data_7HYO
# 
_entry.id   7HYO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HYO         pdb_00007hyo 10.2210/pdb7hyo/pdb 
WWPDB D_1001408096 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HYO 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                               15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '3-[3-(3-methylphenyl)-2-oxo-1,3-diazinan-1-yl]propanamide' 261.320   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                  65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                        78.133    3   ?         ? ? ? 
5 water       nat water                                                       18.015    350 ?         ? ? ? 
# 
_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 '3-[3-(3-methylphenyl)-2-oxo-1,3-diazinan-1-yl]propanamide' A1BO5 
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 
A1BO5 non-polymer         . '3-[3-(3-methylphenyl)-2-oxo-1,3-diazinan-1-yl]propanamide' ? 'C14 H19 N3 O2'  261.320 
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        A1BO5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BO5 
_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 A1BO5 1   201 201 A1BO5 LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 3 ZN    1   201 1   ZN    ZN  C . 
G 4 DMS   1   202 1   DMS   DMS C . 
H 4 DMS   1   203 6   DMS   DMS C . 
I 5 HOH   1   301 316 HOH   HOH A . 
I 5 HOH   2   302 187 HOH   HOH A . 
I 5 HOH   3   303 270 HOH   HOH A . 
I 5 HOH   4   304 84  HOH   HOH A . 
I 5 HOH   5   305 348 HOH   HOH A . 
I 5 HOH   6   306 333 HOH   HOH A . 
I 5 HOH   7   307 177 HOH   HOH A . 
I 5 HOH   8   308 286 HOH   HOH A . 
I 5 HOH   9   309 325 HOH   HOH A . 
I 5 HOH   10  310 121 HOH   HOH A . 
I 5 HOH   11  311 127 HOH   HOH A . 
I 5 HOH   12  312 154 HOH   HOH A . 
I 5 HOH   13  313 145 HOH   HOH A . 
I 5 HOH   14  314 165 HOH   HOH A . 
I 5 HOH   15  315 263 HOH   HOH A . 
I 5 HOH   16  316 300 HOH   HOH A . 
I 5 HOH   17  317 334 HOH   HOH A . 
I 5 HOH   18  318 101 HOH   HOH A . 
I 5 HOH   19  319 210 HOH   HOH A . 
I 5 HOH   20  320 125 HOH   HOH A . 
I 5 HOH   21  321 338 HOH   HOH A . 
I 5 HOH   22  322 99  HOH   HOH A . 
I 5 HOH   23  323 295 HOH   HOH A . 
I 5 HOH   24  324 232 HOH   HOH A . 
I 5 HOH   25  325 85  HOH   HOH A . 
I 5 HOH   26  326 98  HOH   HOH A . 
I 5 HOH   27  327 166 HOH   HOH A . 
I 5 HOH   28  328 21  HOH   HOH A . 
I 5 HOH   29  329 25  HOH   HOH A . 
I 5 HOH   30  330 11  HOH   HOH A . 
I 5 HOH   31  331 242 HOH   HOH A . 
I 5 HOH   32  332 83  HOH   HOH A . 
I 5 HOH   33  333 10  HOH   HOH A . 
I 5 HOH   34  334 331 HOH   HOH A . 
I 5 HOH   35  335 176 HOH   HOH A . 
I 5 HOH   36  336 292 HOH   HOH A . 
I 5 HOH   37  337 86  HOH   HOH A . 
I 5 HOH   38  338 208 HOH   HOH A . 
I 5 HOH   39  339 81  HOH   HOH A . 
I 5 HOH   40  340 303 HOH   HOH A . 
I 5 HOH   41  341 6   HOH   HOH A . 
I 5 HOH   42  342 51  HOH   HOH A . 
I 5 HOH   43  343 156 HOH   HOH A . 
I 5 HOH   44  344 320 HOH   HOH A . 
I 5 HOH   45  345 108 HOH   HOH A . 
I 5 HOH   46  346 209 HOH   HOH A . 
I 5 HOH   47  347 168 HOH   HOH A . 
I 5 HOH   48  348 180 HOH   HOH A . 
I 5 HOH   49  349 68  HOH   HOH A . 
I 5 HOH   50  350 255 HOH   HOH A . 
