C CG  1 
ATOM   2119 C  CD  . ARG   B 1 132 ? 29.292 -25.581 26.441 1.00 12.34  ? 138 ARG   C CD  1 
ATOM   2120 N  NE  . ARG   B 1 132 ? 30.392 -24.683 26.059 1.00 13.38  ? 138 ARG   C NE  1 
ATOM   2121 C  CZ  . ARG   B 1 132 ? 31.642 -25.060 25.916 1.00 14.15  ? 138 ARG   C CZ  1 
ATOM   2122 N  NH1 . ARG   B 1 132 ? 32.023 -26.294 26.281 1.00 14.51  ? 138 ARG   C NH1 1 
ATOM   2123 N  NH2 . ARG   B 1 132 ? 32.541 -24.207 25.428 1.00 14.77  ? 138 ARG   C NH2 1 
ATOM   2124 N  N   . ASP   B 1 133 ? 26.950 -20.738 28.696 1.00 13.85  ? 139 ASP   C N   1 
ATOM   2125 C  CA  . ASP   B 1 133 ? 26.875 -19.882 29.885 1.00 14.99  ? 139 ASP   C CA  1 
ATOM   2126 C  C   . ASP   B 1 133 ? 25.454 -19.329 30.101 1.00 16.17  ? 139 ASP   C C   1 
ATOM   2127 O  O   . ASP   B 1 133 ? 25.234 -18.665 31.119 1.00 17.17  ? 139 ASP   C O   1 
ATOM   2128 C  CB  . ASP   B 1 133 ? 27.845 -18.666 29.754 1.00 16.35  ? 139 ASP   C CB  1 
ATOM   2129 C  CG  . ASP   B 1 133 ? 27.500 -17.761 28.595 1.00 18.25  ? 139 ASP   C CG  1 
ATOM   2130 O  OD1 . ASP   B 1 133 ? 27.147 -18.269 27.516 1.00 17.94  ? 139 ASP   C OD1 1 
ATOM   2131 O  OD2 . ASP   B 1 133 ? 27.527 -16.500 28.769 1.00 21.03  ? 139 ASP   C OD2 1 
ATOM   2132 N  N   . LEU   B 1 134 ? 24.499 -19.544 29.153 1.00 14.98  ? 140 LEU   C N   1 
ATOM   2133 C  CA  . LEU   B 1 134 ? 23.145 -18.975 29.253 1.00 15.42  ? 140 LEU   C CA  1 
ATOM   2134 C  C   . LEU   B 1 134 ? 22.293 -19.962 29.996 1.00 15.29  ? 140 LEU   C C   1 
ATOM   2135 O  O   . LEU   B 1 134 ? 21.497 -20.706 29.434 1.00 15.56  ? 140 LEU   C O   1 
ATOM   2136 C  CB  . LEU   B 1 134 ? 22.611 -18.726 27.832 1.00 15.87  ? 140 LEU   C CB  1 
ATOM   2137 C  CG  . LEU   B 1 134 ? 23.464 -17.774 26.953 1.00 15.78  ? 140 LEU   C CG  1 
ATOM   2138 C  CD1 . LEU   B 1 134 ? 22.896 -17.716 25.506 1.00 16.13  ? 140 LEU   C CD1 1 
ATOM   2139 C  CD2 . LEU   B 1 134 ? 23.583 -16.360 27.582 1.00 17.80  ? 140 LEU   C CD2 1 
ATOM   2140 N  N   . LEU   B 1 135 ? 22.495 -20.012 31.333 1.00 16.31  ? 141 LEU   C N   1 
ATOM   2141 C  CA  . LEU   B 1 135 ? 21.863 -21.059 32.151 1.00 17.72  ? 141 LEU   C CA  1 
ATOM   2142 C  C   . LEU   B 1 135 ? 20.357 -20.979 32.202 1.00 17.50  ? 141 LEU   C C   1 
ATOM   2143 O  O   . LEU   B 1 135 ? 19.671 -21.987 32.368 1.00 17.93  ? 141 LEU   C O   1 
ATOM   2144 C  CB  . LEU   B 1 135 ? 22.421 -21.084 33.600 1.00 17.83  ? 141 LEU   C CB  1 
ATOM   2145 C  CG  . LEU   B 1 135 ? 23.980 -21.072 33.693 1.00 18.56  ? 141 LEU   C CG  1 
ATOM   2146 C  CD1 . LEU   B 1 135 ? 24.506 -21.072 35.168 1.00 20.24  ? 141 LEU   C CD1 1 
ATOM   2147 C  CD2 . LEU   B 1 135 ? 24.636 -22.218 32.918 1.00 19.01  ? 141 LEU   C CD2 1 
ATOM   2148 N  N   . TRP   B 1 136 ? 19.840 -19.773 32.011 1.00 16.55  ? 142 TRP   C N   1 
ATOM   2149 C  CA  . TRP   B 1 136 ? 18.393 -19.506 32.028 1.00 17.61  ? 142 TRP   C CA  1 
ATOM   2150 C  C   . TRP   B 1 136 ? 17.673 -20.192 30.865 1.00 18.75  ? 142 TRP   C C   1 
ATOM   2151 O  O   . TRP   B 1 136 ? 16.453 -20.362 30.912 1.00 19.87  ? 142 TRP   C O   1 
ATOM   2152 C  CB  . TRP   B 1 136 ? 18.106 -17.988 32.024 1.00 17.40  ? 142 TRP   C CB  1 
ATOM   2153 C  CG  . TRP   B 1 136 ? 18.812 -17.243 30.923 1.00 17.60  ? 142 TRP   C CG  1 
ATOM   2154 C  CD1 . TRP   B 1 136 ? 19.982 -16.545 31.013 1.00 18.10  ? 142 TRP   C CD1 1 
ATOM   2155 C  CD2 . TRP   B 1 136 ? 18.297 -16.996 29.588 1.00 17.30  ? 142 TRP   C CD2 1 
ATOM   2156 N  NE1 . TRP   B 1 136 ? 20.270 -15.948 29.789 1.00 18.31  ? 142 TRP   C NE1 1 
ATOM   2157 C  CE2 . TRP   B 1 136 ? 19.242 -16.207 28.907 1.00 17.96  ? 142 TRP   C CE2 1 
ATOM   2158 C  CE3 . TRP   B 1 136 ? 17.148 -17.395 28.926 1.00 17.59  ? 142 TRP   C CE3 1 
ATOM   2159 C  CZ2 . TRP   B 1 136 ? 19.060 -15.813 27.561 1.00 17.67  ? 142 TRP   C CZ2 1 
ATOM   2160 C  CZ3 . TRP   B 1 136 ? 16.944 -16.988 27.627 1.00 17.82  ? 142 TRP   C CZ3 1 
ATOM   2161 C  CH2 . TRP   B 1 136 ? 17.898 -16.217 26.952 1.00 17.95  ? 142 TRP   C CH2 1 
ATOM   2162 N  N   . LEU   B 1 137 ? 18.382 -20.634 29.811 1.00 17.48  ? 143 LEU   C N   1 
ATOM   2163 C  CA  . LEU   B 1 137 ? 17.719 -21.394 28.736 1.00 17.86  ? 143 LEU   C CA  1 
ATOM   2164 C  C   . LEU   B 1 137 ? 17.103 -22.689 29.283 1.00 21.96  ? 143 LEU   C C   1 
ATOM   2165 O  O   . LEU   B 1 137 ? 16.178 -23.198 28.658 1.00 23.50  ? 143 LEU   C O   1 
ATOM   2166 C  CB  . LEU   B 1 137 ? 18.687 -21.735 27.601 1.00 16.59  ? 143 LEU   C CB  1 
ATOM   2167 C  CG  . LEU   B 1 137 ? 19.145 -20.555 26.746 1.00 15.68  ? 143 LEU   C CG  1 
ATOM   2168 C  CD1 . LEU   B 1 137 ? 20.287 -20.992 25.831 1.00 17.64  ? 143 LEU   C CD1 1 
ATOM   2169 C  CD2 . LEU   B 1 137 ? 17.988 -19.996 25.844 1.00 16.51  ? 143 LEU   C CD2 1 
ATOM   2170 N  N   . ASP   B 1 138 ? 17.631 -23.216 30.439 1.00 20.89  ? 144 ASP   C N   1 
ATOM   2171 C  CA  . ASP   B 1 138 ? 17.160 -24.483 31.033 1.00 22.99  ? 144 ASP   C CA  1 
ATOM   2172 C  C   . ASP   B 1 138 ? 15.946 -24.329 31.913 1.00 25.31  ? 144 ASP   C C   1 
ATOM   2173 O  O   . ASP   B 1 138 ? 15.516 -25.347 32.468 1.00 27.26  ? 144 ASP   C O   1 
ATOM   2174 C  CB  . ASP   B 1 138 ? 18.254 -25.146 31.903 1.00 22.95  ? 144 ASP   C CB  1 
ATOM   2175 C  CG  . ASP   B 1 138 ? 19.513 -25.546 31.149 1.00 23.55  ? 144 ASP   C CG  1 
ATOM   2176 O  OD1 . ASP   B 1 138 ? 19.484 -25.569 29.911 1.00 24.92  ? 144 ASP   C OD1 1 
ATOM   2177 O  OD2 . ASP   B 1 138 ? 20.536 -25.825 31.821 1.00 27.86  ? 144 ASP   C OD2 1 
ATOM   2178 N  N   . GLU   B 1 139 ? 15.374 -23.125 32.064 1.00 25.31  ? 145 GLU   C N   1 
ATOM   2179 C  CA  . GLU   B 1 139 ? 14.250 -22.924 32.984 1.00 30.74  ? 145 GLU   C CA  1 
ATOM   2180 C  C   . GLU   B 1 139 ? 13.194 -21.938 32.421 1.00 36.05  ? 145 GLU   C C   1 
ATOM   2181 O  O   . GLU   B 1 139 ? 13.400 -21.344 31.363 1.00 36.89  ? 145 GLU   C O   1 
ATOM   2182 C  CB  . GLU   B 1 139 ? 14.836 -22.375 34.305 1.00 35.55  ? 145 GLU   C CB  1 
ATOM   2183 C  CG  . GLU   B 1 139 ? 15.523 -21.035 34.094 1.00 43.41  ? 145 GLU   C CG  1 
ATOM   2184 C  CD  . GLU   B 1 139 ? 16.424 -20.508 35.193 1.00 51.62  ? 145 GLU   C CD  1 
ATOM   2185 O  OE1 . GLU   B 1 139 ? 16.524 -19.264 35.331 1.00 51.59  ? 145 GLU   C OE1 1 
ATOM   2186 O  OE2 . GLU   B 1 139 ? 17.034 -21.334 35.909 1.00 54.69  ? 145 GLU   C OE2 1 
ATOM   2187 N  N   . GLU   B 1 140 ? 12.095 -21.724 33.186 1.00 39.50  ? 146 GLU   C N   1 
ATOM   2188 C  CA  . GLU   B 1 140 ? 10.991 -20.770 32.949 1.00 43.28  ? 146 GLU   C CA  1 
ATOM   2189 C  C   . GLU   B 1 140 ? 10.018 -21.248 31.883 1.00 46.41  ? 146 GLU   C C   1 
ATOM   2190 O  O   . GLU   B 1 140 ? 8.803  -21.174 32.106 1.00 48.22  ? 146 GLU   C O   1 
ATOM   2191 C  CB  . GLU   B 1 140 ? 11.502 -19.345 32.676 1.00 45.48  ? 146 GLU   C CB  1 
ATOM   2192 C  CG  . GLU   B 1 140 ? 10.508 -18.359 32.086 1.00 51.35  ? 146 GLU   C CG  1 
ATOM   2193 C  CD  . GLU   B 1 140 ? 9.840  -17.453 33.105 1.00 59.45  ? 146 GLU   C CD  1 
ATOM   2194 O  OE1 . GLU   B 1 140 ? 10.235 -16.267 33.193 1.00 61.62  ? 146 GLU   C OE1 1 
ATOM   2195 O  OE2 . GLU   B 1 140 ? 8.917  -17.926 33.810 1.00 60.81  ? 146 GLU   C OE2 1 
HETATM 2196 N  N1  . A1B02 C 2 .   ? 9.697  14.525  21.827 0.50 33.53  ? 201 A1B02 A N1  1 
HETATM 2197 N  N3  . A1B02 C 2 .   ? 9.087  11.745  22.312 0.50 34.05  ? 201 A1B02 A N3  1 
HETATM 2198 C  C4  . A1B02 C 2 .   ? 6.959  14.617  24.359 0.50 34.35  ? 201 A1B02 A C4  1 
HETATM 2199 C  C5  . A1B02 C 2 .   ? 7.959  15.055  23.505 0.50 34.19  ? 201 A1B02 A C5  1 
HETATM 2200 C  C6  . A1B02 C 2 .   ? 8.717  14.144  22.768 0.50 33.66  ? 201 A1B02 A C6  1 
HETATM 2201 C  C7  . A1B02 C 2 .   ? 10.612 15.502  21.942 0.50 33.13  ? 201 A1B02 A C7  1 
HETATM 2202 C  C8  . A1B02 C 2 .   ? 11.472 15.721  20.719 0.50 33.57  ? 201 A1B02 A C8  1 
HETATM 2203 C  C10 . A1B02 C 2 .   ? 10.364 16.116  18.408 0.50 34.68  ? 201 A1B02 A C10 1 
HETATM 2204 O  O   . A1B02 C 2 .   ? 10.736 16.201  22.935 0.50 31.70  ? 201 A1B02 A O   1 
HETATM 2205 C  C9  . A1B02 C 2 .   ? 10.658 16.425  19.676 0.50 34.36  ? 201 A1B02 A C9  1 
HETATM 2206 N  N2  . A1B02 C 2 .   ? 10.025 17.613  20.001 0.50 34.96  ? 201 A1B02 A N2  1 
HETATM 2207 C  C11 . A1B02 C 2 .   ? 9.395  17.929  18.935 0.50 35.41  ? 201 A1B02 A C11 1 
HETATM 2208 O  O1  . A1B02 C 2 .   ? 9.540  17.076  17.899 0.50 35.59  ? 201 A1B02 A O1  1 
HETATM 2209 C  C3  . A1B02 C 2 .   ? 6.705  13.265  24.506 0.50 34.31  ? 201 A1B02 A C3  1 
HETATM 2210 C  C12 . A1B02 C 2 .   ? 8.461  12.769  22.928 0.50 33.71  ? 201 A1B02 A C12 1 
HETATM 2211 C  C2  . A1B02 C 2 .   ? 7.462  12.325  23.805 0.50 33.98  ? 201 A1B02 A C2  1 
HETATM 2212 C  C1  . A1B02 C 2 .   ? 7.512  10.889  23.713 0.50 33.75  ? 201 A1B02 A C1  1 
HETATM 2213 N  N   . A1B02 C 2 .   ? 8.476  10.632  22.819 0.50 33.15  ? 201 A1B02 A N   1 
HETATM 2214 C  C   . A1B02 C 2 .   ? 8.920  9.337   22.306 0.50 33.79  ? 201 A1B02 A C   1 
HETATM 2215 ZN ZN  . ZN    D 3 .   ? 10.728 -3.522  5.706  1.00 20.29  2 202 ZN    A ZN  1 
HETATM 2216 S  S   . DMS   E 4 .   ? 19.258 -2.179  24.525 1.00 75.45  ? 203 DMS   A S   1 
HETATM 2217 O  O   . DMS   E 4 .   ? 18.420 -2.681  23.386 1.00 75.30  ? 203 DMS   A O   1 
HETATM 2218 C  C1  . DMS   E 4 .   ? 19.651 -3.597  25.588 1.00 75.50  ? 203 DMS   A C1  1 
HETATM 2219 C  C2  . DMS   E 4 .   ? 20.950 -1.924  23.916 1.00 75.41  ? 203 DMS   A C2  1 
HETATM 2220 ZN ZN  . ZN    F 3 .   ? 30.473 -31.122 26.767 1.00 14.13  2 201 ZN    C ZN  1 
HETATM 2221 S  S   . DMS   G 4 .   ? 20.303 -31.675 9.221  1.00 116.58 ? 202 DMS   C S   1 
HETATM 2222 O  O   . DMS   G 4 .   ? 20.803 -30.313 8.853  1.00 116.57 ? 202 DMS   C O   1 
HETATM 2223 C  C1  . DMS   G 4 .   ? 20.979 -32.083 10.846 1.00 116.52 ? 202 DMS   C C1  1 
HETATM 2224 C  C2  . DMS   G 4 .   ? 18.595 -31.473 9.802  1.00 116.61 ? 202 DMS   C C2  1 
HETATM 2225 O  O   . HOH   H 5 .   ? 12.115 16.731  27.969 1.00 40.62  ? 301 HOH   A O   1 
HETATM 2226 O  O   . HOH   H 5 .   ? 35.316 -3.838  7.844  1.00 25.75  ? 302 HOH   A O   1 
HETATM 2227 O  O   . HOH   H 5 .   ? 2.002  22.738  21.479 1.00 30.91  ? 303 HOH   A O   1 
HETATM 2228 O  O   . HOH   H 5 .   ? 11.179 9.074   4.416  1.00 24.38  ? 304 HOH   A O   1 
HETATM 2229 O  O   . HOH   H 5 .   ? 10.633 10.159  31.467 1.00 24.32  ? 305 HOH   A O   1 
HETATM 2230 O  O   . HOH   H 5 .   ? 4.308  9.491   27.928 1.00 42.57  ? 306 HOH   A O   1 
HETATM 2231 O  O   . HOH   H 5 .   ? 8.034  17.212  26.460 1.00 49.36  ? 307 HOH   A O   1 
HETATM 2232 O  O   . HOH   H 5 .   ? 20.211 19.704  5.700  1.00 43.85  ? 308 HOH   A O   1 
HETATM 2233 O  O   . HOH   H 5 .   ? 8.344  24.640  23.766 1.00 33.25  ? 309 HOH   A O   1 
HETATM 2234 O  O   . HOH   H 5 .   ? 8.378  -2.878  31.822 1.00 29.21  ? 310 HOH   A O   1 
HETATM 2235 O  O   . HOH   H 5 .   ? 21.795 2.239   -0.900 1.00 33.58  ? 311 HOH   A O   1 
HETATM 2236 O  O   . HOH   H 5 .   ? 2.957  9.510   9.064  1.00 29.60  ? 312 HOH   A O   1 
HETATM 2237 O  O   . HOH   H 5 .   ? 6.071  2.487   5.583  1.00 28.92  ? 313 HOH   A O   1 
HETATM 2238 O  O   . HOH   H 5 .   ? 37.632 14.802  14.041 1.00 42.27  ? 314 HOH   A O   1 
HETATM 2239 O  O   . HOH   H 5 .   ? 13.818 2.935   1.256  1.00 20.42  ? 315 HOH   A O   1 
HETATM 2240 O  O   . HOH   H 5 .   ? 3.490  -1.569  2.965  1.00 48.41  ? 316 HOH   A O   1 
HETATM 2241 O  O   . HOH   H 5 .   ? 33.822 -2.330  13.522 1.00 33.49  ? 317 HOH   A O   1 
HETATM 2242 O  O   . HOH   H 5 .   ? 17.451 0.933   28.156 1.00 27.04  ? 318 HOH   A O   1 
HETATM 2243 O  O   . HOH   H 5 .   ? 30.470 10.343  15.562 1.00 33.11  ? 319 HOH   A O   1 
HETATM 2244 O  O   . HOH   H 5 .   ? 29.558 22.229  19.379 1.00 24.16  ? 320 HOH   A O   1 
HETATM 2245 O  O   . HOH   H 5 .   ? 4.649  -3.593  28.889 1.00 27.44  ? 321 HOH   A O   1 
HETATM 2246 O  O   . HOH   H 5 .   ? 2.826  9.724   10.986 1.00 181.36 ? 322 HOH   A O   1 
HETATM 2247 O  O   . HOH   H 5 .   ? 28.116 3.257   4.860  1.00 34.04  ? 323 HOH   A O   1 
HETATM 2248 O  O   . HOH   H 5 .   ? 23.376 21.652  7.248  1.00 24.55  ? 324 HOH   A O   1 
HETATM 2249 O  O   . HOH   H 5 .   ? 3.866  -8.017  9.915  1.00 44.76  ? 325 HOH   A O   1 
HETATM 2250 O  O   . HOH   H 5 .   ? 19.450 9.986   19.669 1.00 13.87  ? 326 HOH   A O   1 
HETATM 2251 O  O   . HOH   H 5 .   ? 0.437  -0.859  19.439 1.00 20.44  ? 327 HOH   A O   1 
HETATM 2252 O  O   . HOH   H 5 .   ? 2.610  -2.864  20.772 1.00 23.45  ? 328 HOH   A O   1 
HETATM 2253 O  O   . HOH   H 5 .   ? -2.546 23.498  9.110  1.00 52.33  ? 329 HOH   A O   1 
HETATM 2254 O  O   . HOH   H 5 .   ? 27.770 8.133   1.598  1.00 32.90  ? 330 HOH   A O   1 
HETATM 2255 O  O   . HOH   H 5 .   ? 33.846 14.094  9.665  1.00 31.15  ? 331 HOH   A O   1 
HETATM 2256 O  O   . HOH   H 5 .   ? 10.748 5.831   3.479  1.00 23.36  ? 332 HOH   A O   1 
HETATM 2257 O  O   . HOH   H 5 .   ? 12.351 22.138  13.135 1.00 35.47  ? 333 HOH   A O   1 
HETATM 2258 O  O   . HOH   H 5 .   ? 23.339 3.796   -2.239 1.00 47.51  ? 334 HOH   A O   1 
HETATM 2259 O  O   . HOH   H 5 .   ? 26.695 -1.191  8.730  1.00 25.24  ? 335 HOH   A O   1 
HETATM 2260 O  O   . HOH   H 5 .   ? 32.249 2.164   5.926  1.00 37.87  ? 336 HOH   A O   1 
HETATM 2261 O  O   . HOH   H 5 .   ? 24.990 4.885   21.339 1.00 33.05  ? 337 HOH   A O   1 
HETATM 2262 O  O   . HOH   H 5 .   ? 14.289 13.628  24.076 1.00 26.69  ? 338 HOH   A O   1 
HETATM 2263 O  O   . HOH   H 5 .   ? -0.035 1.333   15.950 1.00 12.88  ? 339 HOH   A O   1 
HETATM 2264 O  O   . HOH   H 5 .   ? 15.941 23.730  15.155 1.00 43.95  ? 340 HOH   A O   1 
HETATM 2265 O  O   . HOH   H 5 .   ? 16.868 -3.539  27.798 1.00 36.92  ? 341 HOH   A O   1 
HETATM 2266 O  O   . HOH   H 5 .   ? 4.219  0.421   24.005 1.00 18.32  ? 342 HOH   A O   1 
HETATM 2267 O  O   . HOH   H 5 .   ? 20.846 -4.154  14.124 1.00 17.81  ? 343 HOH   A O   1 
HETATM 2268 O  O   . HOH   H 5 .   ? 13.771 3.904   23.547 1.00 12.69  ? 344 HOH   A O   1 
HETATM 2269 O  O   . HOH   H 5 .   ? 5.650  16.632  21.517 1.00 33.47  ? 345 HOH   A O   1 
HETATM 2270 O  O   . HOH   H 5 .   ? 30.016 11.451  18.336 1.00 27.99  ? 346 HOH   A O   1 
HETATM 2271 O  O   . HOH   H 5 .   ? 15.172 14.300  26.331 1.00 35.26  ? 347 HOH   A O   1 
HETATM 2272 O  O   . HOH   H 5 .   ? 22.624 0.801   17.339 1.00 16.54  ? 348 HOH   A O   1 
HETATM 2273 O  O   . HOH   H 5 .   ? 21.823 4.811   24.716 1.00 40.32  ? 349 HOH   A O   1 
HETATM 2274 O  O   . HOH   H 5 .   ? 31.601 19.881  11.718 1.00 21.99  ? 350 HOH   A O   1 
HETATM 2275 O  O   . HOH   H 5 .   ? 28.885 3.317   12.536 1.00 17.80  ? 351 HOH   A O   1 
HETATM 2276 O  O   . HOH   H 5 .   ? 20.550 -0.912  3.028  1.00 32.30  ? 352 HOH   A O   1 
HETATM 2277 O  O   . HOH   H 5 .   ? 16.645 3.774   23.693 1.00 17.77  ? 353 HOH   A O   1 
HETATM 2278 O  O   . HOH   H 5 .   ? 28.862 15.905  4.392  1.00 33.20  ? 354 HOH   A O   1 
HETATM 2279 O  O   . HOH   H 5 .   ? 30.521 2.837   14.644 1.00 25.36  ? 355 HOH   A O   1 
HETATM 2280 O  O   . HOH   H 5 .   ? 7.098  -3.187  -1.208 1.00 69.79  ? 356 HOH   A O   1 
HETATM 2281 O  O   . HOH   H 5 .   ? 11.311 12.784  11.345 1.00 16.37  ? 357 HOH   A O   1 
HETATM 2282 O  O   . HOH   H 5 .   ? 23.979 -3.511  15.989 1.00 37.19  ? 358 HOH   A O   1 
HETATM 2283 O  O   . HOH   H 5 .   ? 18.429 21.902  9.608  1.00 20.02  ? 359 HOH   A O   1 
HETATM 2284 O  O   . HOH   H 5 .   ? 17.675 19.945  17.088 1.00 17.89  ? 360 HOH   A O   1 
HETATM 2285 O  O   . HOH   H 5 .   ? 33.776 11.015  15.482 1.00 40.90  ? 361 HOH   A O   1 
HETATM 2286 O  O   . HOH   H 5 .   ? 1.368  11.491  27.740 1.00 50.28  ? 362 HOH   A O   1 
HETATM 2287 O  O   . HOH   H 5 .   ? 25.485 19.465  21.717 1.00 24.79  ? 363 HOH   A O   1 
HETATM 2288 O  O   . HOH   H 5 .   ? 3.981  12.885  18.018 1.00 29.94  ? 364 HOH   A O   1 
HETATM 2289 O  O   . HOH   H 5 .   ? 3.269  7.678   24.482 1.00 26.30  ? 365 HOH   A O   1 
HETATM 2290 O  O   . HOH   H 5 .   ? 20.685 -2.542  16.792 1.00 15.79  ? 366 HOH   A O   1 
HETATM 2291 O  O   . HOH   H 5 .   ? 6.522  -6.926  23.688 1.00 24.74  ? 367 HOH   A O   1 
HETATM 2292 O  O   . HOH   H 5 .   ? 15.126 11.413  0.121  1.00 39.19  ? 368 HOH   A O   1 
HETATM 2293 O  O   . HOH   H 5 .   ? 25.256 17.897  4.695  1.00 33.53  ? 369 HOH   A O   1 
HETATM 2294 O  O   . HOH   H 5 .   ? 5.433  17.876  24.211 1.00 42.42  ? 370 HOH   A O   1 
HETATM 2295 O  O   . HOH   H 5 .   ? 13.229 11.474  9.325  1.00 14.50  ? 371 HOH   A O   1 
HETATM 2296 O  O   . HOH   H 5 .   ? 36.531 17.875  14.439 1.00 28.37  ? 372 HOH   A O   1 
HETATM 2297 O  O   . HOH   H 5 .   ? 29.946 -1.559  8.510  1.00 38.99  ? 373 HOH   A O   1 
HETATM 2298 O  O   . HOH   H 5 .   ? 23.614 11.524  21.952 1.00 31.10  ? 374 HOH   A O   1 
HETATM 2299 O  O   . HOH   H 5 .   ? 23.136 -6.501  11.897 1.00 32.91  ? 375 HOH   A O   1 
HETATM 2300 O  O   . HOH   H 5 .   ? 19.457 2.859   19.357 1.00 19.20  ? 376 HOH   A O   1 
HETATM 2301 O  O   . HOH   H 5 .   ? 22.702 -0.607  5.327  1.00 22.82  ? 377 HOH   A O   1 
HETATM 2302 O  O   . HOH   H 5 .   ? 14.413 -2.420  17.925 1.00 18.33  ? 378 HOH   A O   1 
HETATM 2303 O  O   . HOH   H 5 .   ? 18.056 17.812  4.383  1.00 33.42  ? 379 HOH   A O   1 
HETATM 2304 O  O   . HOH   H 5 .   ? 20.500 17.572  24.256 1.00 47.38  ? 380 HOH   A O   1 
HETATM 2305 O  O   . HOH   H 5 .   ? 12.335 11.071  29.711 1.00 22.35  ? 381 HOH   A O   1 
HETATM 2306 O  O   . HOH   H 5 .   ? 30.327 4.552   5.656  1.00 24.51  ? 382 HOH   A O   1 
HETATM 2307 O  O   . HOH   H 5 .   ? 35.931 15.028  10.999 1.00 37.23  ? 383 HOH   A O   1 
HETATM 2308 O  O   . HOH   H 5 .   ? 9.643  3.986   33.529 1.00 15.64  ? 384 HOH   A O   1 
HETATM 2309 O  O   . HOH   H 5 .   ? 31.047 15.496  22.753 1.00 24.14  ? 385 HOH   A O   1 
HETATM 2310 O  O   . HOH   H 5 .   ? 3.846  -3.776  6.027  1.00 29.89  ? 386 HOH   A O   1 
HETATM 2311 O  O   . HOH   H 5 .   ? 27.166 -1.296  15.765 1.00 26.79  ? 387 HOH   A O   1 
HETATM 2312 O  O   . HOH   H 5 .   ? 6.012  -3.554  31.458 1.00 31.20  ? 388 HOH   A O   1 
HETATM 2313 O  O   . HOH   H 5 .   ? 17.163 5.939   26.880 1.00 28.32  ? 389 HOH   A O   1 
HETATM 2314 O  O   . HOH   H 5 .   ? 12.715 15.093  1.422  1.00 54.72  ? 390 HOH   A O   1 
HETATM 2315 O  O   . HOH   H 5 .   ? 28.116 11.229  3.000  1.00 50.08  ? 391 HOH   A O   1 
HETATM 2316 O  O   . HOH   H 5 .   ? 32.832 16.506  9.223  1.00 30.68  ? 392 HOH   A O   1 
HETATM 2317 O  O   . HOH   H 5 .   ? 7.404  20.087  17.706 1.00 24.33  ? 393 HOH   A O   1 
HETATM 2318 O  O   . HOH   H 5 .   ? 3.255  0.336   28.883 1.00 36.44  ? 394 HOH   A O   1 
HETATM 2319 O  O   . HOH   H 5 .   ? 31.951 8.705   7.510  1.00 24.44  ? 395 HOH   A O   1 
HETATM 2320 O  O   . HOH   H 5 .   ? 28.023 17.480  24.152 1.00 23.49  ? 396 HOH   A O   1 
HETATM 2321 O  O   . HOH   H 5 .   ? 16.152 9.381   -1.664 1.00 25.59  ? 397 HOH   A O   1 
HETATM 2322 O  O   . HOH   H 5 .   ? 5.573  5.434   32.674 1.00 23.84  ? 398 HOH   A O   1 
HETATM 2323 O  O   . HOH   H 5 .   ? 17.814 10.544  26.197 1.00 23.27  ? 399 HOH   A O   1 
HETATM 2324 O  O   . HOH   H 5 .   ? 16.937 -5.417  12.147 1.00 30.98  ? 400 HOH   A O   1 
HETATM 2325 O  O   . HOH   H 5 .   ? 5.184  26.375  20.119 1.00 33.46  ? 401 HOH   A O   1 
HETATM 2326 O  O   . HOH   H 5 .   ? 34.005 4.930   16.518 1.00 35.87  ? 402 HOH   A O   1 
HETATM 2327 O  O   . HOH   H 5 .   ? 8.362  -6.376  9.440  1.00 29.98  ? 403 HOH   A O   1 
HETATM 2328 O  O   . HOH   H 5 .   ? 7.341  14.001  4.911  1.00 24.08  ? 404 HOH   A O   1 
HETATM 2329 O  O   . HOH   H 5 .   ? 3.368  -0.260  21.474 1.00 20.50  ? 405 HOH   A O   1 
HETATM 2330 O  O   . HOH   H 5 .   ? 31.157 -2.622  15.459 1.00 44.40  ? 406 HOH   A O   1 
HETATM 2331 O  O   . HOH   H 5 .   ? 34.022 18.680  10.690 1.00 25.60  ? 407 HOH   A O   1 
HETATM 2332 O  O   . HOH   H 5 .   ? 15.441 15.382  3.780  1.00 31.88  ? 408 HOH   A O   1 
HETATM 2333 O  O   . HOH   H 5 .   ? 36.364 -0.294  12.319 1.00 37.02  ? 409 HOH   A O   1 
HETATM 2334 O  O   . HOH   H 5 .   ? 0.459  -1.313  9.219  1.00 43.34  ? 410 HOH   A O   1 
HETATM 2335 O  O   . HOH   H 5 .   ? 0.433  -1.282  16.704 1.00 17.72  ? 411 HOH   A O   1 
HETATM 2336 O  O   . HOH   H 5 .   ? 22.289 19.349  19.478 1.00 29.67  ? 412 HOH   A O   1 
HETATM 2337 O  O   . HOH   H 5 .   ? 23.556 8.124   21.599 1.00 25.24  ? 413 HOH   A O   1 
HETATM 2338 O  O   . HOH   H 5 .   ? 35.265 10.635  12.528 1.00 48.71  ? 414 HOH   A O   1 
HETATM 2339 O  O   . HOH   H 5 .   ? 17.454 0.578   20.125 1.00 18.37  ? 415 HOH   A O   1 
HETATM 2340 O  O   . HOH   H 5 .   ? 5.025  8.202   2.355  1.00 35.11  ? 416 HOH   A O   1 
HETATM 2341 O  O   . HOH   H 5 .   ? 3.389  26.936  15.953 1.00 52.51  ? 417 HOH   A O   1 
HETATM 2342 O  O   . HOH   H 5 .   ? 19.753 13.360  2.200  1.00 31.62  ? 418 HOH   A O   1 
HETATM 2343 O  O   . HOH   H 5 .   ? 1.100  -5.035  17.627 1.00 32.99  ? 419 HOH   A O   1 
HETATM 2344 O  O   . HOH   H 5 .   ? 34.112 7.599   16.440 1.00 36.97  ? 420 HOH   A O   1 
HETATM 2345 O  O   . HOH   H 5 .   ? 11.738 17.901  4.750  1.00 45.37  ? 421 HOH   A O   1 
HETATM 2346 O  O   . HOH   H 5 .   ? 6.309  24.171  10.957 1.00 43.21  ? 422 HOH   A O   1 
HETATM 2347 O  O   . HOH   H 5 .   ? 16.648 21.094  19.333 1.00 32.90  ? 423 HOH   A O   1 
HETATM 2348 O  O   . HOH   H 5 .   ? 23.241 19.087  6.314  1.00 20.03  ? 424 HOH   A O   1 
HETATM 2349 O  O   . HOH   H 5 .   ? 19.409 -0.773  33.239 1.00 49.06  ? 425 HOH   A O   1 
HETATM 2350 O  O   . HOH   H 5 .   ? 16.662 -3.917  2.788  1.00 31.04  ? 426 HOH   A O   1 
HETATM 2351 O  O   . HOH   H 5 .   ? 22.819 3.340   20.756 1.00 21.65  ? 427 HOH   A O   1 
HETATM 2352 O  O   . HOH   H 5 .   ? 8.430  6.484   33.826 1.00 22.67  ? 428 HOH   A O   1 
HETATM 2353 O  O   . HOH   H 5 .   ? 19.538 9.287   -0.857 1.00 33.29  ? 429 HOH   A O   1 
HETATM 2354 O  O   . HOH   H 5 .   ? 15.896 21.450  7.389  1.00 25.41  ? 430 HOH   A O   1 
HETATM 2355 O  O   . HOH   H 5 .   ? 21.128 9.866   21.911 1.00 17.27  ? 431 HOH   A O   1 
HETATM 2356 O  O   . HOH   H 5 .   ? 19.200 16.697  26.395 1.00 43.83  ? 432 HOH   A O   1 
HETATM 2357 O  O   . HOH   H 5 .   ? 17.105 -2.444  19.637 1.00 18.76  ? 433 HOH   A O   1 
HETATM 2358 O  O   . HOH   H 5 .   ? 36.758 16.030  16.617 1.00 35.31  ? 434 HOH   A O   1 
HETATM 2359 O  O   . HOH   H 5 .   ? 15.179 -4.938  0.464  1.00 40.18  ? 435 HOH   A O   1 
HETATM 2360 O  O   . HOH   H 5 .   ? 21.043 -4.875  11.477 1.00 28.08  ? 436 HOH   A O   1 
HETATM 2361 O  O   . HOH   H 5 .   ? 8.406  11.581  31.596 1.00 35.54  ? 437 HOH   A O   1 
HETATM 2362 O  O   . HOH   H 5 .   ? 31.659 7.217   5.260  1.00 32.66  ? 438 HOH   A O   1 
HETATM 2363 O  O   . HOH   H 5 .   ? 17.647 8.810   28.479 1.00 29.11  ? 439 HOH   A O   1 
HETATM 2364 O  O   . HOH   H 5 .   ? 4.817  4.473   -0.614 1.00 60.26  ? 440 HOH   A O   1 
HETATM 2365 O  O   . HOH   H 5 .   ? 35.663 3.868   18.576 1.00 58.19  ? 441 HOH   A O   1 
HETATM 2366 O  O   . HOH   H 5 .   ? 8.466  11.560  1.985  1.00 57.25  ? 442 HOH   A O   1 
HETATM 2367 O  O   . HOH   H 5 .   ? 2.183  -5.432  14.691 1.00 38.83  ? 443 HOH   A O   1 
HETATM 2368 O  O   . HOH   H 5 .   ? 18.579 2.149   22.612 1.00 36.82  ? 444 HOH   A O   1 
HETATM 2369 O  O   . HOH   H 5 .   ? 16.714 -5.048  34.329 1.00 30.62  ? 445 HOH   A O   1 
HETATM 2370 O  O   . HOH   H 5 .   ? 38.540 1.059   13.747 1.00 50.42  ? 446 HOH   A O   1 
HETATM 2371 O  O   . HOH   H 5 .   ? 6.402  3.491   3.450  1.00 43.15  ? 447 HOH   A O   1 
HETATM 2372 O  O   . HOH   H 5 .   ? 2.748  -0.117  26.323 1.00 34.24  ? 448 HOH   A O   1 
HETATM 2373 O  O   . HOH   H 5 .   ? 5.112  28.126  17.979 1.00 49.75  ? 449 HOH   A O   1 
HETATM 2374 O  O   . HOH   H 5 .   ? 23.645 6.100   23.282 1.00 44.01  ? 450 HOH   A O   1 
HETATM 2375 O  O   . HOH   H 5 .   ? 11.799 24.242  14.759 1.00 35.32  ? 451 HOH   A O   1 
HETATM 2376 O  O   . HOH   H 5 .   ? 17.847 14.857  2.394  1.00 46.09  ? 452 HOH   A O   1 
HETATM 2377 O  O   . HOH   H 5 .   ? 5.128  12.036  27.606 1.00 60.13  ? 453 HOH   A O   1 
HETATM 2378 O  O   . HOH   H 5 .   ? 18.517 3.117   26.172 1.00 40.84  ? 454 HOH   A O   1 
HETATM 2379 O  O   . HOH   H 5 .   ? 33.188 -4.374  5.314  1.00 45.14  ? 455 HOH   A O   1 
HETATM 2380 O  O   . HOH   H 5 .   ? 9.429  8.176   2.354  1.00 34.65  ? 456 HOH   A O   1 
HETATM 2381 O  O   . HOH   H 5 .   ? 37.713 -4.453  6.787  1.00 36.06  ? 457 HOH   A O   1 
HETATM 2382 O  O   . HOH   H 5 .   ? 2.614  13.811  27.120 1.00 78.73  ? 458 HOH   A O   1 
HETATM 2383 O  O   . HOH   H 5 .   ? 31.275 4.361   16.839 1.00 27.50  ? 459 HOH   A O   1 
HETATM 2384 O  O   . HOH   H 5 .   ? 34.600 9.140   7.873  1.00 43.52  ? 460 HOH   A O   1 
HETATM 2385 O  O   . HOH   H 5 .   ? 2.477  -1.671  22.875 1.00 42.51  ? 461 HOH   A O   1 
HETATM 2386 O  O   . HOH   H 5 .   ? 2.284  -5.002  22.528 1.00 35.45  ? 462 HOH   A O   1 
HETATM 2387 O  O   . HOH   H 5 .   ? 2.049  8.361   2.025  1.00 47.93  ? 463 HOH   A O   1 
HETATM 2388 O  O   . HOH   H 5 .   ? 1.240  -3.928  6.350  1.00 49.30  ? 464 HOH   A O   1 
HETATM 2389 O  O   . HOH   H 5 .   ? 1.056  26.410  17.521 1.00 44.61  ? 465 HOH   A O   1 
HETATM 2390 O  O   . HOH   H 5 .   ? 4.036  -6.928  23.331 1.00 45.02  ? 466 HOH   A O   1 
HETATM 2391 O  O   . HOH   H 5 .   ? 37.957 19.682  15.612 1.00 37.46  ? 467 HOH   A O   1 
HETATM 2392 O  O   . HOH   H 5 .   ? 9.934  25.988  14.055 1.00 42.08  ? 468 HOH   A O   1 
HETATM 2393 O  O   . HOH   H 5 .   ? 1.988  -4.796  25.108 1.00 48.23  ? 469 HOH   A O   1 
HETATM 2394 O  O   . HOH   I 5 .   ? 17.427 -33.396 24.019 1.00 44.53  ? 301 HOH   C O   1 
HETATM 2395 O  O   . HOH   I 5 .   ? 31.055 -23.666 -1.295 1.00 24.73  ? 302 HOH   C O   1 
HETATM 2396 O  O   . HOH   I 5 .   ? 38.237 -7.313  7.058  1.00 25.64  ? 303 HOH   C O   1 
HETATM 2397 O  O   . HOH   I 5 .   ? 24.545 -5.889  15.198 1.00 29.35  ? 304 HOH   C O   1 
HETATM 2398 O  O   . HOH   I 5 .   ? 26.927 -7.941  2.189  1.00 48.86  ? 305 HOH   C O   1 
HETATM 2399 O  O   . HOH   I 5 .   ? 38.400 -18.528 21.565 1.00 27.79  ? 306 HOH   C O   1 
HETATM 2400 O  O   . HOH   I 5 .   ? 24.334 -9.625  26.976 1.00 42.27  ? 307 HOH   C O   1 
HETATM 2401 O  O   . HOH   I 5 .   ? 30.534 -18.092 26.925 1.00 19.67  ? 308 HOH   C O   1 
HETATM 2402 O  O   . HOH   I 5 .   ? 14.488 -18.739 31.729 1.00 37.74  ? 309 HOH   C O   1 
HETATM 2403 O  O   . HOH   I 5 .   ? 17.693 -6.014  24.033 1.00 25.32  ? 310 HOH   C O   1 
HETATM 2404 O  O   . HOH   I 5 .   ? 19.633 -4.102  20.114 1.00 21.77  ? 311 HOH   C O   1 
HETATM 2405 O  O   . HOH   I 5 .   ? 14.512 -9.278  10.928 1.00 31.45  ? 312 HOH   C O   1 
HETATM 2406 O  O   . HOH   I 5 .   ? 18.714 -32.406 19.832 1.00 48.90  ? 313 HOH   C O   1 
HETATM 2407 O  O   . HOH   I 5 .   ? 10.120 -17.592 18.243 1.00 27.97  ? 314 HOH   C O   1 
HETATM 2408 O  O   . HOH   I 5 .   ? 42.997 -3.708  19.142 1.00 47.77  ? 315 HOH   C O   1 
HETATM 2409 O  O   . HOH   I 5 .   ? 35.866 -26.195 34.311 1.00 36.15  ? 316 HOH   C O   1 
HETATM 2410 O  O   . HOH   I 5 .   ? 23.085 -32.802 20.710 1.00 35.71  ? 317 HOH   C O   1 
HETATM 2411 O  O   . HOH   I 5 .   ? 20.637 -18.715 12.787 1.00 14.01  ? 318 HOH   C O   1 
HETATM 2412 O  O   . HOH   I 5 .   ? 42.535 -11.166 11.339 1.00 29.19  ? 319 HOH   C O   1 
HETATM 2413 O  O   . HOH   I 5 .   ? 18.456 -8.847  13.727 1.00 29.40  ? 320 HOH   C O   1 
HETATM 2414 O  O   . HOH   I 5 .   ? 7.249  -30.435 22.096 1.00 33.80  ? 321 HOH   C O   1 
HETATM 2415 O  O   . HOH   I 5 .   ? 22.162 -10.523 7.910  1.00 58.36  ? 322 HOH   C O   1 
HETATM 2416 O  O   . HOH   I 5 .   ? 17.799 -27.553 16.465 1.00 18.24  ? 323 HOH   C O   1 
HETATM 2417 O  O   . HOH   I 5 .   ? 36.985 -18.676 28.239 1.00 29.83  ? 324 HOH   C O   1 
HETATM 2418 O  O   . HOH   I 5 .   ? 28.919 -9.088  25.396 1.00 55.35  ? 325 HOH   C O   1 
HETATM 2419 O  O   . HOH   I 5 .   ? 14.731 -24.005 12.279 1.00 30.26  ? 326 HOH   C O   1 
HETATM 2420 O  O   . HOH   I 5 .   ? 36.028 -17.518 11.752 1.00 26.07  ? 327 HOH   C O   1 
HETATM 2421 O  O   . HOH   I 5 .   ? 21.981 -28.681 4.729  1.00 25.03  ? 328 HOH   C O   1 
HETATM 2422 O  O   . HOH   I 5 .   ? 32.278 -23.672 29.171 1.00 19.58  ? 329 HOH   C O   1 
HETATM 2423 O  O   . HOH   I 5 .   ? 22.722 -5.863  21.101 1.00 20.54  ? 330 HOH   C O   1 
HETATM 2424 O  O   . HOH   I 5 .   ? 36.460 -2.487  11.254 1.00 38.80  ? 331 HOH   C O   1 
HETATM 2425 O  O   . HOH   I 5 .   ? 11.072 -21.821 13.652 1.00 41.89  ? 332 HOH   C O   1 
HETATM 2426 O  O   . HOH   I 5 .   ? 40.447 -27.122 15.344 1.00 12.89  ? 333 HOH   C O   1 
HETATM 2427 O  O   . HOH   I 5 .   ? 41.212 -24.887 7.401  1.00 29.10  ? 334 HOH   C O   1 
HETATM 2428 O  O   . HOH   I 5 .   ? 26.482 -5.438  9.901  1.00 24.15  ? 335 HOH   C O   1 
HETATM 2429 O  O   . HOH   I 5 .   ? 16.737 -31.512 27.902 1.00 48.56  ? 336 HOH   C O   1 
HETATM 2430 O  O   . HOH   I 5 .   ? 37.362 -31.878 10.963 1.00 23.97  ? 337 HOH   C O   1 
HETATM 2431 O  O   . HOH   I 5 .   ? 13.679 -24.170 29.292 1.00 38.01  ? 338 HOH   C O   1 
HETATM 2432 O  O   . HOH   I 5 .   ? 30.717 -21.474 28.450 1.00 17.72  ? 339 HOH   C O   1 
HETATM 2433 O  O   . HOH   I 5 .   ? 9.734  -8.856  23.917 1.00 27.68  ? 340 HOH   C O   1 
HETATM 2434 O  O   . HOH   I 5 .   ? 16.592 -15.325 8.250  1.00 52.43  ? 341 HOH   C O   1 
HETATM 2435 O  O   . HOH   I 5 .   ? 26.009 -25.195 8.792  1.00 14.31  ? 342 HOH   C O   1 
HETATM 2436 O  O   . HOH   I 5 .   ? 21.545 -26.317 34.351 1.00 27.65  ? 343 HOH   C O   1 
HETATM 2437 O  O   . HOH   I 5 .   ? 11.780 -24.283 21.638 1.00 18.84  ? 344 HOH   C O   1 
HETATM 2438 O  O   . HOH   I 5 .   ? 36.051 -28.468 2.918  1.00 37.06  ? 345 HOH   C O   1 
HETATM 2439 O  O   . HOH   I 5 .   ? 24.695 -15.724 7.333  1.00 19.53  ? 346 HOH   C O   1 
HETATM 2440 O  O   . HOH   I 5 .   ? 29.714 -15.212 19.634 1.00 16.99  ? 347 HOH   C O   1 
HETATM 2441 O  O   . HOH   I 5 .   ? 9.066  -8.065  21.218 1.00 24.39  ? 348 HOH   C O   1 
HETATM 2442 O  O   . HOH   I 5 .   ? 35.146 -13.085 8.789  1.00 21.24  ? 349 HOH   C O   1 
HETATM 2443 O  O   . HOH   I 5 .   ? 23.802 -8.176  9.381  1.00 23.05  ? 350 HOH   C O   1 
HETATM 2444 O  O   . HOH   I 5 .   ? 8.727  -13.273 10.756 1.00 23.03  ? 351 HOH   C O   1 
HETATM 2445 O  O   . HOH   I 5 .   ? 36.306 -21.207 7.104  1.00 22.37  ? 352 HOH   C O   1 
HETATM 2446 O  O   . HOH   I 5 .   ? 27.907 -4.602  18.374 1.00 43.19  ? 353 HOH   C O   1 
HETATM 2447 O  O   . HOH   I 5 .   ? 35.373 -32.699 3.442  1.00 30.82  ? 354 HOH   C O   1 
HETATM 2448 O  O   . HOH   I 5 .   ? 13.051 -11.211 28.494 1.00 37.78  ? 355 HOH   C O   1 
HETATM 2449 O  O   . HOH   I 5 .   ? 27.128 -35.502 20.745 1.00 28.13  ? 356 HOH   C O   1 
HETATM 2450 O  O   . HOH   I 5 .   ? 29.632 -15.893 30.543 1.00 31.80  ? 357 HOH   C O   1 
HETATM 2451 O  O   . HOH   I 5 .   ? 20.702 -25.661 13.797 1.00 20.20  ? 358 HOH   C O   1 
HETATM 2452 O  O   . HOH   I 5 .   ? 25.847 -37.900 24.270 1.00 30.47  ? 359 HOH   C O   1 
HETATM 2453 O  O   . HOH   I 5 .   ? 34.809 -34.802 18.172 1.00 29.33  ? 360 HOH   C O   1 
HETATM 2454 O  O   . HOH   I 5 .   ? 22.123 -13.811 29.722 1.00 38.36  ? 361 HOH   C O   1 
HETATM 2455 O  O   . HOH   I 5 .   ? 31.966 -10.388 13.832 1.00 20.53  ? 362 HOH   C O   1 
HETATM 2456 O  O   . HOH   I 5 .   ? 10.294 -16.959 14.882 1.00 32.16  ? 363 HOH   C O   1 
HETATM 2457 O  O   . HOH   I 5 .   ? 4.141  -10.436 19.419 1.00 28.83  ? 364 HOH   C O   1 
HETATM 2458 O  O   . HOH   I 5 .   ? 19.074 -27.736 28.126 1.00 20.00  ? 365 HOH   C O   1 
HETATM 2459 O  O   . HOH   I 5 .   ? 29.661 -13.046 13.007 1.00 16.82  ? 366 HOH   C O   1 
HETATM 2460 O  O   . HOH   I 5 .   ? 22.798 -8.486  14.022 1.00 17.00  ? 367 HOH   C O   1 
HETATM 2461 O  O   . HOH   I 5 .   ? 23.138 -25.340 8.902  1.00 21.57  ? 368 HOH   C O   1 
HETATM 2462 O  O   . HOH   I 5 .   ? 34.395 -23.304 -0.565 1.00 34.07  ? 369 HOH   C O   1 
HETATM 2463 O  O   . HOH   I 5 .   ? 31.649 -34.872 31.820 1.00 44.52  ? 370 HOH   C O   1 
HETATM 2464 O  O   . HOH   I 5 .   ? 23.540 -3.335  19.102 1.00 35.45  ? 371 HOH   C O   1 
HETATM 2465 O  O   . HOH   I 5 .   ? 13.127 -29.561 19.211 1.00 29.67  ? 372 HOH   C O   1 
HETATM 2466 O  O   . HOH   I 5 .   ? 14.495 -28.801 25.606 1.00 37.36  ? 373 HOH   C O   1 
HETATM 2467 O  O   . HOH   I 5 .   ? 11.294 -22.553 28.541 1.00 29.77  ? 374 HOH   C O   1 
HETATM 2468 O  O   . HOH   I 5 .   ? 23.387 -33.609 29.017 1.00 28.41  ? 375 HOH   C O   1 
HETATM 2469 O  O   . HOH   I 5 .   ? 32.861 -9.793  11.147 1.00 16.80  ? 376 HOH   C O   1 
HETATM 2470 O  O   . HOH   I 5 .   ? 32.074 -34.539 24.858 1.00 26.25  ? 377 HOH   C O   1 
HETATM 2471 O  O   . HOH   I 5 .   ? 27.940 -16.303 22.093 1.00 14.61  ? 378 HOH   C O   1 
HETATM 2472 O  O   . HOH   I 5 .   ? 20.095 -23.781 34.587 1.00 32.69  ? 379 HOH   C O   1 
HETATM 2473 O  O   . HOH   I 5 .   ? 34.112 -13.351 25.537 1.00 21.30  ? 380 HOH   C O   1 
HETATM 2474 O  O   . HOH   I 5 .   ? 22.983 -33.254 5.384  1.00 27.36  ? 381 HOH   C O   1 
HETATM 2475 O  O   . HOH   I 5 .   ? 41.652 -13.760 10.220 1.00 41.08  ? 382 HOH   C O   1 
HETATM 2476 O  O   . HOH   I 5 .   ? 10.730 -11.827 8.953  1.00 31.57  ? 383 HOH   C O   1 
HETATM 2477 O  O   . HOH   I 5 .   ? 37.300 -31.505 25.842 1.00 31.24  ? 384 HOH   C O   1 
HETATM 2478 O  O   . HOH   I 5 .   ? 6.802  -9.275  22.630 1.00 32.09  ? 385 HOH   C O   1 
HETATM 2479 O  O   . HOH   I 5 .   ? 17.334 -23.930 8.610  1.00 36.63  ? 386 HOH   C O   1 
HETATM 2480 O  O   . HOH   I 5 .   ? 31.171 -12.118 10.692 1.00 16.68  ? 387 HOH   C O   1 
HETATM 2481 O  O   . HOH   I 5 .   ? 36.980 -29.142 10.235 1.00 20.19  ? 388 HOH   C O   1 
HETATM 2482 O  O   . HOH   I 5 .   ? 10.896 -6.378  13.181 1.00 23.51  ? 389 HOH   C O   1 
HETATM 2483 O  O   . HOH   I 5 .   ? 25.853 -31.002 30.875 1.00 19.51  ? 390 HOH   C O   1 
HETATM 2484 O  O   . HOH   I 5 .   ? 14.697 -18.372 10.345 1.00 33.13  ? 391 HOH   C O   1 
HETATM 2485 O  O   . HOH   I 5 .   ? 26.341 -31.162 14.850 1.00 19.81  ? 392 HOH   C O   1 
HETATM 2486 O  O   . HOH   I 5 .   ? 38.889 -15.820 4.186  1.00 38.45  ? 393 HOH   C O   1 
HETATM 2487 O  O   . HOH   I 5 .   ? 32.919 -30.219 31.784 1.00 20.34  ? 394 HOH   C O   1 
HETATM 2488 O  O   . HOH   I 5 .   ? 26.357 -6.006  22.084 1.00 30.68  ? 395 HOH   C O   1 
HETATM 2489 O  O   . HOH   I 5 .   ? 9.948  -24.916 19.674 1.00 23.01  ? 396 HOH   C O   1 
HETATM 2490 O  O   . HOH   I 5 .   ? 30.301 -18.003 8.399  1.00 27.08  ? 397 HOH   C O   1 
HETATM 2491 O  O   . HOH   I 5 .   ? 22.875 -28.152 12.579 1.00 20.94  ? 398 HOH   C O   1 
HETATM 2492 O  O   . HOH   I 5 .   ? 3.769  -8.112  14.696 1.00 26.61  ? 399 HOH   C O   1 
HETATM 2493 O  O   . HOH   I 5 .   ? 26.485 -12.003 27.664 1.00 29.40  ? 400 HOH   C O   1 
HETATM 2494 O  O   . HOH   I 5 .   ? 33.591 -32.812 0.736  1.00 38.87  ? 401 HOH   C O   1 
HETATM 2495 O  O   . HOH   I 5 .   ? 31.560 -13.489 4.367  1.00 36.27  ? 402 HOH   C O   1 
HETATM 2496 O  O   . HOH   I 5 .   ? 31.038 -5.937  6.038  1.00 50.22  ? 403 HOH   C O   1 
HETATM 2497 O  O   . HOH   I 5 .   ? 4.489  -27.921 23.226 1.00 39.74  ? 404 HOH   C O   1 
HETATM 2498 O  O   . HOH   I 5 .   ? 23.326 -28.129 1.614  1.00 35.77  ? 405 HOH   C O   1 
HETATM 2499 O  O   . HOH   I 5 .   ? 35.418 -24.556 24.785 1.00 21.95  ? 406 HOH   C O   1 
HETATM 2500 O  O   . HOH   I 5 .   ? 35.150 -13.658 6.093  1.00 34.14  ? 407 HOH   C O   1 
HETATM 2501 O  O   . HOH   I 5 .   ? 32.741 -14.310 9.481  1.00 16.77  ? 408 HOH   C O   1 
HETATM 2502 O  O   . HOH   I 5 .   ? 10.347 -30.911 25.338 1.00 33.45  ? 409 HOH   C O   1 
HETATM 2503 O  O   . HOH   I 5 .   ? 35.749 -28.434 7.864  1.00 19.54  ? 410 HOH   C O   1 
HETATM 2504 O  O   . HOH   I 5 .   ? 34.749 -4.029  17.754 1.00 31.65  ? 411 HOH   C O   1 
HETATM 2505 O  O   . HOH   I 5 .   ? 21.656 -18.803 5.911  1.00 26.96  ? 412 HOH   C O   1 
HETATM 2506 O  O   . HOH   I 5 .   ? 17.164 -25.304 12.697 1.00 23.17  ? 413 HOH   C O   1 
HETATM 2507 O  O   . HOH   I 5 .   ? 37.919 -23.358 4.716  1.00 36.36  ? 414 HOH   C O   1 
HETATM 2508 O  O   . HOH   I 5 .   ? 37.747 -20.363 4.961  1.00 36.23  ? 415 HOH   C O   1 
HETATM 2509 O  O   . HOH   I 5 .   ? 20.144 -32.245 22.200 1.00 33.07  ? 416 HOH   C O   1 
HETATM 2510 O  O   . HOH   I 5 .   ? 38.701 -12.898 25.867 1.00 29.49  ? 417 HOH   C O   1 
HETATM 2511 O  O   . HOH   I 5 .   ? 24.391 -13.840 5.482  1.00 36.44  ? 418 HOH   C O   1 
HETATM 2512 O  O   . HOH   I 5 .   ? 9.526  -18.408 26.535 1.00 31.32  ? 419 HOH   C O   1 
HETATM 2513 O  O   . HOH   I 5 .   ? 18.445 -8.341  25.513 1.00 22.64  ? 420 HOH   C O   1 
HETATM 2514 O  O   . HOH   I 5 .   ? 3.894  -12.793 17.027 1.00 37.16  ? 421 HOH   C O   1 
HETATM 2515 O  O   . HOH   I 5 .   ? 39.970 -29.787 14.733 1.00 18.34  ? 422 HOH   C O   1 
HETATM 2516 O  O   . HOH   I 5 .   ? 18.732 -19.102 10.814 1.00 19.62  ? 423 HOH   C O   1 
HETATM 2517 O  O   . HOH   I 5 .   ? 6.326  -22.951 18.123 1.00 33.91  ? 424 HOH   C O   1 
HETATM 2518 O  O   . HOH   I 5 .   ? 5.887  -12.600 23.186 1.00 54.82  ? 425 HOH   C O   1 
HETATM 2519 O  O   . HOH   I 5 .   ? 16.331 -20.512 11.456 1.00 24.74  ? 426 HOH   C O   1 
HETATM 2520 O  O   . HOH   I 5 .   ? 33.902 -35.786 8.908  1.00 33.30  ? 427 HOH   C O   1 
HETATM 2521 O  O   . HOH   I 5 .   ? 33.747 -15.563 27.140 1.00 35.03  ? 428 HOH   C O   1 
HETATM 2522 O  O   . HOH   I 5 .   ? 41.557 -12.391 18.112 1.00 30.80  ? 429 HOH   C O   1 
HETATM 2523 O  O   . HOH   I 5 .   ? 30.100 -6.695  24.748 1.00 53.01  ? 430 HOH   C O   1 
HETATM 2524 O  O   . HOH   I 5 .   ? 23.349 -31.097 13.116 1.00 32.54  ? 431 HOH   C O   1 
HETATM 2525 O  O   . HOH   I 5 .   ? 29.817 -10.109 27.726 1.00 47.09  ? 432 HOH   C O   1 
HETATM 2526 O  O   . HOH   I 5 .   ? 23.028 -17.563 33.302 1.00 22.51  ? 433 HOH   C O   1 
HETATM 2527 O  O   . HOH   I 5 .   ? 3.966  -22.530 26.272 1.00 55.59  ? 434 HOH   C O   1 
HETATM 2528 O  O   . HOH   I 5 .   ? 6.399  -20.039 17.962 1.00 35.20  ? 435 HOH   C O   1 
HETATM 2529 O  O   . HOH   I 5 .   ? 8.777  -12.878 24.928 1.00 57.84  ? 436 HOH   C O   1 
HETATM 2530 O  O   . HOH   I 5 .   ? 36.395 -24.433 27.301 1.00 40.06  ? 437 HOH   C O   1 
HETATM 2531 O  O   . HOH   I 5 .   ? 34.031 -31.765 29.669 1.00 25.95  ? 438 HOH   C O   1 
HETATM 2532 O  O   . HOH   I 5 .   ? 34.604 -20.625 0.656  1.00 61.88  ? 439 HOH   C O   1 
HETATM 2533 O  O   . HOH   I 5 .   ? 9.882  -20.116 28.874 1.00 36.64  ? 440 HOH   C O   1 
HETATM 2534 O  O   . HOH   I 5 .   ? 20.824 -17.493 34.618 1.00 28.71  ? 441 HOH   C O   1 
HETATM 2535 O  O   . HOH   I 5 .   ? 23.424 -15.537 31.543 1.00 31.49  ? 442 HOH   C O   1 
HETATM 2536 O  O   . HOH   I 5 .   ? 21.369 -26.874 10.005 1.00 37.79  ? 443 HOH   C O   1 
HETATM 2537 O  O   . HOH   I 5 .   ? 39.155 -25.390 5.733  1.00 56.59  ? 444 HOH   C O   1 
HETATM 2538 O  O   . HOH   I 5 .   ? 24.306 -12.414 28.997 1.00 54.99  ? 445 HOH   C O   1 
HETATM 2539 O  O   . HOH   I 5 .   ? 33.657 -34.312 30.263 1.00 47.59  ? 446 HOH   C O   1 
HETATM 2540 O  O   . HOH   I 5 .   ? 16.301 -27.538 14.088 1.00 29.40  ? 447 HOH   C O   1 
HETATM 2541 O  O   . HOH   I 5 .   ? 6.733  -18.556 26.315 1.00 51.38  ? 448 HOH   C O   1 
HETATM 2542 O  O   . HOH   I 5 .   ? 6.147  -12.445 10.567 1.00 46.94  ? 449 HOH   C O   1 
HETATM 2543 O  O   . HOH   I 5 .   ? 9.936  -21.414 16.094 1.00 35.41  ? 450 HOH   C O   1 
HETATM 2544 O  O   . HOH   I 5 .   ? 32.261 -19.347 29.226 1.00 33.83  ? 451 HOH   C O   1 
HETATM 2545 O  O   . HOH   I 5 .   ? 18.389 -26.106 10.127 1.00 35.05  ? 452 HOH   C O   1 
HETATM 2546 O  O   . HOH   I 5 .   ? 12.962 -28.348 28.964 1.00 70.90  ? 453 HOH   C O   1 
HETATM 2547 O  O   . HOH   I 5 .   ? 18.110 -17.887 8.214  1.00 32.64  ? 454 HOH   C O   1 
HETATM 2548 O  O   . HOH   I 5 .   ? 16.847 -28.911 28.858 1.00 41.03  ? 455 HOH   C O   1 
HETATM 2549 O  O   . HOH   I 5 .   ? 35.068 -20.146 29.363 1.00 46.51  ? 456 HOH   C O   1 
HETATM 2550 O  O   . HOH   I 5 .   ? 8.855  -23.592 17.519 1.00 30.87  ? 457 HOH   C O   1 
HETATM 2551 O  O   . HOH   I 5 .   ? 39.635 -35.834 13.279 1.00 43.59  ? 458 HOH   C O   1 
HETATM 2552 O  O   . HOH   I 5 .   ? 34.952 -22.859 29.049 1.00 33.23  ? 459 HOH   C O   1 
HETATM 2553 O  O   . HOH   I 5 .   ? 37.626 -34.106 9.352  1.00 37.44  ? 460 HOH   C O   1 
HETATM 2554 O  O   . HOH   I 5 .   ? 11.292 -26.972 15.056 1.00 56.09  ? 461 HOH   C O   1 
HETATM 2555 O  O   . HOH   I 5 .   ? 34.115 -10.853 26.612 1.00 42.43  ? 462 HOH   C O   1 
HETATM 2556 O  O   . HOH   I 5 .   ? 5.591  -24.196 15.657 1.00 63.15  ? 463 HOH   C O   1 
HETATM 2557 O  O   . HOH   I 5 .   ? 18.999 -15.325 34.658 1.00 37.20  ? 464 HOH   C O   1 
HETATM 2558 O  O   . HOH   I 5 .   ? 19.256 -17.671 5.926  1.00 36.86  ? 465 HOH   C O   1 
HETATM 2559 O  O   . HOH   I 5 .   ? 39.175 -2.707  10.684 1.00 37.16  ? 466 HOH   C O   1 
HETATM 2560 O  O   . HOH   I 5 .   ? 3.035  -9.369  17.073 1.00 32.89  ? 467 HOH   C O   1 
HETATM 2561 O  O   . HOH   I 5 .   ? 38.436 -36.095 10.639 1.00 46.51  ? 468 HOH   C O   1 
HETATM 2562 O  O   . HOH   I 5 .   ? 13.722 -28.241 14.130 1.00 44.32  ? 469 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   ? 0.2291 0.2253 0.1936 -0.0317 -0.0033 -0.0109 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2208 0.2196 0.1925 -0.0286 -0.0078 -0.0068 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2121 0.2135 0.1945 -0.0203 -0.0120 -0.0003 7   SER   A C   
4    O O   . SER   A 1   ? 0.2157 0.2180 0.1982 -0.0188 -0.0128 0.0019  7   SER   A O   
5    C CB  . SER   A 1   ? 0.2525 0.2582 0.2176 -0.0387 -0.0135 -0.0034 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2940 0.3071 0.2584 -0.0416 -0.0200 0.0044  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1893 0.1915 0.1804 -0.0159 -0.0136 0.0019  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1733 0.1770 0.1748 -0.0097 -0.0155 0.0066  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1486 0.1498 0.1568 -0.0047 -0.0130 0.0046  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1709 0.1688 0.1765 -0.0043 -0.0098 0.0004  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1424 0.1452 0.1599 -0.0016 -0.0139 0.0078  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1491 0.1503 0.1721 0.0015  -0.0112 0.0058  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1453 0.1458 0.1757 0.0043  -0.0085 0.0065  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1619 0.1631 0.1967 0.0045  -0.0091 0.0097  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1699 0.1740 0.1978 -0.0001 -0.0136 0.0079  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1417 0.1408 0.1738 0.0052  -0.0050 0.0034  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1339 0.1316 0.1724 0.0056  -0.0005 0.0020  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1432 0.1418 0.1919 0.0060  0.0007  0.0028  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1440 0.1437 0.1905 0.0054  -0.0005 0.0019  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1346 0.1318 0.1666 0.0037  0.0029  -0.0019 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1679 0.1659 0.1919 0.0036  0.0014  -0.0015 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1586 0.1539 0.1951 0.0014  0.0093  -0.0051 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1695 0.1702 0.1883 0.0010  0.0027  -0.0023 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1420 0.1401 0.2037 0.0070  0.0038  0.0048  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1578 0.1571 0.2331 0.0077  0.0063  0.0059  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1588 0.1536 0.2399 0.0064  0.0159  0.0002  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1668 0.1586 0.2584 0.0072  0.0210  0.0007  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1655 0.1690 0.2557 0.0095  0.0025  0.0146  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1494 0.1584 0.2314 0.0077  -0.0065 0.0194  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1629 0.1756 0.2441 0.0061  -0.0097 0.0202  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1757 0.1861 0.2501 0.0063  -0.0110 0.0224  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1741 0.1909 0.2453 0.0023  -0.0165 0.0225  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1844 0.1993 0.2487 0.0023  -0.0177 0.0249  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1894 0.2072 0.2520 -0.0001 -0.0201 0.0246  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2249 0.2466 0.2765 -0.0061 -0.0253 0.0257  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1621 0.1560 0.2358 0.0032  0.0194  -0.0056 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1766 0.1669 0.2517 -0.0012 0.0293  -0.0127 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1784 0.1695 0.2609 -0.0024 0.0330  -0.0147 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1720 0.1664 0.2476 -0.0025 0.0276  -0.0134 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2012 0.1920 0.2581 -0.0068 0.0296  -0.0171 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1991 0.1944 0.2446 -0.0072 0.0224  -0.0147 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2157 0.2038 0.2711 -0.0145 0.0401  -0.0251 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1905 0.1780 0.2888 -0.0031 0.0430  -0.0178 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2006 0.1889 0.3080 -0.0041 0.0474  -0.0198 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1795 0.1737 0.2936 0.0010  0.0380  -0.0116 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1796 0.1766 0.3024 0.0056  0.0320  -0.0036 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1664 0.1632 0.2734 -0.0012 0.0358  -0.0132 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1626 0.1649 0.2716 0.0018  0.0268  -0.0066 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1612 0.1646 0.2506 0.0009  0.0184  -0.0059 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1631 0.1690 0.2490 0.0004  0.0139  -0.0044 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1896 0.1941 0.3090 0.0008  0.0304  -0.0076 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2386 0.2436 0.3843 0.0036  0.0373  -0.0048 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2580 0.2689 0.4188 0.0073  0.0318  0.0044  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2159 0.2152 0.3684 0.0012  0.0497  -0.0119 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1452 0.1466 0.2243 0.0008  0.0167  -0.0065 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1455 0.1474 0.2098 0.0006  0.0103  -0.0054 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1387 0.1410 0.2015 0.0031  0.0052  -0.0015 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1489 0.1503 0.2170 0.0043  0.0070  -0.0005 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1663 0.1670 0.2187 -0.0031 0.0130  -0.0092 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1698 0.1713 0.2201 -0.0080 0.0175  -0.0127 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1811 0.1843 0.2308 -0.0083 0.0149  -0.0114 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2008 0.2015 0.2490 -0.0136 0.0249  -0.0178 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1973 0.2018 0.2447 -0.0136 0.0189  -0.0143 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2121 0.2144 0.2561 -0.0203 0.0292  -0.0214 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2181 0.2226 0.2615 -0.0200 0.0257  -0.0190 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2697 0.2763 0.3087 -0.0274 0.0298  -0.0221 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1340 0.1370 0.1884 0.0030  -0.0001 0.0000  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1324 0.1355 0.1814 0.0035  -0.0041 0.0022  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1338 0.1343 0.1719 0.0031  -0.0039 -0.0002 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1433 0.1430 0.1787 0.0023  -0.0040 -0.0011 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1565 0.1630 0.2067 0.0018  -0.0091 0.0057  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1623 0.1688 0.2030 -0.0004 -0.0125 0.0063  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1851 0.1968 0.2259 -0.0051 -0.0175 0.0101  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1859 0.1953 0.2138 -0.0098 -0.0179 0.0066  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1962 0.2064 0.2162 -0.0138 -0.0195 0.0069  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2065 0.2199 0.2299 -0.0127 -0.0219 0.0115  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2078 0.2144 0.2168 -0.0190 -0.0174 0.0018  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1258 0.1253 0.1598 0.0038  -0.0031 -0.0005 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1268 0.1253 0.1543 0.0038  -0.0026 -0.0011 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1407 0.1377 0.1642 0.0041  -0.0042 -0.0008 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1479 0.1455 0.1707 0.0042  -0.0052 -0.0001 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1357 0.1356 0.1613 0.0029  -0.0004 -0.0014 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1479 0.1492 0.1703 0.0027  -0.0007 0.0006  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1496 0.1506 0.1775 0.0001  0.0029  -0.0034 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1297 0.1245 0.1510 0.0036  -0.0035 -0.0018 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1336 0.1260 0.1503 0.0021  -0.0029 -0.0034 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1576 0.1502 0.1743 0.0021  -0.0031 -0.0033 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1384 0.1278 0.1564 0.0034  0.0011  -0.0041 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1480 0.1379 0.1710 0.0051  0.0023  -0.0020 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1262 0.1181 0.1398 -0.0022 -0.0042 -0.0050 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2002 0.1926 0.2145 -0.0021 -0.0047 -0.0046 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1517 0.1485 0.1663 -0.0040 -0.0090 -0.0017 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2096 0.2002 0.2164 -0.0069 -0.0036 -0.0073 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0899 0.0796 0.1061 -0.0026 -0.0026 -0.0062 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2335 0.2308 0.2517 -0.0027 -0.0089 -0.0013 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1396 0.1262 0.1546 0.0021  0.0038  -0.0064 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1480 0.1308 0.1684 0.0036  0.0095  -0.0071 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1538 0.1321 0.1764 0.0017  0.0125  -0.0095 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1632 0.1399 0.1790 -0.0031 0.0119  -0.0133 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1564 0.1358 0.1728 0.0010  0.0138  -0.0112 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1575 0.1409 0.1715 0.0024  0.0113  -0.0091 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1641 0.1498 0.1708 0.0000  0.0072  -0.0093 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1649 0.1500 0.1865 0.0061  0.0134  -0.0058 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1546 0.1316 0.1873 0.0049  0.0156  -0.0063 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1450 0.1168 0.1810 0.0033  0.0192  -0.0083 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1830 0.1470 0.2148 -0.0018 0.0261  -0.0162 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1912 0.1521 0.2176 -0.0067 0.0269  -0.0205 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1623 0.1341 0.2124 0.0074  0.0220  -0.0020 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1682 0.1347 0.2236 0.0063  0.0254  -0.0027 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1863 0.1537 0.2588 0.0105  0.0283  0.0059  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1923 0.1554 0.2715 0.0099  0.0309  0.0072  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2071 0.1600 0.2939 0.0089  0.0403  0.0028  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2181 0.1636 0.3042 0.0072  0.0482  -0.0048 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2240 0.1733 0.3187 0.0088  0.0426  0.0054  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1783 0.1397 0.2114 -0.0018 0.0313  -0.0185 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2085 0.1617 0.2368 -0.0085 0.0402  -0.0275 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2116 0.1671 0.2221 -0.0174 0.0360  -0.0326 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2544 0.2042 0.2572 -0.0261 0.0427  -0.0407 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2279 0.1767 0.2641 -0.0069 0.0492  -0.0296 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2125 0.1668 0.2414 -0.0069 0.0450  -0.0287 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2028 0.1647 0.2372 -0.0002 0.0387  -0.0206 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2225 0.1757 0.2386 -0.0141 0.0470  -0.0351 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2180 0.1824 0.2441 -0.0024 0.0372  -0.0224 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2247 0.1841 0.2400 -0.0105 0.0420  -0.0307 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2095 0.1738 0.2139 -0.0163 0.0255  -0.0276 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2132 0.1827 0.2047 -0.0240 0.0195  -0.0285 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2237 0.1983 0.2150 -0.0249 0.0125  -0.0249 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2340 0.2152 0.2184 -0.0305 0.0063  -0.0228 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2065 0.1818 0.1944 -0.0228 0.0143  -0.0248 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2123 0.1834 0.1992 -0.0233 0.0211  -0.0286 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2201 0.1975 0.2032 -0.0221 0.0150  -0.0242 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2471 0.2131 0.2232 -0.0348 0.0286  -0.0375 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2059 0.1784 0.2063 -0.0194 0.0134  -0.0231 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1950 0.1722 0.1964 -0.0199 0.0078  -0.0201 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2120 0.1893 0.2050 -0.0301 0.0080  -0.0241 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2327 0.2026 0.2211 -0.0359 0.0157  -0.0311 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1967 0.1710 0.2080 -0.0137 0.0099  -0.0181 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2017 0.1876 0.1934 -0.0329 0.0002  -0.0195 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1933 0.1829 0.1768 -0.0441 -0.0016 -0.0213 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2070 0.1941 0.1949 -0.0439 0.0000  -0.0226 24  THR   A C   
141  O O   . THR   A 18  ? 0.1903 0.1746 0.1880 -0.0350 0.0011  -0.0208 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2233 0.2258 0.2069 -0.0474 -0.0116 -0.0129 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2226 0.2290 0.2192 -0.0388 -0.0156 -0.0069 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2322 0.2378 0.2128 -0.0472 -0.0141 -0.0100 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2188 0.2085 0.1992 -0.0547 -0.0007 -0.0250 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2185 0.2070 0.2028 -0.0552 0.0000  -0.0257 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2007 0.1978 0.1966 -0.0476 -0.0075 -0.0172 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.1970 0.1906 0.2005 -0.0416 -0.0055 -0.0172 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2471 0.2395 0.2200 -0.0703 -0.0007 -0.0290 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3314 0.3266 0.3093 -0.0712 -0.0028 -0.0274 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3782 0.3623 0.3596 -0.0686 0.0051  -0.0330 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3675 0.3756 0.3511 -0.0723 -0.0118 -0.0192 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3775 0.3677 0.3624 -0.0706 0.0008  -0.0299 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3921 0.3970 0.3796 -0.0720 -0.0094 -0.0214 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2000 0.2079 0.1988 -0.0475 -0.0152 -0.0098 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1891 0.2037 0.2016 -0.0404 -0.0198 -0.0027 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1746 0.1824 0.1942 -0.0292 -0.0157 -0.0038 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1849 0.1931 0.2128 -0.0246 -0.0151 -0.0026 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2073 0.2338 0.2257 -0.0416 -0.0274 0.0065  26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2957 0.3284 0.3314 -0.0350 -0.0298 0.0130  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3464 0.3846 0.3877 -0.0379 -0.0319 0.0155  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3078 0.3393 0.3530 -0.0266 -0.0286 0.0155  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1674 0.1696 0.1828 -0.0261 -0.0126 -0.0063 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1664 0.1637 0.1870 -0.0177 -0.0091 -0.0068 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1572 0.1487 0.1796 -0.0165 -0.0048 -0.0095 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1687 0.1610 0.1971 -0.0123 -0.0045 -0.0076 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1668 0.1599 0.1832 -0.0157 -0.0065 -0.0085 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1798 0.1781 0.1961 -0.0152 -0.0105 -0.0050 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1872 0.1908 0.2114 -0.0124 -0.0136 -0.0004 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1809 0.1775 0.1902 -0.0180 -0.0095 -0.0068 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1607 0.1459 0.1780 -0.0208 -0.0006 -0.0140 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1704 0.1493 0.1915 -0.0197 0.0042  -0.0157 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1681 0.1511 0.1920 -0.0215 0.0014  -0.0142 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1732 0.1539 0.2024 -0.0184 0.0033  -0.0129 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1816 0.1516 0.1982 -0.0251 0.0113  -0.0219 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1741 0.1380 0.1931 -0.0215 0.0168  -0.0230 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.1991 0.1613 0.2118 -0.0248 0.0192  -0.0268 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1799 0.1401 0.2096 -0.0145 0.0205  -0.0193 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1905 0.1470 0.2105 -0.0196 0.0253  -0.0266 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1836 0.1396 0.2149 -0.0131 0.0255  -0.0210 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.1942 0.1552 0.2327 -0.0102 0.0199  -0.0140 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2138 0.1674 0.2576 -0.0068 0.0294  -0.0162 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2015 0.1611 0.2504 -0.0049 0.0227  -0.0086 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2069 0.1627 0.2598 -0.0031 0.0276  -0.0093 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1648 0.1548 0.1863 -0.0266 -0.0033 -0.0133 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1690 0.1640 0.1950 -0.0284 -0.0058 -0.0114 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1810 0.1818 0.2167 -0.0224 -0.0082 -0.0069 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1983 0.2025 0.2397 -0.0226 -0.0088 -0.0056 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1966 0.1990 0.2185 -0.0371 -0.0103 -0.0105 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1761 0.1776 0.2137 -0.0176 -0.0086 -0.0052 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1685 0.1739 0.2147 -0.0130 -0.0085 -0.0026 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1634 0.1642 0.2070 -0.0092 -0.0053 -0.0037 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1639 0.1665 0.2102 -0.0066 -0.0049 -0.0028 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1837 0.1961 0.2367 -0.0125 -0.0120 0.0016  30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2051 0.2250 0.2632 -0.0171 -0.0161 0.0051  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2382 0.2619 0.3060 -0.0165 -0.0154 0.0067  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2042 0.2270 0.2554 -0.0230 -0.0200 0.0063  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1739 0.1693 0.2135 -0.0093 -0.0030 -0.0049 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1536 0.1467 0.1920 -0.0066 -0.0010 -0.0038 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1678 0.1643 0.2082 -0.0064 -0.0001 -0.0022 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1898 0.1875 0.2320 -0.0084 0.0007  -0.0021 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1664 0.1534 0.2044 -0.0070 0.0018  -0.0037 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1825 0.1685 0.2228 -0.0042 0.0034  -0.0001 31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1742 0.1598 0.2119 -0.0024 0.0033  -0.0010 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2116 0.1917 0.2572 -0.0040 0.0073  0.0017  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1529 0.1511 0.1918 -0.0053 0.0002  -0.0012 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1645 0.1663 0.2024 -0.0078 0.0018  -0.0003 32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1590 0.1617 0.1952 -0.0083 0.0012  0.0047  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1821 0.1881 0.2178 -0.0119 0.0012  0.0081  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1609 0.1646 0.1987 -0.0079 0.0034  -0.0027 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1904 0.1978 0.2241 -0.0132 0.0060  -0.0028 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1754 0.1794 0.2202 -0.0070 0.0044  -0.0052 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1598 0.1607 0.1961 -0.0053 0.0005  0.0063  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1577 0.1611 0.1962 -0.0053 0.0000  0.0128  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1614 0.1605 0.2030 -0.0011 0.0009  0.0129  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1531 0.1499 0.1911 0.0003  0.0010  0.0082  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1746 0.1853 0.2082 -0.0095 -0.0010 0.0147  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1843 0.2007 0.2205 -0.0105 -0.0028 0.0229  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2080 0.2309 0.2481 -0.0140 -0.0048 0.0320  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1743 0.1920 0.2110 -0.0083 -0.0033 0.0242  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2196 0.2485 0.2642 -0.0139 -0.0068 0.0398  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1943 0.2200 0.2362 -0.0106 -0.0057 0.0345  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1869 0.2006 0.2209 -0.0051 -0.0023 0.0186  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2065 0.2365 0.2510 -0.0096 -0.0067 0.0387  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2018 0.2188 0.2364 -0.0045 -0.0031 0.0218  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2073 0.2322 0.2476 -0.0064 -0.0051 0.0315  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1578 0.1558 0.2072 0.0006  0.0023  0.0185  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1642 0.1579 0.2180 0.0041  0.0050  0.0180  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1751 0.1729 0.2403 0.0055  0.0056  0.0277  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1775 0.1788 0.2497 0.0042  0.0046  0.0353  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1958 0.1800 0.2506 0.0048  0.0094  0.0118  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2052 0.1854 0.2669 0.0041  0.0121  0.0137  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2082 0.1855 0.2853 0.0068  0.0169  0.0205  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2135 0.1904 0.2986 0.0064  0.0177  0.0258  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1938 0.1688 0.2772 0.0094  0.0207  0.0209  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1641 0.1619 0.2334 0.0081  0.0072  0.0289  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1606 0.1636 0.2447 0.0100  0.0079  0.0399  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1551 0.1519 0.2469 0.0141  0.0139  0.0372  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1691 0.1669 0.2538 0.0143  0.0131  0.0333  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1763 0.1924 0.2558 0.0060  0.0015  0.0470  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2136 0.2392 0.3085 0.0063  0.0000  0.0611  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2394 0.2612 0.3486 0.0114  0.0048  0.0635  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2624 0.3005 0.3551 0.0004  -0.0058 0.0699  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1636 0.1531 0.2704 0.0170  0.0210  0.0386  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1672 0.1488 0.2832 0.0200  0.0297  0.0346  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.1815 0.1631 0.2966 0.0199  0.0295  0.0342  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1750 0.1651 0.3021 0.0226  0.0286  0.0435  36  SER   A C   