I 5 HOH   51  351 266 HOH   HOH A . 
I 5 HOH   52  352 233 HOH   HOH A . 
I 5 HOH   53  353 43  HOH   HOH A . 
I 5 HOH   54  354 327 HOH   HOH A . 
I 5 HOH   55  355 343 HOH   HOH A . 
I 5 HOH   56  356 116 HOH   HOH A . 
I 5 HOH   57  357 207 HOH   HOH A . 
I 5 HOH   58  358 19  HOH   HOH A . 
I 5 HOH   59  359 75  HOH   HOH A . 
I 5 HOH   60  360 46  HOH   HOH A . 
I 5 HOH   61  361 183 HOH   HOH A . 
I 5 HOH   62  362 128 HOH   HOH A . 
I 5 HOH   63  363 178 HOH   HOH A . 
I 5 HOH   64  364 63  HOH   HOH A . 
I 5 HOH   65  365 48  HOH   HOH A . 
I 5 HOH   66  366 212 HOH   HOH A . 
I 5 HOH   67  367 104 HOH   HOH A . 
I 5 HOH   68  368 103 HOH   HOH A . 
I 5 HOH   69  369 88  HOH   HOH A . 
I 5 HOH   70  370 307 HOH   HOH A . 
I 5 HOH   71  371 251 HOH   HOH A . 
I 5 HOH   72  372 95  HOH   HOH A . 
I 5 HOH   73  373 272 HOH   HOH A . 
I 5 HOH   74  374 291 HOH   HOH A . 
I 5 HOH   75  375 315 HOH   HOH A . 
I 5 HOH   76  376 261 HOH   HOH A . 
I 5 HOH   77  377 23  HOH   HOH A . 
I 5 HOH   78  378 18  HOH   HOH A . 
I 5 HOH   79  379 27  HOH   HOH A . 
I 5 HOH   80  380 24  HOH   HOH A . 
I 5 HOH   81  381 254 HOH   HOH A . 
I 5 HOH   82  382 289 HOH   HOH A . 
I 5 HOH   83  383 42  HOH   HOH A . 
I 5 HOH   84  384 62  HOH   HOH A . 
I 5 HOH   85  385 65  HOH   HOH A . 
I 5 HOH   86  386 163 HOH   HOH A . 
I 5 HOH   87  387 167 HOH   HOH A . 
I 5 HOH   88  388 225 HOH   HOH A . 
I 5 HOH   89  389 35  HOH   HOH A . 
I 5 HOH   90  390 158 HOH   HOH A . 
I 5 HOH   91  391 49  HOH   HOH A . 
I 5 HOH   92  392 8   HOH   HOH A . 
I 5 HOH   93  393 30  HOH   HOH A . 
I 5 HOH   94  394 190 HOH   HOH A . 
I 5 HOH   95  395 146 HOH   HOH A . 
I 5 HOH   96  396 114 HOH   HOH A . 
I 5 HOH   97  397 157 HOH   HOH A . 
I 5 HOH   98  398 199 HOH   HOH A . 
I 5 HOH   99  399 117 HOH   HOH A . 
I 5 HOH   100 400 182 HOH   HOH A . 
I 5 HOH   101 401 301 HOH   HOH A . 
I 5 HOH   102 402 72  HOH   HOH A . 
I 5 HOH   103 403 196 HOH   HOH A . 
I 5 HOH   104 404 76  HOH   HOH A . 
I 5 HOH   105 405 87  HOH   HOH A . 
I 5 HOH   106 406 29  HOH   HOH A . 
I 5 HOH   107 407 234 HOH   HOH A . 
I 5 HOH   108 408 143 HOH   HOH A . 
I 5 HOH   109 409 141 HOH   HOH A . 
I 5 HOH   110 410 193 HOH   HOH A . 
I 5 HOH   111 411 185 HOH   HOH A . 
I 5 HOH   112 412 268 HOH   HOH A . 
I 5 HOH   113 413 74  HOH   HOH A . 
I 5 HOH   114 414 312 HOH   HOH A . 
I 5 HOH   115 415 310 HOH   HOH A . 
I 5 HOH   116 416 67  HOH   HOH A . 
I 5 HOH   117 417 259 HOH   HOH A . 