248  O O   . SER   A 30  ? 0.1848 0.1720 0.3091 0.0235  0.0322  0.0376  36  SER   A O   
249  C CB  A SER   A 30  ? 0.1781 0.1499 0.3116 0.0220  0.0392  0.0353  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2317 0.2022 0.3616 0.0214  0.0394  0.0327  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.1756 0.1394 0.3202 0.0242  0.0497  0.0311  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2984 0.2743 0.4478 0.0238  0.0386  0.0466  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1794 0.1816 0.3173 0.0226  0.0230  0.0578  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1780 0.1911 0.3273 0.0240  0.0209  0.0682  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1690 0.1869 0.2995 0.0212  0.0157  0.0625  37  SER   A C   
256  O O   . SER   A 31  ? 0.1805 0.2030 0.3179 0.0227  0.0166  0.0659  37  SER   A O   
257  C CB  . SER   A 31  ? 0.1954 0.2235 0.3582 0.0220  0.0141  0.0864  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2589 0.2971 0.4028 0.0150  0.0045  0.0878  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1506 0.1668 0.2592 0.0173  0.0114  0.0534  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1535 0.1726 0.2448 0.0145  0.0074  0.0473  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1544 0.1623 0.2348 0.0158  0.0114  0.0340  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1504 0.1597 0.2187 0.0141  0.0089  0.0293  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1590 0.1845 0.2360 0.0086  0.0008  0.0472  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1834 0.2230 0.2663 0.0039  -0.0044 0.0604  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1824 0.2270 0.2499 -0.0037 -0.0087 0.0581  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1553 0.2007 0.2084 -0.0072 -0.0095 0.0507  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1667 0.2195 0.2080 -0.0159 -0.0120 0.0503  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1949 0.2565 0.2352 -0.0231 -0.0151 0.0572  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1722 0.2239 0.2028 -0.0187 -0.0110 0.0431  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1516 0.1491 0.2345 0.0173  0.0172  0.0280  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1485 0.1373 0.2190 0.0158  0.0198  0.0164  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1442 0.1349 0.1988 0.0128  0.0135  0.0121  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1553 0.1439 0.1999 0.0113  0.0127  0.0062  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1621 0.1485 0.2318 0.0164  0.0239  0.0124  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1683 0.1469 0.2247 0.0127  0.0265  0.0015  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.1765 0.1483 0.2310 0.0103  0.0301  -0.0037 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1899 0.1697 0.2378 0.0113  0.0253  -0.0015 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1454 0.1399 0.1993 0.0116  0.0097  0.0154  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1411 0.1370 0.1837 0.0090  0.0055  0.0115  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1395 0.1319 0.1812 0.0077  0.0056  0.0090  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1502 0.1421 0.1992 0.0081  0.0070  0.0127  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1440 0.1485 0.1847 0.0067  0.0016  0.0163  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1632 0.1720 0.2007 0.0062  0.0005  0.0171  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1734 0.1906 0.2068 0.0012  -0.0023 0.0206  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1757 0.1800 0.2059 0.0068  0.0009  0.0104  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1380 0.1293 0.1723 0.0061  0.0037  0.0040  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1349 0.1250 0.1684 0.0044  0.0029  0.0023  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1346 0.1281 0.1642 0.0032  0.0000  0.0007  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1416 0.1356 0.1684 0.0035  -0.0011 -0.0007 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1449 0.1288 0.1770 0.0028  0.0055  -0.0023 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1508 0.1338 0.1821 0.0003  0.0046  -0.0041 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1805 0.1565 0.2128 -0.0021 0.0095  -0.0075 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1594 0.1459 0.1861 -0.0020 0.0007  -0.0058 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1358 0.1314 0.1668 0.0018  -0.0006 0.0010  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1299 0.1280 0.1612 0.0008  -0.0012 -0.0007 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1397 0.1374 0.1738 -0.0003 -0.0018 -0.0018 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1432 0.1402 0.1780 -0.0014 -0.0010 -0.0013 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1379 0.1395 0.1684 -0.0016 0.0004  0.0000  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1545 0.1569 0.1881 -0.0028 0.0025  -0.0031 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1529 0.1565 0.1803 -0.0017 0.0003  0.0018  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1360 0.1350 0.1728 -0.0003 -0.0033 -0.0023 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1311 0.1320 0.1724 -0.0018 -0.0045 -0.0021 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1423 0.1466 0.1927 -0.0011 -0.0032 -0.0013 43  SER   A C   
304  O O   . SER   A 37  ? 0.1462 0.1503 0.1987 0.0002  -0.0011 -0.0015 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1532 0.1546 0.1919 -0.0041 -0.0077 -0.0014 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1582 0.1618 0.1973 -0.0037 -0.0099 0.0006  43  SER   A OG  
307  N N   . SER   A 38  ? 0.1497 0.1566 0.2068 -0.0023 -0.0031 -0.0008 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1637 0.1735 0.2336 -0.0014 -0.0001 0.0000  44  SER   A CA  
309  C C   . SER   A 38  ? 0.1907 0.2054 0.2707 -0.0004 -0.0039 0.0057  44  SER   A C   
310  O O   . SER   A 38  ? 0.2135 0.2313 0.2896 -0.0027 -0.0096 0.0088  44  SER   A O   
311  C CB  . SER   A 38  ? 0.1899 0.2008 0.2641 -0.0032 0.0025  -0.0016 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2252 0.2389 0.2990 -0.0047 -0.0023 0.0009  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1890 0.2049 0.2831 0.0019  -0.0003 0.0077  45  THR   A N   
314  C CA  . THR   A 39  ? 0.2083 0.2304 0.3162 0.0030  -0.0040 0.0158  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2211 0.2473 0.3515 0.0045  0.0002  0.0192  45  THR   A C   
316  O O   . THR   A 39  ? 0.2067 0.2284 0.3418 0.0051  0.0087  0.0132  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2122 0.2318 0.3218 0.0052  -0.0028 0.0171  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2226 0.2369 0.3393 0.0070  0.0064  0.0122  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2284 0.2443 0.3183 0.0040  -0.0060 0.0141  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2266 0.2619 0.3717 0.0044  -0.0054 0.0293  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2487 0.2892 0.4204 0.0067  -0.0014 0.0349  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2485 0.2854 0.4383 0.0110  0.0061  0.0366  46  THR   A C   
323  O O   . THR   A 40  ? 0.2795 0.3124 0.4853 0.0131  0.0169  0.0327  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2973 0.3512 0.4788 0.0037  -0.0111 0.0470  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3552 0.4146 0.5345 0.0020  -0.0190 0.0554  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.3154 0.3709 0.4787 -0.0015 -0.0162 0.0432  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2552 0.2925 0.4422 0.0117  0.0018  0.0415  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2598 0.2926 0.4638 0.0156  0.0094  0.0430  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2477 0.2681 0.4348 0.0153  0.0175  0.0301  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2476 0.2654 0.4090 0.0127  0.0131  0.0244  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2882 0.3281 0.4992 0.0159  0.0010  0.0556  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2265 0.2400 0.4288 0.0172  0.0295  0.0264  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2373 0.2405 0.4235 0.0149  0.0373  0.0146  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2347 0.2368 0.4140 0.0159  0.0326  0.0183  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2330 0.2391 0.4299 0.0190  0.0295  0.0290  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2626 0.2580 0.4664 0.0144  0.0538  0.0074  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3437 0.3387 0.5494 0.0115  0.0604  0.0006  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4544 0.4405 0.6752 0.0092  0.0785  -0.0085 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4665 0.4517 0.7189 0.0134  0.0865  -0.0032 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4790 0.4589 0.6785 0.0015  0.0857  -0.0217 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1929 0.1908 0.3469 0.0129  0.0311  0.0107  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.2006 0.1973 0.3452 0.0133  0.0269  0.0129  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1953 0.1838 0.3448 0.0125  0.0375  0.0074  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.2039 0.1865 0.3582 0.0098  0.0493  -0.0011 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1783 0.1661 0.3231 0.0133  0.0337  0.0108  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1923 0.1724 0.3427 0.0124  0.0434  0.0066  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1815 0.1582 0.3078 0.0078  0.0438  -0.0017 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1961 0.1663 0.3249 0.0056  0.0523  -0.0062 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.2078 0.1895 0.3770 0.0166  0.0409  0.0180  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2442 0.2311 0.4494 0.0216  0.0420  0.0305  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1707 0.1521 0.2763 0.0065  0.0348  -0.0023 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1773 0.1574 0.2629 0.0023  0.0347  -0.0081 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1957 0.1731 0.2741 -0.0045 0.0434  -0.0178 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2173 0.1956 0.2981 -0.0058 0.0458  -0.0202 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1657 0.1515 0.2356 0.0032  0.0238  -0.0050 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1706 0.1595 0.2429 0.0069  0.0158  0.0030  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1837 0.1705 0.2622 0.0078  0.0172  0.0059  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1848 0.1781 0.2523 0.0078  0.0087  0.0063  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2112 0.1864 0.2789 -0.0100 0.0476  -0.0232 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2381 0.2128 0.2937 -0.0199 0.0549  -0.0321 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2177 0.1996 0.2533 -0.0233 0.0463  -0.0303 52  THR   A C   
362  O O   . THR   A 46  ? 0.2189 0.2022 0.2512 -0.0201 0.0407  -0.0262 52  THR   A O   
363  C CB  . THR   A 46  ? 0.3252 0.2921 0.3854 -0.0257 0.0678  -0.0396 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3737 0.3339 0.4564 -0.0225 0.0774  -0.0410 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3766 0.3448 0.4189 -0.0391 0.0741  -0.0487 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.2076 0.1948 0.2319 -0.0300 0.0456  -0.0324 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1928 0.1882 0.2026 -0.0333 0.0378  -0.0285 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.2063 0.2041 0.2046 -0.0446 0.0426  -0.0331 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2209 0.2167 0.2154 -0.0547 0.0519  -0.0409 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1909 0.1928 0.1961 -0.0347 0.0328  -0.0254 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.2014 0.2007 0.2173 -0.0253 0.0293  -0.0221 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1869 0.1982 0.1826 -0.0367 0.0245  -0.0185 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2007 0.1993 0.2209 -0.0157 0.0217  -0.0160 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1945 0.1969 0.1865 -0.0446 0.0371  -0.0290 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.2007 0.2082 0.1804 -0.0563 0.0396  -0.0315 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.2019 0.2208 0.1702 -0.0669 0.0365  -0.0290 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.2018 0.2270 0.1718 -0.0624 0.0283  -0.0212 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.2028 0.2145 0.1808 -0.0520 0.0325  -0.0253 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2307 0.2523 0.1871 -0.0827 0.0436  -0.0357 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2496 0.2846 0.1931 -0.0962 0.0400  -0.0321 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2771 0.3210 0.2079 -0.1091 0.0395  -0.0314 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.3018 0.3427 0.2226 -0.1232 0.0498  -0.0419 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2741 0.3055 0.2132 -0.1062 0.0496  -0.0412 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2657 0.2885 0.2189 -0.0934 0.0506  -0.0419 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2458 0.2754 0.2040 -0.0839 0.0386  -0.0304 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2347 0.2561 0.2052 -0.0733 0.0402  -0.0320 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2399 0.2630 0.2175 -0.0626 0.0317  -0.0239 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2156 0.2474 0.1911 -0.0607 0.0221  -0.0139 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2620 0.2782 0.2501 -0.0543 0.0332  -0.0257 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2653 0.3202 0.1976 -0.1048 0.0282  -0.0193 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2548 0.3187 0.1793 -0.1132 0.0257  -0.0162 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2551 0.3333 0.1856 -0.1078 0.0129  -0.0004 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2828 0.3620 0.2244 -0.0963 0.0068  0.0076  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2614 0.3114 0.1910 -0.1056 0.0321  -0.0240 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2511 0.2949 0.1979 -0.0829 0.0248  -0.0167 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2836 0.3722 0.2087 -0.1155 0.0098  0.0041  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3155 0.4172 0.2502 -0.1095 -0.0008 0.0192  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3064 0.4018 0.2453 -0.1017 0.0006  0.0167  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3088 0.4166 0.2509 -0.1032 -0.0054 0.0263  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3759 0.5008 0.3033 -0.1265 -0.0081 0.0312  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.4709 0.6016 0.3810 -0.1451 -0.0040 0.0251  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.4925 0.6075 0.3968 -0.1448 0.0059  0.0103  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5284 0.6801 0.4310 -0.1613 -0.0106 0.0355  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2628 0.3395 0.2038 -0.0927 0.0081  0.0050  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2395 0.3101 0.1848 -0.0849 0.0089  0.0035  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2383 0.3149 0.1964 -0.0730 0.0010  0.0149  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2307 0.3073 0.1980 -0.0647 -0.0024 0.0200  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2578 0.3092 0.2072 -0.0757 0.0163  -0.0068 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2855 0.3259 0.2255 -0.0877 0.0294  -0.0214 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2065 0.2867 0.1661 -0.0722 -0.0004 0.0175  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.2005 0.2843 0.1731 -0.0612 -0.0051 0.0260  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1757 0.2481 0.1490 -0.0540 -0.0016 0.0198  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.1825 0.2578 0.1642 -0.0474 -0.0039 0.0249  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2434 0.3470 0.2209 -0.0675 -0.0116 0.0390  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.2621 0.3789 0.2455 -0.0712 -0.0172 0.0503  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.3251 0.4627 0.3194 -0.0753 -0.0241 0.0663  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3442 0.4984 0.3312 -0.0903 -0.0283 0.0731  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.2799 0.4180 0.2924 -0.0633 -0.0250 0.0731  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.1740 0.2332 0.1401 -0.0552 0.0046  0.0091  60  THR   A N   
420  C CA  . THR   A 54  ? 0.1803 0.2282 0.1487 -0.0476 0.0074  0.0046  60  THR   A CA  
421  C C   . THR   A 54  ? 0.1724 0.2061 0.1427 -0.0422 0.0116  -0.0021 60  THR   A C   
422  O O   . THR   A 54  ? 0.1972 0.2282 0.1643 -0.0474 0.0154  -0.0066 60  THR   A O   
423  C CB  . THR   A 54  ? 0.2223 0.2700 0.1838 -0.0548 0.0106  0.0010  60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.3145 0.3569 0.2680 -0.0642 0.0171  -0.0070 60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.2134 0.2767 0.1734 -0.0615 0.0062  0.0083  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.1588 0.1851 0.1348 -0.0327 0.0109  -0.0019 61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.1621 0.1775 0.1423 -0.0275 0.0135  -0.0056 61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.1397 0.1501 0.1241 -0.0197 0.0115  -0.0037 61  GLY   A C   
429  O O   . GLY   A 55  ? 0.1474 0.1601 0.1301 -0.0196 0.0103  -0.0021 61  GLY   A O   
430  N N   . VAL   A 56  ? 0.1366 0.1409 0.1262 -0.0145 0.0110  -0.0038 62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.1273 0.1280 0.1193 -0.0096 0.0088  -0.0016 62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.1251 0.1256 0.1200 -0.0054 0.0057  0.0000  62  VAL   A C   
433  O O   . VAL   A 56  ? 0.1392 0.1385 0.1372 -0.0051 0.0065  -0.0010 62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.1545 0.1477 0.1516 -0.0097 0.0119  -0.0022 62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.1811 0.1724 0.1812 -0.0062 0.0084  0.0022  62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.1661 0.1579 0.1602 -0.0146 0.0162  -0.0047 62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1273 0.1288 0.1206 -0.0032 0.0032  0.0017  63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1295 0.1302 0.1243 -0.0008 0.0012  0.0023  63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.1359 0.1347 0.1291 -0.0011 -0.0011 0.0040  63  TYR   A C   
440  O O   . TYR   A 57  ? 0.1483 0.1471 0.1383 -0.0027 -0.0013 0.0050  63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.1332 0.1373 0.1281 0.0004  0.0016  0.0021  63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.1328 0.1374 0.1256 0.0003  0.0027  0.0017  63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.1403 0.1479 0.1322 -0.0007 0.0040  0.0023  63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.1423 0.1443 0.1335 0.0001  0.0035  0.0000  63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.1539 0.1617 0.1447 -0.0011 0.0064  0.0012  63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.1558 0.1575 0.1448 -0.0014 0.0066  -0.0020 63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.1654 0.1699 0.1550 -0.0015 0.0083  -0.0013 63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.1949 0.1988 0.1832 -0.0033 0.0125  -0.0038 63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.1309 0.1290 0.1257 -0.0007 -0.0032 0.0050  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.1354 0.1341 0.1273 -0.0035 -0.0063 0.0078  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.1418 0.1411 0.1265 -0.0059 -0.0053 0.0045  64  TYR   A C   
452  O O   . TYR   A 58  ? 0.1433 0.1417 0.1289 -0.0048 -0.0036 0.0017  64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.1516 0.1509 0.1501 -0.0032 -0.0094 0.0116  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.1585 0.1612 0.1540 -0.0080 -0.0140 0.0167  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.1650 0.1691 0.1606 -0.0102 -0.0159 0.0215  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.1642 0.1695 0.1554 -0.0118 -0.0166 0.0167  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.1814 0.1907 0.1730 -0.0165 -0.0211 0.0276  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.1834 0.1938 0.1692 -0.0190 -0.0213 0.0217  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.1822 0.1953 0.1685 -0.0215 -0.0240 0.0278  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2247 0.2449 0.2048 -0.0304 -0.0297 0.0344  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.1492 0.1493 0.1271 -0.0102 -0.0056 0.0047  65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.1511 0.1507 0.1212 -0.0147 -0.0024 0.0002  65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.1656 0.1678 0.1279 -0.0225 -0.0063 0.0026  65  CYS   A C   
464  O O   . CYS   A 59  ? 0.1730 0.1780 0.1308 -0.0269 -0.0091 0.0065  65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.1527 0.1521 0.1202 -0.0150 0.0014  -0.0020 65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.1823 0.1799 0.1420 -0.0214 0.0083  -0.0091 65  CYS   A SG  
467  N N   . SER   A 60  ? 0.1669 0.1693 0.1274 -0.0254 -0.0067 0.0010  66  SER   A N   
468  C CA  . SER   A 60  ? 0.1846 0.1917 0.1371 -0.0348 -0.0114 0.0045  66  SER   A CA  
469  C C   . SER   A 60  ? 0.1866 0.1947 0.1254 -0.0450 -0.0086 0.0006  66  SER   A C   
470  O O   . SER   A 60  ? 0.2150 0.2294 0.1464 -0.0538 -0.0142 0.0065  66  SER   A O   
471  C CB  . SER   A 60  ? 0.2060 0.2135 0.1588 -0.0369 -0.0123 0.0033  66  SER   A CB  
472  O OG  . SER   A 60  ? 0.2422 0.2445 0.1897 -0.0394 -0.0047 -0.0062 66  SER   A OG  
473  N N   . SER   A 61  ? 0.1820 0.1844 0.1183 -0.0443 0.0004  -0.0084 67  SER   A N   
474  C CA  . SER   A 61  ? 0.1978 0.1997 0.1216 -0.0543 0.0057  -0.0140 67  SER   A CA  
475  C C   . SER   A 61  ? 0.2018 0.2066 0.1230 -0.0551 0.0035  -0.0101 67  SER   A C   
476  O O   . SER   A 61  ? 0.2142 0.2197 0.1240 -0.0646 0.0071  -0.0139 67  SER   A O   
477  C CB  . SER   A 61  ? 0.2104 0.2048 0.1364 -0.0531 0.0177  -0.0247 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.2032 0.1953 0.1418 -0.0421 0.0207  -0.0243 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.1969 0.2034 0.1278 -0.0467 -0.0024 -0.0023 68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.1924 0.2017 0.1219 -0.0477 -0.0055 0.0030  68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.2116 0.2257 0.1475 -0.0467 -0.0148 0.0147  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.2099 0.2259 0.1473 -0.0470 -0.0174 0.0205  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.1964 0.2019 0.1341 -0.0385 -0.0008 0.0000  68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.2130 0.2150 0.1487 -0.0391 0.0088  -0.0091 68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.2193 0.2226 0.1436 -0.0483 0.0118  -0.0117 68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2421 0.2416 0.1679 -0.0486 0.0229  -0.0209 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.2396 0.2356 0.1602 -0.0553 0.0307  -0.0290 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.2621 0.2590 0.1731 -0.0635 0.0278  -0.0295 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.2700 0.2619 0.1957 -0.0551 0.0424  -0.0369 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.2180 0.2338 0.1609 -0.0445 -0.0188 0.0187  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.2139 0.2333 0.1694 -0.0411 -0.0257 0.0301  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.2397 0.2546 0.2056 -0.0326 -0.0234 0.0313  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.2688 0.2858 0.2417 -0.0328 -0.0269 0.0402  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.2465 0.2752 0.1986 -0.0512 -0.0337 0.0415  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.2535 0.2883 0.1985 -0.0598 -0.0372 0.0424  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.2877 0.3345 0.2341 -0.0692 -0.0471 0.0577  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.3299 0.3846 0.2642 -0.0818 -0.0508 0.0582  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.3147 0.3752 0.2289 -0.0976 -0.0515 0.0562  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.3030 0.3621 0.2075 -0.1018 -0.0489 0.0539  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.3242 0.3915 0.2268 -0.1102 -0.0540 0.0555  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.1982 0.2074 0.1656 -0.0260 -0.0175 0.0231  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.2060 0.2116 0.1799 -0.0206 -0.0147 0.0229  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.1938 0.1957 0.1738 -0.0140 -0.0108 0.0176  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.1866 0.1882 0.1638 -0.0130 -0.0087 0.0124  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.2479 0.2532 0.2124 -0.0234 -0.0114 0.0185  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.3682 0.3767 0.3277 -0.0299 -0.0150 0.0250  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.4826 0.4899 0.4368 -0.0309 -0.0113 0.0215  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.5723 0.5834 0.5202 -0.0385 -0.0150 0.0280  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.6329 0.6489 0.5687 -0.0483 -0.0174 0.0281  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.1698 0.1689 0.1581 -0.0105 -0.0089 0.0188  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.1581 0.1548 0.1498 -0.0067 -0.0048 0.0137  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.1757 0.1725 0.1624 -0.0075 -0.0016 0.0104  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.2182 0.2140 0.2045 -0.0093 -0.0013 0.0124  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.1508 0.1439 0.1540 -0.0046 -0.0028 0.0158  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.1677 0.1615 0.1790 -0.0032 -0.0054 0.0197  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2122 0.2052 0.2270 -0.0010 -0.0037 0.0165  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.1638 0.1605 0.1809 -0.0045 -0.0101 0.0279  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.1740 0.1689 0.1975 -0.0005 -0.0068 0.0222  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.1989 0.1967 0.2241 -0.0027 -0.0110 0.0296  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.1594 0.1583 0.1438 -0.0065 0.0004  0.0063  72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.1517 0.1531 0.1330 -0.0077 0.0027  0.0045  72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.1503 0.1534 0.1340 -0.0080 0.0047  0.0029  72  TYR   A C   