I 5 HOH   118 418 317 HOH   HOH A . 
I 5 HOH   119 419 130 HOH   HOH A . 
I 5 HOH   120 420 319 HOH   HOH A . 
I 5 HOH   121 421 15  HOH   HOH A . 
I 5 HOH   122 422 119 HOH   HOH A . 
I 5 HOH   123 423 70  HOH   HOH A . 
I 5 HOH   124 424 341 HOH   HOH A . 
I 5 HOH   125 425 13  HOH   HOH A . 
I 5 HOH   126 426 309 HOH   HOH A . 
I 5 HOH   127 427 329 HOH   HOH A . 
I 5 HOH   128 428 184 HOH   HOH A . 
I 5 HOH   129 429 31  HOH   HOH A . 
I 5 HOH   130 430 297 HOH   HOH A . 
I 5 HOH   131 431 241 HOH   HOH A . 
I 5 HOH   132 432 194 HOH   HOH A . 
I 5 HOH   133 433 236 HOH   HOH A . 
I 5 HOH   134 434 71  HOH   HOH A . 
I 5 HOH   135 435 224 HOH   HOH A . 
I 5 HOH   136 436 148 HOH   HOH A . 
I 5 HOH   137 437 28  HOH   HOH A . 
I 5 HOH   138 438 79  HOH   HOH A . 
I 5 HOH   139 439 59  HOH   HOH A . 
I 5 HOH   140 440 280 HOH   HOH A . 
I 5 HOH   141 441 73  HOH   HOH A . 
I 5 HOH   142 442 285 HOH   HOH A . 
I 5 HOH   143 443 64  HOH   HOH A . 
I 5 HOH   144 444 293 HOH   HOH A . 
I 5 HOH   145 445 304 HOH   HOH A . 
I 5 HOH   146 446 181 HOH   HOH A . 
I 5 HOH   147 447 345 HOH   HOH A . 
I 5 HOH   148 448 260 HOH   HOH A . 
I 5 HOH   149 449 257 HOH   HOH A . 
I 5 HOH   150 450 279 HOH   HOH A . 
I 5 HOH   151 451 344 HOH   HOH A . 
I 5 HOH   152 452 298 HOH   HOH A . 
I 5 HOH   153 453 313 HOH   HOH A . 
I 5 HOH   154 454 222 HOH   HOH A . 
I 5 HOH   155 455 282 HOH   HOH A . 
I 5 HOH   156 456 264 HOH   HOH A . 
I 5 HOH   157 457 250 HOH   HOH A . 
I 5 HOH   158 458 218 HOH   HOH A . 
I 5 HOH   159 459 195 HOH   HOH A . 
I 5 HOH   160 460 201 HOH   HOH A . 
I 5 HOH   161 461 171 HOH   HOH A . 
I 5 HOH   162 462 276 HOH   HOH A . 
I 5 HOH   163 463 173 HOH   HOH A . 
I 5 HOH   164 464 269 HOH   HOH A . 
I 5 HOH   165 465 267 HOH   HOH A . 
I 5 HOH   166 466 340 HOH   HOH A . 
I 5 HOH   167 467 349 HOH   HOH A . 
I 5 HOH   168 468 332 HOH   HOH A . 
I 5 HOH   169 469 161 HOH   HOH A . 
I 5 HOH   170 470 159 HOH   HOH A . 
I 5 HOH   171 471 92  HOH   HOH A . 
I 5 HOH   172 472 258 HOH   HOH A . 
I 5 HOH   173 473 283 HOH   HOH A . 
I 5 HOH   174 474 115 HOH   HOH A . 
I 5 HOH   175 475 350 HOH   HOH A . 
I 5 HOH   176 476 227 HOH   HOH A . 
I 5 HOH   177 477 219 HOH   HOH A . 
J 5 HOH   1   301 105 HOH   HOH C . 
J 5 HOH   2   302 170 HOH   HOH C . 
J 5 HOH   3   303 337 HOH   HOH C . 
J 5 HOH   4   304 139 HOH   HOH C . 
J 5 HOH   5   305 133 HOH   HOH C . 
J 5 HOH   6   306 61  HOH   HOH C . 
J 5 HOH   7   307 89  HOH   HOH C . 