523  O O   . TYR   A 66  ? 0.1469 0.1515 0.1330 -0.0066 0.0045  0.0024  72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.1590 0.1637 0.1382 -0.0072 0.0038  0.0029  72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.1832 0.1870 0.1569 -0.0098 0.0036  0.0026  72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.2046 0.2088 0.1737 -0.0128 0.0041  0.0031  72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.1842 0.1867 0.1558 -0.0108 0.0031  0.0014  72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.2109 0.2150 0.1730 -0.0172 0.0043  0.0025  72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.2000 0.2024 0.1640 -0.0160 0.0036  0.0002  72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2100 0.2133 0.1688 -0.0194 0.0041  0.0008  72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.2464 0.2502 0.1957 -0.0266 0.0050  -0.0007 72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.1518 0.1559 0.1337 -0.0110 0.0067  0.0022  73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.1499 0.1582 0.1313 -0.0143 0.0084  0.0008  73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.1606 0.1777 0.1427 -0.0140 0.0069  0.0031  73  PRO   A C   
535  O O   . PRO   A 67  ? 0.1814 0.2010 0.1636 -0.0131 0.0068  0.0044  73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.1842 0.1904 0.1626 -0.0190 0.0115  -0.0009 73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.2055 0.2096 0.1829 -0.0172 0.0103  0.0010  73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.1660 0.1678 0.1456 -0.0129 0.0073  0.0031  73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.1376 0.1598 0.1216 -0.0154 0.0062  0.0042  74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.1492 0.1811 0.1385 -0.0147 0.0046  0.0091  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.1469 0.1879 0.1353 -0.0210 0.0033  0.0119  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.1550 0.1939 0.1390 -0.0250 0.0041  0.0091  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.1747 0.2046 0.1703 -0.0089 0.0041  0.0102  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.1969 0.2208 0.1924 -0.0053 0.0058  0.0079  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.1932 0.2186 0.1875 -0.0085 0.0035  0.0082  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.1465 0.1992 0.1408 -0.0225 0.0013  0.0186  75  SER   A N   
547  C CA  . SER   A 69  ? 0.1500 0.2155 0.1465 -0.0285 -0.0018 0.0252  75  SER   A CA  
548  C C   . SER   A 69  ? 0.1335 0.2017 0.1421 -0.0224 -0.0033 0.0310  75  SER   A C   
549  O O   . SER   A 69  ? 0.1466 0.2117 0.1645 -0.0151 -0.0014 0.0320  75  SER   A O   
550  C CB  . SER   A 69  ? 0.1887 0.2673 0.1884 -0.0333 -0.0037 0.0318  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.2906 0.3660 0.2788 -0.0397 -0.0017 0.0258  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1414 0.2144 0.1500 -0.0259 -0.0056 0.0343  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1415 0.2159 0.1622 -0.0201 -0.0066 0.0398  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1392 0.2292 0.1651 -0.0267 -0.0113 0.0507  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1601 0.2578 0.1754 -0.0374 -0.0137 0.0513  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1504 0.2110 0.1663 -0.0157 -0.0044 0.0318  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1510 0.2083 0.1546 -0.0220 -0.0041 0.0259  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1551 0.2033 0.1495 -0.0235 -0.0010 0.0175  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1453 0.2077 0.1481 -0.0265 -0.0060 0.0288  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1672 0.2113 0.1537 -0.0291 0.0014  0.0117  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1698 0.2282 0.1618 -0.0331 -0.0038 0.0221  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1687 0.2178 0.1537 -0.0342 0.0005  0.0134  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1360 0.2310 0.1788 -0.0214 -0.0123 0.0599  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1467 0.2586 0.1984 -0.0273 -0.0178 0.0737  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1605 0.2714 0.2030 -0.0323 -0.0197 0.0720  77  SER   A C   
566  O O   . SER   A 71  ? 0.1575 0.2537 0.1914 -0.0287 -0.0161 0.0609  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1686 0.2858 0.2463 -0.0190 -0.0170 0.0853  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1789 0.2818 0.2626 -0.0098 -0.0120 0.0798  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1587 0.2863 0.2028 -0.0419 -0.0255 0.0836  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1647 0.2926 0.2007 -0.0477 -0.0271 0.0830  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1710 0.2921 0.2223 -0.0371 -0.0259 0.0864  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1814 0.3049 0.2534 -0.0288 -0.0253 0.0951  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.1833 0.3331 0.2162 -0.0629 -0.0342 0.0959  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.2259 0.3813 0.2405 -0.0759 -0.0343 0.0904  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.2937 0.4703 0.2988 -0.0951 -0.0407 0.1004  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.3737 0.5526 0.3580 -0.1091 -0.0384 0.0913  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4408 0.6356 0.4080 -0.1310 -0.0418 0.0948  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1640 0.2774 0.2075 -0.0377 -0.0247 0.0804  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1663 0.2725 0.2235 -0.0283 -0.0230 0.0828  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.1729 0.2940 0.2517 -0.0281 -0.0273 0.1017  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.1989 0.3374 0.2763 -0.0391 -0.0339 0.1134  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.1976 0.2971 0.2402 -0.0327 -0.0223 0.0744  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2379 0.3341 0.2611 -0.0400 -0.0204 0.0632  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.1954 0.3046 0.2175 -0.0470 -0.0233 0.0695  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1695 0.2841 0.2689 -0.0166 -0.0231 0.1048  80  SER   A N   
586  C CA  . SER   A 74  ? 0.1838 0.3112 0.3104 -0.0141 -0.0252 0.1235  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1618 0.2757 0.3069 -0.0027 -0.0180 0.1224  80  SER   A C   
588  O O   . SER   A 74  ? 0.1536 0.2493 0.2897 0.0029  -0.0117 0.1069  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2429 0.3799 0.3834 -0.0126 -0.0251 0.1313  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.3658 0.5120 0.4874 -0.0228 -0.0299 0.1290  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.1697 0.2938 0.3442 0.0005  -0.0184 0.1404  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.1939 0.3064 0.3913 0.0107  -0.0101 0.1415  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.2022 0.3108 0.4194 0.0185  -0.0019 0.1412  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2234 0.3481 0.4611 0.0180  -0.0046 0.1572  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.2052 0.3322 0.4261 0.0089  -0.0150 0.1633  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2455 0.3605 0.4911 0.0182  -0.0062 0.1655  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2631 0.3609 0.4885 0.0186  -0.0031 0.1493  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2436 0.3764 0.5187 0.0166  -0.0116 0.1916  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.1918 0.2809 0.4022 0.0244  0.0079  0.1237  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.2022 0.2848 0.4254 0.0303  0.0174  0.1189  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2177 0.2829 0.4580 0.0378  0.0311  0.1119  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2020 0.2535 0.4288 0.0378  0.0340  0.1003  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2474 0.3219 0.4402 0.0273  0.0169  0.1014  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2984 0.3875 0.4720 0.0188  0.0053  0.1052  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2621 0.3277 0.4623 0.0320  0.0273  0.0930  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.3490 0.4542 0.5353 0.0170  0.0025  0.1168  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2105 0.2756 0.4810 0.0437  0.0408  0.1179  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2208 0.2679 0.5077 0.0494  0.0568  0.1090  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2522 0.2837 0.5150 0.0477  0.0640  0.0871  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.2812 0.3170 0.5348 0.0461  0.0623  0.0838  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2212 0.2736 0.5514 0.0559  0.0666  0.1229  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2680 0.3017 0.6196 0.0610  0.0841  0.1158  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.2950 0.3250 0.6580 0.0626  0.0848  0.1219  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3193 0.3382 0.6772 0.0630  0.1008  0.1014  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.3289 0.3404 0.7115 0.0664  0.1025  0.1143  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3344 0.3351 0.7113 0.0659  0.1190  0.0933  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.3389 0.3357 0.7291 0.0679  0.1200  0.0999  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2401 0.2550 0.4881 0.0463  0.0698  0.0723  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2328 0.2340 0.4557 0.0426  0.0755  0.0523  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.2292 0.2139 0.4681 0.0441  0.0939  0.0427  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.2323 0.2103 0.4849 0.0459  0.0994  0.0447  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.2171 0.2145 0.4069 0.0374  0.0660  0.0432  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2298 0.2151 0.3952 0.0325  0.0710  0.0249  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2216 0.2343 0.3973 0.0351  0.0501  0.0518  84  VAL   A CG2 
625  N N   A GLU   A 79  ? 0.2326 0.2096 0.4662 0.0417  0.1038  0.0306  85  GLU   A N   
626  N N   B GLU   A 79  ? 0.2380 0.2151 0.4733 0.0420  0.1043  0.0311  85  GLU   A N   
627  C CA  A GLU   A 79  ? 0.2504 0.2106 0.4958 0.0405  0.1235  0.0184  85  GLU   A CA  
628  C CA  B GLU   A 79  ? 0.2594 0.2197 0.5084 0.0412  0.1243  0.0196  85  GLU   A CA  
629  C C   A GLU   A 79  ? 0.2665 0.2130 0.4913 0.0345  0.1267  0.0046  85  GLU   A C   
630  C C   B GLU   A 79  ? 0.2717 0.2181 0.4972 0.0346  0.1271  0.0046  85  GLU   A C   
631  O O   A GLU   A 79  ? 0.2691 0.2184 0.4648 0.0303  0.1138  0.0011  85  GLU   A O   
632  O O   B GLU   A 79  ? 0.2754 0.2249 0.4709 0.0302  0.1141  0.0008  85  GLU   A O   
633  C CB  A GLU   A 79  ? 0.2800 0.2364 0.5181 0.0369  0.1321  0.0074  85  GLU   A CB  
634  C CB  B GLU   A 79  ? 0.3045 0.2606 0.5551 0.0390  0.1358  0.0103  85  GLU   A CB  
635  C CG  A GLU   A 79  ? 0.2907 0.2589 0.5563 0.0431  0.1334  0.0205  85  GLU   A CG  
636  C CG  B GLU   A 79  ? 0.3868 0.3380 0.5990 0.0299  0.1327  -0.0059 85  GLU   A CG  
637  C CD  A GLU   A 79  ? 0.3495 0.3164 0.6600 0.0506  0.1459  0.0317  85  GLU   A CD  
638  C CD  B GLU   A 79  ? 0.4241 0.3888 0.6197 0.0296  0.1182  -0.0007 85  GLU   A CD  
639  O OE1 A GLU   A 79  ? 0.3715 0.3218 0.6947 0.0493  0.1656  0.0201  85  GLU   A OE1 
640  O OE1 B GLU   A 79  ? 0.4717 0.4348 0.6595 0.0259  0.1234  -0.0085 85  GLU   A OE1 
641  O OE2 A GLU   A 79  ? 0.3646 0.3465 0.6971 0.0567  0.1365  0.0520  85  GLU   A OE2 
642  O OE2 B GLU   A 79  ? 0.3764 0.3530 0.5666 0.0322  0.1023  0.0105  85  GLU   A OE2 
643  N N   . ALA   A 80  ? 0.2830 0.2143 0.5237 0.0333  0.1450  -0.0037 86  ALA   A N   
644  C CA  . ALA   A 80  ? 0.3117 0.2295 0.5329 0.0257  0.1500  -0.0182 86  ALA   A CA  
645  C C   . ALA   A 80  ? 0.3443 0.2596 0.5271 0.0151  0.1460  -0.0333 86  ALA   A C   
646  O O   . ALA   A 80  ? 0.3560 0.2726 0.5320 0.0122  0.1491  -0.0386 86  ALA   A O   
647  C CB  . ALA   A 80  ? 0.3352 0.2360 0.5796 0.0243  0.1735  -0.0271 86  ALA   A CB  
648  N N   A SER   A 81  ? 0.3356 0.2489 0.4939 0.0092  0.1381  -0.0389 87  SER   A N   
649  N N   B SER   A 81  ? 0.3570 0.2700 0.5157 0.0092  0.1385  -0.0390 87  SER   A N   
650  C CA  A SER   A 81  ? 0.3362 0.2488 0.4596 -0.0016 0.1329  -0.0508 87  SER   A CA  
651  C CA  B SER   A 81  ? 0.3791 0.2915 0.5030 -0.0016 0.1333  -0.0509 87  SER   A CA  
652  C C   A SER   A 81  ? 0.3573 0.2579 0.4682 -0.0114 0.1408  -0.0633 87  SER   A C   
653  C C   B SER   A 81  ? 0.3793 0.2802 0.4902 -0.0112 0.1401  -0.0629 87  SER   A C   
654  O O   A SER   A 81  ? 0.3580 0.2492 0.4884 -0.0095 0.1525  -0.0644 87  SER   A O   
655  O O   B SER   A 81  ? 0.3820 0.2738 0.5121 -0.0090 0.1512  -0.0635 87  SER   A O   
656  C CB  A SER   A 81  ? 0.3127 0.2390 0.4182 0.0008  0.1117  -0.0419 87  SER   A CB  
657  C CB  B SER   A 81  ? 0.4169 0.3434 0.5235 0.0011  0.1121  -0.0417 87  SER   A CB  
658  O OG  A SER   A 81  ? 0.2432 0.1708 0.3478 0.0029  0.1039  -0.0369 87  SER   A OG  
659  O OG  B SER   A 81  ? 0.4735 0.4010 0.5500 -0.0085 0.1058  -0.0501 87  SER   A OG  
660  N N   . GLU   A 82  ? 0.3806 0.2827 0.4603 -0.0223 0.1337  -0.0715 88  GLU   A N   
661  C CA  . GLU   A 82  ? 0.3841 0.2780 0.4493 -0.0332 0.1384  -0.0820 88  GLU   A CA  
662  C C   . GLU   A 82  ? 0.3433 0.2402 0.4149 -0.0264 0.1287  -0.0728 88  GLU   A C   
663  O O   . GLU   A 82  ? 0.3670 0.2554 0.4373 -0.0320 0.1354  -0.0792 88  GLU   A O   
664  C CB  . GLU   A 82  ? 0.4551 0.3550 0.4866 -0.0460 0.1288  -0.0881 88  GLU   A CB  
665  C CG  . GLU   A 82  ? 0.5678 0.4618 0.5805 -0.0608 0.1331  -0.0993 88  GLU   A CG  
666  C CD  . GLU   A 82  ? 0.7096 0.6135 0.6921 -0.0731 0.1207  -0.1008 88  GLU   A CD  
667  O OE1 . GLU   A 82  ? 0.7465 0.6529 0.7149 -0.0812 0.1145  -0.1021 88  GLU   A OE1 
668  O OE2 . GLU   A 82  ? 0.7218 0.6317 0.6961 -0.0746 0.1168  -0.0996 88  GLU   A OE2 
669  N N   . TYR   A 83  ? 0.3064 0.2154 0.3842 -0.0155 0.1134  -0.0583 89  TYR   A N   
670  C CA  . TYR   A 83  ? 0.2786 0.1926 0.3575 -0.0108 0.1023  -0.0499 89  TYR   A CA  
671  C C   . TYR   A 83  ? 0.2780 0.1929 0.3851 0.0001  0.1038  -0.0379 89  TYR   A C   
672  O O   . TYR   A 83  ? 0.2803 0.1956 0.3901 0.0018  0.0996  -0.0336 89  TYR   A O   
673  C CB  . TYR   A 83  ? 0.2791 0.2064 0.3412 -0.0095 0.0843  -0.0434 89  TYR   A CB  
674  C CG  . TYR   A 83  ? 0.2985 0.2266 0.3351 -0.0206 0.0813  -0.0522 89  TYR   A CG  
675  C CD1 . TYR   A 83  ? 0.3320 0.2584 0.3538 -0.0293 0.0791  -0.0576 89  TYR   A CD1 
676  C CD2 . TYR   A 83  ? 0.3263 0.2574 0.3543 -0.0235 0.0811  -0.0546 89  TYR   A CD2 
677  C CE1 . TYR   A 83  ? 0.3782 0.3089 0.3778 -0.0402 0.0739  -0.0625 89  TYR   A CE1 
678  C CE2 . TYR   A 83  ? 0.3651 0.2987 0.3702 -0.0347 0.0773  -0.0606 89  TYR   A CE2 
679  C CZ  . TYR   A 83  ? 0.3975 0.3314 0.3888 -0.0434 0.0735  -0.0640 89  TYR   A CZ  
680  O OH  . TYR   A 83  ? 0.4429 0.3821 0.4128 -0.0554 0.0682  -0.0672 89  TYR   A OH  
681  N N   . TYR   A 84  ? 0.2842 0.2013 0.4123 0.0071  0.1086  -0.0310 90  TYR   A N   
682  C CA  . TYR   A 84  ? 0.2588 0.1797 0.4160 0.0168  0.1089  -0.0166 90  TYR   A CA  
683  C C   . TYR   A 84  ? 0.2742 0.1886 0.4595 0.0204  0.1252  -0.0161 90  TYR   A C   
684  O O   . TYR   A 84  ? 0.2761 0.1899 0.4571 0.0182  0.1301  -0.0222 90  TYR   A O   
685  C CB  . TYR   A 84  ? 0.2394 0.1774 0.3963 0.0227  0.0923  -0.0020 90  TYR   A CB  
686  C CG  . TYR   A 84  ? 0.2220 0.1670 0.3554 0.0200  0.0772  -0.0013 90  TYR   A CG  
687  C CD1 . TYR   A 84  ? 0.2221 0.1675 0.3579 0.0207  0.0732  0.0033  90  TYR   A CD1 
688  C CD2 . TYR   A 84  ? 0.2098 0.1607 0.3205 0.0168  0.0679  -0.0051 90  TYR   A CD2 
689  C CE1 . TYR   A 84  ? 0.2113 0.1628 0.3278 0.0183  0.0609  0.0034  90  TYR   A CE1 
690  C CE2 . TYR   A 84  ? 0.2037 0.1602 0.2967 0.0146  0.0561  -0.0046 90  TYR   A CE2 
691  C CZ  . TYR   A 84  ? 0.2019 0.1583 0.2978 0.0152  0.0532  -0.0011 90  TYR   A CZ  
692  O OH  . TYR   A 84  ? 0.2055 0.1669 0.2865 0.0132  0.0432  -0.0009 90  TYR   A OH  
693  N N   . PRO   A 85  ? 0.2801 0.1913 0.4961 0.0266  0.1329  -0.0069 91  PRO   A N   
694  C CA  . PRO   A 85  ? 0.2820 0.1900 0.5320 0.0322  0.1474  -0.0021 91  PRO   A CA  
695  C C   . PRO   A 85  ? 0.2763 0.2026 0.5350 0.0388  0.1349  0.0139  91  PRO   A C   
696  O O   . PRO   A 85  ? 0.2711 0.2110 0.5111 0.0388  0.1162  0.0213  91  PRO   A O   
697  C CB  . PRO   A 85  ? 0.2973 0.2000 0.5783 0.0375  0.1549  0.0075  91  PRO   A CB  
698  C CG  . PRO   A 85  ? 0.3107 0.2239 0.5780 0.0381  0.1368  0.0169  91  PRO   A CG  
699  C CD  . PRO   A 85  ? 0.2861 0.1986 0.5108 0.0295  0.1277  0.0022  91  PRO   A CD  
700  N N   . ALA   A 86  ? 0.2826 0.2102 0.5706 0.0440  0.1450  0.0202  92  ALA   A N   
701  C CA  . ALA   A 86  ? 0.2796 0.2258 0.5792 0.0495  0.1337  0.0370  92  ALA   A CA  
702  C C   . ALA   A 86  ? 0.2870 0.2463 0.6012 0.0541  0.1210  0.0573  92  ALA   A C   
703  O O   . ALA   A 86  ? 0.3072 0.2601 0.6434 0.0569  0.1283  0.0625  92  ALA   A O   
704  C CB  . ALA   A 86  ? 0.2707 0.2150 0.6058 0.0546  0.1494  0.0410  92  ALA   A CB  
705  N N   . ARG   A 87  ? 0.2827 0.2583 0.5785 0.0527  0.1023  0.0658  93  ARG   A N   
706  C CA  . ARG   A 87  ? 0.2683 0.2569 0.5690 0.0536  0.0891  0.0824  93  ARG   A CA  
707  C C   . ARG   A 87  ? 0.2570 0.2648 0.5421 0.0510  0.0721  0.0915  93  ARG   A C   
708  O O   . ARG   A 87  ? 0.2645 0.2736 0.5319 0.0488  0.0702  0.0831  93  ARG   A O   
709  C CB  . ARG   A 87  ? 0.2738 0.2529 0.5497 0.0492  0.0860  0.0716  93  ARG   A CB  
710  C CG  . ARG   A 87  ? 0.2911 0.2723 0.5263 0.0432  0.0749  0.0594  93  ARG   A CG  
711  C CD  . ARG   A 87  ? 0.3086 0.2774 0.5210 0.0386  0.0763  0.0447  93  ARG   A CD  
712  N NE  . ARG   A 87  ? 0.2838 0.2603 0.4674 0.0345  0.0617  0.0428  93  ARG   A NE  
713  C CZ  . ARG   A 87  ? 0.3371 0.3167 0.4978 0.0313  0.0554  0.0358  93  ARG   A CZ  
714  N NH1 . ARG   A 87  ? 0.3287 0.3074 0.4897 0.0316  0.0601  0.0315  93  ARG   A NH1 
715  N NH2 . ARG   A 87  ? 0.2739 0.2582 0.4131 0.0279  0.0446  0.0340  93  ARG   A NH2 
716  N N   . TYR   A 88  ? 0.2470 0.2693 0.5361 0.0499  0.0600  0.1075  94  TYR   A N   
717  C CA  . TYR   A 88  ? 0.2450 0.2847 0.5155 0.0448  0.0444  0.1145  94  TYR   A CA  
718  C C   . TYR   A 88  ? 0.2285 0.2625 0.4622 0.0392  0.0374  0.1007  94  TYR   A C   
719  O O   . TYR   A 88  ? 0.2423 0.2704 0.4728 0.0384  0.0374  0.0989  94  TYR   A O   
720  C CB  . TYR   A 88  ? 0.2464 0.3056 0.5374 0.0437  0.0350  0.1385  94  TYR   A CB  
721  C CG  . TYR   A 88  ? 0.2463 0.3174 0.5726 0.0481  0.0381  0.1556  94  TYR   A CG  
722  C CD1 . TYR   A 88  ? 0.2637 0.3487 0.5849 0.0452  0.0316  0.1600  94  TYR   A CD1 
723  C CD2 . TYR   A 88  ? 0.2500 0.3171 0.6167 0.0553  0.0492  0.1662  94  TYR   A CD2 
724  C CE1 . TYR   A 88  ? 0.2790 0.3760 0.6339 0.0491  0.0343  0.1761  94  TYR   A CE1 
725  C CE2 . TYR   A 88  ? 0.2561 0.3341 0.6591 0.0600  0.0533  0.1822  94  TYR   A CE2 
726  C CZ  . TYR   A 88  ? 0.2698 0.3635 0.6667 0.0569  0.0454  0.1874  94  TYR   A CZ  
727  O OH  . TYR   A 88  ? 0.2974 0.4036 0.7313 0.0613  0.0488  0.2044  94  TYR   A OH  
728  N N   . GLN   A 89  ? 0.1938 0.2305 0.4017 0.0352  0.0316  0.0918  95  GLN   A N   
729  C CA  . GLN   A 89  ? 0.1785 0.2116 0.3542 0.0300  0.0248  0.0802  95  GLN   A CA  
730  C C   . GLN   A 89  ? 0.1661 0.2167 0.3320 0.0239  0.0125  0.0901  95  GLN   A C   
731  O O   . GLN   A 89  ? 0.1718 0.2340 0.3426 0.0225  0.0092  0.0977  95  GLN   A O   
732  C CB  . GLN   A 89  ? 0.1885 0.2107 0.3446 0.0294  0.0288  0.0631  95  GLN   A CB  
733  C CG  . GLN   A 89  ? 0.2011 0.2205 0.3293 0.0248  0.0223  0.0534  95  GLN   A CG  
734  C CD  . GLN   A 89  ? 0.2001 0.2068 0.3121 0.0241  0.0270  0.0376  95  GLN   A CD  
735  O OE1 . GLN   A 89  ? 0.2053 0.2009 0.3225 0.0255  0.0364  0.0304  95  GLN   A OE1 
736  N NE2 . GLN   A 89  ? 0.1747 0.1829 0.2664 0.0207  0.0207  0.0321  95  GLN   A NE2 
737  N N   . SER   A 90  ? 0.1506 0.2039 0.3031 0.0190  0.0061  0.0903  96  SER   A N   
738  C CA  . SER   A 90  ? 0.1500 0.2191 0.2918 0.0109  -0.0040 0.0984  96  SER   A CA  
739  C C   . SER   A 90  ? 0.1468 0.2119 0.2600 0.0061  -0.0064 0.0841  96  SER   A C   
740  O O   . SER   A 90  ? 0.1496 0.2007 0.2519 0.0092  -0.0020 0.0700  96  SER   A O   
741  C CB  . SER   A 90  ? 0.1776 0.2525 0.3218 0.0069  -0.0084 0.1071  96  SER   A CB  
742  O OG  . SER   A 90  ? 0.2278 0.2889 0.3571 0.0076  -0.0057 0.0934  96  SER   A OG  
743  N N   . HIS   A 91  ? 0.1545 0.2330 0.2578 -0.0021 -0.0131 0.0891  97  HIS   A N   
744  C CA  . HIS   A 91  ? 0.1504 0.2265 0.2299 -0.0079 -0.0145 0.0776  97  HIS   A CA  
745  C C   . HIS   A 91  ? 0.1413 0.2067 0.2162 -0.0024 -0.0098 0.0664  97  HIS   A C   
746  O O   . HIS   A 91  ? 0.1556 0.2120 0.2149 -0.0030 -0.0084 0.0543  97  HIS   A O   
747  C CB  . HIS   A 91  ? 0.1745 0.2432 0.2405 -0.0105 -0.0143 0.0690  97  HIS   A CB  
748  C CG  . HIS   A 91  ? 0.1856 0.2655 0.2527 -0.0179 -0.0190 0.0790  97  HIS   A CG  
749  N ND1 . HIS   A 91  ? 0.2060 0.2958 0.2577 -0.0299 -0.0228 0.0793  97  HIS   A ND1 
750  C CD2 . HIS   A 91  ? 0.2118 0.2942 0.2933 -0.0158 -0.0199 0.0889  97  HIS   A CD2 
751  C CE1 . HIS   A 91  ? 0.2147 0.3138 0.2706 -0.0354 -0.0266 0.0897  97  HIS   A CE1 
752  N NE2 . HIS   A 91  ? 0.2241 0.3193 0.2987 -0.0267 -0.0254 0.0964  97  HIS   A NE2 
753  N N   . LEU   A 92  ? 0.1245 0.1920 0.2130 0.0020  -0.0075 0.0712  98  LEU   A N   
754  C CA  . LEU   A 92  ? 0.1334 0.1912 0.2188 0.0067  -0.0025 0.0616  98  LEU   A CA  
755  C C   . LEU   A 92  ? 0.1330 0.2005 0.2142 0.0024  -0.0055 0.0644  98  LEU   A C   
756  O O   . LEU   A 92  ? 0.1339 0.2160 0.2253 -0.0010 -0.0094 0.0772  98  LEU   A O   
757  C CB  . LEU   A 92  ? 0.1486 0.2004 0.2541 0.0143  0.0047  0.0636  98  LEU   A CB  
758  C CG  . LEU   A 92  ? 0.1757 0.2167 0.2770 0.0176  0.0112  0.0526  98  LEU   A CG  
759  C CD1 . LEU   A 92  ? 0.1750 0.2032 0.2589 0.0172  0.0127  0.0392  98  LEU   A CD1 
760  C CD2 . LEU   A 92  ? 0.2055 0.2417 0.3287 0.0234  0.0204  0.0546  98  LEU   A CD2 
761  N N   . MET   A 93  ? 0.1370 0.1970 0.2039 0.0022  -0.0038 0.0535  99  MET   A N   
762  C CA  . MET   A 93  ? 0.1369 0.2038 0.1979 -0.0020 -0.0057 0.0542  99  MET   A CA  
763  C C   . MET   A 93  ? 0.1362 0.1954 0.2007 0.0036  -0.0005 0.0487  99  MET   A C   
764  O O   . MET   A 93  ? 0.1489 0.1953 0.2078 0.0072  0.0034  0.0393  99  MET   A O   
765  C CB  . MET   A 93  ? 0.1459 0.2093 0.1867 -0.0081 -0.0073 0.0454  99  MET   A CB  
766  C CG  . MET   A 93  ? 0.1584 0.2288 0.1936 -0.0155 -0.0108 0.0488  99  MET   A CG  
767  S SD  . MET   A 93  ? 0.2071 0.2707 0.2223 -0.0226 -0.0093 0.0369  99  MET   A SD  
768  C CE  . MET   A 93  ? 0.2414 0.2875 0.2571 -0.0128 -0.0054 0.0273  99  MET   A CE  
769  N N   . LEU   A 94  ? 0.1227 0.1900 0.1955 0.0034  -0.0002 0.0544  100 LEU   A N   
770  C CA  . LEU   A 94  ? 0.1348 0.1947 0.2104 0.0078  0.0056  0.0487  100 LEU   A CA  
771  C C   . LEU   A 94  ? 0.1288 0.1902 0.1911 0.0037  0.0039  0.0444  100 LEU   A C   
772  O O   . LEU   A 94  ? 0.1498 0.2219 0.2073 -0.0026 -0.0010 0.0494  100 LEU   A O   
773  C CB  . LEU   A 94  ? 0.1488 0.2154 0.2492 0.0121  0.0098  0.0582  100 LEU   A CB  
774  C CG  . LEU   A 94  ? 0.1975 0.2606 0.3164 0.0174  0.0144  0.0623  100 LEU   A CG  
775  C CD1 . LEU   A 94  ? 0.2188 0.2870 0.3659 0.0223  0.0211  0.0710  100 LEU   A CD1 
776  C CD2 . LEU   A 94  ? 0.2387 0.2845 0.3495 0.0202  0.0210  0.0491  100 LEU   A CD2 
777  N N   . ALA   A 95  ? 0.1341 0.1853 0.1899 0.0060  0.0082  0.0355  101 ALA   A N   
778  C CA  . ALA   A 95  ? 0.1223 0.1736 0.1674 0.0029  0.0076  0.0317  101 ALA   A CA  
779  C C   . ALA   A 95  ? 0.1339 0.1794 0.1835 0.0062  0.0140  0.0274  101 ALA   A C   
780  O O   . ALA   A 95  ? 0.1401 0.1785 0.1964 0.0098  0.0194  0.0243  101 ALA   A O   
781  C CB  . ALA   A 95  ? 0.1506 0.1937 0.1778 0.0001  0.0056  0.0237  101 ALA   A CB  
782  N N   . VAL   A 96  ? 0.1249 0.1728 0.1697 0.0039  0.0142  0.0262  102 VAL   A N   
783  C CA  . VAL   A 96  ? 0.1247 0.1667 0.1699 0.0052  0.0203  0.0208  102 VAL   A CA  
784  C C   . VAL   A 96  ? 0.1465 0.1778 0.1736 0.0030  0.0196  0.0120  102 VAL   A C   
785  O O   . VAL   A 96  ? 0.1793 0.2102 0.1950 0.0000  0.0151  0.0111  102 VAL   A O   
786  C CB  . VAL   A 96  ? 0.1223 0.1728 0.1713 0.0033  0.0204  0.0246  102 VAL   A CB  
787  C CG1 . VAL   A 96  ? 0.1496 0.1934 0.1959 0.0033  0.0271  0.0177  102 VAL   A CG1 
788  C CG2 . VAL   A 96  ? 0.1222 0.1856 0.1923 0.0051  0.0204  0.0358  102 VAL   A CG2 
789  N N   . GLY   A 97  ? 0.1580 0.1809 0.1840 0.0038  0.0245  0.0063  103 GLY   A N   
790  C CA  . GLY   A 97  ? 0.1834 0.1986 0.1938 0.0006  0.0230  0.0002  103 GLY   A CA  
791  C C   . GLY   A 97  ? 0.1982 0.2062 0.2079 -0.0005 0.0289  -0.0057 103 GLY   A C   
792  O O   . GLY   A 97  ? 0.2180 0.2249 0.2397 0.0019  0.0348  -0.0059 103 GLY   A O   
793  N N   . HIS   A 98  ? 0.2302 0.2334 0.2256 -0.0055 0.0275  -0.0102 104 HIS   A N   
794  C CA  . HIS   A 98  ? 0.2426 0.2397 0.2328 -0.0099 0.0325  -0.0165 104 HIS   A CA  
795  C C   . HIS   A 98  ? 0.2317 0.2260 0.2218 -0.0090 0.0302  -0.0167 104 HIS   A C   
796  O O   . HIS   A 98  ? 0.2263 0.2225 0.2124 -0.0080 0.0222  -0.0128 104 HIS   A O   
797  C CB  . HIS   A 98  ? 0.2642 0.2602 0.2385 -0.0177 0.0309  -0.0193 104 HIS   A CB  
798  C CG  . HIS   A 98  ? 0.2709 0.2621 0.2371 -0.0254 0.0370  -0.0265 104 HIS   A CG  
799  N ND1 . HIS   A 98  ? 0.2794 0.2668 0.2501 -0.0279 0.0487  -0.0334 104 HIS   A ND1 
800  C CD2 . HIS   A 98  ? 0.2938 0.2838 0.2489 -0.0318 0.0336  -0.0279 104 HIS   A CD2 
801  C CE1 . HIS   A 98  ? 0.2854 0.2685 0.2452 -0.0368 0.0525  -0.0401 104 HIS   A CE1 
802  N NE2 . HIS   A 98  ? 0.2947 0.2801 0.2442 -0.0397 0.0427  -0.0363 104 HIS   A NE2 
803  N N   . SER   A 99  ? 0.2343 0.2238 0.2292 -0.0098 0.0373  -0.0213 105 SER   A N   
804  C CA  . SER   A 99  ? 0.2582 0.2449 0.2528 -0.0096 0.0354  -0.0217 105 SER   A CA  
805  C C   . SER   A 99  ? 0.2848 0.2642 0.2793 -0.0147 0.0457  -0.0300 105 SER   A C   
806  O O   . SER   A 99  ? 0.3186 0.2947 0.3279 -0.0114 0.0554  -0.0318 105 SER   A O   
807  C CB  . SER   A 99  ? 0.2762 0.2660 0.2847 -0.0018 0.0329  -0.0154 105 SER   A CB  
808  O OG  . SER   A 99  ? 0.3696 0.3600 0.3937 0.0018  0.0405  -0.0143 105 SER   A OG  
809  N N   . GLU   A 100 ? 0.2336 0.2109 0.2133 -0.0230 0.0440  -0.0342 106 GLU   A N   
810  C CA  . GLU   A 100 ? 0.2488 0.2191 0.2238 -0.0309 0.0532  -0.0432 106 GLU   A CA  
811  C C   . GLU   A 100 ? 0.2588 0.2277 0.2363 -0.0290 0.0499  -0.0418 106 GLU   A C   
812  O O   . GLU   A 100 ? 0.2377 0.2115 0.2176 -0.0231 0.0398  -0.0342 106 GLU   A O   
813  C CB  . GLU   A 100 ? 0.2756 0.2472 0.2299 -0.0441 0.0517  -0.0476 106 GLU   A CB  
814  C CG  . GLU   A 100 ? 0.3168 0.2893 0.2681 -0.0468 0.0561  -0.0497 106 GLU   A CG  
815  C CD  . GLU   A 100 ? 0.3545 0.3304 0.2848 -0.0606 0.0533  -0.0520 106 GLU   A CD  
816  O OE1 . GLU   A 100 ? 0.4139 0.3895 0.3312 -0.0717 0.0531  -0.0558 106 GLU   A OE1 
817  O OE2 . GLU   A 100 ? 0.3226 0.3023 0.2491 -0.0614 0.0509  -0.0494 106 GLU   A OE2 
818  N N   . PRO   A 101 ? 0.2733 0.2349 0.2518 -0.0338 0.0592  -0.0492 107 PRO   A N   
819  C CA  . PRO   A 101 ? 0.2610 0.2211 0.2440 -0.0310 0.0564  -0.0474 107 PRO   A CA  
820  C C   . PRO   A 101 ? 0.2446 0.2112 0.2166 -0.0330 0.0433  -0.0421 107 PRO   A C   
821  O O   . PRO   A 101 ? 0.2422 0.2116 0.2221 -0.0254 0.0369  -0.0357 107 PRO   A O   
822  C CB  . PRO   A 101 ? 0.2861 0.2366 0.2669 -0.0398 0.0696  -0.0585 107 PRO   A CB  
823  C CG  . PRO   A 101 ? 0.3088 0.2542 0.2975 -0.0400 0.0824  -0.0639 107 PRO   A CG  
824  C CD  . PRO   A 101 ? 0.2883 0.2415 0.2671 -0.0411 0.0747  -0.0601 107 PRO   A CD  
825  N N   . GLY   A 102 ? 0.2394 0.2100 0.1951 -0.0431 0.0389  -0.0431 108 GLY   A N   
826  C CA  . GLY   A 102 ? 0.2377 0.2159 0.1865 -0.0452 0.0267  -0.0362 108 GLY   A CA  
827  C C   . GLY   A 102 ? 0.2034 0.1875 0.1586 -0.0363 0.0175  -0.0269 108 GLY   A C   
828  O O   . GLY   A 102 ? 0.2103 0.2000 0.1648 -0.0363 0.0087  -0.0205 108 GLY   A O   
829  N N   . ASP   A 103 ? 0.1929 0.1762 0.1557 -0.0290 0.0199  -0.0258 109 ASP   A N   
830  C CA  . ASP   A 103 ? 0.1814 0.1691 0.1506 -0.0212 0.0128  -0.0182 109 ASP   A CA  
831  C C   . ASP   A 103 ? 0.1701 0.1578 0.1500 -0.0136 0.0110  -0.0152 109 ASP   A C   
832  O O   . ASP   A 103 ? 0.1636 0.1547 0.1473 -0.0091 0.0056  -0.0100 109 ASP   A O   
833  C CB  . ASP   A 103 ? 0.1765 0.1644 0.1493 -0.0176 0.0160  -0.0181 109 ASP   A CB  
834  C CG  . ASP   A 103 ? 0.1952 0.1848 0.1568 -0.0251 0.0157  -0.0193 109 ASP   A CG  
835  O OD1 . ASP   A 103 ? 0.2006 0.1941 0.1547 -0.0302 0.0089  -0.0154 109 ASP   A OD1 
836  O OD2 . ASP   A 103 ? 0.2028 0.1904 0.1645 -0.0260 0.0224  -0.0232 109 ASP   A OD2 
837  N N   . CYS   A 104 ? 0.1642 0.1476 0.1487 -0.0128 0.0161  -0.0187 110 CYS   A N   
838  C CA  . CYS   A 104 ? 0.1694 0.1536 0.1628 -0.0069 0.0137  -0.0152 110 CYS   A CA  
839  C C   . CYS   A 104 ? 0.1630 0.1509 0.1535 -0.0076 0.0060  -0.0115 110 CYS   A C   
840  O O   . CYS   A 104 ? 0.1746 0.1638 0.1582 -0.0135 0.0034  -0.0120 110 CYS   A O   
841  C CB  . CYS   A 104 ? 0.1693 0.1480 0.1676 -0.0074 0.0202  -0.0191 110 CYS   A CB  
842  S SG  . CYS   A 104 ? 0.2022 0.1771 0.2145 -0.0029 0.0303  -0.0199 110 CYS   A SG  
843  N N   . GLY   A 105 ? 0.1399 0.1303 0.1370 -0.0023 0.0030  -0.0075 111 GLY   A N   
844  C CA  . GLY   A 105 ? 0.1501 0.1434 0.1484 -0.0020 -0.0022 -0.0042 111 GLY   A CA  
845  C C   . GLY   A 105 ? 0.1499 0.1458 0.1491 -0.0008 -0.0050 -0.0009 111 GLY   A C   
846  O O   . GLY   A 105 ? 0.1490 0.1464 0.1533 0.0006  -0.0072 0.0018  111 GLY   A O   
847  N N   . GLY   A 106 ? 0.1417 0.1376 0.1371 -0.0018 -0.0039 -0.0013 112 GLY   A N   
848  C CA  . GLY   A 106 ? 0.1483 0.1457 0.1450 -0.0008 -0.0056 0.0016  112 GLY   A CA  
849  C C   . GLY   A 106 ? 0.1264 0.1241 0.1283 0.0026  -0.0040 0.0017  112 GLY   A C   
850  O O   . GLY   A 106 ? 0.1362 0.1344 0.1389 0.0039  -0.0018 0.0005  112 GLY   A O   
851  N N   . ILE   A 107 ? 0.1296 0.1271 0.1355 0.0030  -0.0045 0.0034  113 ILE   A N   
852  C CA  . ILE   A 107 ? 0.1256 0.1232 0.1343 0.0035  -0.0017 0.0020  113 ILE   A CA  
853  C C   . ILE   A 107 ? 0.1186 0.1173 0.1238 0.0023  0.0001  0.0013  113 ILE   A C   