J 5 HOH   8   308 123 HOH   HOH C . 
J 5 HOH   9   309 90  HOH   HOH C . 
J 5 HOH   10  310 39  HOH   HOH C . 
J 5 HOH   11  311 12  HOH   HOH C . 
J 5 HOH   12  312 221 HOH   HOH C . 
J 5 HOH   13  313 243 HOH   HOH C . 
J 5 HOH   14  314 36  HOH   HOH C . 
J 5 HOH   15  315 97  HOH   HOH C . 
J 5 HOH   16  316 169 HOH   HOH C . 
J 5 HOH   17  317 328 HOH   HOH C . 
J 5 HOH   18  318 186 HOH   HOH C . 
J 5 HOH   19  319 82  HOH   HOH C . 
J 5 HOH   20  320 162 HOH   HOH C . 
J 5 HOH   21  321 311 HOH   HOH C . 
J 5 HOH   22  322 175 HOH   HOH C . 
J 5 HOH   23  323 155 HOH   HOH C . 
J 5 HOH   24  324 32  HOH   HOH C . 
J 5 HOH   25  325 323 HOH   HOH C . 
J 5 HOH   26  326 20  HOH   HOH C . 
J 5 HOH   27  327 230 HOH   HOH C . 
J 5 HOH   28  328 37  HOH   HOH C . 
J 5 HOH   29  329 296 HOH   HOH C . 
J 5 HOH   30  330 91  HOH   HOH C . 
J 5 HOH   31  331 326 HOH   HOH C . 
J 5 HOH   32  332 188 HOH   HOH C . 
J 5 HOH   33  333 217 HOH   HOH C . 
J 5 HOH   34  334 248 HOH   HOH C . 
J 5 HOH   35  335 112 HOH   HOH C . 
J 5 HOH   36  336 53  HOH   HOH C . 
J 5 HOH   37  337 294 HOH   HOH C . 
J 5 HOH   38  338 214 HOH   HOH C . 
J 5 HOH   39  339 2   HOH   HOH C . 
J 5 HOH   40  340 151 HOH   HOH C . 
J 5 HOH   41  341 321 HOH   HOH C . 
J 5 HOH   42  342 135 HOH   HOH C . 
J 5 HOH   43  343 203 HOH   HOH C . 
J 5 HOH   44  344 45  HOH   HOH C . 
J 5 HOH   45  345 14  HOH   HOH C . 
J 5 HOH   46  346 314 HOH   HOH C . 
J 5 HOH   47  347 198 HOH   HOH C . 
J 5 HOH   48  348 44  HOH   HOH C . 
J 5 HOH   49  349 202 HOH   HOH C . 
J 5 HOH   50  350 290 HOH   HOH C . 
J 5 HOH   51  351 164 HOH   HOH C . 
J 5 HOH   52  352 3   HOH   HOH C . 
J 5 HOH   53  353 192 HOH   HOH C . 
J 5 HOH   54  354 16  HOH   HOH C . 
J 5 HOH   55  355 34  HOH   HOH C . 
J 5 HOH   56  356 273 HOH   HOH C . 
J 5 HOH   57  357 229 HOH   HOH C . 
J 5 HOH   58  358 54  HOH   HOH C . 
J 5 HOH   59  359 140 HOH   HOH C . 
J 5 HOH   60  360 342 HOH   HOH C . 
J 5 HOH   61  361 271 HOH   HOH C . 
J 5 HOH   62  362 265 HOH   HOH C . 
J 5 HOH   63  363 106 HOH   HOH C . 
J 5 HOH   64  364 111 HOH   HOH C . 
J 5 HOH   65  365 22  HOH   HOH C . 
J 5 HOH   66  366 138 HOH   HOH C . 
J 5 HOH   67  367 134 HOH   HOH C . 
J 5 HOH   68  368 58  HOH   HOH C . 
J 5 HOH   69  369 107 HOH   HOH C . 
J 5 HOH   70  370 55  HOH   HOH C . 
J 5 HOH   71  371 5   HOH   HOH C . 
J 5 HOH   72  372 102 HOH   HOH C . 
J 5 HOH   73  373 56  HOH   HOH C . 
J 5 HOH   74  374 60  HOH   HOH C . 
J 5 HOH   75  375 197 HOH   HOH C . 
J 5 HOH   76  376 179 HOH   HOH C . 
J 5 HOH   77  377 17  HOH   HOH C . 
J 5 HOH   78  378 253 HOH   HOH C . 
J 5 HOH   79  379 204 HOH   HOH C . 
J 5 HOH   80  380 302 HOH   HOH C . 
J 5 HOH   81  381 136 HOH   HOH C . 
J 5 HOH   82  382 322 HOH   HOH C . 
J 5 HOH   83  383 40  HOH   HOH C . 
J 5 HOH   84  384 262 HOH   HOH C . 
J 5 HOH   85  385 52  HOH   HOH C . 
J 5 HOH   86  386 113 HOH   HOH C . 
J 5 HOH   87  387 80  HOH   HOH C . 
J 5 HOH   88  388 299 HOH   HOH C . 
J 5 HOH   89  389 215 HOH   HOH C . 
J 5 HOH   90  390 237 HOH   HOH C . 
J 5 HOH   91  391 77  HOH   HOH C . 
J 5 HOH   92  392 305 HOH   HOH C . 
J 5 HOH   93  393 206 HOH   HOH C . 
J 5 HOH   94  394 142 HOH   HOH C . 
J 5 HOH   95  395 256 HOH   HOH C . 
J 5 HOH   96  396 7   HOH   HOH C . 
J 5 HOH   97  397 1   HOH   HOH C . 
J 5 HOH   98  398 66  HOH   HOH C . 
J 5 HOH   99  399 120 HOH   HOH C . 
J 5 HOH   100 400 223 HOH   HOH C . 
J 5 HOH   101 401 96  HOH   HOH C . 
J 5 HOH   102 402 4   HOH   HOH C . 
J 5 HOH   103 403 100 HOH   HOH C . 
J 5 HOH   104 404 252 HOH   HOH C . 
J 5 HOH   105 405 94  HOH   HOH C . 
J 5 HOH   106 406 47  HOH   HOH C . 
J 5 HOH   107 407 152 HOH   HOH C . 
J 5 HOH   108 408 287 HOH   HOH C . 
J 5 HOH   109 409 288 HOH   HOH C . 
J 5 HOH   110 410 122 HOH   HOH C . 
J 5 HOH   111 411 41  HOH   HOH C . 
J 5 HOH   112 412 38  HOH   HOH C . 
J 5 HOH   113 413 78  HOH   HOH C . 
J 5 HOH   114 414 245 HOH   HOH C . 
J 5 HOH   115 415 339 HOH   HOH C . 
J 5 HOH   116 416 124 HOH   HOH C . 
J 5 HOH   117 417 131 HOH   HOH C . 
J 5 HOH   118 418 132 HOH   HOH C . 
J 5 HOH   119 419 129 HOH   HOH C . 
J 5 HOH   120 420 144 HOH   HOH C . 
J 5 HOH   121 421 220 HOH   HOH C . 
J 5 HOH   122 422 126 HOH   HOH C . 
J 5 HOH   123 423 213 HOH   HOH C . 
J 5 HOH   124 424 330 HOH   HOH C . 
J 5 HOH   125 425 336 HOH   HOH C . 
J 5 HOH   126 426 57  HOH   HOH C . 
J 5 HOH   127 427 150 HOH   HOH C . 
J 5 HOH   128 428 33  HOH   HOH C . 
J 5 HOH   129 429 9   HOH   HOH C . 
J 5 HOH   130 430 50  HOH   HOH C . 
J 5 HOH   131 431 160 HOH   HOH C . 
J 5 HOH   132 432 110 HOH   HOH C . 
J 5 HOH   133 433 216 HOH   HOH C . 
J 5 HOH   134 434 69  HOH   HOH C . 
J 5 HOH   135 435 26  HOH   HOH C . 
J 5 HOH   136 436 249 HOH   HOH C . 
J 5 HOH   137 437 137 HOH   HOH C . 
J 5 HOH   138 438 284 HOH   HOH C . 
J 5 HOH   139 439 109 HOH   HOH C . 
J 5 HOH   140 440 153 HOH   HOH C . 
J 5 HOH   141 441 281 HOH   HOH C . 