854  O O   . ILE   A 107 ? 0.1281 0.1259 0.1319 0.0018  -0.0003 0.0023  113 ILE   A O   
855  C CB  . ILE   A 107 ? 0.1326 0.1282 0.1491 0.0037  -0.0004 0.0028  113 ILE   A CB  
856  C CG1 . ILE   A 107 ? 0.1553 0.1514 0.1762 0.0046  -0.0015 0.0032  113 ILE   A CG1 
857  C CG2 . ILE   A 107 ? 0.1526 0.1469 0.1704 0.0018  0.0046  -0.0002 113 ILE   A CG2 
858  C CD1 . ILE   A 107 ? 0.1902 0.1851 0.2228 0.0054  0.0001  0.0051  113 ILE   A CD1 
859  N N   . LEU   A 108 ? 0.1158 0.1175 0.1199 0.0010  0.0016  0.0005  114 LEU   A N   
860  C CA  . LEU   A 108 ? 0.1191 0.1236 0.1202 -0.0021 0.0032  0.0002  114 LEU   A CA  
861  C C   . LEU   A 108 ? 0.1154 0.1186 0.1169 -0.0061 0.0068  -0.0027 114 LEU   A C   
862  O O   . LEU   A 108 ? 0.1320 0.1358 0.1348 -0.0072 0.0075  -0.0036 114 LEU   A O   
863  C CB  . LEU   A 108 ? 0.1213 0.1325 0.1222 -0.0029 0.0022  0.0029  114 LEU   A CB  
864  C CG  . LEU   A 108 ? 0.1302 0.1478 0.1278 -0.0081 0.0028  0.0042  114 LEU   A CG  
865  C CD1 . LEU   A 108 ? 0.1483 0.1654 0.1440 -0.0079 0.0032  0.0040  114 LEU   A CD1 
866  C CD2 . LEU   A 108 ? 0.1525 0.1793 0.1536 -0.0092 0.0006  0.0101  114 LEU   A CD2 
867  N N   . ARG   A 109 ? 0.1247 0.1255 0.1253 -0.0088 0.0100  -0.0048 115 ARG   A N   
868  C CA  . ARG   A 109 ? 0.1319 0.1293 0.1334 -0.0139 0.0162  -0.0095 115 ARG   A CA  
869  C C   . ARG   A 109 ? 0.1458 0.1451 0.1407 -0.0206 0.0194  -0.0120 115 ARG   A C   
870  O O   . ARG   A 109 ? 0.1475 0.1483 0.1399 -0.0199 0.0174  -0.0100 115 ARG   A O   
871  C CB  . ARG   A 109 ? 0.1508 0.1406 0.1629 -0.0104 0.0194  -0.0100 115 ARG   A CB  
872  C CG  . ARG   A 109 ? 0.1584 0.1451 0.1731 -0.0083 0.0190  -0.0075 115 ARG   A CG  
873  C CD  . ARG   A 109 ? 0.1749 0.1561 0.2038 -0.0047 0.0211  -0.0048 115 ARG   A CD  
874  N NE  . ARG   A 109 ? 0.1890 0.1731 0.2216 -0.0002 0.0147  0.0005  115 ARG   A NE  
875  C CZ  . ARG   A 109 ? 0.1837 0.1670 0.2267 0.0018  0.0154  0.0021  115 ARG   A CZ  
876  N NH1 . ARG   A 109 ? 0.1972 0.1764 0.2476 0.0002  0.0231  -0.0024 115 ARG   A NH1 
877  N NH2 . ARG   A 109 ? 0.2016 0.1885 0.2468 0.0045  0.0089  0.0075  115 ARG   A NH2 
878  N N   . CYS   A 110 ? 0.1813 0.1803 0.1729 -0.0286 0.0254  -0.0172 116 CYS   A N   
879  C CA  . CYS   A 110 ? 0.2244 0.2253 0.2077 -0.0384 0.0299  -0.0210 116 CYS   A CA  
880  C C   . CYS   A 110 ? 0.2640 0.2549 0.2515 -0.0426 0.0406  -0.0288 116 CYS   A C   
881  O O   . CYS   A 110 ? 0.2609 0.2442 0.2603 -0.0366 0.0437  -0.0295 116 CYS   A O   
882  C CB  . CYS   A 110 ? 0.2124 0.2248 0.1855 -0.0474 0.0271  -0.0195 116 CYS   A CB  
883  S SG  . CYS   A 110 ? 0.2243 0.2369 0.1948 -0.0546 0.0318  -0.0242 116 CYS   A SG  
884  N N   . GLN   A 111 ? 0.2801 0.2709 0.2592 -0.0540 0.0473  -0.0349 117 GLN   A N   
885  C CA  . GLN   A 111 ? 0.3178 0.2976 0.3018 -0.0596 0.0604  -0.0441 117 GLN   A CA  
886  C C   . GLN   A 111 ? 0.3354 0.3123 0.3230 -0.0623 0.0665  -0.0490 117 GLN   A C   
887  O O   . GLN   A 111 ? 0.3800 0.3458 0.3791 -0.0625 0.0779  -0.0552 117 GLN   A O   
888  C CB  . GLN   A 111 ? 0.3728 0.3534 0.3444 -0.0740 0.0675  -0.0511 117 GLN   A CB  
889  C CG  . GLN   A 111 ? 0.4075 0.3995 0.3626 -0.0880 0.0664  -0.0532 117 GLN   A CG  
890  C CD  . GLN   A 111 ? 0.4857 0.4798 0.4272 -0.1043 0.0731  -0.0600 117 GLN   A CD  
891  O OE1 . GLN   A 111 ? 0.5244 0.5291 0.4574 -0.1077 0.0657  -0.0545 117 GLN   A OE1 
892  N NE2 . GLN   A 111 ? 0.4722 0.4564 0.4121 -0.1152 0.0882  -0.0723 117 GLN   A NE2 
893  N N   . HIS   A 112 ? 0.2765 0.2629 0.2569 -0.0639 0.0597  -0.0458 118 HIS   A N   
894  C CA  . HIS   A 112 ? 0.2776 0.2624 0.2593 -0.0678 0.0651  -0.0505 118 HIS   A CA  
895  C C   . HIS   A 112 ? 0.2829 0.2646 0.2794 -0.0545 0.0611  -0.0455 118 HIS   A C   
896  O O   . HIS   A 112 ? 0.3138 0.2931 0.3144 -0.0562 0.0660  -0.0492 118 HIS   A O   
897  C CB  . HIS   A 112 ? 0.2874 0.2857 0.2527 -0.0787 0.0596  -0.0485 118 HIS   A CB  
898  C CG  . HIS   A 112 ? 0.3237 0.3279 0.2735 -0.0942 0.0627  -0.0523 118 HIS   A CG  
899  N ND1 . HIS   A 112 ? 0.2760 0.2930 0.2175 -0.0962 0.0524  -0.0439 118 HIS   A ND1 
900  C CD2 . HIS   A 112 ? 0.3582 0.3588 0.2991 -0.1100 0.0752  -0.0635 118 HIS   A CD2 
901  C CE1 . HIS   A 112 ? 0.3471 0.3677 0.2753 -0.1124 0.0581  -0.0496 118 HIS   A CE1 
902  N NE2 . HIS   A 112 ? 0.3936 0.4039 0.3200 -0.1216 0.0722  -0.0622 118 HIS   A NE2 
903  N N   . GLY   A 113 ? 0.2485 0.2316 0.2511 -0.0427 0.0514  -0.0369 119 GLY   A N   
904  C CA  . GLY   A 113 ? 0.2294 0.2114 0.2432 -0.0323 0.0466  -0.0318 119 GLY   A CA  
905  C C   . GLY   A 113 ? 0.1878 0.1773 0.1970 -0.0260 0.0344  -0.0237 119 GLY   A C   
906  O O   . GLY   A 113 ? 0.1839 0.1776 0.1860 -0.0266 0.0300  -0.0209 119 GLY   A O   
907  N N   . VAL   A 114 ? 0.1650 0.1557 0.1790 -0.0205 0.0300  -0.0204 120 VAL   A N   
908  C CA  . VAL   A 114 ? 0.1593 0.1552 0.1705 -0.0149 0.0206  -0.0140 120 VAL   A CA  
909  C C   . VAL   A 114 ? 0.1428 0.1467 0.1446 -0.0196 0.0174  -0.0122 120 VAL   A C   
910  O O   . VAL   A 114 ? 0.1554 0.1622 0.1540 -0.0255 0.0196  -0.0142 120 VAL   A O   
911  C CB  . VAL   A 114 ? 0.1530 0.1474 0.1722 -0.0088 0.0177  -0.0115 120 VAL   A CB  
912  C CG1 . VAL   A 114 ? 0.1700 0.1684 0.1855 -0.0051 0.0105  -0.0069 120 VAL   A CG1 
913  C CG2 . VAL   A 114 ? 0.1775 0.1669 0.2083 -0.0043 0.0190  -0.0098 120 VAL   A CG2 
914  N N   . VAL   A 115 ? 0.1319 0.1404 0.1307 -0.0178 0.0125  -0.0078 121 VAL   A N   
915  C CA  . VAL   A 115 ? 0.1305 0.1482 0.1249 -0.0213 0.0087  -0.0031 121 VAL   A CA  
916  C C   . VAL   A 115 ? 0.1276 0.1471 0.1270 -0.0154 0.0043  0.0020  121 VAL   A C   
917  O O   . VAL   A 115 ? 0.1430 0.1689 0.1427 -0.0179 0.0021  0.0063  121 VAL   A O   
918  C CB  . VAL   A 115 ? 0.1540 0.1764 0.1451 -0.0233 0.0073  -0.0006 121 VAL   A CB  
919  C CG1 . VAL   A 115 ? 0.1821 0.2160 0.1735 -0.0256 0.0025  0.0074  121 VAL   A CG1 
920  C CG2 . VAL   A 115 ? 0.1792 0.2000 0.1642 -0.0310 0.0125  -0.0060 121 VAL   A CG2 
921  N N   . GLY   A 116 ? 0.1317 0.1459 0.1354 -0.0082 0.0030  0.0020  122 GLY   A N   
922  C CA  . GLY   A 116 ? 0.1417 0.1558 0.1499 -0.0035 0.0006  0.0052  122 GLY   A CA  
923  C C   . GLY   A 116 ? 0.1239 0.1321 0.1334 0.0013  0.0003  0.0035  122 GLY   A C   
924  O O   . GLY   A 116 ? 0.1295 0.1343 0.1376 0.0013  0.0009  0.0012  122 GLY   A O   
925  N N   . ILE   A 117 ? 0.1218 0.1289 0.1344 0.0042  0.0000  0.0048  123 ILE   A N   
926  C CA  . ILE   A 117 ? 0.1253 0.1276 0.1365 0.0059  0.0001  0.0024  123 ILE   A CA  
927  C C   . ILE   A 117 ? 0.1315 0.1337 0.1451 0.0072  0.0024  0.0031  123 ILE   A C   
928  O O   . ILE   A 117 ? 0.1357 0.1407 0.1560 0.0084  0.0037  0.0065  123 ILE   A O   
929  C CB  . ILE   A 117 ? 0.1385 0.1375 0.1504 0.0062  -0.0005 0.0008  123 ILE   A CB  
930  C CG1 . ILE   A 117 ? 0.1617 0.1610 0.1780 0.0070  0.0005  0.0021  123 ILE   A CG1 
931  C CG2 . ILE   A 117 ? 0.1608 0.1594 0.1730 0.0054  -0.0020 0.0004  123 ILE   A CG2 
932  C CD1 . ILE   A 117 ? 0.1741 0.1698 0.1902 0.0065  0.0003  -0.0002 123 ILE   A CD1 
933  N N   . VAL   A 118 ? 0.1311 0.1304 0.1407 0.0065  0.0034  0.0006  124 VAL   A N   
934  C CA  . VAL   A 118 ? 0.1352 0.1332 0.1476 0.0070  0.0077  -0.0004 124 VAL   A CA  
935  C C   . VAL   A 118 ? 0.1451 0.1395 0.1631 0.0078  0.0113  -0.0016 124 VAL   A C   
936  O O   . VAL   A 118 ? 0.1366 0.1277 0.1506 0.0060  0.0103  -0.0043 124 VAL   A O   
937  C CB  . VAL   A 118 ? 0.1383 0.1334 0.1427 0.0039  0.0085  -0.0041 124 VAL   A CB  
938  C CG1 . VAL   A 118 ? 0.1440 0.1361 0.1510 0.0031  0.0153  -0.0073 124 VAL   A CG1 
939  C CG2 . VAL   A 118 ? 0.1448 0.1426 0.1450 0.0033  0.0056  -0.0024 124 VAL   A CG2 
940  N N   . SER   A 119 ? 0.1388 0.1339 0.1676 0.0102  0.0157  0.0009  125 SER   A N   
941  C CA  . SER   A 119 ? 0.1539 0.1447 0.1921 0.0115  0.0209  0.0005  125 SER   A CA  
942  C C   . SER   A 119 ? 0.1668 0.1539 0.2147 0.0124  0.0297  -0.0013 125 SER   A C   
943  O O   . SER   A 119 ? 0.1869 0.1666 0.2393 0.0115  0.0368  -0.0057 125 SER   A O   
944  C CB  . SER   A 119 ? 0.1528 0.1492 0.1999 0.0140  0.0178  0.0080  125 SER   A CB  
945  O OG  . SER   A 119 ? 0.1823 0.1750 0.2416 0.0159  0.0228  0.0096  125 SER   A OG  
946  N N   . THR   A 120 ? 0.1686 0.1602 0.2218 0.0139  0.0309  0.0017  126 THR   A N   
947  C CA  . THR   A 120 ? 0.1817 0.1697 0.2481 0.0153  0.0410  0.0004  126 THR   A CA  
948  C C   . THR   A 120 ? 0.2092 0.1979 0.2675 0.0128  0.0422  -0.0035 126 THR   A C   
949  O O   . THR   A 120 ? 0.1882 0.1818 0.2348 0.0114  0.0345  -0.0022 126 THR   A O   
950  C CB  . THR   A 120 ? 0.1892 0.1842 0.2790 0.0207  0.0424  0.0117  126 THR   A CB  
951  O OG1 . THR   A 120 ? 0.1962 0.2024 0.2858 0.0212  0.0355  0.0191  126 THR   A OG1 
952  C CG2 . THR   A 120 ? 0.1885 0.1846 0.2853 0.0224  0.0396  0.0173  126 THR   A CG2 
953  N N   . GLY   A 121 ? 0.2371 0.2204 0.3024 0.0118  0.0529  -0.0086 127 GLY   A N   
954  C CA  . GLY   A 121 ? 0.2669 0.2508 0.3249 0.0087  0.0550  -0.0125 127 GLY   A CA  
955  C C   . GLY   A 121 ? 0.3087 0.2881 0.3826 0.0093  0.0688  -0.0158 127 GLY   A C   
956  O O   . GLY   A 121 ? 0.3403 0.3141 0.4301 0.0114  0.0778  -0.0166 127 GLY   A O   
957  N N   . GLY   A 122 ? 0.3231 0.3042 0.3920 0.0068  0.0709  -0.0186 128 GLY   A N   
958  C CA  . GLY   A 122 ? 0.3335 0.3101 0.4148 0.0057  0.0850  -0.0237 128 GLY   A CA  
959  C C   . GLY   A 122 ? 0.3582 0.3439 0.4495 0.0093  0.0835  -0.0168 128 GLY   A C   
960  O O   . GLY   A 122 ? 0.3637 0.3599 0.4630 0.0145  0.0742  -0.0053 128 GLY   A O   
961  N N   . ASN   A 123 ? 0.3437 0.3258 0.4349 0.0054  0.0935  -0.0240 129 ASN   A N   
962  C CA  . ASN   A 123 ? 0.3564 0.3463 0.4608 0.0085  0.0955  -0.0185 129 ASN   A CA  
963  C C   . ASN   A 123 ? 0.3331 0.3348 0.4293 0.0102  0.0808  -0.0094 129 ASN   A C   
964  O O   . ASN   A 123 ? 0.3247 0.3367 0.4373 0.0145  0.0791  0.0002  129 ASN   A O   
965  C CB  . ASN   A 123 ? 0.3775 0.3698 0.5172 0.0160  0.1049  -0.0107 129 ASN   A CB  
966  C CG  . ASN   A 123 ? 0.4287 0.4078 0.5806 0.0137  0.1240  -0.0214 129 ASN   A CG  
967  O OD1 . ASN   A 123 ? 0.4721 0.4443 0.6138 0.0067  0.1339  -0.0334 129 ASN   A OD1 
968  N ND2 . ASN   A 123 ? 0.4090 0.3844 0.5826 0.0187  0.1299  -0.0175 129 ASN   A ND2 
969  N N   . GLY   A 124 ? 0.2989 0.2990 0.3693 0.0054  0.0718  -0.0134 130 GLY   A N   
970  C CA  . GLY   A 124 ? 0.2759 0.2845 0.3363 0.0054  0.0601  -0.0074 130 GLY   A CA  
971  C C   . GLY   A 124 ? 0.2051 0.2210 0.2706 0.0096  0.0504  0.0022  130 GLY   A C   
972  O O   . GLY   A 124 ? 0.2128 0.2355 0.2717 0.0088  0.0425  0.0065  130 GLY   A O   
973  N N   . LEU   A 125 ? 0.1956 0.2091 0.2701 0.0125  0.0513  0.0042  131 LEU   A N   
974  C CA  . LEU   A 125 ? 0.1821 0.2024 0.2575 0.0146  0.0417  0.0124  131 LEU   A CA  
975  C C   . LEU   A 125 ? 0.2025 0.2152 0.2630 0.0127  0.0381  0.0068  131 LEU   A C   
976  O O   . LEU   A 125 ? 0.2500 0.2532 0.3070 0.0110  0.0444  -0.0010 131 LEU   A O   
977  C CB  . LEU   A 125 ? 0.1849 0.2112 0.2852 0.0194  0.0443  0.0221  131 LEU   A CB  
978  C CG  . LEU   A 125 ? 0.1848 0.2213 0.3046 0.0215  0.0471  0.0306  131 LEU   A CG  
979  C CD1 . LEU   A 125 ? 0.2171 0.2565 0.3682 0.0270  0.0544  0.0393  131 LEU   A CD1 
980  C CD2 . LEU   A 125 ? 0.1840 0.2341 0.2969 0.0187  0.0359  0.0388  131 LEU   A CD2 
981  N N   . VAL   A 126 ? 0.1499 0.1669 0.2027 0.0122  0.0292  0.0106  132 VAL   A N   
982  C CA  . VAL   A 126 ? 0.1543 0.1660 0.1968 0.0111  0.0255  0.0073  132 VAL   A CA  
983  C C   . VAL   A 126 ? 0.1484 0.1669 0.1990 0.0130  0.0208  0.0152  132 VAL   A C   
984  O O   . VAL   A 126 ? 0.1523 0.1802 0.2050 0.0120  0.0163  0.0217  132 VAL   A O   
985  C CB  . VAL   A 126 ? 0.1604 0.1698 0.1850 0.0075  0.0203  0.0031  132 VAL   A CB  
986  C CG1 . VAL   A 126 ? 0.1854 0.2016 0.2064 0.0063  0.0153  0.0070  132 VAL   A CG1 
987  C CG2 . VAL   A 126 ? 0.1589 0.1640 0.1762 0.0067  0.0167  0.0009  132 VAL   A CG2 
988  N N   . GLY   A 127 ? 0.1421 0.1565 0.1962 0.0144  0.0218  0.0147  133 GLY   A N   
989  C CA  . GLY   A 127 ? 0.1343 0.1550 0.1940 0.0149  0.0171  0.0221  133 GLY   A CA  
990  C C   . GLY   A 127 ? 0.1367 0.1535 0.1835 0.0129  0.0128  0.0179  133 GLY   A C   
991  O O   . GLY   A 127 ? 0.1581 0.1663 0.1979 0.0126  0.0148  0.0108  133 GLY   A O   
992  N N   . PHE   A 128 ? 0.1268 0.1505 0.1708 0.0106  0.0074  0.0224  134 PHE   A N   
993  C CA  . PHE   A 128 ? 0.1299 0.1504 0.1636 0.0084  0.0043  0.0186  134 PHE   A CA  
994  C C   . PHE   A 128 ? 0.1264 0.1513 0.1654 0.0076  0.0023  0.0238  134 PHE   A C   
995  O O   . PHE   A 128 ? 0.1334 0.1682 0.1788 0.0055  0.0001  0.0321  134 PHE   A O   
996  C CB  . PHE   A 128 ? 0.1310 0.1545 0.1545 0.0043  0.0014  0.0170  134 PHE   A CB  
997  C CG  . PHE   A 128 ? 0.1235 0.1444 0.1422 0.0044  0.0027  0.0136  134 PHE   A CG  
998  C CD1 . PHE   A 128 ? 0.1305 0.1437 0.1427 0.0050  0.0033  0.0079  134 PHE   A CD1 
999  C CD2 . PHE   A 128 ? 0.1438 0.1713 0.1651 0.0031  0.0027  0.0172  134 PHE   A CD2 
1000 C CE1 . PHE   A 128 ? 0.1325 0.1441 0.1402 0.0043  0.0040  0.0059  134 PHE   A CE1 
1001 C CE2 . PHE   A 128 ? 0.1506 0.1756 0.1670 0.0028  0.0039  0.0141  134 PHE   A CE2 
1002 C CZ  . PHE   A 128 ? 0.1455 0.1623 0.1548 0.0033  0.0045  0.0084  134 PHE   A CZ  
1003 N N   . ALA   A 129 ? 0.1234 0.1423 0.1599 0.0083  0.0026  0.0201  135 ALA   A N   
1004 C CA  . ALA   A 129 ? 0.1336 0.1560 0.1731 0.0067  0.0006  0.0243  135 ALA   A CA  
1005 C C   . ALA   A 129 ? 0.1273 0.1539 0.1566 0.0012  -0.0024 0.0229  135 ALA   A C   
1006 O O   . ALA   A 129 ? 0.1374 0.1581 0.1591 0.0007  -0.0017 0.0160  135 ALA   A O   
1007 C CB  . ALA   A 129 ? 0.1274 0.1415 0.1675 0.0090  0.0027  0.0198  135 ALA   A CB  
1008 N N   . ASP   A 130 ? 0.1306 0.1675 0.1606 -0.0041 -0.0050 0.0296  136 ASP   A N   
1009 C CA  . ASP   A 130 ? 0.1459 0.1864 0.1650 -0.0118 -0.0059 0.0269  136 ASP   A CA  
1010 C C   . ASP   A 130 ? 0.1385 0.1751 0.1546 -0.0132 -0.0050 0.0231  136 ASP   A C   
1011 O O   . ASP   A 130 ? 0.1500 0.1862 0.1725 -0.0106 -0.0058 0.0266  136 ASP   A O   
1012 C CB  . ASP   A 130 ? 0.1679 0.2228 0.1877 -0.0196 -0.0094 0.0363  136 ASP   A CB  
1013 C CG  . ASP   A 130 ? 0.2046 0.2640 0.2113 -0.0304 -0.0090 0.0326  136 ASP   A CG  
1014 O OD1 . ASP   A 130 ? 0.2107 0.2644 0.2096 -0.0320 -0.0057 0.0244  136 ASP   A OD1 
1015 O OD2 . ASP   A 130 ? 0.2494 0.3168 0.2535 -0.0380 -0.0111 0.0372  136 ASP   A OD2 
1016 N N   . VAL   A 131 ? 0.1398 0.1728 0.1476 -0.0172 -0.0025 0.0158  137 VAL   A N   
1017 C CA  . VAL   A 131 ? 0.1471 0.1773 0.1526 -0.0198 -0.0006 0.0118  137 VAL   A CA  
1018 C C   . VAL   A 131 ? 0.1562 0.1912 0.1526 -0.0308 0.0021  0.0089  137 VAL   A C   
1019 O O   . VAL   A 131 ? 0.1543 0.1872 0.1486 -0.0344 0.0051  0.0046  137 VAL   A O   
1020 C CB  . VAL   A 131 ? 0.1476 0.1673 0.1555 -0.0139 0.0021  0.0050  137 VAL   A CB  
1021 C CG1 . VAL   A 131 ? 0.1583 0.1739 0.1722 -0.0061 0.0000  0.0069  137 VAL   A CG1 
1022 C CG2 . VAL   A 131 ? 0.1549 0.1701 0.1606 -0.0145 0.0055  -0.0005 137 VAL   A CG2 
1023 N N   . ARG   A 132 ? 0.1601 0.2018 0.1509 -0.0375 0.0017  0.0105  138 ARG   A N   
1024 C CA  . ARG   A 132 ? 0.1634 0.2086 0.1433 -0.0503 0.0059  0.0054  138 ARG   A CA  
1025 C C   . ARG   A 132 ? 0.1822 0.2368 0.1566 -0.0604 0.0043  0.0095  138 ARG   A C   
1026 O O   . ARG   A 132 ? 0.1993 0.2546 0.1637 -0.0722 0.0099  0.0026  138 ARG   A O   
1027 C CB  . ARG   A 132 ? 0.1803 0.2315 0.1543 -0.0564 0.0055  0.0066  138 ARG   A CB  
1028 C CG  . ARG   A 132 ? 0.1600 0.2008 0.1374 -0.0486 0.0087  0.0009  138 ARG   A CG  
1029 C CD  . ARG   A 132 ? 0.1876 0.2347 0.1590 -0.0550 0.0081  0.0024  138 ARG   A CD  
1030 N NE  . ARG   A 132 ? 0.1743 0.2320 0.1513 -0.0519 0.0004  0.0140  138 ARG   A NE  
1031 C CZ  . ARG   A 132 ? 0.2084 0.2740 0.1844 -0.0550 -0.0021 0.0186  138 ARG   A CZ  
1032 N NH1 . ARG   A 132 ? 0.2110 0.2763 0.1772 -0.0636 0.0018  0.0126  138 ARG   A NH1 
1033 N NH2 . ARG   A 132 ? 0.2104 0.2840 0.1963 -0.0498 -0.0077 0.0292  138 ARG   A NH2 
1034 N N   . ASP   A 133 ? 0.1659 0.2280 0.1471 -0.0573 -0.0025 0.0206  139 ASP   A N   
1035 C CA  . ASP   A 133 ? 0.1842 0.2561 0.1612 -0.0672 -0.0048 0.0262  139 ASP   A CA  
1036 C C   . ASP   A 133 ? 0.1849 0.2488 0.1637 -0.0640 -0.0017 0.0209  139 ASP   A C   
1037 O O   . ASP   A 133 ? 0.2100 0.2810 0.1841 -0.0729 -0.0027 0.0241  139 ASP   A O   
1038 C CB  . ASP   A 133 ? 0.2059 0.2900 0.1931 -0.0652 -0.0132 0.0425  139 ASP   A CB  
1039 C CG  . ASP   A 133 ? 0.2268 0.3025 0.2296 -0.0498 -0.0142 0.0454  139 ASP   A CG  
1040 O OD1 . ASP   A 133 ? 0.2151 0.2793 0.2209 -0.0402 -0.0111 0.0380  139 ASP   A OD1 
1041 O OD2 . ASP   A 133 ? 0.2581 0.3389 0.2703 -0.0482 -0.0179 0.0556  139 ASP   A OD2 
1042 N N   . LEU   A 134 ? 0.1674 0.2181 0.1533 -0.0523 0.0015  0.0140  140 LEU   A N   
1043 C CA  . LEU   A 134 ? 0.1636 0.2075 0.1532 -0.0485 0.0038  0.0101  140 LEU   A CA  
1044 C C   . LEU   A 134 ? 0.1785 0.2174 0.1619 -0.0554 0.0121  -0.0012 140 LEU   A C   
1045 O O   . LEU   A 134 ? 0.1839 0.2129 0.1729 -0.0490 0.0170  -0.0085 140 LEU   A O   
1046 C CB  . LEU   A 134 ? 0.1656 0.2001 0.1657 -0.0347 0.0028  0.0093  140 LEU   A CB  
1047 C CG  . LEU   A 134 ? 0.1756 0.2127 0.1837 -0.0277 -0.0026 0.0185  140 LEU   A CG  
1048 C CD1 . LEU   A 134 ? 0.1877 0.2148 0.2024 -0.0173 -0.0019 0.0150  140 LEU   A CD1 
1049 C CD2 . LEU   A 134 ? 0.2031 0.2469 0.2156 -0.0299 -0.0062 0.0276  140 LEU   A CD2 
1050 N N   . LEU   A 135 ? 0.1785 0.2250 0.1512 -0.0697 0.0145  -0.0022 141 LEU   A N   
1051 C CA  . LEU   A 135 ? 0.1992 0.2403 0.1656 -0.0785 0.0251  -0.0145 141 LEU   A CA  
1052 C C   . LEU   A 135 ? 0.2026 0.2348 0.1772 -0.0733 0.0309  -0.0212 141 LEU   A C   
1053 O O   . LEU   A 135 ? 0.2241 0.2476 0.2025 -0.0739 0.0407  -0.0312 141 LEU   A O   
1054 C CB  . LEU   A 135 ? 0.2247 0.2769 0.1750 -0.0981 0.0271  -0.0149 141 LEU   A CB  
1055 C CG  . LEU   A 135 ? 0.2388 0.3041 0.1812 -0.1057 0.0198  -0.0056 141 LEU   A CG  
1056 C CD1 . LEU   A 135 ? 0.2811 0.3575 0.2053 -0.1283 0.0232  -0.0079 141 LEU   A CD1 
1057 C CD2 . LEU   A 135 ? 0.2654 0.3258 0.2098 -0.1008 0.0214  -0.0088 141 LEU   A CD2 
1058 N N   . TRP   A 136 ? 0.1866 0.2204 0.1665 -0.0674 0.0251  -0.0148 142 TRP   A N   
1059 C CA  . TRP   A 136 ? 0.1909 0.2180 0.1791 -0.0624 0.0289  -0.0193 142 TRP   A CA  
1060 C C   . TRP   A 136 ? 0.1919 0.2092 0.1933 -0.0499 0.0309  -0.0227 142 TRP   A C   
1061 O O   . TRP   A 136 ? 0.2113 0.2234 0.2214 -0.0471 0.0360  -0.0273 142 TRP   A O   
1062 C CB  . TRP   A 136 ? 0.1964 0.2277 0.1865 -0.0596 0.0218  -0.0112 142 TRP   A CB  
1063 C CG  . TRP   A 136 ? 0.1748 0.2070 0.1708 -0.0496 0.0132  -0.0019 142 TRP   A CG  
1064 C CD1 . TRP   A 136 ? 0.1841 0.2248 0.1778 -0.0519 0.0066  0.0081  142 TRP   A CD1 
1065 C CD2 . TRP   A 136 ? 0.1757 0.2006 0.1819 -0.0371 0.0110  -0.0016 142 TRP   A CD2 
1066 N NE1 . TRP   A 136 ? 0.1935 0.2308 0.1965 -0.0407 0.0021  0.0133  142 TRP   A NE1 
1067 C CE2 . TRP   A 136 ? 0.1836 0.2111 0.1924 -0.0324 0.0047  0.0069  142 TRP   A CE2 
1068 C CE3 . TRP   A 136 ? 0.1807 0.1980 0.1946 -0.0304 0.0138  -0.0069 142 TRP   A CE3 
1069 C CZ2 . TRP   A 136 ? 0.1904 0.2118 0.2069 -0.0223 0.0025  0.0079  142 TRP   A CZ2 
1070 C CZ3 . TRP   A 136 ? 0.1958 0.2092 0.2163 -0.0211 0.0098  -0.0043 142 TRP   A CZ3 
1071 C CH2 . TRP   A 136 ? 0.1891 0.2039 0.2095 -0.0179 0.0048  0.0020  142 TRP   A CH2 
1072 N N   . LEU   A 137 ? 0.1771 0.1927 0.1809 -0.0430 0.0269  -0.0196 143 LEU   A N   
1073 C CA  . LEU   A 137 ? 0.1908 0.1989 0.2063 -0.0333 0.0285  -0.0217 143 LEU   A CA  
1074 C C   . LEU   A 137 ? 0.2196 0.2220 0.2412 -0.0366 0.0393  -0.0300 143 LEU   A C   
1075 O O   . LEU   A 137 ? 0.2326 0.2298 0.2681 -0.0294 0.0414  -0.0305 143 LEU   A O   
1076 C CB  . LEU   A 137 ? 0.1881 0.1961 0.2028 -0.0280 0.0233  -0.0176 143 LEU   A CB  
1077 C CG  . LEU   A 137 ? 0.1810 0.1917 0.1955 -0.0220 0.0147  -0.0101 143 LEU   A CG  
1078 C CD1 . LEU   A 137 ? 0.2013 0.2125 0.2139 -0.0191 0.0117  -0.0074 143 LEU   A CD1 
1079 C CD2 . LEU   A 137 ? 0.1947 0.2015 0.2178 -0.0146 0.0125  -0.0092 143 LEU   A CD2 
1080 N N   . ASP   A 138 ? 0.2456 0.2491 0.2577 -0.0486 0.0468  -0.0364 144 ASP   A N   
1081 C CA  . ASP   A 138 ? 0.2751 0.2713 0.2937 -0.0532 0.0602  -0.0461 144 ASP   A CA  
1082 C C   . ASP   A 138 ? 0.3298 0.3233 0.3553 -0.0568 0.0690  -0.0521 144 ASP   A C   
1083 O O   . ASP   A 138 ? 0.3612 0.3479 0.3945 -0.0611 0.0824  -0.0610 144 ASP   A O   
1084 C CB  . ASP   A 138 ? 0.3000 0.2978 0.3039 -0.0670 0.0665  -0.0523 144 ASP   A CB  
1085 C CG  . ASP   A 138 ? 0.3164 0.3169 0.3140 -0.0652 0.0599  -0.0477 144 ASP   A CG  
1086 O OD1 . ASP   A 138 ? 0.3305 0.3290 0.3372 -0.0527 0.0531  -0.0415 144 ASP   A OD1 
1087 O OD2 . ASP   A 138 ? 0.4075 0.4130 0.3906 -0.0773 0.0616  -0.0500 144 ASP   A OD2 
1088 N N   . GLU   A 139 ? 0.3391 0.3373 0.3626 -0.0559 0.0633  -0.0481 145 GLU   A N   
1089 C CA  . GLU   A 139 ? 0.3947 0.3913 0.4234 -0.0606 0.0719  -0.0541 145 GLU   A CA  
1090 C C   . GLU   A 139 ? 0.4360 0.4337 0.4756 -0.0509 0.0654  -0.0481 145 GLU   A C   
1091 O O   . GLU   A 139 ? 0.4351 0.4353 0.4749 -0.0424 0.0539  -0.0396 145 GLU   A O   
1092 C CB  . GLU   A 139 ? 0.4526 0.4558 0.4615 -0.0764 0.0738  -0.0573 145 GLU   A CB  
1093 C CG  . GLU   A 139 ? 0.5534 0.5661 0.5509 -0.0759 0.0594  -0.0464 145 GLU   A CG  
1094 C CD  . GLU   A 139 ? 0.6580 0.6806 0.6359 -0.0919 0.0580  -0.0452 145 GLU   A CD  
1095 O OE1 . GLU   A 139 ? 0.6673 0.6975 0.6406 -0.0926 0.0491  -0.0365 145 GLU   A OE1 
1096 O OE2 . GLU   A 139 ? 0.7026 0.7259 0.6702 -0.1044 0.0655  -0.0521 145 GLU   A OE2 
1097 N N   . GLU   A 140 ? 0.4758 0.4718 0.5239 -0.0536 0.0735  -0.0531 146 GLU   A N   
1098 C CA  . GLU   A 140 ? 0.5185 0.5163 0.5766 -0.0470 0.0690  -0.0486 146 GLU   A CA  
1099 C C   . GLU   A 140 ? 0.5437 0.5392 0.6217 -0.0342 0.0655  -0.0430 146 GLU   A C   
1100 O O   . GLU   A 140 ? 0.5576 0.5525 0.6527 -0.0307 0.0697  -0.0431 146 GLU   A O   
1101 C CB  . GLU   A 140 ? 0.5726 0.5769 0.6163 -0.0480 0.0573  -0.0418 146 GLU   A CB  
1102 C CG  . GLU   A 140 ? 0.6633 0.6689 0.7160 -0.0397 0.0503  -0.0359 146 GLU   A CG  
1103 C CD  . GLU   A 140 ? 0.7824 0.7907 0.8324 -0.0455 0.0523  -0.0374 146 GLU   A CD  
1104 O OE1 . GLU   A 140 ? 0.8119 0.8240 0.8531 -0.0459 0.0441  -0.0317 146 GLU   A OE1 
1105 O OE2 . GLU   A 140 ? 0.8147 0.8211 0.8727 -0.0497 0.0629  -0.0444 146 GLU   A OE2 
1106 N N   . SER   B 1   ? 0.2209 0.2399 0.2351 0.0105  -0.0129 0.0394  7   SER   C N   
1107 C CA  . SER   B 1   ? 0.2067 0.2270 0.2302 0.0081  -0.0140 0.0390  7   SER   C CA  
1108 C C   . SER   B 1   ? 0.2093 0.2269 0.2332 0.0059  -0.0142 0.0347  7   SER   C C   
1109 O O   . SER   B 1   ? 0.2333 0.2486 0.2503 0.0060  -0.0147 0.0320  7   SER   C O   
1110 C CB  . SER   B 1   ? 0.2477 0.2704 0.2720 0.0084  -0.0190 0.0402  7   SER   C CB  
1111 O OG  . SER   B 1   ? 0.3160 0.3371 0.3327 0.0085  -0.0233 0.0368  7   SER   C OG  
1112 N N   . GLY   B 2   ? 0.1925 0.2102 0.2243 0.0042  -0.0131 0.0345  8   GLY   C N   
1113 C CA  . GLY   B 2   ? 0.1909 0.2058 0.2233 0.0028  -0.0125 0.0316  8   GLY   C CA  
1114 C C   . GLY   B 2   ? 0.1747 0.1886 0.2132 0.0025  -0.0089 0.0319  8   GLY   C C   
1115 O O   . GLY   B 2   ? 0.1755 0.1903 0.2167 0.0032  -0.0067 0.0332  8   GLY   C O   
1116 N N   . ALA   B 3   ? 0.1641 0.1759 0.2049 0.0017  -0.0078 0.0308  9   ALA   C N   
1117 C CA  . ALA   B 3   ? 0.1657 0.1756 0.2103 0.0022  -0.0038 0.0311  9   ALA   C CA  
1118 C C   . ALA   B 3   ? 0.1545 0.1603 0.1955 0.0027  -0.0016 0.0294  9   ALA   C C   
1119 O O   . ALA   B 3   ? 0.1730 0.1777 0.2114 0.0020  -0.0032 0.0282  9   ALA   C O   
1120 C CB  . ALA   B 3   ? 0.1815 0.1934 0.2361 0.0014  -0.0034 0.0338  9   ALA   C CB  
1121 N N   . ILE   B 4   ? 0.1500 0.1530 0.1902 0.0043  0.0022  0.0291  10  ILE   C N   
1122 C CA  . ILE   B 4   ? 0.1640 0.1625 0.2007 0.0058  0.0054  0.0286  10  ILE   C CA  
1123 C C   . ILE   B 4   ? 0.1588 0.1565 0.2035 0.0059  0.0091  0.0313  10  ILE   C C   
1124 O O   . ILE   B 4   ? 0.1682 0.1670 0.2172 0.0063  0.0105  0.0323  10  ILE   C O   
1125 C CB  . ILE   B 4   ? 0.1648 0.1602 0.1934 0.0086  0.0070  0.0264  10  ILE   C CB  
1126 C CG1 . ILE   B 4   ? 0.1933 0.1903 0.2172 0.0085  0.0035  0.0240  10  ILE   C CG1 
1127 C CG2 . ILE   B 4   ? 0.1949 0.1853 0.2177 0.0110  0.0104  0.0265  10  ILE   C CG2 
1128 C CD1 . ILE   B 4   ? 0.1834 0.1782 0.2023 0.0113  0.0038  0.0213  10  ILE   C CD1 
1129 N N   . TYR   B 5   ? 0.1590 0.1544 0.2069 0.0057  0.0115  0.0326  11  TYR   C N   
1130 C CA  . TYR   B 5   ? 0.1702 0.1645 0.2275 0.0060  0.0160  0.0356  11  TYR   C CA  
1131 C C   . TYR   B 5   ? 0.1820 0.1703 0.2333 0.0094  0.0222  0.0365  11  TYR   C C   
1132 O O   . TYR   B 5   ? 0.1994 0.1854 0.2498 0.0095  0.0230  0.0367  11  TYR   C O   
1133 C CB  . TYR   B 5   ? 0.1754 0.1725 0.2453 0.0030  0.0135  0.0369  11  TYR   C CB  
1134 C CG  . TYR   B 5   ? 0.1719 0.1746 0.2463 0.0007  0.0073  0.0365  11  TYR   C CG  
1135 C CD1 . TYR   B 5   ? 0.1687 0.1742 0.2516 0.0004  0.0079  0.0388  11  TYR   C CD1 
1136 C CD2 . TYR   B 5   ? 0.1759 0.1808 0.2451 -0.0006 0.0014  0.0341  11  TYR   C CD2 
1137 C CE1 . TYR   B 5   ? 0.1870 0.1975 0.2728 -0.0009 0.0025  0.0390  11  TYR   C CE1 
1138 C CE2 . TYR   B 5   ? 0.1942 0.2038 0.2651 -0.0017 -0.0037 0.0342  11  TYR   C CE2 
1139 C CZ  . TYR   B 5   ? 0.1896 0.2020 0.2690 -0.0018 -0.0033 0.0369  11  TYR   C CZ  
1140 O OH  . TYR   B 5   ? 0.2263 0.2432 0.3068 -0.0021 -0.0081 0.0377  11  TYR   C OH  
1141 N N   . VAL   B 6   ? 0.2018 0.1868 0.2476 0.0128  0.0265  0.0368  12  VAL   C N   
1142 C CA  . VAL   B 6   ? 0.2154 0.1940 0.2525 0.0175  0.0327  0.0379  12  VAL   C CA  
1143 C C   . VAL   B 6   ? 0.2299 0.2059 0.2722 0.0197  0.0396  0.0411  12  VAL   C C   
1144 O O   . VAL   B 6   ? 0.2111 0.1887 0.2552 0.0197  0.0392  0.0402  12  VAL   C O   
1145 C CB  . VAL   B 6   ? 0.2412 0.2176 0.2630 0.0206  0.0304  0.0341  12  VAL   C CB  
1146 C CG1 . VAL   B 6   ? 0.2464 0.2250 0.2673 0.0205  0.0276  0.0313  12  VAL   C CG1 
1147 C CG2 . VAL   B 6   ? 0.2638 0.2333 0.2747 0.0263  0.0363  0.0353  12  VAL   C CG2 
1148 N N   . GLY   B 7   ? 0.2335 0.2055 0.2798 0.0217  0.0466  0.0451  13  GLY   C N   
1149 C CA  . GLY   B 7   ? 0.2386 0.2078 0.2907 0.0243  0.0543  0.0487  13  GLY   C CA  
1150 C C   . GLY   B 7   ? 0.2335 0.2084 0.3018 0.0201  0.0520  0.0496  13  GLY   C C   
1151 O O   . GLY   B 7   ? 0.2400 0.2200 0.3193 0.0155  0.0466  0.0495  13  GLY   C O   
1152 N N   . ASN   B 8   ? 0.2268 0.2009 0.2948 0.0220  0.0548  0.0497  14  ASN   C N   
1153 C CA  . ASN   B 8   ? 0.2218 0.2015 0.3046 0.0185  0.0523  0.0507  14  ASN   C CA  
1154 C C   . ASN   B 8   ? 0.2085 0.1918 0.2857 0.0170  0.0456  0.0467  14  ASN   C C   
1155 O O   . ASN   B 8   ? 0.2013 0.1869 0.2857 0.0164  0.0458  0.0473  14  ASN   C O   
1156 C CB  . ASN   B 8   ? 0.2644 0.2414 0.3562 0.0209  0.0608  0.0547  14  ASN   C CB  
1157 C CG  . ASN   B 8   ? 0.3459 0.3217 0.4513 0.0206  0.0665  0.0596  14  ASN   C CG  
1158 O OD1 . ASN   B 8   ? 0.3665 0.3475 0.4900 0.0165  0.0637  0.0615  14  ASN   C OD1 
1159 N ND2 . ASN   B 8   ? 0.3976 0.3667 0.4945 0.0249  0.0738  0.0615  14  ASN   C ND2 
1160 N N   . TYR   B 9   ? 0.1777 0.1620 0.2448 0.0162  0.0398  0.0431  15  TYR   C N   
1161 C CA  . TYR   B 9   ? 0.1738 0.1614 0.2368 0.0149  0.0338  0.0396  15  TYR   C CA  
1162 C C   . TYR   B 9   ? 0.1681 0.1610 0.2336 0.0110  0.0266  0.0388  15  TYR   C C   
1163 O O   . TYR   B 9   ? 0.1832 0.1755 0.2466 0.0102  0.0254  0.0388  15  TYR   C O   
1164 C CB  . TYR   B 9   ? 0.1963 0.1795 0.2436 0.0185  0.0337  0.0354  15  TYR   C CB  
1165 C CG  . TYR   B 9   ? 0.2051 0.1822 0.2461 0.0235  0.0401  0.0351  15  TYR   C CG  
1166 C CD1 . TYR   B 9   ? 0.2342 0.2115 0.2814 0.0240  0.0425  0.0353  15  TYR   C CD1 
1167 C CD2 . TYR   B 9   ? 0.2516 0.2224 0.2797 0.0282  0.0439  0.0346  15  TYR   C CD2 
1168 C CE1 . TYR   B 9   ? 0.2838 0.2548 0.3242 0.0290  0.0487  0.0345  15  TYR   C CE1 
1169 C CE2 . TYR   B 9   ? 0.2920 0.2565 0.3118 0.0337  0.0497  0.0340  15  TYR   C CE2 
1170 C CZ  . TYR   B 9   ? 0.3246 0.2890 0.3502 0.0340  0.0520  0.0336  15  TYR   C CZ  
1171 O OH  . TYR   B 9   ? 0.3975 0.3552 0.4147 0.0398  0.0582  0.0328  15  TYR   C OH  
1172 N N   . ARG   B 10  ? 0.1550 0.1524 0.2242 0.0091  0.0223  0.0383  16  ARG   C N   
1173 C CA  . ARG   B 10  ? 0.1508 0.1526 0.2195 0.0065  0.0159  0.0374  16  ARG   C CA  
1174 C C   . ARG   B 10  ? 0.1470 0.1489 0.2089 0.0074  0.0141  0.0345  16  ARG   C C   
1175 O O   . ARG   B 10  ? 0.1576 0.1601 0.2235 0.0081  0.0155  0.0347  16  ARG   C O   
1176 C CB  . ARG   B 10  ? 0.1533 0.1605 0.2339 0.0040  0.0129  0.0403  16  ARG   C CB  
1177 C CG  . ARG   B 10  ? 0.1632 0.1747 0.2420 0.0025  0.0069  0.0399  16  ARG   C CG  
1178 C CD  . ARG   B 10  ? 0.1691 0.1855 0.2585 0.0009  0.0035  0.0429  16  ARG   C CD  
1179 N NE  . ARG   B 10  ? 0.1750 0.1951 0.2639 0.0010  0.0002  0.0441  16  ARG   C NE  
1180 C CZ  . ARG   B 10  ? 0.1830 0.2055 0.2665 0.0008  -0.0047 0.0439  16  ARG   C CZ  
1181 N NH1 . ARG   B 10  ? 0.2094 0.2308 0.2871 0.0001  -0.0075 0.0414  16  ARG   C NH1 
1182 N NH2 . ARG   B 10  ? 0.1950 0.2203 0.2781 0.0017  -0.0060 0.0459  16  ARG   C NH2 
1183 N N   . VAL   B 11  ? 0.1398 0.1414 0.1935 0.0074  0.0112  0.0321  17  VAL   C N   
1184 C CA  . VAL   B 11  ? 0.1373 0.1392 0.1867 0.0082  0.0094  0.0292  17  VAL   C CA  
1185 C C   . VAL   B 11  ? 0.1416 0.1478 0.1929 0.0062  0.0056  0.0303  17  VAL   C C   
1186 O O   . VAL   B 11  ? 0.1523 0.1590 0.1998 0.0053  0.0033  0.0303  17  VAL   C O   
1187 C CB  . VAL   B 11  ? 0.1574 0.1553 0.1962 0.0103  0.0092  0.0257  17  VAL   C CB  
1188 C CG1 . VAL   B 11  ? 0.1806 0.1788 0.2182 0.0112  0.0072  0.0225  17  VAL   C CG1 
1189 C CG2 . VAL   B 11  ? 0.1886 0.1813 0.2225 0.0133  0.0135  0.0254  17  VAL   C CG2 
1190 N N   . VAL   B 12  ? 0.1301 0.1389 0.1867 0.0060  0.0051  0.0312  18  VAL   C N   
1191 C CA  A VAL   B 12  ? 0.1244 0.1369 0.1821 0.0050  0.0024  0.0331  18  VAL   C CA  
1192 C CA  B VAL   B 12  ? 0.1496 0.1621 0.2072 0.0050  0.0024  0.0332  18  VAL   C CA  
1193 C C   . VAL   B 12  ? 0.1381 0.1511 0.1980 0.0058  0.0030  0.0321  18  VAL   C C   
1194 O O   . VAL   B 12  ? 0.1419 0.1529 0.2045 0.0068  0.0047  0.0297  18  VAL   C O   
1195 C CB  A VAL   B 12  ? 0.1141 0.1303 0.1791 0.0041  0.0016  0.0374  18  VAL   C CB  
1196 C CB  B VAL   B 12  ? 0.1960 0.2120 0.2615 0.0041  0.0019  0.0374  18  VAL   C CB  
1197 C CG1 A VAL   B 12  ? 0.1287 0.1453 0.1932 0.0030  -0.0004 0.0381  18  VAL   C CG1 
1198 C CG1 B VAL   B 12  ? 0.2083 0.2278 0.2731 0.0040  -0.0009 0.0400  18  VAL   C CG1 
1199 C CG2 A VAL   B 12  ? 0.0698 0.0863 0.1439 0.0046  0.0046  0.0388  18  VAL   C CG2 
1200 C CG2 B VAL   B 12  ? 0.2391 0.2546 0.3061 0.0032  0.0015  0.0380  18  VAL   C CG2 
1201 N N   . ASN   B 13  ? 0.1295 0.1448 0.1889 0.0057  0.0017  0.0338  19  ASN   C N   
1202 C CA  . ASN   B 13  ? 0.1268 0.1430 0.1918 0.0065  0.0031  0.0340  19  ASN   C CA  
1203 C C   . ASN   B 13  ? 0.1301 0.1480 0.2051 0.0065  0.0051  0.0370  19  ASN   C C   
1204 O O   . ASN   B 13  ? 0.1260 0.1462 0.2026 0.0062  0.0046  0.0409  19  ASN   C O   
1205 C CB  . ASN   B 13  ? 0.1342 0.1525 0.1971 0.0070  0.0028  0.0370  19  ASN   C CB  
1206 C CG  . ASN   B 13  ? 0.1417 0.1583 0.1957 0.0071  0.0012  0.0344  19  ASN   C CG  
1207 O OD1 . ASN   B 13  ? 0.1508 0.1671 0.1976 0.0066  -0.0007 0.0345  19  ASN   C OD1 
1208 N ND2 . ASN   B 13  ? 0.1502 0.1656 0.2060 0.0076  0.0019  0.0317  19  ASN   C ND2 
1209 N N   . ARG   B 14  ? 0.1253 0.1421 0.2075 0.0070  0.0069  0.0349  20  ARG   C N   
1210 C CA  . ARG   B 14  ? 0.1237 0.1416 0.2162 0.0071  0.0092  0.0373  20  ARG   C CA  
1211 C C   . ARG   B 14  ? 0.1440 0.1656 0.2410 0.0074  0.0100  0.0437  20  ARG   C C   
1212 O O   . ARG   B 14  ? 0.1407 0.1643 0.2426 0.0075  0.0108  0.0476  20  ARG   C O   
1213 C CB  . ARG   B 14  ? 0.1379 0.1536 0.2380 0.0077  0.0106  0.0333  20  ARG   C CB  
1214 C CG  . ARG   B 14  ? 0.1293 0.1454 0.2408 0.0079  0.0134  0.0350  20  ARG   C CG  
1215 C CD  . ARG   B 14  ? 0.1319 0.1456 0.2515 0.0085  0.0140  0.0299  20  ARG   C CD  
1216 N NE  . ARG   B 14  ? 0.1360 0.1488 0.2662 0.0088  0.0168  0.0299  20  ARG   C NE  
1217 C CZ  . ARG   B 14  ? 0.1307 0.1457 0.2736 0.0087  0.0196  0.0343  20  ARG   C CZ  
1218 N NH1 . ARG   B 14  ? 0.1521 0.1706 0.2976 0.0086  0.0203  0.0401  20  ARG   C NH1 
1219 N NH2 . ARG   B 14  ? 0.1414 0.1549 0.2945 0.0091  0.0221  0.0333  20  ARG   C NH2 
1220 N N   . HIS   B 15  ? 0.1328 0.1553 0.2276 0.0081  0.0100  0.0451  21  HIS   C N   
1221 C CA  . HIS   B 15  ? 0.1417 0.1671 0.2390 0.0095  0.0115  0.0517  21  HIS   C CA  
1222 C C   . HIS   B 15  ? 0.1503 0.1777 0.2391 0.0099  0.0086  0.0550  21  HIS   C C   
1223 O O   . HIS   B 15  ? 0.1744 0.2041 0.2642 0.0117  0.0092  0.0606  21  HIS   C O   
1224 C CB  . HIS   B 15  ? 0.1553 0.1807 0.2536 0.0108  0.0138  0.0531  21  HIS   C CB  
1225 C CG  . HIS   B 15  ? 0.1417 0.1662 0.2277 0.0110  0.0117  0.0515  21  HIS   C CG  
1226 N ND1 . HIS   B 15  ? 0.1501 0.1724 0.2326 0.0099  0.0100  0.0456  21  HIS   C ND1 
1227 C CD2 . HIS   B 15  ? 0.1620 0.1873 0.2388 0.0128  0.0113  0.0552  21  HIS   C CD2 
1228 C CE1 . HIS   B 15  ? 0.1670 0.1890 0.2393 0.0106  0.0090  0.0461  21  HIS   C CE1 
1229 N NE2 . HIS   B 15  ? 0.1605 0.1841 0.2288 0.0124  0.0097  0.0515  21  HIS   C NE2 
1230 N N   . LEU   B 16  ? 0.1318 0.1581 0.2131 0.0086  0.0053  0.0517  22  LEU   C N   
1231 C CA  . LEU   B 16  ? 0.1457 0.1737 0.2208 0.0087  0.0015  0.0534  22  LEU   C CA  
1232 C C   . LEU   B 16  ? 0.1546 0.1832 0.2356 0.0073  0.0005  0.0532  22  LEU   C C   
1233 O O   . LEU   B 16  ? 0.1632 0.1932 0.2418 0.0069  -0.0031 0.0538  22  LEU   C O   
1234 C CB  . LEU   B 16  ? 0.1534 0.1798 0.2172 0.0083  -0.0012 0.0501  22  LEU   C CB  
1235 C CG  . LEU   B 16  ? 0.1653 0.1911 0.2233 0.0100  0.0001  0.0509  22  LEU   C CG  
1236 C CD1 . LEU   B 16  ? 0.1759 0.1996 0.2232 0.0095  -0.0024 0.0471  22  LEU   C CD1 
1237 C CD2 . LEU   B 16  ? 0.1804 0.2084 0.2365 0.0128  0.0004  0.0567  22  LEU   C CD2 
1238 N N   . ALA   B 17  ? 0.1506 0.1778 0.2396 0.0067  0.0038  0.0518  23  ALA   C N   
1239 C CA  . ALA   B 17  ? 0.1430 0.1701 0.2379 0.0058  0.0042  0.0518  23  ALA   C CA  
1240 C C   . ALA   B 17  ? 0.1561 0.1871 0.2578 0.0063  0.0028  0.0571  23  ALA   C C   
1241 O O   . ALA   B 17  ? 0.1737 0.2069 0.2787 0.0078  0.0035  0.0612  23  ALA   C O   
1242 C CB  . ALA   B 17  ? 0.1704 0.1946 0.2712 0.0059  0.0083  0.0492  23  ALA   C CB  
1243 N N   . THR   B 18  ? 0.1639 0.1959 0.2684 0.0054  0.0007  0.0574  24  THR   C N   
1244 C CA  . THR   B 18  ? 0.1675 0.2036 0.2795 0.0060  -0.0018 0.0621  24  THR   C CA  
1245 C C   . THR   B 18  ? 0.1520 0.1881 0.2768 0.0059  0.0024  0.0639  24  THR   C C   
1246 O O   . THR   B 18  ? 0.1625 0.1951 0.2891 0.0055  0.0070  0.0611  24  THR   C O   
1247 C CB  . THR   B 18  ? 0.1785 0.2159 0.2897 0.0049  -0.0069 0.0610  24  THR   C CB  
1248 O OG1 . THR   B 18  ? 0.1846 0.2193 0.3006 0.0033  -0.0038 0.0585  24  THR   C OG1 
1249 C CG2 . THR   B 18  ? 0.1980 0.2345 0.2965 0.0048  -0.0111 0.0581  24  THR   C CG2 
1250 N N   . HIS   B 19  ? 0.1806 0.2207 0.3143 0.0067  0.0007  0.0689  25  HIS   C N   
1251 C CA  . HIS   B 19  ? 0.1866 0.2269 0.3335 0.0067  0.0047  0.0710  25  HIS   C CA  
1252 C C   . HIS   B 19  ? 0.1473 0.1850 0.2973 0.0052  0.0067  0.0679  25  HIS   C C   
1253 O O   . HIS   B 19  ? 0.1731 0.2074 0.3271 0.0054  0.0125  0.0665  25  HIS   C O   
1254 C CB  . HIS   B 19  ? 0.1971 0.2427 0.3537 0.0078  0.0014  0.0768  25  HIS   C CB  
1255 C CG  . HIS   B 19  ? 0.1899 0.2357 0.3614 0.0076  0.0053  0.0789  25  HIS   C CG  
1256 N ND1 . HIS   B 19  ? 0.2250 0.2690 0.4034 0.0084  0.0114  0.0801  25  HIS   C ND1 
1257 C CD2 . HIS   B 19  ? 0.2107 0.2576 0.3914 0.0065  0.0045  0.0792  25  HIS   C CD2 
1258 C CE1 . HIS   B 19  ? 0.2263 0.2707 0.4172 0.0081  0.0140  0.0818  25  HIS   C CE1 
1259 N NE2 . HIS   B 19  ? 0.2176 0.2637 0.4107 0.0070  0.0104  0.0814  25  HIS   C NE2 
1260 N N   . ASN   B 20  ? 0.1575 0.1960 0.3048 0.0040  0.0025  0.0665  26  ASN   C N   
1261 C CA  . ASN   B 20  ? 0.1746 0.2099 0.3254 0.0030  0.0057  0.0644  26  ASN   C CA  
1262 C C   . ASN   B 20  ? 0.1604 0.1899 0.3019 0.0033  0.0108  0.0601  26  ASN   C C   
1263 O O   . ASN   B 20  ? 0.1565 0.1823 0.3011 0.0039  0.0164  0.0592  26  ASN   C O   
1264 C CB  . ASN   B 20  ? 0.1905 0.2274 0.3415 0.0016  0.0004  0.0634  26  ASN   C CB  
1265 C CG  . ASN   B 20  ? 0.2757 0.3098 0.4343 0.0007  0.0048  0.0627  26  ASN   C CG  
1266 O OD1 . ASN   B 20  ? 0.3049 0.3402 0.4776 0.0008  0.0074  0.0657  26  ASN   C OD1 
1267 N ND2 . ASN   B 20  ? 0.2913 0.3213 0.4414 0.0003  0.0064  0.0592  26  ASN   C ND2 
1268 N N   . ASP   B 21  ? 0.1476 0.1758 0.2769 0.0035  0.0090  0.0572  27  ASP   C N   
1269 C CA  . ASP   B 21  ? 0.1525 0.1755 0.2734 0.0042  0.0129  0.0529  27  ASP   C CA  
1270 C C   . ASP   B 21  ? 0.1356 0.1562 0.2614 0.0056  0.0180  0.0525  27  ASP   C C   
1271 O O   . ASP   B 21  ? 0.1503 0.1663 0.2738 0.0067  0.0223  0.0498  27  ASP   C O   
1272 C CB  . ASP   B 21  ? 0.1495 0.1722 0.2593 0.0042  0.0099  0.0504  27  ASP   C CB  
1273 C CG  . ASP   B 21  ? 0.1582 0.1813 0.2604 0.0032  0.0059  0.0490  27  ASP   C CG  
1274 O OD1 . ASP   B 21  ? 0.1775 0.1985 0.2798 0.0027  0.0068  0.0480  27  ASP   C OD1 
1275 O OD2 . ASP   B 21  ? 0.1646 0.1897 0.2613 0.0032  0.0022  0.0493  27  ASP   C OD2 
1276 N N   . TRP   B 22  ? 0.1394 0.1630 0.2718 0.0058  0.0176  0.0553  28  TRP   C N   
1277 C CA  . TRP   B 22  ? 0.1376 0.1590 0.2765 0.0070  0.0223  0.0546  28  TRP   C CA  
1278 C C   . TRP   B 22  ? 0.1377 0.1579 0.2860 0.0076  0.0266  0.0565  28  TRP   C C   
1279 O O   . TRP   B 22  ? 0.1626 0.1783 0.3113 0.0090  0.0314  0.0536  28  TRP   C O   
1280 C CB  . TRP   B 22  ? 0.1493 0.1741 0.2947 0.0073  0.0215  0.0579  28  TRP   C CB  
1281 C CG  . TRP   B 22  ? 0.1450 0.1689 0.2836 0.0074  0.0201  0.0553  28  TRP   C CG  
1282 C CD1 . TRP   B 22  ? 0.1693 0.1960 0.3022 0.0071  0.0165  0.0570  28  TRP   C CD1 
1283 C CD2 . TRP   B 22  ? 0.1348 0.1548 0.2727 0.0080  0.0224  0.0502  28  TRP   C CD2 
1284 N NE1 . TRP   B 22  ? 0.1617 0.1867 0.2919 0.0075  0.0171  0.0541  28  TRP   C NE1 
1285 C CE2 . TRP   B 22  ? 0.1560 0.1771 0.2900 0.0078  0.0202  0.0497  28  TRP   C CE2 
1286 C CE3 . TRP   B 22  ? 0.1730 0.1885 0.3140 0.0090  0.0259  0.0459  28  TRP   C CE3 
1287 C CZ2 . TRP   B 22  ? 0.1526 0.1711 0.2877 0.0082  0.0210  0.0451  28  TRP   C CZ2 
1288 C CZ3 . TRP   B 22  ? 0.1777 0.1904 0.3183 0.0096  0.0260  0.0407  28  TRP   C CZ3 
1289 C CH2 . TRP   B 22  ? 0.1677 0.1822 0.3064 0.0090  0.0234  0.0404  28  TRP   C CH2 
1290 N N   . ALA   B 23  ? 0.1442 0.1680 0.2991 0.0067  0.0248  0.0606  29  ALA   C N   
1291 C CA  . ALA   B 23  ? 0.1431 0.1664 0.3092 0.0072  0.0291  0.0630  29  ALA   C CA  
1292 C C   . ALA   B 23  ? 0.1721 0.1900 0.3331 0.0080  0.0336  0.0603  29  ALA   C C   
1293 O O   . ALA   B 23  ? 0.1813 0.1970 0.3501 0.0091  0.0391  0.0619  29  ALA   C O   
1294 C CB  . ALA   B 23  ? 0.1580 0.1873 0.3349 0.0060  0.0249  0.0682  29  ALA   C CB  
1295 N N   . ASN   B 24  ? 0.1752 0.1907 0.3231 0.0078  0.0316  0.0566  30  ASN   C N   
1296 C CA  . ASN   B 24  ? 0.1671 0.1771 0.3078 0.0092  0.0359  0.0544  30  ASN   C CA  
1297 C C   . ASN   B 24  ? 0.1727 0.1779 0.2979 0.0108  0.0359  0.0487  30  ASN   C C   
1298 O O   . ASN   B 24  ? 0.1685 0.1710 0.2835 0.0114  0.0356  0.0466  30  ASN   C O   
1299 C CB  . ASN   B 24  ? 0.1837 0.1960 0.3260 0.0073  0.0326  0.0560  30  ASN   C CB  
1300 C CG  . ASN   B 24  ? 0.1983 0.2148 0.3575 0.0061  0.0325  0.0608  30  ASN   C CG  
1301 O OD1 . ASN   B 24  ? 0.2247 0.2386 0.3921 0.0074  0.0389  0.0629  30  ASN   C OD1 
1302 N ND2 . ASN   B 24  ? 0.2100 0.2327 0.3752 0.0043  0.0257  0.0629  30  ASN   C ND2 
1303 N N   . LEU   B 25  ? 0.1798 0.1844 0.3042 0.0115  0.0357  0.0464  31  LEU   C N   
1304 C CA  . LEU   B 25  ? 0.1724 0.1734 0.2845 0.0129  0.0343  0.0406  31  LEU   C CA  
1305 C C   . LEU   B 25  ? 0.1979 0.1917 0.2992 0.0163  0.0385  0.0366  31  LEU   C C   
1306 O O   . LEU   B 25  ? 0.2100 0.2000 0.3138 0.0187  0.0442  0.0368  31  LEU   C O   
1307 C CB  . LEU   B 25  ? 0.1805 0.1827 0.2988 0.0128  0.0337  0.0393  31  LEU   C CB  
1308 C CG  . LEU   B 25  ? 0.1827 0.1823 0.2926 0.0137  0.0311  0.0333  31  LEU   C CG  
1309 C CD1 . LEU   B 25  ? 0.1825 0.1855 0.2869 0.0118  0.0258  0.0336  31  LEU   C CD1 
1310 C CD2 . LEU   B 25  ? 0.2017 0.2016 0.3207 0.0138  0.0315  0.0317  31  LEU   C CD2 
1311 N N   . VAL   B 26  ? 0.1785 0.1700 0.2671 0.0172  0.0359  0.0328  32  VAL   C N   
1312 C CA  . VAL   B 26  ? 0.1970 0.1813 0.2724 0.0214  0.0388  0.0285  32  VAL   C CA  
1313 C C   . VAL   B 26  ? 0.2065 0.1892 0.2763 0.0227  0.0350  0.0220  32  VAL   C C   
1314 O O   . VAL   B 26  ? 0.2347 0.2119 0.2994 0.0263  0.0372  0.0175  32  VAL   C O   
1315 C CB  . VAL   B 26  ? 0.2170 0.1998 0.2826 0.0221  0.0386  0.0293  32  VAL   C CB  
1316 C CG1 . VAL   B 26  ? 0.2500 0.2254 0.2996 0.0272  0.0407  0.0248  32  VAL   C CG1 
1317 C CG2 . VAL   B 26  ? 0.2179 0.2019 0.2915 0.0210  0.0427  0.0352  32  VAL   C CG2 
1318 N N   . TRP   B 27  ? 0.1854 0.1724 0.2565 0.0200  0.0292  0.0211  33  TRP   C N   
1319 C CA  . TRP   B 27  ? 0.1870 0.1726 0.2549 0.0210  0.0253  0.0149  33  TRP   C CA  
1320 C C   . TRP   B 27  ? 0.1777 0.1694 0.2529 0.0174  0.0209  0.0165  33  TRP   C C   
1321 O O   . TRP   B 27  ? 0.1747 0.1699 0.2493 0.0152  0.0196  0.0207  33  TRP   C O   
1322 C CB  . TRP   B 27  ? 0.2233 0.2039 0.2750 0.0245  0.0237  0.0102  33  TRP   C CB  
1323 C CG  . TRP   B 27  ? 0.2291 0.2093 0.2779 0.0253  0.0180  0.0038  33  TRP   C CG  
1324 C CD1 . TRP   B 27  ? 0.2604 0.2370 0.3087 0.0279  0.0162  -0.0030 33  TRP   C CD1 
1325 C CD2 . TRP   B 27  ? 0.2101 0.1935 0.2576 0.0234  0.0131  0.0033  33  TRP   C CD2 
1326 N NE1 . TRP   B 27  ? 0.2709 0.2486 0.3183 0.0278  0.0101  -0.0078 33  TRP   C NE1 
1327 C CE2 . TRP   B 27  ? 0.2356 0.2174 0.2825 0.0251  0.0086  -0.0036 33  TRP   C CE2 
1328 C CE3 . TRP   B 27  ? 0.2030 0.1904 0.2504 0.0206  0.0121  0.0078  33  TRP   C CE3 
1329 C CZ2 . TRP   B 27  ? 0.2299 0.2142 0.2769 0.0241  0.0036  -0.0056 33  TRP   C CZ2 
1330 C CZ3 . TRP   B 27  ? 0.2226 0.2116 0.2676 0.0200  0.0076  0.0056  33  TRP   C CZ3 
1331 C CH2 . TRP   B 27  ? 0.2311 0.2189 0.2771 0.0215  0.0037  -0.0005 33  TRP   C CH2 
1332 N N   . GLU   B 28  ? 0.1667 0.1591 0.2485 0.0170  0.0187  0.0133  34  GLU   C N   
1333 C CA  . GLU   B 28  ? 0.1766 0.1740 0.2651 0.0144  0.0156  0.0152  34  GLU   C CA  
1334 C C   . GLU   B 28  ? 0.1694 0.1655 0.2613 0.0152  0.0127  0.0091  34  GLU   C C   
1335 O O   . GLU   B 28  ? 0.1763 0.1687 0.2709 0.0171  0.0132  0.0041  34  GLU   C O   
1336 C CB  . GLU   B 28  ? 0.1785 0.1807 0.2791 0.0121  0.0175  0.0217  34  GLU   C CB  
1337 C CG  . GLU   B 28  ? 0.1884 0.1897 0.3003 0.0126  0.0208  0.0217  34  GLU   C CG  
1338 C CD  . GLU   B 28  ? 0.1966 0.1979 0.3187 0.0126  0.0199  0.0184  34  GLU   C CD  
1339 O OE1 . GLU   B 28  ? 0.2266 0.2252 0.3557 0.0137  0.0221  0.0156  34  GLU   C OE1 
1340 O OE2 . GLU   B 28  ? 0.1920 0.1960 0.3171 0.0114  0.0177  0.0191  34  GLU   C OE2 
1341 N N   . ASP   B 29  ? 0.1548 0.1539 0.2484 0.0138  0.0097  0.0093  35  ASP   C N   
1342 C CA  . ASP   B 29  ? 0.1638 0.1623 0.2643 0.0142  0.0067  0.0039  35  ASP   C CA  
1343 C C   . ASP   B 29  ? 0.1645 0.1678 0.2738 0.0120  0.0064  0.0082  35  ASP   C C   
1344 O O   . ASP   B 29  ? 0.1573 0.1623 0.2597 0.0114  0.0050  0.0100  35  ASP   C O   
1345 C CB  . ASP   B 29  ? 0.1883 0.1830 0.2765 0.0168  0.0027  -0.0028 35  ASP   C CB  
1346 C CG  . ASP   B 29  ? 0.2370 0.2309 0.3319 0.0177  -0.0018 -0.0096 35  ASP   C CG  
1347 O OD1 . ASP   B 29  ? 0.2378 0.2354 0.3461 0.0155  -0.0020 -0.0079 35  ASP   C OD1 
1348 O OD2 . ASP   B 29  ? 0.2883 0.2780 0.3748 0.0208  -0.0054 -0.0167 35  ASP   C OD2 
1349 N N   . SER   B 30  ? 0.1538 0.1591 0.2787 0.0110  0.0085  0.0100  36  SER   C N   
1350 C CA  A SER   B 30  ? 0.1581 0.1674 0.2920 0.0097  0.0097  0.0150  36  SER   C CA  
1351 C CA  B SER   B 30  ? 0.1632 0.1726 0.2965 0.0097  0.0097  0.0151  36  SER   C CA  
1352 C C   . SER   B 30  ? 0.1627 0.1720 0.2978 0.0099  0.0065  0.0110  36  SER   C C   
1353 O O   . SER   B 30  ? 0.1645 0.1764 0.2978 0.0093  0.0071  0.0152  36  SER   C O   
1354 C CB  A SER   B 30  ? 0.1659 0.1764 0.3177 0.0093  0.0131  0.0174  36  SER   C CB  
1355 C CB  B SER   B 30  ? 0.1896 0.2005 0.3397 0.0092  0.0135  0.0187  36  SER   C CB  
1356 O OG  A SER   B 30  ? 0.1672 0.1808 0.3284 0.0087  0.0150  0.0220  36  SER   C OG  
1357 O OG  B SER   B 30  ? 0.2080 0.2161 0.3686 0.0098  0.0124  0.0119  36  SER   C OG  
1358 N N   . SER   B 31  ? 0.1639 0.1701 0.3009 0.0110  0.0027  0.0027  37  SER   C N   
1359 C CA  . SER   B 31  ? 0.1730 0.1796 0.3130 0.0113  -0.0010 -0.0014 37  SER   C CA  
1360 C C   . SER   B 31  ? 0.1677 0.1745 0.2918 0.0117  -0.0030 -0.0004 37  SER   C C   
1361 O O   . SER   B 31  ? 0.1723 0.1806 0.2994 0.0115  -0.0045 -0.0007 37  SER   C O   
1362 C CB  . SER   B 31  ? 0.2220 0.2254 0.3666 0.0130  -0.0060 -0.0111 37  SER   C CB  
1363 O OG  . SER   B 31  ? 0.2940 0.2935 0.4210 0.0153  -0.0092 -0.0160 37  SER   C OG  
1364 N N   . ARG   B 32  ? 0.1603 0.1654 0.2687 0.0123  -0.0025 0.0009  38  ARG   C N   
1365 C CA  . ARG   B 32  ? 0.1559 0.1608 0.2499 0.0126  -0.0039 0.0021  38  ARG   C CA  
1366 C C   . ARG   B 32  ? 0.1397 0.1475 0.2304 0.0109  -0.0006 0.0098  38  ARG   C C   
1367 O O   . ARG   B 32  ? 0.1433 0.1511 0.2235 0.0109  -0.0014 0.0110  38  ARG   C O   
1368 C CB  . ARG   B 32  ? 0.1865 0.1872 0.2660 0.0148  -0.0051 -0.0013 38  ARG   C CB  
1369 C CG  . ARG   B 32  ? 0.2088 0.2060 0.2870 0.0176  -0.0094 -0.0095 38  ARG   C CG  
1370 C CD  . ARG   B 32  ? 0.1829 0.1752 0.2452 0.0208  -0.0096 -0.0121 38  ARG   C CD  
1371 N NE  . ARG   B 32  ? 0.1850 0.1767 0.2343 0.0216  -0.0099 -0.0099 38  ARG   C NE  
1372 C CZ  . ARG   B 32  ? 0.1887 0.1761 0.2236 0.0253  -0.0114 -0.0128 38  ARG   C CZ  
1373 N NH1 . ARG   B 32  ? 0.2180 0.2010 0.2477 0.0290  -0.0129 -0.0183 38  ARG   C NH1 
1374 N NH2 . ARG   B 32  ? 0.1948 0.1821 0.2203 0.0257  -0.0115 -0.0104 38  ARG   C NH2 
1375 N N   . ASP   B 33  ? 0.1289 0.1389 0.2275 0.0098  0.0028  0.0147  39  ASP   C N   
1376 C CA  . ASP   B 33  ? 0.1271 0.1395 0.2212 0.0088  0.0050  0.0214  39  ASP   C CA  
1377 C C   . ASP   B 33  ? 0.1331 0.1439 0.2151 0.0088  0.0043  0.0215  39  ASP   C C   
1378 O O   . ASP   B 33  ? 0.1362 0.1483 0.2113 0.0082  0.0040  0.0247  39  ASP   C O   
1379 C CB  . ASP   B 33  ? 0.1286 0.1431 0.2213 0.0086  0.0052  0.0245  39  ASP   C CB  
1380 C CG  . ASP   B 33  ? 0.1423 0.1591 0.2302 0.0083  0.0069  0.0310  39  ASP   C CG  
1381 O OD1 . ASP   B 33  ? 0.1536 0.1718 0.2463 0.0082  0.0087  0.0348  39  ASP   C OD1 
1382 O OD2 . ASP   B 33  ? 0.1476 0.1647 0.2272 0.0084  0.0061  0.0323  39  ASP   C OD2 
1383 N N   . LEU   B 34  ? 0.1269 0.1348 0.2067 0.0097  0.0044  0.0184  40  LEU   C N   
1384 C CA  . LEU   B 34  ? 0.1362 0.1424 0.2065 0.0100  0.0050  0.0194  40  LEU   C CA  
1385 C C   . LEU   B 34  ? 0.1387 0.1446 0.2141 0.0100  0.0079  0.0215  40  LEU   C C   
1386 O O   . LEU   B 34  ? 0.1370 0.1419 0.2196 0.0107  0.0091  0.0195  40  LEU   C O   
1387 C CB  . LEU   B 34  ? 0.1501 0.1520 0.2109 0.0121  0.0035  0.0141  40  LEU   C CB  
1388 C CG  . LEU   B 34  ? 0.1588 0.1605 0.2123 0.0124  0.0007  0.0125  40  LEU   C CG  
1389 C CD1 . LEU   B 34  ? 0.1895 0.1865 0.2326 0.0155  -0.0007 0.0076  40  LEU   C CD1 
1390 C CD2 . LEU   B 34  ? 0.1606 0.1641 0.2095 0.0108  0.0011  0.0168  40  LEU   C CD2 
1391 N N   . LEU   B 35  ? 0.1289 0.1354 0.2010 0.0093  0.0089  0.0249  41  LEU   C N   
1392 C CA  . LEU   B 35  ? 0.1443 0.1502 0.2209 0.0095  0.0119  0.0270  41  LEU   C CA  
1393 C C   . LEU   B 35  ? 0.1349 0.1390 0.2047 0.0097  0.0128  0.0280  41  LEU   C C   
1394 O O   . LEU   B 35  ? 0.1463 0.1518 0.2119 0.0086  0.0107  0.0293  41  LEU   C O   
1395 C CB  . LEU   B 35  ? 0.1408 0.1514 0.2275 0.0079  0.0123  0.0325  41  LEU   C CB  
1396 C CG  . LEU   B 35  ? 0.1416 0.1524 0.2358 0.0080  0.0153  0.0353  41  LEU   C CG  
1397 C CD1 . LEU   B 35  ? 0.1698 0.1839 0.2755 0.0076  0.0162  0.0390  41  LEU   C CD1 
1398 C CD2 . LEU   B 35  ? 0.1520 0.1642 0.2446 0.0070  0.0147  0.0386  41  LEU   C CD2 
1399 N N   . VAL   B 36  ? 0.1409 0.1414 0.2102 0.0115  0.0164  0.0273  42  VAL   C N   
1400 C CA  . VAL   B 36  ? 0.1481 0.1463 0.2135 0.0122  0.0189  0.0290  42  VAL   C CA  
1401 C C   . VAL   B 36  ? 0.1508 0.1499 0.2260 0.0118  0.0226  0.0329  42  VAL   C C   
1402 O O   . VAL   B 36  ? 0.1640 0.1617 0.2436 0.0131  0.0253  0.0321  42  VAL   C O   
1403 C CB  . VAL   B 36  ? 0.1614 0.1535 0.2155 0.0158  0.0210  0.0252  42  VAL   C CB  
1404 C CG1 . VAL   B 36  ? 0.1907 0.1798 0.2418 0.0169  0.0251  0.0280  42  VAL   C CG1 
1405 C CG2 . VAL   B 36  ? 0.1743 0.1658 0.2195 0.0163  0.0168  0.0214  42  VAL   C CG2 
1406 N N   . SER   B 37  ? 0.1467 0.1482 0.2268 0.0101  0.0225  0.0367  43  SER   C N   
1407 C CA  . SER   B 37  ? 0.1466 0.1493 0.2381 0.0097  0.0257  0.0408  43  SER   C CA  
1408 C C   . SER   B 37  ? 0.1501 0.1496 0.2410 0.0106  0.0296  0.0423  43  SER   C C   
1409 O O   . SER   B 37  ? 0.1662 0.1635 0.2485 0.0111  0.0290  0.0408  43  SER   C O   
1410 C CB  . SER   B 37  ? 0.1389 0.1481 0.2402 0.0069  0.0214  0.0444  43  SER   C CB  
1411 O OG  . SER   B 37  ? 0.1658 0.1771 0.2639 0.0052  0.0170  0.0445  43  SER   C OG  
1412 N N   . SER   B 38  ? 0.1675 0.1664 0.2681 0.0113  0.0345  0.0454  44  SER   C N   
1413 C CA  . SER   B 38  ? 0.1842 0.1799 0.2872 0.0123  0.0395  0.0478  44  SER   C CA  
1414 C C   . SER   B 38  ? 0.2144 0.2152 0.3298 0.0089  0.0358  0.0509  44  SER   C C   
1415 O O   . SER   B 38  ? 0.2243 0.2309 0.3486 0.0064  0.0309  0.0523  44  SER   C O   
1416 C CB  . SER   B 38  ? 0.2090 0.2009 0.3170 0.0152  0.0475  0.0498  44  SER   C CB  
1417 O OG  . SER   B 38  ? 0.2572 0.2539 0.3802 0.0132  0.0466  0.0527  44  SER   C OG  
1418 N N   . THR   B 39  ? 0.2045 0.2030 0.3209 0.0091  0.0383  0.0520  45  THR   C N   
1419 C CA  . THR   B 39  ? 0.2213 0.2237 0.3499 0.0060  0.0344  0.0539  45  THR   C CA  
1420 C C   . THR   B 39  ? 0.2513 0.2515 0.3938 0.0069  0.0417  0.0579  45  THR   C C   
1421 O O   . THR   B 39  ? 0.2381 0.2321 0.3751 0.0104  0.0501  0.0591  45  THR   C O   
1422 C CB  . THR   B 39  ? 0.2263 0.2280 0.3458 0.0049  0.0303  0.0511  45  THR   C CB  
1423 O OG1 . THR   B 39  ? 0.2427 0.2380 0.3541 0.0079  0.0369  0.0512  45  THR   C OG1 
1424 C CG2 . THR   B 39  ? 0.2275 0.2311 0.3339 0.0043  0.0240  0.0474  45  THR   C CG2 
1425 N N   . THR   B 40  ? 0.2664 0.2714 0.4264 0.0039  0.0382  0.0600  46  THR   C N   
1426 C CA  . THR   B 40  ? 0.2896 0.2928 0.4662 0.0043  0.0448  0.0641  46  THR   C CA  
1427 C C   . THR   B 40  ? 0.2999 0.2994 0.4743 0.0045  0.0471  0.0637  46  THR   C C   
1428 O O   . THR   B 40  ? 0.3303 0.3240 0.5064 0.0074  0.0568  0.0668  46  THR   C O   
1429 C CB  . THR   B 40  ? 0.3403 0.3504 0.5388 0.0013  0.0396  0.0661  46  THR   C CB  
1430 O OG1 . THR   B 40  ? 0.3867 0.4015 0.5851 -0.0019 0.0289  0.0629  46  THR   C OG1 
1431 C CG2 . THR   B 40  ? 0.3392 0.3526 0.5395 0.0017  0.0384  0.0672  46  THR   C CG2 
1432 N N   . ALA   B 41  ? 0.2760 0.2779 0.4454 0.0020  0.0387  0.0601  47  ALA   C N   
1433 C CA  . ALA   B 41  ? 0.2905 0.2889 0.4579 0.0020  0.0403  0.0594  47  ALA   C CA  
1434 C C   . ALA   B 41  ? 0.2902 0.2831 0.4349 0.0050  0.0432  0.0574  47  ALA   C C   
1435 O O   . ALA   B 41  ? 0.2861 0.2801 0.4166 0.0054  0.0392  0.0544  47  ALA   C O   
1436 C CB  . ALA   B 41  ? 0.3090 0.3121 0.4825 -0.0020 0.0300  0.0560  47  ALA   C CB  
1437 N N   . GLN   B 42  ? 0.2895 0.2770 0.4316 0.0071  0.0494  0.0588  48  GLN   C N   
1438 C CA  . GLN   B 42  ? 0.2929 0.2754 0.4142 0.0104  0.0514  0.0571  48  GLN   C CA  
1439 C C   . GLN   B 42  ? 0.2728 0.2579 0.3875 0.0076  0.0427  0.0527  48  GLN   C C   
1440 O O   . GLN   B 42  ? 0.2942 0.2820 0.4206 0.0042  0.0383  0.0518  48  GLN   C O   
1441 C CB  . GLN   B 42  ? 0.3590 0.3343 0.4795 0.0145  0.0618  0.0612  48  GLN   C CB  
1442 C CG  . GLN   B 42  ? 0.4736 0.4446 0.5940 0.0189  0.0717  0.0652  48  GLN   C CG  
1443 C CD  . GLN   B 42  ? 0.6140 0.5772 0.7290 0.0241  0.0821  0.0694  48  GLN   C CD  
1444 O OE1 . GLN   B 42  ? 0.6487 0.6108 0.7790 0.0233  0.0868  0.0732  48  GLN   C OE1 
1445 N NE2 . GLN   B 42  ? 0.6561 0.6137 0.7493 0.0297  0.0857  0.0687  48  GLN   C NE2 
1446 N N   . GLY   B 43  ? 0.2362 0.2202 0.3324 0.0092  0.0401  0.0495  49  GLY   C N   
1447 C CA  . GLY   B 43  ? 0.2296 0.2152 0.3171 0.0074  0.0332  0.0456  49  GLY   C CA  
1448 C C   . GLY   B 43  ? 0.2331 0.2131 0.3107 0.0103  0.0372  0.0459  49  GLY   C C   
1449 O O   . GLY   B 43  ? 0.2715 0.2462 0.3455 0.0145  0.0454  0.0490  49  GLY   C O   
1450 N N   . CYS   B 44  ? 0.2200 0.2010 0.2930 0.0086  0.0320  0.0429  50  CYS   C N   
1451 C CA  . CYS   B 44  ? 0.2392 0.2155 0.3054 0.0108  0.0350  0.0432  50  CYS   C CA  
1452 C C   . CYS   B 44  ? 0.2420 0.2176 0.2921 0.0122  0.0314  0.0399  50  CYS   C C   
1453 O O   . CYS   B 44  ? 0.2690 0.2412 0.3139 0.0138  0.0331  0.0401  50  CYS   C O   
1454 C CB  . CYS   B 44  ? 0.2396 0.2166 0.3191 0.0074  0.0333  0.0430  50  CYS   C CB  
1455 S SG  . CYS   B 44  ? 0.3079 0.2853 0.4107 0.0060  0.0381  0.0472  50  CYS   C SG  
1456 N N   . ASP   B 45  ? 0.2093 0.1884 0.2529 0.0114  0.0263  0.0370  51  ASP   C N   
1457 C CA  . ASP   B 45  ? 0.2118 0.1904 0.2420 0.0128  0.0230  0.0340  51  ASP   C CA  
1458 C C   . ASP   B 45  ? 0.2284 0.2021 0.2473 0.0182  0.0278  0.0349  51  ASP   C C   
1459 O O   . ASP   B 45  ? 0.2479 0.2195 0.2669 0.0206  0.0323  0.0369  51  ASP   C O   
1460 C CB  . ASP   B 45  ? 0.2036 0.1871 0.2320 0.0109  0.0172  0.0311  51  ASP   C CB  
1461 C CG  . ASP   B 45  ? 0.2682 0.2561 0.3034 0.0068  0.0118  0.0298  51  ASP   C CG  
1462 O OD1 . ASP   B 45  ? 0.3079 0.2950 0.3446 0.0055  0.0105  0.0291  51  ASP   C OD1 
1463 O OD2 . ASP   B 45  ? 0.2324 0.2244 0.2706 0.0052  0.0086  0.0295  51  ASP   C OD2 
1464 N N   . THR   B 46  ? 0.2109 0.1822 0.2196 0.0205  0.0268  0.0335  52  THR   C N   
1465 C CA  . THR   B 46  ? 0.2233 0.1901 0.2190 0.0262  0.0295  0.0336  52  THR   C CA  
1466 C C   . THR   B 46  ? 0.2115 0.1809 0.2000 0.0263  0.0231  0.0289  52  THR   C C   
1467 O O   . THR   B 46  ? 0.2154 0.1879 0.2049 0.0237  0.0184  0.0267  52  THR   C O   
1468 C CB  . THR   B 46  ? 0.2583 0.2207 0.2484 0.0292  0.0324  0.0355  52  THR   C CB  
1469 O OG1 . THR   B 46  ? 0.2863 0.2460 0.2857 0.0290  0.0391  0.0402  52  THR   C OG1 
1470 C CG2 . THR   B 46  ? 0.2985 0.2562 0.2728 0.0359  0.0339  0.0352  52  THR   C CG2 
1471 N N   . ILE   B 47  ? 0.2253 0.1933 0.2071 0.0296  0.0233  0.0272  53  ILE   C N   
1472 C CA  . ILE   B 47  ? 0.2178 0.1878 0.1948 0.0301  0.0174  0.0226  53  ILE   C CA  
1473 C C   . ILE   B 47  ? 0.2228 0.1894 0.1880 0.0347  0.0159  0.0211  53  ILE   C C   
1474 O O   . ILE   B 47  ? 0.2478 0.2090 0.2037 0.0400  0.0200  0.0230  53  ILE   C O   
1475 C CB  . ILE   B 47  ? 0.2250 0.1944 0.2007 0.0320  0.0177  0.0206  53  ILE   C CB  
1476 C CG1 . ILE   B 47  ? 0.2338 0.2061 0.2212 0.0282  0.0200  0.0229  53  ILE   C CG1 
1477 C CG2 . ILE   B 47  ? 0.2355 0.2072 0.2093 0.0321  0.0113  0.0153  53  ILE   C CG2 
1478 C CD1 . ILE   B 47  ? 0.2482 0.2268 0.2458 0.0224  0.0154  0.0225  53  ILE   C CD1 
1479 N N   . ALA   B 48  ? 0.2051 0.1746 0.1703 0.0334  0.0104  0.0180  54  ALA   C N   
1480 C CA  . ALA   B 48  ? 0.2055 0.1725 0.1608 0.0378  0.0079  0.0163  54  ALA   C CA  
1481 C C   . ALA   B 48  ? 0.2135 0.1779 0.1598 0.0430  0.0058  0.0128  54  ALA   C C   
1482 O O   . ALA   B 48  ? 0.2122 0.1788 0.1630 0.0415  0.0035  0.0097  54  ALA   C O   
1483 C CB  . ALA   B 48  ? 0.1961 0.1675 0.1564 0.0347  0.0024  0.0136  54  ALA   C CB  
1484 N N   . ARG   B 49  ? 0.2184 0.1778 0.1518 0.0494  0.0065  0.0131  55  ARG   C N   
1485 C CA  . ARG   B 49  ? 0.2309 0.1871 0.1531 0.0554  0.0032  0.0088  55  ARG   C CA  
1486 C C   . ARG   B 49  ? 0.2300 0.1858 0.1454 0.0589  -0.0023 0.0065  55  ARG   C C   
1487 O O   . ARG   B 49  ? 0.2563 0.2079 0.1614 0.0639  0.0003  0.0097  55  ARG   C O   
1488 C CB  . ARG   B 49  ? 0.2475 0.1970 0.1582 0.0614  0.0098  0.0116  55  ARG   C CB  
1489 C CG  . ARG   B 49  ? 0.2423 0.1925 0.1621 0.0576  0.0158  0.0144  55  ARG   C CG  
1490 C CD  . ARG   B 49  ? 0.2545 0.2083 0.1824 0.0542  0.0121  0.0099  55  ARG   C CD  
1491 N NE  . ARG   B 49  ? 0.2516 0.2059 0.1883 0.0511  0.0181  0.0134  55  ARG   C NE  
1492 C CZ  . ARG   B 49  ? 0.2364 0.1949 0.1842 0.0466  0.0164  0.0115  55  ARG   C CZ  
1493 N NH1 . ARG   B 49  ? 0.2270 0.1888 0.1782 0.0451  0.0096  0.0061  55  ARG   C NH1 
1494 N NH2 . ARG   B 49  ? 0.2530 0.2123 0.2097 0.0439  0.0217  0.0153  55  ARG   C NH2 
1495 N N   . CYS   B 50  ? 0.2181 0.1786 0.1409 0.0563  -0.0097 0.0015  56  CYS   C N   
1496 C CA  . CYS   B 50  ? 0.2223 0.1843 0.1442 0.0579  -0.0155 -0.0005 56  CYS   C CA  
1497 C C   . CYS   B 50  ? 0.2179 0.1851 0.1509 0.0550  -0.0229 -0.0063 56  CYS   C C   
1498 O O   . CYS   B 50  ? 0.2242 0.1937 0.1656 0.0516  -0.0232 -0.0084 56  CYS   C O   
1499 C CB  . CYS   B 50  ? 0.2162 0.1799 0.1439 0.0541  -0.0118 0.0045  56  CYS   C CB  
1500 S SG  . CYS   B 50  ? 0.2111 0.1812 0.1565 0.0449  -0.0112 0.0048  56  CYS   C SG  
1501 N N   . ASP   B 51  ? 0.2339 0.2029 0.1682 0.0566  -0.0288 -0.0086 57  ASP   C N   
1502 C CA  . ASP   B 51  ? 0.2469 0.2210 0.1949 0.0536  -0.0351 -0.0133 57  ASP   C CA  
1503 C C   . ASP   B 51  ? 0.2230 0.2007 0.1802 0.0496  -0.0339 -0.0102 57  ASP   C C   
1504 O O   . ASP   B 51  ? 0.2437 0.2247 0.2098 0.0492  -0.0391 -0.0132 57  ASP   C O   
1505 C CB  . ASP   B 51  ? 0.2862 0.2595 0.2302 0.0592  -0.0439 -0.0199 57  ASP   C CB  
1506 C CG  . ASP   B 51  ? 0.3374 0.3084 0.2712 0.0648  -0.0468 -0.0191 57  ASP   C CG  
1507 O OD1 . ASP   B 51  ? 0.3293 0.2990 0.2589 0.0644  -0.0413 -0.0131 57  ASP   C OD1 
1508 O OD2 . ASP   B 51  ? 0.4053 0.3762 0.3366 0.0696  -0.0554 -0.0247 57  ASP   C OD2 
1509 N N   . CYS   B 52  ? 0.2096 0.1866 0.1658 0.0467  -0.0271 -0.0045 58  CYS   C N   
1510 C CA  . CYS   B 52  ? 0.2025 0.1824 0.1669 0.0429  -0.0258 -0.0022 58  CYS   C CA  
1511 C C   . CYS   B 52  ? 0.1862 0.1712 0.1652 0.0386  -0.0278 -0.0044 58  CYS   C C   
1512 O O   . CYS   B 52  ? 0.1941 0.1805 0.1782 0.0364  -0.0276 -0.0057 58  CYS   C O   
1513 C CB  . CYS   B 52  ? 0.2042 0.1827 0.1673 0.0398  -0.0188 0.0029  58  CYS   C CB  
1514 S SG  . CYS   B 52  ? 0.2199 0.1925 0.1701 0.0443  -0.0146 0.0070  58  CYS   C SG  
1515 N N   . GLN   B 53  ? 0.1792 0.1665 0.1650 0.0376  -0.0290 -0.0042 59  GLN   C N   
1516 C CA  . GLN   B 53  ? 0.1856 0.1772 0.1856 0.0338  -0.0291 -0.0048 59  GLN   C CA  
1517 C C   . GLN   B 53  ? 0.1613 0.1534 0.1631 0.0311  -0.0245 -0.0011 59  GLN   C C   
1518 O O   . GLN   B 53  ? 0.1665 0.1616 0.1786 0.0290  -0.0239 -0.0008 59  GLN   C O   
1519 C CB  . GLN   B 53  ? 0.1938 0.1880 0.2034 0.0358  -0.0355 -0.0091 59  GLN   C CB  
1520 C CG  . GLN   B 53  ? 0.2576 0.2521 0.2699 0.0375  -0.0406 -0.0142 59  GLN   C CG  
1521 C CD  . GLN   B 53  ? 0.2662 0.2638 0.2921 0.0387  -0.0471 -0.0187 59  GLN   C CD  
1522 O OE1 . GLN   B 53  ? 0.2952 0.2917 0.3168 0.0432  -0.0538 -0.0229 59  GLN   C OE1 
1523 N NE2 . GLN   B 53  ? 0.2420 0.2436 0.2848 0.0350  -0.0452 -0.0179 59  GLN   C NE2 
1524 N N   . THR   B 54  ? 0.1601 0.1490 0.1525 0.0311  -0.0208 0.0020  60  THR   C N   
1525 C CA  . THR   B 54  ? 0.1670 0.1561 0.1611 0.0283  -0.0166 0.0048  60  THR   C CA  
1526 C C   . THR   B 54  ? 0.1740 0.1609 0.1622 0.0263  -0.0128 0.0071  60  THR   C C   
1527 O O   . THR   B 54  ? 0.1885 0.1727 0.1699 0.0282  -0.0124 0.0076  60  THR   C O   
1528 C CB  . THR   B 54  ? 0.2097 0.1971 0.2018 0.0301  -0.0163 0.0056  60  THR   C CB  
1529 O OG1 . THR   B 54  ? 0.2620 0.2456 0.2447 0.0329  -0.0158 0.0068  60  THR   C OG1 
1530 C CG2 . THR   B 54  ? 0.2069 0.1965 0.2061 0.0323  -0.0205 0.0034  60  THR   C CG2 
1531 N N   . GLY   B 55  ? 0.1565 0.1444 0.1475 0.0229  -0.0101 0.0085  61  GLY   C N   
1532 C CA  . GLY   B 55  ? 0.1610 0.1475 0.1487 0.0209  -0.0074 0.0102  61  GLY   C CA  
1533 C C   . GLY   B 55  ? 0.1449 0.1327 0.1351 0.0179  -0.0057 0.0109  61  GLY   C C   
1534 O O   . GLY   B 55  ? 0.1574 0.1457 0.1496 0.0180  -0.0053 0.0106  61  GLY   C O   