J 5 HOH   142 442 247 HOH   HOH C . 
J 5 HOH   143 443 308 HOH   HOH C . 
J 5 HOH   144 444 211 HOH   HOH C . 
J 5 HOH   145 445 277 HOH   HOH C . 
J 5 HOH   146 446 174 HOH   HOH C . 
J 5 HOH   147 447 306 HOH   HOH C . 
J 5 HOH   148 448 324 HOH   HOH C . 
J 5 HOH   149 449 244 HOH   HOH C . 
J 5 HOH   150 450 93  HOH   HOH C . 
J 5 HOH   151 451 240 HOH   HOH C . 
J 5 HOH   152 452 149 HOH   HOH C . 
J 5 HOH   153 453 118 HOH   HOH C . 
J 5 HOH   154 454 274 HOH   HOH C . 
J 5 HOH   155 455 189 HOH   HOH C . 
J 5 HOH   156 456 335 HOH   HOH C . 
J 5 HOH   157 457 238 HOH   HOH C . 
J 5 HOH   158 458 275 HOH   HOH C . 
J 5 HOH   159 459 235 HOH   HOH C . 
J 5 HOH   160 460 239 HOH   HOH C . 
J 5 HOH   161 461 172 HOH   HOH C . 
J 5 HOH   162 462 191 HOH   HOH C . 
J 5 HOH   163 463 347 HOH   HOH C . 
J 5 HOH   164 464 278 HOH   HOH C . 
J 5 HOH   165 465 231 HOH   HOH C . 
J 5 HOH   166 466 318 HOH   HOH C . 
J 5 HOH   167 467 200 HOH   HOH C . 
J 5 HOH   168 468 228 HOH   HOH C . 
J 5 HOH   169 469 147 HOH   HOH C . 
J 5 HOH   170 470 346 HOH   HOH C . 
J 5 HOH   171 471 205 HOH   HOH C . 
J 5 HOH   172 472 246 HOH   HOH C . 
J 5 HOH   173 473 226 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           7HYO 
_cell.length_a           86.808 
_cell.length_b           57.314 
_cell.length_c           64.849 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.78 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYO 
_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          7HYO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.53 
_exptl_crystal.density_percent_sol   51.36 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-09 
_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   0.92199 
_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        0.92199 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HYO 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.60 
_reflns.d_resolution_high            1.17 
_reflns.number_obs                   76744 
_reflns.percent_possible_obs         71.9 
_reflns.pdbx_Rmerge_I_obs            0.057 
_reflns.pdbx_netI_over_sigmaI        18.8 
_reflns.pdbx_redundancy              5.9 
_reflns.pdbx_Rrim_I_all              0.062 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     453896 
_reflns.pdbx_chi_squared             1.15 
_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                  1.17 
_reflns_shell.d_res_low                   1.19 
_reflns_shell.number_measured_all         789 
_reflns_shell.number_unique_obs           609 
_reflns_shell.Rmerge_I_obs                0.920 
_reflns_shell.pdbx_chi_squared            0.40 
_reflns_shell.pdbx_redundancy             1.3 
_reflns_shell.percent_possible_obs        11.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             1.298 
_reflns_shell.pdbx_Rpim_I_all             0.915 
_reflns_shell.pdbx_CC_half                0.186 
_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                                 7HYO 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     76689 
_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                             16.96 
_refine.ls_d_res_high                            1.170 
_refine.ls_percent_reflns_obs                    71.9 
_refine.ls_R_factor_obs                          0.1887 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1880 
_refine.ls_R_factor_R_free                       0.2027 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.970 
_refine.ls_number_reflns_R_free                  3815 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_refine.B_iso_mean                               20.28 
_refine.aniso_B[1][1]                            -0.22460 
_refine.aniso_B[2][2]                            -1.35920 
_refine.aniso_B[3][3]                            1.58380 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.40270 
_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             0.048 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.048 
_refine.pdbx_overall_SU_R_Blow_DPI               0.051 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.050 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYO 
_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         33 
_refine_hist.number_atoms_solvent             350 
_refine_hist.number_atoms_total               2549 
_refine_hist.d_res_high                       1.170 
_refine_hist.d_res_low                        16.96 
# 
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  2265 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.14  ? 2.00  3084 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  756  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2265 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.15  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.38 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  278  '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  2045 '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                       1.17 
_refine_ls_shell.d_res_low                        1.21 
_refine_ls_shell.number_reflns_R_work             1450 
_refine_ls_shell.R_factor_R_work                  0.3253 
_refine_ls_shell.percent_reflns_obs               14.02 
_refine_ls_shell.R_factor_R_free                  0.3231 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.48 
_refine_ls_shell.number_reflns_R_free             84 
_refine_ls_shell.number_reflns_all                1534 
_refine_ls_shell.R_factor_all                     0.3252 
# 
_struct.entry_id                  7HYO 
_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-0036262-001 (A71EV2A-x4402)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYO 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HYO A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HYO C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,I 
2 1 B,F,G,H,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 109.2 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 104.8 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.7 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 105.8 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 102.1 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 118.7 ? 
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_555 109.8 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.5 ? 
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_555 106.2 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.5 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O 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                   7HYO 
_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 391 ? ? O A HOH 418 ? ? 1.48 
2 1 CB  C SER 66  ? ? O C HOH 303 ? ? 1.61 
3 1 O   C HOH 368 ? ? O C HOH 380 ? ? 1.99 
4 1 O   C HOH 359 ? ? O C HOH 382 ? ? 2.03 
5 1 O   A HOH 315 ? ? O A HOH 369 ? ? 2.13 
6 1 OE2 C GLU 106 ? ? O C HOH 301 ? ? 2.16 
# 
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 ASN A 14 ? ? -106.24 41.86 
2 1 ASN C 14 ? ? -105.81 41.02 
# 
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 14.9529 8.2532   14.2926 -0.0126 -0.0255 0.0040 0.0138 0.0112 0.0022 1.3857 0.8908 0.6643 0.8770  
-0.4085 -0.4529 -0.0026 0.0473  0.1224 0.0546 0.0593 0.0351 -0.0435 -0.0688 -0.0567 
'X-RAY DIFFRACTION' 2 ? refined 25.8527 -20.2547 17.7998 -0.0217 -0.0173 0.0157 0.0078 0.0099 0.0164 0.5745 0.9003 0.3506 -0.0232 
-0.1194 -0.2128 0.0172  -0.0014 0.1212 0.0219 0.0496 0.0478 0.0494  -0.0020 -0.0668 
# 
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 
A1BO5 N1   N  N N 1   
A1BO5 C4   C  Y N 2   
A1BO5 C5   C  Y N 3   
A1BO5 C6   C  N N 4   
A1BO5 C7   C  N N 5   
A1BO5 C8   C  N N 6   
A1BO5 C10  C  N N 7   
A1BO5 C13  C  Y N 8   
A1BO5 O1   O  N N 9   
A1BO5 C12  C  N N 10  
A1BO5 C9   C  N N 11  
A1BO5 C11  C  N N 12  
A1BO5 O    O  N N 13  
A1BO5 N2   N  N N 14  
A1BO5 N    N  N N 15  
A1BO5 C3   C  Y N 16  
A1BO5 C2   C  Y N 17  
A1BO5 C1   C  Y N 18  
A1BO5 C    C  N N 19  
A1BO5 H5   H  N N 20  
A1BO5 H6   H  N N 21  
A1BO5 H7   H  N N 22  
A1BO5 H9   H  N N 23  
A1BO5 H8   H  N N 24  
A1BO5 H10  H  N N 25  
A1BO5 H11  H  N N 26  
A1BO5 H14  H  N N 27  
A1BO5 H15  H  N N 28  
A1BO5 H18  H  N N 29  
A1BO5 H13  H  N N 30  
A1BO5 H12  H  N N 31  
A1BO5 H17  H  N N 32  
A1BO5 H16  H  N N 33  
A1BO5 H4   H  N N 34  
A1BO5 H3   H  N N 35  
A1BO5 H1   H  N N 36  
A1BO5 H2   H  N N 37  
A1BO5 H    H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
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 
A1BO5 C   C1   sing N N 1   
A1BO5 C1  C2   doub Y N 2   
A1BO5 C2  C3   sing Y N 3   
A1BO5 C3  C4   doub Y N 4   
A1BO5 C4  C5   sing Y N 5   
A1BO5 C5  N    sing N N 6   
A1BO5 N   C6   sing N N 7   
A1BO5 C6  C7   sing N N 8   