1535 N N   . VAL   B 56  ? 0.1490 0.1367 0.1384 0.0158  -0.0046 0.0119  62  VAL   C N   
1536 C CA  . VAL   B 56  ? 0.1310 0.1194 0.1208 0.0136  -0.0038 0.0122  62  VAL   C CA  
1537 C C   . VAL   B 56  ? 0.1358 0.1267 0.1279 0.0120  -0.0043 0.0132  62  VAL   C C   
1538 O O   . VAL   B 56  ? 0.1416 0.1324 0.1343 0.0116  -0.0044 0.0137  62  VAL   C O   
1539 C CB  . VAL   B 56  ? 0.1453 0.1304 0.1322 0.0128  -0.0028 0.0120  62  VAL   C CB  
1540 C CG1 . VAL   B 56  ? 0.1739 0.1593 0.1600 0.0109  -0.0032 0.0114  62  VAL   C CG1 
1541 C CG2 . VAL   B 56  ? 0.1668 0.1491 0.1519 0.0146  -0.0019 0.0115  62  VAL   C CG2 
1542 N N   . TYR   B 57  ? 0.1396 0.1327 0.1329 0.0113  -0.0040 0.0138  63  TYR   C N   
1543 C CA  . TYR   B 57  ? 0.1264 0.1220 0.1219 0.0101  -0.0045 0.0152  63  TYR   C CA  
1544 C C   . TYR   B 57  ? 0.1425 0.1380 0.1343 0.0094  -0.0049 0.0156  63  TYR   C C   
1545 O O   . TYR   B 57  ? 0.1528 0.1467 0.1407 0.0102  -0.0041 0.0148  63  TYR   C O   
1546 C CB  . TYR   B 57  ? 0.1352 0.1337 0.1365 0.0108  -0.0039 0.0163  63  TYR   C CB  
1547 C CG  . TYR   B 57  ? 0.1320 0.1317 0.1342 0.0116  -0.0020 0.0178  63  TYR   C CG  
1548 C CD1 . TYR   B 57  ? 0.1439 0.1426 0.1466 0.0129  -0.0007 0.0171  63  TYR   C CD1 
1549 C CD2 . TYR   B 57  ? 0.1324 0.1339 0.1349 0.0115  -0.0011 0.0203  63  TYR   C CD2 
1550 C CE1 . TYR   B 57  ? 0.1447 0.1440 0.1487 0.0142  0.0022  0.0190  63  TYR   C CE1 
1551 C CE2 . TYR   B 57  ? 0.1422 0.1442 0.1448 0.0131  0.0017  0.0224  63  TYR   C CE2 
1552 C CZ  . TYR   B 57  ? 0.1448 0.1456 0.1484 0.0144  0.0037  0.0218  63  TYR   C CZ  
1553 O OH  . TYR   B 57  ? 0.1756 0.1765 0.1798 0.0165  0.0077  0.0245  63  TYR   C OH  
1554 N N   . TYR   B 58  ? 0.1358 0.1328 0.1289 0.0082  -0.0062 0.0167  64  TYR   C N   
1555 C CA  . TYR   B 58  ? 0.1431 0.1405 0.1325 0.0080  -0.0078 0.0168  64  TYR   C CA  
1556 C C   . TYR   B 58  ? 0.1549 0.1548 0.1439 0.0094  -0.0067 0.0195  64  TYR   C C   
1557 O O   . TYR   B 58  ? 0.1484 0.1509 0.1430 0.0092  -0.0061 0.0216  64  TYR   C O   
1558 C CB  . TYR   B 58  ? 0.1504 0.1484 0.1426 0.0062  -0.0104 0.0167  64  TYR   C CB  
1559 C CG  . TYR   B 58  ? 0.1645 0.1628 0.1524 0.0065  -0.0135 0.0158  64  TYR   C CG  
1560 C CD1 . TYR   B 58  ? 0.1709 0.1663 0.1526 0.0071  -0.0146 0.0130  64  TYR   C CD1 
1561 C CD2 . TYR   B 58  ? 0.1694 0.1706 0.1587 0.0065  -0.0156 0.0178  64  TYR   C CD2 
1562 C CE1 . TYR   B 58  ? 0.1838 0.1789 0.1598 0.0080  -0.0183 0.0113  64  TYR   C CE1 
1563 C CE2 . TYR   B 58  ? 0.1758 0.1771 0.1597 0.0075  -0.0195 0.0167  64  TYR   C CE2 
1564 C CZ  . TYR   B 58  ? 0.1859 0.1840 0.1627 0.0083  -0.0210 0.0132  64  TYR   C CZ  
1565 O OH  . TYR   B 58  ? 0.2277 0.2252 0.1970 0.0100  -0.0253 0.0113  64  TYR   C OH  
1566 N N   . CYS   B 59  ? 0.1487 0.1474 0.1309 0.0112  -0.0061 0.0195  65  CYS   C N   
1567 C CA  . CYS   B 59  ? 0.1572 0.1573 0.1371 0.0135  -0.0040 0.0227  65  CYS   C CA  
1568 C C   . CYS   B 59  ? 0.1596 0.1594 0.1315 0.0147  -0.0071 0.0226  65  CYS   C C   
1569 O O   . CYS   B 59  ? 0.1828 0.1798 0.1460 0.0161  -0.0081 0.0203  65  CYS   C O   
1570 C CB  . CYS   B 59  ? 0.1492 0.1475 0.1269 0.0156  -0.0001 0.0231  65  CYS   C CB  
1571 S SG  . CYS   B 59  ? 0.1873 0.1865 0.1624 0.0194  0.0044  0.0281  65  CYS   C SG  
1572 N N   . SER   B 60  ? 0.1774 0.1800 0.1524 0.0142  -0.0093 0.0247  66  SER   C N   
1573 C CA  . SER   B 60  ? 0.1898 0.1927 0.1581 0.0155  -0.0136 0.0243  66  SER   C CA  
1574 C C   . SER   B 60  ? 0.1960 0.1972 0.1525 0.0200  -0.0119 0.0261  66  SER   C C   
1575 O O   . SER   B 60  ? 0.2204 0.2195 0.1673 0.0216  -0.0159 0.0232  66  SER   C O   
1576 C CB  . SER   B 60  ? 0.2383 0.2448 0.2133 0.0145  -0.0159 0.0269  66  SER   C CB  
1577 O OG  . SER   B 60  ? 0.3511 0.3597 0.3295 0.0161  -0.0119 0.0318  66  SER   C OG  
1578 N N   . SER   B 61  ? 0.1933 0.1950 0.1512 0.0221  -0.0059 0.0305  67  SER   C N   
1579 C CA  . SER   B 61  ? 0.2058 0.2053 0.1527 0.0272  -0.0025 0.0333  67  SER   C CA  
1580 C C   . SER   B 61  ? 0.2205 0.2157 0.1589 0.0287  -0.0009 0.0300  67  SER   C C   
1581 O O   . SER   B 61  ? 0.2596 0.2522 0.1867 0.0334  0.0020  0.0318  67  SER   C O   
1582 C CB  . SER   B 61  ? 0.2098 0.2110 0.1637 0.0290  0.0043  0.0394  67  SER   C CB  
1583 O OG  . SER   B 61  ? 0.2236 0.2245 0.1869 0.0271  0.0084  0.0387  67  SER   C OG  
1584 N N   . ARG   B 62  ? 0.1999 0.1937 0.1418 0.0254  -0.0027 0.0252  68  ARG   C N   
1585 C CA  . ARG   B 62  ? 0.2054 0.1948 0.1394 0.0266  -0.0020 0.0214  68  ARG   C CA  
1586 C C   . ARG   B 62  ? 0.2147 0.2025 0.1468 0.0240  -0.0085 0.0153  68  ARG   C C   
1587 O O   . ARG   B 62  ? 0.2342 0.2181 0.1612 0.0245  -0.0085 0.0114  68  ARG   C O   
1588 C CB  . ARG   B 62  ? 0.2031 0.1920 0.1450 0.0255  0.0031  0.0218  68  ARG   C CB  
1589 C CG  . ARG   B 62  ? 0.2552 0.2453 0.2017 0.0280  0.0099  0.0274  68  ARG   C CG  
1590 C CD  . ARG   B 62  ? 0.2578 0.2442 0.1925 0.0331  0.0145  0.0291  68  ARG   C CD  
1591 N NE  . ARG   B 62  ? 0.2911 0.2784 0.2319 0.0359  0.0223  0.0352  68  ARG   C NE  
1592 C CZ  . ARG   B 62  ? 0.3333 0.3222 0.2741 0.0385  0.0250  0.0406  68  ARG   C CZ  
1593 N NH1 . ARG   B 62  ? 0.3304 0.3202 0.2631 0.0393  0.0203  0.0408  68  ARG   C NH1 
1594 N NH2 . ARG   B 62  ? 0.3734 0.3626 0.3217 0.0410  0.0329  0.0462  68  ARG   C NH2 
1595 N N   . ARG   B 63  ? 0.2066 0.1973 0.1454 0.0211  -0.0135 0.0146  69  ARG   C N   
1596 C CA  . ARG   B 63  ? 0.2286 0.2181 0.1707 0.0179  -0.0188 0.0094  69  ARG   C CA  
1597 C C   . ARG   B 63  ? 0.2395 0.2264 0.1856 0.0160  -0.0162 0.0069  69  ARG   C C   
1598 O O   . ARG   B 63  ? 0.2733 0.2568 0.2168 0.0156  -0.0185 0.0022  69  ARG   C O   
1599 C CB  . ARG   B 63  ? 0.2581 0.2453 0.1899 0.0200  -0.0246 0.0050  69  ARG   C CB  
1600 C CG  . ARG   B 63  ? 0.3348 0.3250 0.2638 0.0217  -0.0289 0.0072  69  ARG   C CG  
1601 C CD  . ARG   B 63  ? 0.4871 0.4769 0.4167 0.0206  -0.0374 0.0016  69  ARG   C CD  
1602 N NE  . ARG   B 63  ? 0.5633 0.5568 0.4934 0.0216  -0.0423 0.0036  69  ARG   C NE  
1603 C CZ  . ARG   B 63  ? 0.6512 0.6440 0.5686 0.0262  -0.0468 0.0029  69  ARG   C CZ  
1604 N NH1 . ARG   B 63  ? 0.6852 0.6732 0.5870 0.0304  -0.0464 0.0000  69  ARG   C NH1 
1605 N NH2 . ARG   B 63  ? 0.6539 0.6505 0.5731 0.0272  -0.0517 0.0051  69  ARG   C NH2 
1606 N N   . LYS   B 64  ? 0.2094 0.1978 0.1625 0.0151  -0.0116 0.0099  70  LYS   C N   
1607 C CA  . LYS   B 64  ? 0.2099 0.1959 0.1660 0.0142  -0.0091 0.0083  70  LYS   C CA  
1608 C C   . LYS   B 64  ? 0.1915 0.1799 0.1575 0.0122  -0.0076 0.0103  70  LYS   C C   
1609 O O   . LYS   B 64  ? 0.1983 0.1899 0.1683 0.0123  -0.0066 0.0135  70  LYS   C O   
1610 C CB  . LYS   B 64  ? 0.2640 0.2482 0.2149 0.0172  -0.0043 0.0095  70  LYS   C CB  
1611 C CG  . LYS   B 64  ? 0.3946 0.3744 0.3344 0.0196  -0.0049 0.0060  70  LYS   C CG  
1612 C CD  . LYS   B 64  ? 0.4935 0.4704 0.4306 0.0221  0.0007  0.0066  70  LYS   C CD  
1613 C CE  . LYS   B 64  ? 0.5667 0.5387 0.4912 0.0251  0.0005  0.0031  70  LYS   C CE  
1614 N NZ  . LYS   B 64  ? 0.6304 0.6024 0.5441 0.0284  -0.0007 0.0043  70  LYS   C NZ  
1615 N N   . HIS   B 65  ? 0.1763 0.1627 0.1456 0.0108  -0.0074 0.0085  71  HIS   C N   
1616 C CA  . HIS   B 65  ? 0.1734 0.1609 0.1494 0.0101  -0.0058 0.0100  71  HIS   C CA  
1617 C C   . HIS   B 65  ? 0.1989 0.1853 0.1747 0.0118  -0.0028 0.0102  71  HIS   C C   
1618 O O   . HIS   B 65  ? 0.2476 0.2309 0.2201 0.0125  -0.0018 0.0083  71  HIS   C O   
1619 C CB  . HIS   B 65  ? 0.1699 0.1555 0.1495 0.0084  -0.0069 0.0086  71  HIS   C CB  
1620 C CG  . HIS   B 65  ? 0.1652 0.1522 0.1483 0.0066  -0.0095 0.0087  71  HIS   C CG  
1621 N ND1 . HIS   B 65  ? 0.2031 0.1921 0.1917 0.0058  -0.0091 0.0108  71  HIS   C ND1 
1622 C CD2 . HIS   B 65  ? 0.1619 0.1484 0.1441 0.0057  -0.0128 0.0065  71  HIS   C CD2 
1623 C CE1 . HIS   B 65  ? 0.1791 0.1690 0.1712 0.0042  -0.0117 0.0104  71  HIS   C CE1 
1624 N NE2 . HIS   B 65  ? 0.2025 0.1911 0.1913 0.0040  -0.0144 0.0077  71  HIS   C NE2 
1625 N N   . TYR   B 66  ? 0.1701 0.1589 0.1506 0.0125  -0.0013 0.0122  72  TYR   C N   
1626 C CA  . TYR   B 66  ? 0.1602 0.1486 0.1429 0.0142  0.0011  0.0125  72  TYR   C CA  
1627 C C   . TYR   B 66  ? 0.1596 0.1485 0.1473 0.0143  0.0001  0.0122  72  TYR   C C   
1628 O O   . TYR   B 66  ? 0.1518 0.1427 0.1429 0.0138  -0.0013 0.0127  72  TYR   C O   
1629 C CB  . TYR   B 66  ? 0.1688 0.1600 0.1554 0.0155  0.0033  0.0150  72  TYR   C CB  
1630 C CG  . TYR   B 66  ? 0.1856 0.1758 0.1658 0.0169  0.0055  0.0162  72  TYR   C CG  
1631 C CD1 . TYR   B 66  ? 0.2219 0.2093 0.1976 0.0189  0.0084  0.0158  72  TYR   C CD1 
1632 C CD2 . TYR   B 66  ? 0.1983 0.1903 0.1765 0.0168  0.0048  0.0181  72  TYR   C CD2 
1633 C CE1 . TYR   B 66  ? 0.2284 0.2143 0.1962 0.0212  0.0108  0.0169  72  TYR   C CE1 
1634 C CE2 . TYR   B 66  ? 0.2100 0.2009 0.1804 0.0192  0.0066  0.0195  72  TYR   C CE2 
1635 C CZ  . TYR   B 66  ? 0.2075 0.1950 0.1720 0.0215  0.0096  0.0188  72  TYR   C CZ  
1636 O OH  . TYR   B 66  ? 0.2569 0.2428 0.2117 0.0247  0.0118  0.0203  72  TYR   C OH  
1637 N N   . PRO   B 67  ? 0.1578 0.1447 0.1456 0.0155  0.0008  0.0112  73  PRO   C N   
1638 C CA  . PRO   B 67  ? 0.1606 0.1479 0.1520 0.0166  -0.0006 0.0110  73  PRO   C CA  
1639 C C   . PRO   B 67  ? 0.1629 0.1534 0.1618 0.0177  -0.0008 0.0115  73  PRO   C C   
1640 O O   . PRO   B 67  ? 0.2012 0.1922 0.2029 0.0184  0.0017  0.0123  73  PRO   C O   
1641 C CB  . PRO   B 67  ? 0.1860 0.1701 0.1755 0.0179  0.0004  0.0103  73  PRO   C CB  
1642 C CG  . PRO   B 67  ? 0.2140 0.1966 0.2010 0.0177  0.0029  0.0099  73  PRO   C CG  
1643 C CD  . PRO   B 67  ? 0.1732 0.1570 0.1572 0.0162  0.0028  0.0102  73  PRO   C CD  
1644 N N   . VAL   B 68  ? 0.1440 0.1362 0.1464 0.0181  -0.0034 0.0109  74  VAL   C N   
1645 C CA  . VAL   B 68  ? 0.1515 0.1467 0.1632 0.0189  -0.0043 0.0106  74  VAL   C CA  
1646 C C   . VAL   B 68  ? 0.1575 0.1531 0.1715 0.0207  -0.0083 0.0084  74  VAL   C C   
1647 O O   . VAL   B 68  ? 0.1619 0.1557 0.1694 0.0213  -0.0100 0.0077  74  VAL   C O   
1648 C CB  . VAL   B 68  ? 0.1810 0.1788 0.1965 0.0174  -0.0036 0.0118  74  VAL   C CB  
1649 C CG1 . VAL   B 68  ? 0.2187 0.2166 0.2329 0.0167  0.0003  0.0143  74  VAL   C CG1 
1650 C CG2 . VAL   B 68  ? 0.1850 0.1821 0.1955 0.0164  -0.0054 0.0113  74  VAL   C CG2 
1651 N N   . SER   B 69  ? 0.1391 0.1370 0.1631 0.0219  -0.0100 0.0073  75  SER   C N   
1652 C CA  . SER   B 69  ? 0.1506 0.1497 0.1791 0.0237  -0.0151 0.0042  75  SER   C CA  
1653 C C   . SER   B 69  ? 0.1318 0.1334 0.1678 0.0223  -0.0156 0.0036  75  SER   C C   
1654 O O   . SER   B 69  ? 0.1494 0.1528 0.1923 0.0206  -0.0120 0.0058  75  SER   C O   
1655 C CB  . SER   B 69  ? 0.1791 0.1799 0.2176 0.0255  -0.0173 0.0029  75  SER   C CB  
1656 O OG  . SER   B 69  ? 0.2569 0.2553 0.2889 0.0270  -0.0166 0.0038  75  SER   C OG  
1657 N N   . PHE   B 70  ? 0.1355 0.1367 0.1693 0.0233  -0.0194 0.0009  76  PHE   C N   
1658 C CA  . PHE   B 70  ? 0.1380 0.1411 0.1790 0.0220  -0.0197 0.0000  76  PHE   C CA  
1659 C C   . PHE   B 70  ? 0.1389 0.1424 0.1845 0.0242  -0.0257 -0.0050 76  PHE   C C   
1660 O O   . PHE   B 70  ? 0.1538 0.1552 0.1918 0.0272  -0.0298 -0.0075 76  PHE   C O   
1661 C CB  . PHE   B 70  ? 0.1479 0.1497 0.1807 0.0202  -0.0168 0.0023  76  PHE   C CB  
1662 C CG  . PHE   B 70  ? 0.1467 0.1451 0.1665 0.0217  -0.0178 0.0016  76  PHE   C CG  
1663 C CD1 . PHE   B 70  ? 0.1565 0.1526 0.1674 0.0216  -0.0155 0.0039  76  PHE   C CD1 
1664 C CD2 . PHE   B 70  ? 0.1542 0.1514 0.1712 0.0235  -0.0206 -0.0012 76  PHE   C CD2 
1665 C CE1 . PHE   B 70  ? 0.1504 0.1432 0.1511 0.0234  -0.0155 0.0040  76  PHE   C CE1 
1666 C CE2 . PHE   B 70  ? 0.1574 0.1509 0.1622 0.0255  -0.0202 -0.0009 76  PHE   C CE2 
1667 C CZ  . PHE   B 70  ? 0.1584 0.1498 0.1559 0.0255  -0.0175 0.0020  76  PHE   C CZ  
1668 N N   . SER   B 71  ? 0.1341 0.1399 0.1927 0.0232  -0.0266 -0.0066 77  SER   C N   
1669 C CA  . SER   B 71  ? 0.1467 0.1530 0.2123 0.0252  -0.0331 -0.0124 77  SER   C CA  
1670 C C   . SER   B 71  ? 0.1695 0.1729 0.2241 0.0268  -0.0355 -0.0152 77  SER   C C   
1671 O O   . SER   B 71  ? 0.1836 0.1851 0.2277 0.0258  -0.0315 -0.0122 77  SER   C O   
1672 C CB  . SER   B 71  ? 0.1556 0.1653 0.2418 0.0234  -0.0327 -0.0132 77  SER   C CB  
1673 O OG  . SER   B 71  ? 0.1795 0.1896 0.2677 0.0210  -0.0279 -0.0103 77  SER   C OG  
1674 N N   . LYS   B 72  ? 0.1979 0.2007 0.2546 0.0297  -0.0422 -0.0214 78  LYS   C N   
1675 C CA  . LYS   B 72  ? 0.1944 0.1937 0.2397 0.0320  -0.0443 -0.0246 78  LYS   C CA  
1676 C C   . LYS   B 72  ? 0.1927 0.1931 0.2472 0.0292  -0.0415 -0.0246 78  LYS   C C   
1677 O O   . LYS   B 72  ? 0.2065 0.2101 0.2786 0.0268  -0.0410 -0.0247 78  LYS   C O   
1678 C CB  . LYS   B 72  ? 0.2568 0.2549 0.3017 0.0366  -0.0534 -0.0321 78  LYS   C CB  
1679 C CG  . LYS   B 72  ? 0.3060 0.3038 0.3450 0.0398  -0.0571 -0.0323 78  LYS   C CG  
1680 C CD  . LYS   B 72  ? 0.4588 0.4530 0.4848 0.0462  -0.0650 -0.0384 78  LYS   C CD  
1681 C CE  . LYS   B 72  ? 0.5588 0.5504 0.5687 0.0501  -0.0649 -0.0353 78  LYS   C CE  
1682 N NZ  . LYS   B 72  ? 0.6146 0.6020 0.6088 0.0573  -0.0715 -0.0400 78  LYS   C NZ  
1683 N N   . PRO   B 73  ? 0.1893 0.1867 0.2330 0.0298  -0.0392 -0.0241 79  PRO   C N   
1684 C CA  . PRO   B 73  ? 0.1896 0.1879 0.2421 0.0272  -0.0360 -0.0235 79  PRO   C CA  
1685 C C   . PRO   B 73  ? 0.1930 0.1924 0.2610 0.0276  -0.0410 -0.0298 79  PRO   C C   
1686 O O   . PRO   B 73  ? 0.2317 0.2290 0.2961 0.0313  -0.0478 -0.0366 79  PRO   C O   
1687 C CB  . PRO   B 73  ? 0.2124 0.2065 0.2497 0.0291  -0.0339 -0.0231 79  PRO   C CB  
1688 C CG  . PRO   B 73  ? 0.2642 0.2558 0.2856 0.0315  -0.0334 -0.0209 79  PRO   C CG  
1689 C CD  . PRO   B 73  ? 0.2180 0.2109 0.2421 0.0331  -0.0385 -0.0233 79  PRO   C CD  
1690 N N   . SER   B 74  ? 0.1687 0.1716 0.2546 0.0241  -0.0379 -0.0275 80  SER   C N   
1691 C CA  . SER   B 74  ? 0.1809 0.1854 0.2862 0.0239  -0.0421 -0.0331 80  SER   C CA  
1692 C C   . SER   B 74  ? 0.1753 0.1816 0.2951 0.0207  -0.0365 -0.0296 80  SER   C C   
1693 O O   . SER   B 74  ? 0.1815 0.1884 0.2962 0.0187  -0.0298 -0.0226 80  SER   C O   
1694 C CB  . SER   B 74  ? 0.2088 0.2166 0.3278 0.0235  -0.0445 -0.0335 80  SER   C CB  
1695 O OG  . SER   B 74  ? 0.3256 0.3322 0.4320 0.0263  -0.0488 -0.0350 80  SER   C OG  
1696 N N   . LEU   B 75  ? 0.1840 0.1914 0.3235 0.0203  -0.0394 -0.0345 81  LEU   C N   
1697 C CA  . LEU   B 75  ? 0.1901 0.1994 0.3474 0.0175  -0.0341 -0.0313 81  LEU   C CA  
1698 C C   . LEU   B 75  ? 0.2007 0.2139 0.3754 0.0157  -0.0304 -0.0264 81  LEU   C C   
1699 O O   . LEU   B 75  ? 0.2249 0.2395 0.4142 0.0162  -0.0351 -0.0309 81  LEU   C O   
1700 C CB  . LEU   B 75  ? 0.2073 0.2150 0.3782 0.0184  -0.0394 -0.0400 81  LEU   C CB  
1701 C CG  . LEU   B 75  ? 0.2312 0.2401 0.4210 0.0160  -0.0341 -0.0375 81  LEU   C CG  
1702 C CD1 . LEU   B 75  ? 0.2394 0.2465 0.4161 0.0155  -0.0286 -0.0328 81  LEU   C CD1 
1703 C CD2 . LEU   B 75  ? 0.2580 0.2657 0.4659 0.0168  -0.0406 -0.0474 81  LEU   C CD2 
1704 N N   . ILE   B 76  ? 0.2055 0.2202 0.3781 0.0139  -0.0223 -0.0174 82  ILE   C N   
1705 C CA  . ILE   B 76  ? 0.2302 0.2477 0.4142 0.0130  -0.0172 -0.0114 82  ILE   C CA  
1706 C C   . ILE   B 76  ? 0.2232 0.2422 0.4208 0.0115  -0.0094 -0.0047 82  ILE   C C   
1707 O O   . ILE   B 76  ? 0.2062 0.2243 0.3949 0.0110  -0.0060 -0.0012 82  ILE   C O   
1708 C CB  . ILE   B 76  ? 0.2687 0.2859 0.4322 0.0133  -0.0144 -0.0060 82  ILE   C CB  
1709 C CG1 . ILE   B 76  ? 0.3138 0.3293 0.4627 0.0151  -0.0212 -0.0114 82  ILE   C CG1 
1710 C CG2 . ILE   B 76  ? 0.2990 0.3182 0.4699 0.0129  -0.0077 0.0011  82  ILE   C CG2 
1711 C CD1 . ILE   B 76  ? 0.3254 0.3424 0.4849 0.0161  -0.0249 -0.0142 82  ILE   C CD1 
1712 N N   . PHE   B 77  ? 0.2131 0.2342 0.4328 0.0112  -0.0058 -0.0023 83  PHE   C N   
1713 C CA  . PHE   B 77  ? 0.2094 0.2317 0.4414 0.0106  0.0030  0.0057  83  PHE   C CA  
1714 C C   . PHE   B 77  ? 0.2209 0.2434 0.4369 0.0113  0.0098  0.0147  83  PHE   C C   
1715 O O   . PHE   B 77  ? 0.2484 0.2712 0.4600 0.0121  0.0102  0.0160  83  PHE   C O   
1716 C CB  . PHE   B 77  ? 0.2084 0.2325 0.4703 0.0104  0.0055  0.0058  83  PHE   C CB  
1717 C CG  . PHE   B 77  ? 0.2136 0.2383 0.4898 0.0102  0.0146  0.0135  83  PHE   C CG  
1718 C CD1 . PHE   B 77  ? 0.2231 0.2470 0.5060 0.0093  0.0140  0.0114  83  PHE   C CD1 
1719 C CD2 . PHE   B 77  ? 0.2342 0.2598 0.5148 0.0114  0.0243  0.0235  83  PHE   C CD2 
1720 C CE1 . PHE   B 77  ? 0.2356 0.2598 0.5310 0.0095  0.0226  0.0192  83  PHE   C CE1 
1721 C CE2 . PHE   B 77  ? 0.2356 0.2613 0.5274 0.0121  0.0330  0.0315  83  PHE   C CE2 
1722 C CZ  . PHE   B 77  ? 0.2330 0.2583 0.5334 0.0110  0.0321  0.0294  83  PHE   C CZ  
1723 N N   . VAL   B 78  ? 0.1847 0.2068 0.3911 0.0113  0.0142  0.0205  84  VAL   C N   
1724 C CA  . VAL   B 78  ? 0.1853 0.2073 0.3749 0.0124  0.0193  0.0281  84  VAL   C CA  
1725 C C   . VAL   B 78  ? 0.1766 0.1995 0.3784 0.0136  0.0284  0.0370  84  VAL   C C   
1726 O O   . VAL   B 78  ? 0.1740 0.1972 0.3862 0.0132  0.0301  0.0381  84  VAL   C O   
1727 C CB  . VAL   B 78  ? 0.1999 0.2208 0.3681 0.0118  0.0163  0.0275  84  VAL   C CB  
1728 C CG1 . VAL   B 78  ? 0.2046 0.2253 0.3560 0.0130  0.0203  0.0344  84  VAL   C CG1 
1729 C CG2 . VAL   B 78  ? 0.2128 0.2321 0.3698 0.0112  0.0084  0.0194  84  VAL   C CG2 
1730 N N   . GLU   B 79  ? 0.1710 0.1939 0.3696 0.0157  0.0347  0.0438  85  GLU   C N   
1731 C CA  . GLU   B 79  ? 0.1758 0.1989 0.3822 0.0180  0.0442  0.0533  85  GLU   C CA  
1732 C C   . GLU   B 79  ? 0.1716 0.1944 0.3630 0.0188  0.0454  0.0580  85  GLU   C C   
1733 O O   . GLU   B 79  ? 0.1629 0.1853 0.3356 0.0177  0.0397  0.0548  85  GLU   C O   
1734 C CB  . GLU   B 79  ? 0.2123 0.2347 0.4173 0.0209  0.0512  0.0595  85  GLU   C CB  
1735 C CG  . GLU   B 79  ? 0.2607 0.2839 0.4865 0.0203  0.0515  0.0562  85  GLU   C CG  
1736 C CD  . GLU   B 79  ? 0.3187 0.3430 0.5751 0.0197  0.0547  0.0566  85  GLU   C CD  
1737 O OE1 . GLU   B 79  ? 0.3630 0.3872 0.6261 0.0209  0.0611  0.0632  85  GLU   C OE1 
1738 O OE2 . GLU   B 79  ? 0.3600 0.3855 0.6348 0.0179  0.0503  0.0500  85  GLU   C OE2 
1739 N N   . ALA   B 80  ? 0.1814 0.2045 0.3818 0.0210  0.0530  0.0661  86  ALA   C N   
1740 C CA  . ALA   B 80  ? 0.2013 0.2245 0.3893 0.0222  0.0541  0.0713  86  ALA   C CA  
1741 C C   . ALA   B 80  ? 0.2090 0.2313 0.3699 0.0240  0.0525  0.0733  86  ALA   C C   
1742 O O   . ALA   B 80  ? 0.2346 0.2558 0.3883 0.0259  0.0549  0.0749  86  ALA   C O   
1743 C CB  . ALA   B 80  ? 0.2160 0.2393 0.4175 0.0254  0.0637  0.0810  86  ALA   C CB  
1744 N N   . SER   B 81  ? 0.1969 0.2196 0.3444 0.0231  0.0476  0.0720  87  SER   C N   
1745 C CA  . SER   B 81  ? 0.2156 0.2377 0.3400 0.0246  0.0453  0.0735  87  SER   C CA  
1746 C C   . SER   B 81  ? 0.2316 0.2545 0.3504 0.0271  0.0471  0.0804  87  SER   C C   
1747 O O   . SER   B 81  ? 0.2379 0.2619 0.3715 0.0275  0.0508  0.0842  87  SER   C O   
1748 C CB  . SER   B 81  ? 0.1887 0.2107 0.3023 0.0212  0.0368  0.0653  87  SER   C CB  
1749 O OG  . SER   B 81  ? 0.1886 0.2116 0.3057 0.0192  0.0335  0.0635  87  SER   C OG  
1750 N N   . GLU   B 82  ? 0.2414 0.2641 0.3399 0.0287  0.0439  0.0815  88  GLU   C N   
1751 C CA  . GLU   B 82  ? 0.2634 0.2872 0.3568 0.0313  0.0445  0.0877  88  GLU   C CA  
1752 C C   . GLU   B 82  ? 0.2513 0.2771 0.3527 0.0279  0.0401  0.0848  88  GLU   C C   
1753 O O   . GLU   B 82  ? 0.2638 0.2910 0.3682 0.0297  0.0417  0.0903  88  GLU   C O   
1754 C CB  . GLU   B 82  ? 0.3401 0.3631 0.4108 0.0344  0.0415  0.0894  88  GLU   C CB  
1755 C CG  . GLU   B 82  ? 0.4649 0.4885 0.5244 0.0312  0.0326  0.0825  88  GLU   C CG  
1756 C CD  . GLU   B 82  ? 0.5524 0.5752 0.5916 0.0346  0.0291  0.0840  88  GLU   C CD  
1757 O OE1 . GLU   B 82  ? 0.5573 0.5780 0.5872 0.0392  0.0334  0.0882  88  GLU   C OE1 
1758 O OE2 . GLU   B 82  ? 0.5802 0.6042 0.6132 0.0328  0.0222  0.0808  88  GLU   C OE2 
1759 N N   . TYR   B 83  ? 0.2163 0.2420 0.3222 0.0235  0.0355  0.0766  89  TYR   C N   
1760 C CA  . TYR   B 83  ? 0.2007 0.2275 0.3121 0.0208  0.0319  0.0735  89  TYR   C CA  
1761 C C   . TYR   B 83  ? 0.2151 0.2415 0.3449 0.0181  0.0328  0.0689  89  TYR   C C   
1762 O O   . TYR   B 83  ? 0.2206 0.2474 0.3558 0.0166  0.0310  0.0670  89  TYR   C O   
1763 C CB  . TYR   B 83  ? 0.1929 0.2195 0.2900 0.0186  0.0249  0.0681  89  TYR   C CB  
1764 C CG  . TYR   B 83  ? 0.1803 0.2051 0.2706 0.0173  0.0225  0.0621  89  TYR   C CG  
1765 C CD1 . TYR   B 83  ? 0.1869 0.2107 0.2645 0.0192  0.0226  0.0634  89  TYR   C CD1 
1766 C CD2 . TYR   B 83  ? 0.1808 0.2045 0.2767 0.0145  0.0201  0.0552  89  TYR   C CD2 
1767 C CE1 . TYR   B 83  ? 0.1903 0.2123 0.2623 0.0180  0.0206  0.0582  89  TYR   C CE1 
1768 C CE2 . TYR   B 83  ? 0.1897 0.2118 0.2797 0.0137  0.0179  0.0503  89  TYR   C CE2 
1769 C CZ  . TYR   B 83  ? 0.1850 0.2064 0.2638 0.0153  0.0183  0.0520  89  TYR   C CZ  
1770 O OH  . TYR   B 83  ? 0.1935 0.2132 0.2678 0.0147  0.0168  0.0477  89  TYR   C OH  
1771 N N   . TYR   B 84  ? 0.1810 0.2064 0.3209 0.0178  0.0351  0.0666  90  TYR   C N   
1772 C CA  . TYR   B 84  ? 0.1782 0.2032 0.3370 0.0159  0.0354  0.0619  90  TYR   C CA  
1773 C C   . TYR   B 84  ? 0.1704 0.1953 0.3457 0.0174  0.0416  0.0654  90  TYR   C C   
1774 O O   . TYR   B 84  ? 0.1788 0.2034 0.3485 0.0193  0.0444  0.0686  90  TYR   C O   
1775 C CB  . TYR   B 84  ? 0.1577 0.1812 0.3132 0.0133  0.0292  0.0521  90  TYR   C CB  
1776 C CG  . TYR   B 84  ? 0.1451 0.1680 0.2897 0.0117  0.0240  0.0476  90  TYR   C CG  
1777 C CD1 . TYR   B 84  ? 0.1537 0.1766 0.3047 0.0111  0.0242  0.0475  90  TYR   C CD1 
1778 C CD2 . TYR   B 84  ? 0.1532 0.1751 0.2820 0.0111  0.0197  0.0441  90  TYR   C CD2 
1779 C CE1 . TYR   B 84  ? 0.1615 0.1835 0.3032 0.0101  0.0205  0.0440  90  TYR   C CE1 
1780 C CE2 . TYR   B 84  ? 0.1479 0.1690 0.2679 0.0100  0.0160  0.0407  90  TYR   C CE2 
1781 C CZ  . TYR   B 84  ? 0.1545 0.1754 0.2812 0.0095  0.0165  0.0404  90  TYR   C CZ  
1782 O OH  . TYR   B 84  ? 0.1498 0.1696 0.2688 0.0087  0.0140  0.0377  90  TYR   C OH  
1783 N N   . PRO   B 85  ? 0.1670 0.1919 0.3637 0.0166  0.0442  0.0646  91  PRO   C N   
1784 C CA  . PRO   B 85  ? 0.1652 0.1900 0.3811 0.0175  0.0495  0.0665  91  PRO   C CA  
1785 C C   . PRO   B 85  ? 0.1734 0.1976 0.3906 0.0156  0.0445  0.0581  91  PRO   C C   
1786 O O   . PRO   B 85  ? 0.1645 0.1881 0.3689 0.0138  0.0372  0.0508  91  PRO   C O   
1787 C CB  . PRO   B 85  ? 0.1764 0.2011 0.4149 0.0165  0.0516  0.0658  91  PRO   C CB  
1788 C CG  . PRO   B 85  ? 0.1703 0.1944 0.4015 0.0140  0.0444  0.0579  91  PRO   C CG  
1789 C CD  . PRO   B 85  ? 0.1700 0.1946 0.3753 0.0146  0.0415  0.0601  91  PRO   C CD  
1790 N N   . ALA   B 86  ? 0.1655 0.1898 0.4004 0.0163  0.0486  0.0591  92  ALA   C N   
1791 C CA  . ALA   B 86  ? 0.1819 0.2060 0.4237 0.0146  0.0436  0.0510  92  ALA   C CA  
1792 C C   . ALA   B 86  ? 0.1969 0.2204 0.4480 0.0121  0.0364  0.0411  92  ALA   C C   
1793 O O   . ALA   B 86  ? 0.2057 0.2291 0.4720 0.0116  0.0386  0.0417  92  ALA   C O   
1794 C CB  . ALA   B 86  ? 0.1806 0.2052 0.4449 0.0158  0.0501  0.0547  92  ALA   C CB  
1795 N N   . ARG   B 87  ? 0.2014 0.2242 0.4404 0.0109  0.0281  0.0325  93  ARG   C N   
1796 C CA  . ARG   B 87  ? 0.1962 0.2176 0.4386 0.0094  0.0212  0.0232  93  ARG   C CA  
1797 C C   . ARG   B 87  ? 0.1896 0.2100 0.4203 0.0092  0.0129  0.0146  93  ARG   C C   
1798 O O   . ARG   B 87  ? 0.1798 0.2007 0.3969 0.0098  0.0127  0.0166  93  ARG   C O   
1799 C CB  . ARG   B 87  ? 0.2038 0.2243 0.4328 0.0092  0.0213  0.0248  93  ARG   C CB  
1800 C CG  . ARG   B 87  ? 0.1862 0.2064 0.3881 0.0095  0.0189  0.0259  93  ARG   C CG  
1801 C CD  . ARG   B 87  ? 0.1867 0.2063 0.3786 0.0093  0.0189  0.0274  93  ARG   C CD  
1802 N NE  . ARG   B 87  ? 0.1790 0.1978 0.3483 0.0093  0.0153  0.0262  93  ARG   C NE  
1803 C CZ  . ARG   B 87  ? 0.1936 0.2109 0.3524 0.0090  0.0126  0.0234  93  ARG   C CZ  
1804 N NH1 . ARG   B 87  ? 0.1918 0.2081 0.3588 0.0087  0.0133  0.0218  93  ARG   C NH1 
1805 N NH2 . ARG   B 87  ? 0.2072 0.2237 0.3479 0.0090  0.0100  0.0226  93  ARG   C NH2 
1806 N N   . TYR   B 88  ? 0.2056 0.2243 0.4385 0.0088  0.0060  0.0052  94  TYR   C N   
1807 C CA  . TYR   B 88  ? 0.2235 0.2407 0.4415 0.0094  -0.0019 -0.0025 94  TYR   C CA  
1808 C C   . TYR   B 88  ? 0.2004 0.2158 0.3937 0.0098  -0.0025 -0.0014 94  TYR   C C   
1809 O O   . TYR   B 88  ? 0.2155 0.2299 0.4074 0.0095  -0.0007 -0.0005 94  TYR   C O   
1810 C CB  . TYR   B 88  ? 0.2532 0.2686 0.4823 0.0098  -0.0094 -0.0134 94  TYR   C CB  
1811 C CG  . TYR   B 88  ? 0.2797 0.2969 0.5323 0.0095  -0.0112 -0.0164 94  TYR   C CG  
1812 C CD1 . TYR   B 88  ? 0.2886 0.3067 0.5382 0.0103  -0.0156 -0.0191 94  TYR   C CD1 
1813 C CD2 . TYR   B 88  ? 0.2881 0.3064 0.5679 0.0085  -0.0074 -0.0153 94  TYR   C CD2 
1814 C CE1 . TYR   B 88  ? 0.3028 0.3230 0.5764 0.0101  -0.0170 -0.0214 94  TYR   C CE1 
1815 C CE2 . TYR   B 88  ? 0.2936 0.3139 0.5981 0.0081  -0.0082 -0.0173 94  TYR   C CE2 
1816 C CZ  . TYR   B 88  ? 0.3072 0.3285 0.6088 0.0089  -0.0133 -0.0205 94  TYR   C CZ  
1817 O OH  . TYR   B 88  ? 0.3312 0.3547 0.6600 0.0085  -0.0141 -0.0225 94  TYR   C OH  
1818 N N   . GLN   B 89  ? 0.1746 0.1896 0.3496 0.0104  -0.0047 -0.0011 95  GLN   C N   
1819 C CA  . GLN   B 89  ? 0.1657 0.1788 0.3188 0.0108  -0.0056 -0.0006 95  GLN   C CA  
1820 C C   . GLN   B 89  ? 0.1538 0.1644 0.2960 0.0125  -0.0126 -0.0086 95  GLN   C C   
1821 O O   . GLN   B 89  ? 0.1705 0.1817 0.3149 0.0132  -0.0159 -0.0112 95  GLN   C O   
1822 C CB  . GLN   B 89  ? 0.1793 0.1940 0.3207 0.0104  -0.0015 0.0071  95  GLN   C CB  
1823 C CG  . GLN   B 89  ? 0.1937 0.2067 0.3155 0.0106  -0.0023 0.0078  95  GLN   C CG  
1824 C CD  . GLN   B 89  ? 0.1652 0.1797 0.2786 0.0099  0.0018  0.0153  95  GLN   C CD  
1825 O OE1 . GLN   B 89  ? 0.1824 0.1989 0.3030 0.0097  0.0061  0.0212  95  GLN   C OE1 
1826 N NE2 . GLN   B 89  ? 0.1521 0.1652 0.2495 0.0101  0.0001  0.0151  95  GLN   C NE2 
1827 N N   . SER   B 90  ? 0.1535 0.1611 0.2846 0.0137  -0.0146 -0.0120 96  SER   C N   
1828 C CA  . SER   B 90  ? 0.1566 0.1610 0.2752 0.0163  -0.0206 -0.0190 96  SER   C CA  
1829 C C   . SER   B 90  ? 0.1512 0.1543 0.2493 0.0172  -0.0199 -0.0159 96  SER   C C   
1830 O O   . SER   B 90  ? 0.1512 0.1554 0.2440 0.0156  -0.0151 -0.0093 96  SER   C O   
1831 C CB  . SER   B 90  ? 0.1774 0.1781 0.2952 0.0181  -0.0230 -0.0253 96  SER   C CB  
1832 O OG  . SER   B 90  ? 0.1913 0.1909 0.2996 0.0177  -0.0182 -0.0208 96  SER   C OG  
1833 N N   . HIS   B 91  ? 0.1667 0.1673 0.2542 0.0199  -0.0250 -0.0209 97  HIS   C N   
1834 C CA  . HIS   B 91  ? 0.1614 0.1600 0.2301 0.0214  -0.0244 -0.0186 97  HIS   C CA  
1835 C C   . HIS   B 91  ? 0.1508 0.1524 0.2194 0.0189  -0.0207 -0.0118 97  HIS   C C   
1836 O O   . HIS   B 91  ? 0.1622 0.1630 0.2195 0.0184  -0.0176 -0.0076 97  HIS   C O   
1837 C CB  . HIS   B 91  ? 0.1808 0.1762 0.2379 0.0224  -0.0213 -0.0174 97  HIS   C CB  
1838 C CG  . HIS   B 91  ? 0.2033 0.1946 0.2571 0.0259  -0.0246 -0.0243 97  HIS   C CG  
1839 N ND1 . HIS   B 91  ? 0.2386 0.2254 0.2763 0.0304  -0.0275 -0.0281 97  HIS   C ND1 
1840 C CD2 . HIS   B 91  ? 0.2032 0.1939 0.2674 0.0257  -0.0250 -0.0279 97  HIS   C CD2 
1841 C CE1 . HIS   B 91  ? 0.2436 0.2271 0.2808 0.0332  -0.0299 -0.0342 97  HIS   C CE1 
1842 N NE2 . HIS   B 91  ? 0.2357 0.2214 0.2893 0.0303  -0.0287 -0.0348 97  HIS   C NE2 
1843 N N   . LEU   B 92  ? 0.1394 0.1442 0.2205 0.0176  -0.0211 -0.0112 98  LEU   C N   
1844 C CA  . LEU   B 92  ? 0.1410 0.1480 0.2219 0.0158  -0.0171 -0.0051 98  LEU   C CA  
1845 C C   . LEU   B 92  ? 0.1450 0.1521 0.2231 0.0171  -0.0200 -0.0068 98  LEU   C C   
1846 O O   . LEU   B 92  ? 0.1493 0.1564 0.2341 0.0186  -0.0249 -0.0120 98  LEU   C O   
1847 C CB  . LEU   B 92  ? 0.1497 0.1600 0.2481 0.0139  -0.0135 -0.0018 98  LEU   C CB  
1848 C CG  . LEU   B 92  ? 0.1637 0.1759 0.2610 0.0128  -0.0086 0.0050  98  LEU   C CG  
1849 C CD1 . LEU   B 92  ? 0.1729 0.1846 0.2581 0.0119  -0.0056 0.0096  98  LEU   C CD1 
1850 C CD2 . LEU   B 92  ? 0.1816 0.1963 0.2967 0.0121  -0.0047 0.0082  98  LEU   C CD2 
1851 N N   . MET   B 93  ? 0.1381 0.1450 0.2065 0.0166  -0.0175 -0.0027 99  MET   C N   
1852 C CA  . MET   B 93  ? 0.1380 0.1447 0.2031 0.0178  -0.0194 -0.0034 99  MET   C CA  
1853 C C   . MET   B 93  ? 0.1485 0.1573 0.2182 0.0161  -0.0147 0.0017  99  MET   C C   
1854 O O   . MET   B 93  ? 0.1493 0.1583 0.2143 0.0147  -0.0106 0.0061  99  MET   C O   
1855 C CB  . MET   B 93  ? 0.1644 0.1680 0.2121 0.0190  -0.0197 -0.0030 99  MET   C CB  
1856 C CG  . MET   B 93  ? 0.1808 0.1815 0.2213 0.0216  -0.0233 -0.0074 99  MET   C CG  
1857 S SD  . MET   B 93  ? 0.1997 0.1963 0.2216 0.0235  -0.0217 -0.0055 99  MET   C SD  
1858 C CE  . MET   B 93  ? 0.1945 0.1920 0.2159 0.0197  -0.0156 0.0004  99  MET   C CE  
1859 N N   . LEU   B 94  ? 0.1315 0.1416 0.2095 0.0168  -0.0152 0.0012  100 LEU   C N   
1860 C CA  . LEU   B 94  ? 0.1421 0.1535 0.2238 0.0160  -0.0099 0.0061  100 LEU   C CA  
1861 C C   . LEU   B 94  ? 0.1311 0.1411 0.2039 0.0169  -0.0099 0.0066  100 LEU   C C   
1862 O O   . LEU   B 94  ? 0.1470 0.1562 0.2178 0.0184  -0.0143 0.0030  100 LEU   C O   
1863 C CB  . LEU   B 94  ? 0.1509 0.1649 0.2527 0.0160  -0.0084 0.0064  100 LEU   C CB  
1864 C CG  . LEU   B 94  ? 0.1702 0.1857 0.2855 0.0151  -0.0072 0.0067  100 LEU   C CG  
1865 C CD1 . LEU   B 94  ? 0.2095 0.2274 0.3470 0.0153  -0.0050 0.0075  100 LEU   C CD1 
1866 C CD2 . LEU   B 94  ? 0.1678 0.1833 0.2768 0.0141  -0.0020 0.0121  100 LEU   C CD2 
1867 N N   . ALA   B 95  ? 0.1379 0.1477 0.2060 0.0164  -0.0049 0.0111  101 ALA   C N   
1868 C CA  . ALA   B 95  ? 0.1381 0.1464 0.2002 0.0173  -0.0035 0.0120  101 ALA   C CA  
1869 C C   . ALA   B 95  ? 0.1372 0.1461 0.2042 0.0176  0.0027  0.0165  101 ALA   C C   
1870 O O   . ALA   B 95  ? 0.1368 0.1468 0.2071 0.0172  0.0062  0.0197  101 ALA   C O   
1871 C CB  . ALA   B 95  ? 0.1543 0.1598 0.1994 0.0168  -0.0038 0.0123  101 ALA   C CB  
1872 N N   . VAL   B 96  ? 0.1359 0.1438 0.2021 0.0188  0.0047  0.0171  102 VAL   C N   
1873 C CA  . VAL   B 96  ? 0.1499 0.1574 0.2174 0.0199  0.0114  0.0216  102 VAL   C CA  
1874 C C   . VAL   B 96  ? 0.1508 0.1555 0.2005 0.0198  0.0132  0.0232  102 VAL   C C   
1875 O O   . VAL   B 96  ? 0.1729 0.1754 0.2120 0.0196  0.0108  0.0210  102 VAL   C O   
1876 C CB  . VAL   B 96  ? 0.1584 0.1656 0.2333 0.0215  0.0129  0.0212  102 VAL   C CB  
1877 C CG1 . VAL   B 96  ? 0.1858 0.1915 0.2599 0.0233  0.0210  0.0261  102 VAL   C CG1 
1878 C CG2 . VAL   B 96  ? 0.1617 0.1720 0.2561 0.0215  0.0099  0.0190  102 VAL   C CG2 
1879 N N   . GLY   B 97  ? 0.1686 0.1735 0.2156 0.0201  0.0166  0.0268  103 GLY   C N   
1880 C CA  . GLY   B 97  ? 0.1946 0.1972 0.2254 0.0203  0.0171  0.0277  103 GLY   C CA  
1881 C C   . GLY   B 97  ? 0.1918 0.1953 0.2207 0.0211  0.0198  0.0317  103 GLY   C C   
1882 O O   . GLY   B 97  ? 0.2104 0.2161 0.2510 0.0212  0.0219  0.0342  103 GLY   C O   
1883 N N   . HIS   B 98  ? 0.1878 0.1893 0.2024 0.0218  0.0196  0.0324  104 HIS   C N   
1884 C CA  . HIS   B 98  ? 0.1909 0.1929 0.2010 0.0233  0.0216  0.0363  104 HIS   C CA  
1885 C C   . HIS   B 98  ? 0.1820 0.1862 0.1930 0.0210  0.0173  0.0358  104 HIS   C C   
1886 O O   . HIS   B 98  ? 0.1817 0.1855 0.1880 0.0188  0.0123  0.0321  104 HIS   C O   
1887 C CB  . HIS   B 98  ? 0.2313 0.2299 0.2253 0.0258  0.0226  0.0367  104 HIS   C CB  
1888 C CG  . HIS   B 98  ? 0.2660 0.2648 0.2539 0.0286  0.0250  0.0413  104 HIS   C CG  
1889 N ND1 . HIS   B 98  ? 0.2834 0.2826 0.2776 0.0318  0.0321  0.0472  104 HIS   C ND1 
1890 C CD2 . HIS   B 98  ? 0.2978 0.2968 0.2760 0.0288  0.0210  0.0412  104 HIS   C CD2 
1891 C CE1 . HIS   B 98  ? 0.3194 0.3186 0.3052 0.0342  0.0324  0.0507  104 HIS   C CE1 
1892 N NE2 . HIS   B 98  ? 0.3276 0.3268 0.3034 0.0325  0.0253  0.0470  104 HIS   C NE2 
1893 N N   . SER   B 99  ? 0.1839 0.1902 0.2011 0.0218  0.0196  0.0399  105 SER   C N   
1894 C CA  . SER   B 99  ? 0.1920 0.2004 0.2105 0.0200  0.0161  0.0400  105 SER   C CA  
1895 C C   . SER   B 99  ? 0.2115 0.2212 0.2322 0.0224  0.0202  0.0461  105 SER   C C   
1896 O O   . SER   B 99  ? 0.2420 0.2525 0.2742 0.0237  0.0253  0.0494  105 SER   C O   
1897 C CB  . SER   B 99  ? 0.2019 0.2120 0.2332 0.0174  0.0142  0.0371  105 SER   C CB  
1898 O OG  . SER   B 99  ? 0.1943 0.2062 0.2287 0.0161  0.0123  0.0379  105 SER   C OG  
1899 N N   . GLU   B 100 ? 0.2137 0.2235 0.2245 0.0234  0.0181  0.0476  106 GLU   C N   
1900 C CA  . GLU   B 100 ? 0.2306 0.2417 0.2413 0.0261  0.0208  0.0536  106 GLU   C CA  
1901 C C   . GLU   B 100 ? 0.1981 0.2118 0.2141 0.0236  0.0169  0.0532  106 GLU   C C   
1902 O O   . GLU   B 100 ? 0.1840 0.1979 0.2002 0.0203  0.0120  0.0483  106 GLU   C O   
1903 C CB  . GLU   B 100 ? 0.2817 0.2907 0.2747 0.0297  0.0198  0.0551  106 GLU   C CB  
1904 C CG  . GLU   B 100 ? 0.3850 0.3907 0.3714 0.0332  0.0250  0.0564  106 GLU   C CG  
1905 C CD  . GLU   B 100 ? 0.4221 0.4250 0.3892 0.0372  0.0234  0.0565  106 GLU   C CD  
1906 O OE1 . GLU   B 100 ? 0.5143 0.5182 0.4740 0.0388  0.0197  0.0581  106 GLU   C OE1 
1907 O OE2 . GLU   B 100 ? 0.4170 0.4165 0.3764 0.0390  0.0256  0.0548  106 GLU   C OE2 
1908 N N   . PRO   B 101 ? 0.2022 0.2177 0.2228 0.0254  0.0192  0.0585  107 PRO   C N   
1909 C CA  . PRO   B 101 ? 0.1893 0.2072 0.2165 0.0229  0.0158  0.0580  107 PRO   C CA  
1910 C C   . PRO   B 101 ? 0.1954 0.2135 0.2136 0.0211  0.0090  0.0544  107 PRO   C C   
1911 O O   . PRO   B 101 ? 0.1976 0.2166 0.2221 0.0179  0.0063  0.0513  107 PRO   C O   
1912 C CB  . PRO   B 101 ? 0.2164 0.2358 0.2466 0.0262  0.0197  0.0654  107 PRO   C CB  
1913 C CG  . PRO   B 101 ? 0.2591 0.2770 0.2920 0.0292  0.0267  0.0692  107 PRO   C CG  
1914 C CD  . PRO   B 101 ? 0.2293 0.2445 0.2522 0.0296  0.0262  0.0656  107 PRO   C CD  
1915 N N   . GLY   B 102 ? 0.1997 0.2165 0.2040 0.0233  0.0065  0.0543  108 GLY   C N   
1916 C CA  . GLY   B 102 ? 0.2056 0.2227 0.2039 0.0216  -0.0004 0.0506  108 GLY   C CA  
1917 C C   . GLY   B 102 ? 0.1921 0.2077 0.1916 0.0180  -0.0027 0.0444  108 GLY   C C   
1918 O O   . GLY   B 102 ? 0.2020 0.2176 0.2003 0.0159  -0.0076 0.0413  108 GLY   C O   
1919 N N   . ASP   B 103 ? 0.1729 0.1867 0.1748 0.0175  0.0007  0.0428  109 ASP   C N   
1920 C CA  . ASP   B 103 ? 0.1668 0.1790 0.1694 0.0147  -0.0012 0.0376  109 ASP   C CA  
1921 C C   . ASP   B 103 ? 0.1592 0.1725 0.1717 0.0121  -0.0017 0.0360  109 ASP   C C   
1922 O O   . ASP   B 103 ? 0.1543 0.1661 0.1664 0.0102  -0.0034 0.0324  109 ASP   C O   
1923 C CB  . ASP   B 103 ? 0.1825 0.1927 0.1842 0.0157  0.0022  0.0365  109 ASP   C CB  
1924 C CG  . ASP   B 103 ? 0.2057 0.2135 0.1955 0.0185  0.0028  0.0369  109 ASP   C CG  
1925 O OD1 . ASP   B 103 ? 0.2041 0.2110 0.1857 0.0184  -0.0013 0.0348  109 ASP   C OD1 
1926 O OD2 . ASP   B 103 ? 0.2200 0.2268 0.2096 0.0209  0.0076  0.0392  109 ASP   C OD2 
1927 N N   . CYS   B 104 ? 0.1454 0.1609 0.1667 0.0121  0.0002  0.0390  110 CYS   C N   
1928 C CA  . CYS   B 104 ? 0.1415 0.1574 0.1711 0.0101  -0.0002 0.0372  110 CYS   C CA  
1929 C C   . CYS   B 104 ? 0.1441 0.1596 0.1712 0.0084  -0.0035 0.0352  110 CYS   C C   
1930 O O   . CYS   B 104 ? 0.1589 0.1755 0.1829 0.0085  -0.0059 0.0367  110 CYS   C O   
1931 C CB  . CYS   B 104 ? 0.1393 0.1574 0.1785 0.0106  0.0022  0.0407  110 CYS   C CB  
1932 S SG  . CYS   B 104 ? 0.1666 0.1850 0.2149 0.0121  0.0069  0.0425  110 CYS   C SG  
1933 N N   . GLY   B 105 ? 0.1254 0.1392 0.1543 0.0072  -0.0036 0.0320  111 GLY   C N   
1934 C CA  . GLY   B 105 ? 0.1389 0.1518 0.1671 0.0058  -0.0054 0.0305  111 GLY   C CA  
1935 C C   . GLY   B 105 ? 0.1372 0.1474 0.1586 0.0054  -0.0067 0.0277  111 GLY   C C   
1936 O O   . GLY   B 105 ? 0.1502 0.1589 0.1722 0.0045  -0.0071 0.0265  111 GLY   C O   
1937 N N   . GLY   B 106 ? 0.1419 0.1513 0.1578 0.0063  -0.0067 0.0269  112 GLY   C N   
1938 C CA  . GLY   B 106 ? 0.1565 0.1631 0.1666 0.0061  -0.0076 0.0242  112 GLY   C CA  
1939 C C   . GLY   B 106 ? 0.1389 0.1433 0.1500 0.0062  -0.0062 0.0222  112 GLY   C C   
1940 O O   . GLY   B 106 ? 0.1406 0.1453 0.1547 0.0070  -0.0050 0.0219  112 GLY   C O   
1941 N N   . ILE   B 107 ? 0.1355 0.1374 0.1444 0.0057  -0.0066 0.0208  113 ILE   C N   
1942 C CA  . ILE   B 107 ? 0.1348 0.1341 0.1429 0.0066  -0.0051 0.0195  113 ILE   C CA  
1943 C C   . ILE   B 107 ? 0.1331 0.1307 0.1370 0.0080  -0.0050 0.0177  113 ILE   C C   
1944 O O   . ILE   B 107 ? 0.1383 0.1353 0.1391 0.0078  -0.0055 0.0172  113 ILE   C O   
1945 C CB  . ILE   B 107 ? 0.1654 0.1623 0.1739 0.0060  -0.0044 0.0197  113 ILE   C CB  
1946 C CG1 . ILE   B 107 ? 0.2235 0.2217 0.2382 0.0054  -0.0034 0.0216  113 ILE   C CG1 
1947 C CG2 . ILE   B 107 ? 0.1766 0.1697 0.1814 0.0078  -0.0025 0.0188  113 ILE   C CG2 
1948 C CD1 . ILE   B 107 ? 0.2739 0.2706 0.2931 0.0045  -0.0021 0.0228  113 ILE   C CD1 
1949 N N   . LEU   B 108 ? 0.1279 0.1248 0.1320 0.0097  -0.0047 0.0166  114 LEU   C N   
1950 C CA  . LEU   B 108 ? 0.1267 0.1218 0.1276 0.0115  -0.0051 0.0148  114 LEU   C CA  
1951 C C   . LEU   B 108 ? 0.1341 0.1257 0.1306 0.0131  -0.0041 0.0146  114 LEU   C C   
1952 O O   . LEU   B 108 ? 0.1382 0.1289 0.1348 0.0141  -0.0033 0.0148  114 LEU   C O   
1953 C CB  . LEU   B 108 ? 0.1309 0.1276 0.1358 0.0128  -0.0062 0.0132  114 LEU   C CB  
1954 C CG  . LEU   B 108 ? 0.1395 0.1347 0.1423 0.0152  -0.0078 0.0109  114 LEU   C CG  
1955 C CD1 . LEU   B 108 ? 0.1527 0.1480 0.1551 0.0150  -0.0074 0.0113  114 LEU   C CD1 
1956 C CD2 . LEU   B 108 ? 0.1597 0.1565 0.1685 0.0164  -0.0099 0.0086  114 LEU   C CD2 
1957 N N   . ARG   B 109 ? 0.1318 0.1208 0.1245 0.0138  -0.0035 0.0145  115 ARG   C N   
1958 C CA  . ARG   B 109 ? 0.1427 0.1279 0.1314 0.0159  -0.0016 0.0153  115 ARG   C CA  
1959 C C   . ARG   B 109 ? 0.1499 0.1330 0.1339 0.0186  -0.0022 0.0143  115 ARG   C C   
1960 O O   . ARG   B 109 ? 0.1609 0.1451 0.1459 0.0180  -0.0033 0.0134  115 ARG   C O   
1961 C CB  . ARG   B 109 ? 0.1820 0.1658 0.1729 0.0139  0.0005  0.0170  115 ARG   C CB  
1962 C CG  . ARG   B 109 ? 0.2120 0.1957 0.2031 0.0123  -0.0005 0.0160  115 ARG   C CG  
1963 C CD  . ARG   B 109 ? 0.2506 0.2328 0.2456 0.0102  0.0006  0.0167  115 ARG   C CD  
1964 N NE  . ARG   B 109 ? 0.3115 0.2969 0.3110 0.0077  -0.0013 0.0167  115 ARG   C NE  
1965 C CZ  . ARG   B 109 ? 0.4269 0.4124 0.4322 0.0064  -0.0005 0.0180  115 ARG   C CZ  
1966 N NH1 . ARG   B 109 ? 0.4777 0.4601 0.4853 0.0074  0.0030  0.0198  115 ARG   C NH1 
1967 N NH2 . ARG   B 109 ? 0.4510 0.4397 0.4603 0.0044  -0.0030 0.0180  115 ARG   C NH2 
1968 N N   . CYS   B 110 ? 0.1596 0.1394 0.1382 0.0221  -0.0010 0.0149  116 CYS   C N   
1969 C CA  . CYS   B 110 ? 0.1757 0.1530 0.1490 0.0257  -0.0016 0.0146  116 CYS   C CA  
1970 C C   . CYS   B 110 ? 0.1944 0.1673 0.1641 0.0275  0.0028  0.0178  116 CYS   C C   
1971 O O   . CYS   B 110 ? 0.2000 0.1721 0.1732 0.0255  0.0059  0.0198  116 CYS   C O   
1972 C CB  . CYS   B 110 ? 0.1776 0.1550 0.1467 0.0295  -0.0049 0.0123  116 CYS   C CB  
1973 S SG  . CYS   B 110 ? 0.1895 0.1636 0.1518 0.0330  -0.0029 0.0130  116 CYS   C SG  
1974 N N   . GLN   B 111 ? 0.2053 0.1750 0.1689 0.0316  0.0033  0.0187  117 GLN   C N   
1975 C CA  . GLN   B 111 ? 0.2304 0.1953 0.1910 0.0340  0.0084  0.0226  117 GLN   C CA  
1976 C C   . GLN   B 111 ? 0.2402 0.2027 0.1975 0.0364  0.0119  0.0247  117 GLN   C C   
1977 O O   . GLN   B 111 ? 0.2724 0.2312 0.2308 0.0373  0.0176  0.0285  117 GLN   C O   
1978 C CB  . GLN   B 111 ? 0.2553 0.2171 0.2090 0.0390  0.0084  0.0238  117 GLN   C CB  
1979 C CG  . GLN   B 111 ? 0.2832 0.2443 0.2274 0.0446  0.0051  0.0223  117 GLN   C CG  
1980 C CD  . GLN   B 111 ? 0.4327 0.3910 0.3697 0.0500  0.0043  0.0236  117 GLN   C CD  
1981 O OE1 . GLN   B 111 ? 0.4870 0.4478 0.4256 0.0501  -0.0005 0.0210  117 GLN   C OE1 
1982 N NE2 . GLN   B 111 ? 0.4533 0.4063 0.3829 0.0549  0.0093  0.0280  117 GLN   C NE2 
1983 N N   . HIS   B 112 ? 0.2121 0.1761 0.1661 0.0376  0.0092  0.0223  118 HIS   C N   
1984 C CA  . HIS   B 112 ? 0.2355 0.1964 0.1852 0.0404  0.0130  0.0241  118 HIS   C CA  
1985 C C   . HIS   B 112 ? 0.2393 0.2025 0.1981 0.0359  0.0150  0.0247  118 HIS   C C   
1986 O O   . HIS   B 112 ? 0.2541 0.2149 0.2113 0.0379  0.0190  0.0267  118 HIS   C O   
1987 C CB  . HIS   B 112 ? 0.2502 0.2107 0.1908 0.0450  0.0090  0.0207  118 HIS   C CB  
1988 C CG  . HIS   B 112 ? 0.2216 0.1800 0.1530 0.0501  0.0059  0.0198  118 HIS   C CG  
1989 N ND1 . HIS   B 112 ? 0.2097 0.1719 0.1435 0.0493  -0.0010 0.0156  118 HIS   C ND1 
1990 C CD2 . HIS   B 112 ? 0.2735 0.2265 0.1937 0.0566  0.0089  0.0229  118 HIS   C CD2 
1991 C CE1 . HIS   B 112 ? 0.2532 0.2125 0.1782 0.0548  -0.0025 0.0161  118 HIS   C CE1 
1992 N NE2 . HIS   B 112 ? 0.2947 0.2485 0.2106 0.0595  0.0032  0.0205  118 HIS   C NE2 
1993 N N   . GLY   B 113 ? 0.2094 0.1774 0.1772 0.0303  0.0119  0.0229  119 GLY   C N   
1994 C CA  . GLY   B 113 ? 0.2043 0.1750 0.1808 0.0263  0.0127  0.0234  119 GLY   C CA  
1995 C C   . GLY   B 113 ? 0.1843 0.1602 0.1649 0.0231  0.0077  0.0203  119 GLY   C C   
1996 O O   . GLY   B 113 ? 0.1793 0.1571 0.1591 0.0225  0.0041  0.0180  119 GLY   C O   
1997 N N   . VAL   B 114 ? 0.1747 0.1526 0.1606 0.0212  0.0082  0.0206  120 VAL   C N   
1998 C CA  . VAL   B 114 ? 0.1627 0.1453 0.1536 0.0183  0.0045  0.0187  120 VAL   C CA  
1999 C C   . VAL   B 114 ? 0.1663 0.1491 0.1536 0.0209  0.0021  0.0157  120 VAL   C C   
2000 O O   . VAL   B 114 ? 0.1776 0.1578 0.1609 0.0239  0.0034  0.0151  120 VAL   C O   
2001 C CB  . VAL   B 114 ? 0.1694 0.1541 0.1680 0.0157  0.0059  0.0205  120 VAL   C CB  
2002 C CG1 . VAL   B 114 ? 0.1903 0.1794 0.1936 0.0137  0.0029  0.0193  120 VAL   C CG1 
2003 C CG2 . VAL   B 114 ? 0.1921 0.1771 0.1962 0.0130  0.0069  0.0226  120 VAL   C CG2 
2004 N N   . VAL   B 115 ? 0.1445 0.1301 0.1338 0.0199  -0.0015 0.0135  121 VAL   C N   
2005 C CA  . VAL   B 115 ? 0.1472 0.1336 0.1366 0.0217  -0.0047 0.0101  121 VAL   C CA  
2006 C C   . VAL   B 115 ? 0.1536 0.1431 0.1510 0.0197  -0.0053 0.0095  121 VAL   C C   
2007 O O   . VAL   B 115 ? 0.1617 0.1507 0.1599 0.0215  -0.0068 0.0067  121 VAL   C O   
2008 C CB  . VAL   B 115 ? 0.1509 0.1385 0.1406 0.0220  -0.0077 0.0084  121 VAL   C CB  
2009 C CG1 . VAL   B 115 ? 0.1704 0.1595 0.1638 0.0235  -0.0116 0.0046  121 VAL   C CG1 
2010 C CG2 . VAL   B 115 ? 0.1875 0.1717 0.1694 0.0245  -0.0070 0.0092  121 VAL   C CG2 
2011 N N   . GLY   B 116 ? 0.1412 0.1339 0.1446 0.0162  -0.0045 0.0119  122 GLY   C N   
2012 C CA  . GLY   B 116 ? 0.1569 0.1528 0.1685 0.0144  -0.0047 0.0123  122 GLY   C CA  
2013 C C   . GLY   B 116 ? 0.1293 0.1282 0.1445 0.0115  -0.0041 0.0153  122 GLY   C C   
2014 O O   . GLY   B 116 ? 0.1411 0.1391 0.1525 0.0107  -0.0037 0.0166  122 GLY   C O   
2015 N N   . ILE   B 117 ? 0.1231 0.1251 0.1455 0.0103  -0.0039 0.0166  123 ILE   C N   
2016 C CA  . ILE   B 117 ? 0.1267 0.1312 0.1509 0.0086  -0.0036 0.0197  123 ILE   C CA  
2017 C C   . ILE   B 117 ? 0.1256 0.1324 0.1548 0.0087  -0.0033 0.0204  123 ILE   C C   
2018 O O   . ILE   B 117 ? 0.1305 0.1379 0.1662 0.0094  -0.0033 0.0190  123 ILE   C O   
2019 C CB  . ILE   B 117 ? 0.1405 0.1465 0.1685 0.0074  -0.0027 0.0224  123 ILE   C CB  
2020 C CG1 . ILE   B 117 ? 0.1528 0.1593 0.1874 0.0080  -0.0017 0.0219  123 ILE   C CG1 
2021 C CG2 . ILE   B 117 ? 0.1699 0.1739 0.1946 0.0069  -0.0024 0.0227  123 ILE   C CG2 
2022 C CD1 . ILE   B 117 ? 0.1579 0.1664 0.1984 0.0069  -0.0005 0.0252  123 ILE   C CD1 
2023 N N   . VAL   B 118 ? 0.1198 0.1278 0.1468 0.0084  -0.0029 0.0226  124 VAL   C N   
2024 C CA  . VAL   B 118 ? 0.1245 0.1343 0.1562 0.0091  -0.0013 0.0245  124 VAL   C CA  
2025 C C   . VAL   B 118 ? 0.1291 0.1411 0.1694 0.0090  0.0001  0.0268  124 VAL   C C   
2026 O O   . VAL   B 118 ? 0.1266 0.1396 0.1669 0.0083  0.0000  0.0289  124 VAL   C O   
2027 C CB  . VAL   B 118 ? 0.1256 0.1356 0.1508 0.0095  -0.0007 0.0270  124 VAL   C CB  
2028 C CG1 . VAL   B 118 ? 0.1346 0.1461 0.1640 0.0110  0.0024  0.0302  124 VAL   C CG1 
2029 C CG2 . VAL   B 118 ? 0.1416 0.1492 0.1591 0.0097  -0.0017 0.0246  124 VAL   C CG2 
2030 N N   . SER   B 119 ? 0.1242 0.1371 0.1736 0.0096  0.0016  0.0266  125 SER   C N   
2031 C CA  . SER   B 119 ? 0.1251 0.1398 0.1852 0.0096  0.0035  0.0287  125 SER   C CA  
2032 C C   . SER   B 119 ? 0.1427 0.1588 0.2112 0.0107  0.0070  0.0320  125 SER   C C   
2033 O O   . SER   B 119 ? 0.1374 0.1551 0.2131 0.0111  0.0097  0.0359  125 SER   C O   
2034 C CB  . SER   B 119 ? 0.1402 0.1538 0.2061 0.0093  0.0018  0.0242  125 SER   C CB  
2035 O OG  . SER   B 119 ? 0.1544 0.1693 0.2322 0.0093  0.0037  0.0255  125 SER   C OG  
2036 N N   . THR   B 120 ? 0.1346 0.1501 0.2043 0.0114  0.0076  0.0308  126 THR   C N   
2037 C CA  . THR   B 120 ? 0.1293 0.1460 0.2095 0.0128  0.0120  0.0343  126 THR   C CA  
2038 C C   . THR   B 120 ? 0.1232 0.1390 0.1958 0.0142  0.0141  0.0363  126 THR   C C   
2039 O O   . THR   B 120 ? 0.1338 0.1480 0.1954 0.0139  0.0113  0.0334  126 THR   C O   
2040 C CB  . THR   B 120 ? 0.1357 0.1528 0.2319 0.0124  0.0113  0.0305  126 THR   C CB  
2041 O OG1 . THR   B 120 ? 0.1481 0.1642 0.2418 0.0125  0.0082  0.0260  126 THR   C OG1 
2042 C CG2 . THR   B 120 ? 0.1654 0.1827 0.2684 0.0113  0.0089  0.0273  126 THR   C CG2 
2043 N N   . GLY   B 121 ? 0.1395 0.1558 0.2182 0.0162  0.0195  0.0411  127 GLY   C N   
2044 C CA  . GLY   B 121 ? 0.1687 0.1836 0.2412 0.0182  0.0228  0.0433  127 GLY   C CA  
2045 C C   . GLY   B 121 ? 0.1934 0.2089 0.2787 0.0205  0.0297  0.0484  127 GLY   C C   
2046 O O   . GLY   B 121 ? 0.2345 0.2512 0.3284 0.0212  0.0330  0.0525  127 GLY   C O   
2047 N N   . GLY   B 122 ? 0.2358 0.2500 0.3208 0.0222  0.0330  0.0493  128 GLY   C N   
2048 C CA  . GLY   B 122 ? 0.2599 0.2743 0.3583 0.0247  0.0410  0.0549  128 GLY   C CA  
2049 C C   . GLY   B 122 ? 0.2555 0.2697 0.3643 0.0246  0.0417  0.0522  128 GLY   C C   
2050 O O   . GLY   B 122 ? 0.2487 0.2636 0.3605 0.0222  0.0354  0.0457  128 GLY   C O   
2051 N N   . ASN   B 123 ? 0.2418 0.2551 0.3576 0.0277  0.0498  0.0576  129 ASN   C N   
2052 C CA  . ASN   B 123 ? 0.2488 0.2621 0.3776 0.0281  0.0520  0.0565  129 ASN   C CA  
2053 C C   . ASN   B 123 ? 0.2275 0.2395 0.3433 0.0271  0.0465  0.0509  129 ASN   C C   
2054 O O   . ASN   B 123 ? 0.2578 0.2709 0.3856 0.0261  0.0441  0.0471  129 ASN   C O   
2055 C CB  . ASN   B 123 ? 0.2842 0.3005 0.4401 0.0258  0.0498  0.0533  129 ASN   C CB  
2056 C CG  . ASN   B 123 ? 0.3751 0.3922 0.5531 0.0277  0.0587  0.0596  129 ASN   C CG  
2057 O OD1 . ASN   B 123 ? 0.4033 0.4184 0.5791 0.0314  0.0681  0.0670  129 ASN   C OD1 
2058 N ND2 . ASN   B 123 ? 0.3976 0.4171 0.5983 0.0255  0.0564  0.0570  129 ASN   C ND2 
2059 N N   . GLY   B 124 ? 0.2184 0.2282 0.3115 0.0276  0.0445  0.0504  130 GLY   C N   
2060 C CA  . GLY   B 124 ? 0.2022 0.2103 0.2836 0.0267  0.0398  0.0454  130 GLY   C CA  
2061 C C   . GLY   B 124 ? 0.1778 0.1874 0.2599 0.0233  0.0309  0.0386  130 GLY   C C   
2062 O O   . GLY   B 124 ? 0.1807 0.1892 0.2576 0.0228  0.0275  0.0348  130 GLY   C O   
2063 N N   . LEU   B 125 ? 0.1509 0.1625 0.2389 0.0214  0.0277  0.0375  131 LEU   C N   
2064 C CA  . LEU   B 125 ? 0.1600 0.1724 0.2473 0.0190  0.0198  0.0313  131 LEU   C CA  
2065 C C   . LEU   B 125 ? 0.1629 0.1749 0.2372 0.0178  0.0173  0.0313  131 LEU   C C   
2066 O O   . LEU   B 125 ? 0.1963 0.2087 0.2691 0.0184  0.0207  0.0357  131 LEU   C O   
2067 C CB  . LEU   B 125 ? 0.1831 0.1979 0.2903 0.0180  0.0174  0.0286  131 LEU   C CB  
2068 C CG  . LEU   B 125 ? 0.2193 0.2352 0.3434 0.0190  0.0191  0.0281  131 LEU   C CG  
2069 C CD1 . LEU   B 125 ? 0.2631 0.2815 0.4104 0.0184  0.0190  0.0273  131 LEU   C CD1 
2070 C CD2 . LEU   B 125 ? 0.2211 0.2363 0.3406 0.0190  0.0138  0.0234  131 LEU   C CD2 
2071 N N   . VAL   B 126 ? 0.1348 0.1459 0.2007 0.0164  0.0118  0.0270  132 VAL   C N   
2072 C CA  . VAL   B 126 ? 0.1344 0.1453 0.1914 0.0151  0.0091  0.0265  132 VAL   C CA  
2073 C C   . VAL   B 126 ? 0.1165 0.1279 0.1791 0.0139  0.0044  0.0219  132 VAL   C C   
2074 O O   . VAL   B 126 ? 0.1300 0.1408 0.1939 0.0143  0.0012  0.0180  132 VAL   C O   
2075 C CB  . VAL   B 126 ? 0.1357 0.1442 0.1766 0.0148  0.0074  0.0256  132 VAL   C CB  
2076 C CG1 . VAL   B 126 ? 0.1605 0.1674 0.1980 0.0150  0.0052  0.0221  132 VAL   C CG1 
2077 C CG2 . VAL   B 126 ? 0.1557 0.1642 0.1900 0.0134  0.0047  0.0251  132 VAL   C CG2 
2078 N N   . GLY   B 127 ? 0.1224 0.1347 0.1878 0.0130  0.0041  0.0225  133 GLY   C N   
2079 C CA  . GLY   B 127 ? 0.1187 0.1309 0.1879 0.0125  0.0000  0.0180  133 GLY   C CA  
2080 C C   . GLY   B 127 ? 0.1281 0.1389 0.1859 0.0117  -0.0017 0.0175  133 GLY   C C   
2081 O O   . GLY   B 127 ? 0.1271 0.1384 0.1808 0.0111  0.0004  0.0212  133 GLY   C O   
2082 N N   . PHE   B 128 ? 0.1171 0.1260 0.1706 0.0122  -0.0052 0.0132  134 PHE   C N   
2083 C CA  . PHE   B 128 ? 0.1205 0.1275 0.1645 0.0119  -0.0061 0.0128  134 PHE   C CA  
2084 C C   . PHE   B 128 ? 0.1224 0.1286 0.1698 0.0126  -0.0077 0.0096  134 PHE   C C   
2085 O O   . PHE   B 128 ? 0.1339 0.1394 0.1852 0.0141  -0.0106 0.0053  134 PHE   C O   
2086 C CB  . PHE   B 128 ? 0.1319 0.1363 0.1652 0.0129  -0.0077 0.0111  134 PHE   C CB  
2087 C CG  . PHE   B 128 ? 0.1269 0.1316 0.1570 0.0126  -0.0064 0.0131  134 PHE   C CG  
2088 C CD1 . PHE   B 128 ? 0.1302 0.1347 0.1543 0.0114  -0.0047 0.0159  134 PHE   C CD1 
2089 C CD2 . PHE   B 128 ? 0.1371 0.1419 0.1704 0.0137  -0.0071 0.0116  134 PHE   C CD2 
2090 C CE1 . PHE   B 128 ? 0.1376 0.1415 0.1576 0.0116  -0.0037 0.0169  134 PHE   C CE1 
2091 C CE2 . PHE   B 128 ? 0.1448 0.1492 0.1748 0.0137  -0.0053 0.0133  134 PHE   C CE2 
2092 C CZ  . PHE   B 128 ? 0.1320 0.1357 0.1545 0.0128  -0.0036 0.0157  134 PHE   C CZ  
2093 N N   . ALA   B 129 ? 0.1266 0.1327 0.1729 0.0118  -0.0062 0.0114  135 ALA   C N   
2094 C CA  . ALA   B 129 ? 0.1331 0.1376 0.1809 0.0128  -0.0070 0.0085  135 ALA   C CA  
2095 C C   . ALA   B 129 ? 0.1396 0.1403 0.1753 0.0148  -0.0083 0.0062  135 ALA   C C   
2096 O O   . ALA   B 129 ? 0.1436 0.1433 0.1722 0.0142  -0.0064 0.0090  135 ALA   C O   
2097 C CB  . ALA   B 129 ? 0.1350 0.1406 0.1864 0.0114  -0.0043 0.0119  135 ALA   C CB  
2098 N N   . ASP   B 130 ? 0.1394 0.1379 0.1729 0.0174  -0.0114 0.0012  136 ASP   C N   
2099 C CA  . ASP   B 130 ? 0.1526 0.1470 0.1733 0.0204  -0.0121 -0.0004 136 ASP   C CA  
2100 C C   . ASP   B 130 ? 0.1680 0.1598 0.1846 0.0212  -0.0091 0.0007  136 ASP   C C   
2101 O O   . ASP   B 130 ? 0.1700 0.1624 0.1932 0.0208  -0.0085 -0.0004 136 ASP   C O   
2102 C CB  . ASP   B 130 ? 0.1679 0.1604 0.1872 0.0238  -0.0171 -0.0065 136 ASP   C CB  
2103 C CG  . ASP   B 130 ? 0.2131 0.2011 0.2178 0.0280  -0.0180 -0.0080 136 ASP   C CG  
2104 O OD1 . ASP   B 130 ? 0.2098 0.1970 0.2078 0.0280  -0.0162 -0.0048 136 ASP   C OD1 
2105 O OD2 . ASP   B 130 ? 0.2647 0.2494 0.2641 0.0317  -0.0200 -0.0122 136 ASP   C OD2 
2106 N N   . VAL   B 131 ? 0.1657 0.1545 0.1722 0.0227  -0.0068 0.0026  137 VAL   C N   
2107 C CA  . VAL   B 131 ? 0.1755 0.1609 0.1773 0.0244  -0.0031 0.0038  137 VAL   C CA  
2108 C C   . VAL   B 131 ? 0.1944 0.1744 0.1829 0.0296  -0.0028 0.0020  137 VAL   C C   
2109 O O   . VAL   B 131 ? 0.1990 0.1752 0.1821 0.0320  0.0012  0.0032  137 VAL   C O   
2110 C CB  . VAL   B 131 ? 0.1775 0.1643 0.1825 0.0215  0.0011  0.0094  137 VAL   C CB  
2111 C CG1 . VAL   B 131 ? 0.1741 0.1659 0.1906 0.0175  0.0007  0.0113  137 VAL   C CG1 
2112 C CG2 . VAL   B 131 ? 0.1792 0.1653 0.1793 0.0211  0.0019  0.0118  137 VAL   C CG2 
2113 N N   . ARG   B 132 ? 0.1854 0.1645 0.1681 0.0318  -0.0066 -0.0005 138 ARG   C N   
2114 C CA  . ARG   B 132 ? 0.1920 0.1658 0.1605 0.0374  -0.0062 -0.0013 138 ARG   C CA  
2115 C C   . ARG   B 132 ? 0.2095 0.1790 0.1702 0.0425  -0.0074 -0.0057 138 ARG   C C   
2116 O O   . ARG   B 132 ? 0.2346 0.1986 0.1818 0.0479  -0.0049 -0.0050 138 ARG   C O   
2117 C CB  . ARG   B 132 ? 0.1895 0.1640 0.1550 0.0386  -0.0105 -0.0027 138 ARG   C CB  
2118 C CG  . ARG   B 132 ? 0.1839 0.1612 0.1541 0.0345  -0.0085 0.0017  138 ARG   C CG  
2119 C CD  . ARG   B 132 ? 0.1744 0.1522 0.1421 0.0361  -0.0126 0.0000  138 ARG   C CD  
2120 N NE  . ARG   B 132 ? 0.1832 0.1648 0.1603 0.0347  -0.0178 -0.0042 138 ARG   C NE  
2121 C CZ  . ARG   B 132 ? 0.1916 0.1748 0.1713 0.0351  -0.0218 -0.0060 138 ARG   C CZ  
2122 N NH1 . ARG   B 132 ? 0.1994 0.1806 0.1714 0.0377  -0.0220 -0.0047 138 ARG   C NH1 
2123 N NH2 . ARG   B 132 ? 0.1942 0.1812 0.1857 0.0332  -0.0254 -0.0090 138 ARG   C NH2 
2124 N N   . ASP   B 133 ? 0.1954 0.1667 0.1641 0.0414  -0.0106 -0.0102 139 ASP   C N   
2125 C CA  . ASP   B 133 ? 0.2139 0.1806 0.1752 0.0464  -0.0122 -0.0155 139 ASP   C CA  
2126 C C   . ASP   B 133 ? 0.2299 0.1939 0.1907 0.0466  -0.0054 -0.0128 139 ASP   C C   
2127 O O   . ASP   B 133 ? 0.2466 0.2060 0.1998 0.0512  -0.0055 -0.0168 139 ASP   C O   
2128 C CB  . ASP   B 133 ? 0.2265 0.1960 0.1989 0.0451  -0.0189 -0.0223 139 ASP   C CB  
2129 C CG  . ASP   B 133 ? 0.2431 0.2175 0.2327 0.0391  -0.0167 -0.0201 139 ASP   C CG  
2130 O OD1 . ASP   B 133 ? 0.2360 0.2141 0.2315 0.0348  -0.0133 -0.0142 139 ASP   C OD1 
2131 O OD2 . ASP   B 133 ? 0.2758 0.2501 0.2731 0.0389  -0.0182 -0.0244 139 ASP   C OD2 
2132 N N   . LEU   B 134 ? 0.2109 0.1779 0.1803 0.0419  -0.0001 -0.0064 140 LEU   C N   
2133 C CA  . LEU   B 134 ? 0.2161 0.1815 0.1883 0.0416  0.0062  -0.0035 140 LEU   C CA  
2134 C C   . LEU   B 134 ? 0.2199 0.1802 0.1808 0.0455  0.0124  0.0008  140 LEU   C C   
2135 O O   . LEU   B 134 ? 0.2214 0.1831 0.1869 0.0428  0.0170  0.0068  140 LEU   C O   
2136 C CB  . LEU   B 134 ? 0.2145 0.1861 0.2024 0.0349  0.0077  0.0009  140 LEU   C CB  
2137 C CG  . LEU   B 134 ? 0.2075 0.1842 0.2078 0.0312  0.0028  -0.0019 140 LEU   C CG  
2138 C CD1 . LEU   B 134 ? 0.2060 0.1883 0.2187 0.0256  0.0047  0.0036  140 LEU   C CD1 
2139 C CD2 . LEU   B 134 ? 0.2327 0.2075 0.2362 0.0331  0.0014  -0.0073 140 LEU   C CD2 
2140 N N   . LEU   B 135 ? 0.2402 0.1941 0.1855 0.0525  0.0126  -0.0023 141 LEU   C N   
2141 C CA  . LEU   B 135 ? 0.2642 0.2123 0.1967 0.0576  0.0190  0.0023  141 LEU   C CA  
2142 C C   . LEU   B 135 ? 0.2607 0.2067 0.1976 0.0573  0.0282  0.0079  141 LEU   C C   
2143 O O   . LEU   B 135 ? 0.2677 0.2113 0.2023 0.0586  0.0346  0.0139  141 LEU   C O   
2144 C CB  . LEU   B 135 ? 0.2746 0.2156 0.1872 0.0665  0.0172  -0.0022 141 LEU   C CB  
2145 C CG  . LEU   B 135 ? 0.2845 0.2274 0.1934 0.0675  0.0069  -0.0089 141 LEU   C CG  
2146 C CD1 . LEU   B 135 ? 0.3152 0.2508 0.2032 0.0771  0.0038  -0.0139 141 LEU   C CD1 
2147 C CD2 . LEU   B 135 ? 0.2872 0.2344 0.2007 0.0639  0.0046  -0.0056 141 LEU   C CD2 
2148 N N   . TRP   B 136 ? 0.2455 0.1927 0.1908 0.0554  0.0290  0.0062  142 TRP   C N   
2149 C CA  . TRP   B 136 ? 0.2571 0.2029 0.2091 0.0550  0.0375  0.0113  142 TRP   C CA  
2150 C C   . TRP   B 136 ? 0.2647 0.2160 0.2318 0.0486  0.0398  0.0178  142 TRP   C C   
2151 O O   . TRP   B 136 ? 0.2772 0.2272 0.2504 0.0485  0.0471  0.0231  142 TRP   C O   
2152 C CB  . TRP   B 136 ? 0.2521 0.1983 0.2109 0.0542  0.0370  0.0076  142 TRP   C CB  
2153 C CG  . TRP   B 136 ? 0.2476 0.2011 0.2199 0.0480  0.0296  0.0044  142 TRP   C CG  
2154 C CD1 . TRP   B 136 ? 0.2541 0.2084 0.2252 0.0483  0.0222  -0.0027 142 TRP   C CD1 
2155 C CD2 . TRP   B 136 ? 0.2356 0.1960 0.2257 0.0411  0.0297  0.0085  142 TRP   C CD2 
2156 N NE1 . TRP   B 136 ? 0.2490 0.2103 0.2363 0.0420  0.0186  -0.0025 142 TRP   C NE1 
2157 C CE2 . TRP   B 136 ? 0.2399 0.2049 0.2376 0.0378  0.0231  0.0044  142 TRP   C CE2 
2158 C CE3 . TRP   B 136 ? 0.2351 0.1981 0.2352 0.0378  0.0346  0.0152  142 TRP   C CE3 
2159 C CZ2 . TRP   B 136 ? 0.2288 0.2006 0.2420 0.0318  0.0217  0.0075  142 TRP   C CZ2 
2160 C CZ3 . TRP   B 136 ? 0.2306 0.2006 0.2459 0.0319  0.0321  0.0174  142 TRP   C CZ3 
2161 C CH2 . TRP   B 136 ? 0.2291 0.2031 0.2497 0.0292  0.0260  0.0139  142 TRP   C CH2 
2162 N N   . LEU   B 137 ? 0.2444 0.2016 0.2181 0.0435  0.0338  0.0174  143 LEU   C N   
2163 C CA  . LEU   B 137 ? 0.2435 0.2053 0.2297 0.0382  0.0353  0.0228  143 LEU   C CA  
2164 C C   . LEU   B 137 ? 0.2983 0.2558 0.2802 0.0410  0.0418  0.0278  143 LEU   C C   
2165 O O   . LEU   B 137 ? 0.3131 0.2729 0.3069 0.0376  0.0449  0.0324  143 LEU   C O   
2166 C CB  . LEU   B 137 ? 0.2241 0.1916 0.2148 0.0335  0.0282  0.0212  143 LEU   C CB  
2167 C CG  . LEU   B 137 ? 0.2079 0.1806 0.2073 0.0297  0.0230  0.0182  143 LEU   C CG  
2168 C CD1 . LEU   B 137 ? 0.2308 0.2078 0.2315 0.0267  0.0169  0.0166  143 LEU   C CD1 
2169 C CD2 . LEU   B 137 ? 0.2122 0.1891 0.2262 0.0256  0.0251  0.0220  143 LEU   C CD2 
2170 N N   . ASP   B 138 ? 0.2923 0.2435 0.2578 0.0474  0.0435  0.0268  144 ASP   C N   
2171 C CA  . ASP   B 138 ? 0.3222 0.2687 0.2827 0.0510  0.0504  0.0322  144 ASP   C CA  
2172 C C   . ASP   B 138 ? 0.3539 0.2946 0.3132 0.0555  0.0604  0.0366  144 ASP   C C   
2173 O O   . ASP   B 138 ? 0.3812 0.3174 0.3373 0.0590  0.0674  0.0417  144 ASP   C O   
2174 C CB  . ASP   B 138 ? 0.3292 0.2711 0.2716 0.0569  0.0483  0.0301  144 ASP   C CB  
2175 C CG  . ASP   B 138 ? 0.3349 0.2816 0.2781 0.0533  0.0395  0.0266  144 ASP   C CG  
2176 O OD1 . ASP   B 138 ? 0.3457 0.2986 0.3025 0.0465  0.0362  0.0268  144 ASP   C OD1 
2177 O OD2 . ASP   B 138 ? 0.3950 0.3390 0.3246 0.0580  0.0360  0.0237  144 ASP   C OD2 
2178 N N   . GLU   B 139 ? 0.3528 0.2934 0.3156 0.0557  0.0621  0.0351  145 GLU   C N   
2179 C CA  . GLU   B 139 ? 0.4243 0.3586 0.3850 0.0608  0.0725  0.0393  145 GLU   C CA  
2180 C C   . GLU   B 139 ? 0.4847 0.4226 0.4626 0.0565  0.0749  0.0407  145 GLU   C C   
2181 O O   . GLU   B 139 ? 0.4893 0.4341 0.4782 0.0504  0.0679  0.0380  145 GLU   C O   
2182 C CB  . GLU   B 139 ? 0.4950 0.4218 0.4338 0.0693  0.0731  0.0348  145 GLU   C CB  
2183 C CG  . GLU   B 139 ? 0.5939 0.5237 0.5319 0.0675  0.0645  0.0268  145 GLU   C CG  
2184 C CD  . GLU   B 139 ? 0.7067 0.6305 0.6241 0.0749  0.0610  0.0200  145 GLU   C CD  
2185 O OE1 . GLU   B 139 ? 0.7063 0.6299 0.6242 0.0751  0.0581  0.0144  145 GLU   C OE1 
2186 O OE2 . GLU   B 139 ? 0.7525 0.6717 0.6536 0.0806  0.0608  0.0201  145 GLU   C OE2 
2187 N N   . GLU   B 140 ? 0.5295 0.4623 0.5091 0.0606  0.0853  0.0453  146 GLU   C N   
2188 C CA  . GLU   B 140 ? 0.5716 0.5064 0.5664 0.0582  0.0893  0.0473  146 GLU   C CA  
2189 C C   . GLU   B 140 ? 0.6008 0.5433 0.6192 0.0505  0.0879  0.0515  146 GLU   C C   
2190 O O   . GLU   B 140 ? 0.6191 0.5613 0.6517 0.0501  0.0953  0.0569  146 GLU   C O   
2191 C CB  . GLU   B 140 ? 0.6002 0.5361 0.5917 0.0579  0.0838  0.0407  146 GLU   C CB  
2192 C CG  . GLU   B 140 ? 0.6669 0.6072 0.6769 0.0537  0.0852  0.0422  146 GLU   C CG  
2193 C CD  . GLU   B 140 ? 0.7732 0.7069 0.7786 0.0593  0.0931  0.0419  146 GLU   C CD  
2194 O OE1 . GLU   B 140 ? 0.8012 0.7353 0.8050 0.0592  0.0892  0.0364  146 GLU   C OE1 
2195 O OE2 . GLU   B 140 ? 0.7928 0.7208 0.7968 0.0640  0.1037  0.0473  146 GLU   C OE2 
2196 N N1  . A1B02 C .   ? 0.4178 0.3757 0.4805 0.0038  0.0678  -0.0255 201 A1B02 A N1  
2197 N N3  . A1B02 C .   ? 0.4310 0.4012 0.4615 -0.0011 0.0499  -0.0243 201 A1B02 A N3  
2198 C C4  . A1B02 C .   ? 0.4313 0.3810 0.4928 -0.0057 0.0918  -0.0421 201 A1B02 A C4  
2199 C C5  . A1B02 C .   ? 0.4267 0.3767 0.4957 -0.0011 0.0873  -0.0365 201 A1B02 A C5  
2200 C C6  . A1B02 C .   ? 0.4215 0.3787 0.4786 0.0002  0.0724  -0.0306 201 A1B02 A C6  
2201 C C7  . A1B02 C .   ? 0.4179 0.3706 0.4702 -0.0012 0.0675  -0.0310 201 A1B02 A C7  
2202 C C8  . A1B02 C .   ? 0.4199 0.3743 0.4812 0.0038  0.0628  -0.0241 201 A1B02 A C8  
2203 C C10 . A1B02 C .   ? 0.4206 0.3903 0.5069 0.0165  0.0515  -0.0020 201 A1B02 A C10 
2204 O O   . A1B02 C .   ? 0.4067 0.3546 0.4430 -0.0102 0.0706  -0.0404 201 A1B02 A O   
2205 C C9  . A1B02 C .   ? 0.4208 0.3811 0.5037 0.0123  0.0616  -0.0123 201 A1B02 A C9  
2206 N N2  . A1B02 C .   ? 0.4221 0.3789 0.5274 0.0159  0.0729  -0.0103 201 A1B02 A N2  
2207 C C11 . A1B02 C .   ? 0.4197 0.3850 0.5407 0.0221  0.0676  0.0026  201 A1B02 A C11 
2208 O O1  . A1B02 C .   ? 0.4230 0.3968 0.5323 0.0220  0.0546  0.0080  201 A1B02 A O1  
2209 C C3  . A1B02 C .   ? 0.4350 0.3915 0.4771 -0.0089 0.0808  -0.0411 201 A1B02 A C3  
2210 C C12 . A1B02 C .   ? 0.4259 0.3893 0.4654 -0.0026 0.0627  -0.0299 201 A1B02 A C12 
2211 C C2  . A1B02 C .   ? 0.4320 0.3951 0.4640 -0.0071 0.0664  -0.0348 201 A1B02 A C2  
2212 C C1  . A1B02 C .   ? 0.4313 0.4018 0.4492 -0.0079 0.0541  -0.0307 201 A1B02 A C1  
2213 N N   . A1B02 C .   ? 0.4224 0.3962 0.4410 -0.0041 0.0456  -0.0250 201 A1B02 A N   
2214 C C   . A1B02 C .   ? 0.4312 0.4116 0.4412 -0.0030 0.0339  -0.0196 201 A1B02 A C   
# 