A1BO5 C7  C8   sing N N 9   
A1BO5 C8  N1   sing N N 10  
A1BO5 C9  N1   sing N N 11  
A1BO5 C10 C9   sing N N 12  
A1BO5 C11 C10  sing N N 13  
A1BO5 N2  C11  sing N N 14  
A1BO5 O   C11  doub N N 15  
A1BO5 N1  C12  sing N N 16  
A1BO5 N   C12  sing N N 17  
A1BO5 C12 O1   doub N N 18  
A1BO5 C13 C5   doub Y N 19  
A1BO5 C1  C13  sing Y N 20  
A1BO5 C4  H5   sing N N 21  
A1BO5 C6  H6   sing N N 22  
A1BO5 C6  H7   sing N N 23  
A1BO5 C7  H9   sing N N 24  
A1BO5 C7  H8   sing N N 25  
A1BO5 C8  H10  sing N N 26  
A1BO5 C8  H11  sing N N 27  
A1BO5 C10 H14  sing N N 28  
A1BO5 C10 H15  sing N N 29  
A1BO5 C13 H18  sing N N 30  
A1BO5 C9  H13  sing N N 31  
A1BO5 C9  H12  sing N N 32  
A1BO5 N2  H17  sing N N 33  
A1BO5 N2  H16  sing N N 34  
A1BO5 C3  H4   sing N N 35  
A1BO5 C2  H3   sing N N 36  
A1BO5 C   H1   sing N N 37  
A1BO5 C   H2   sing N N 38  
A1BO5 C   H    sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
DMS   S   O    doub N N 122 
DMS   S   C1   sing N N 123 
DMS   S   C2   sing N N 124 
DMS   C1  H11  sing N N 125 
DMS   C1  H12  sing N N 126 
DMS   C1  H13  sing N N 127 
DMS   C2  H21  sing N N 128 
DMS   C2  H22  sing N N 129 
DMS   C2  H23  sing N N 130 
GLN   N   CA   sing N N 131 
GLN   N   H    sing N N 132 
GLN   N   H2   sing N N 133 
GLN   CA  C    sing N N 134 
GLN   CA  CB   sing N N 135 
GLN   CA  HA   sing N N 136 
GLN   C   O    doub N N 137 
GLN   C   OXT  sing N N 138 
GLN   CB  CG   sing N N 139 
GLN   CB  HB2  sing N N 140 
GLN   CB  HB3  sing N N 141 
GLN   CG  CD   sing N N 142 
GLN   CG  HG2  sing N N 143 
GLN   CG  HG3  sing N N 144 
GLN   CD  OE1  doub N N 145 
GLN   CD  NE2  sing N N 146 
GLN   NE2 HE21 sing N N 147 
GLN   NE2 HE22 sing N N 148 
GLN   OXT HXT  sing N N 149 
GLU   N   CA   sing N N 150 
GLU   N   H    sing N N 151 
GLU   N   H2   sing N N 152 
GLU   CA  C    sing N N 153 
GLU   CA  CB   sing N N 154 
GLU   CA  HA   sing N N 155 
GLU   C   O    doub N N 156 
GLU   C   OXT  sing N N 157 
GLU   CB  CG   sing N N 158 
GLU   CB  HB2  sing N N 159 
GLU   CB  HB3  sing N N 160 
GLU   CG  CD   sing N N 161 
GLU   CG  HG2  sing N N 162 
GLU   CG  HG3  sing N N 163 
GLU   CD  OE1  doub N N 164 
GLU   CD  OE2  sing N N 165 
GLU   OE2 HE2  sing N N 166 
GLU   OXT HXT  sing N N 167 
GLY   N   CA   sing N N 168 
GLY   N   H    sing N N 169 
GLY   N   H2   sing N N 170 
GLY   CA  C    sing N N 171 
GLY   CA  HA2  sing N N 172 
GLY   CA  HA3  sing N N 173 
GLY   C   O    doub N N 174 
GLY   C   OXT  sing N N 175 
GLY   OXT HXT  sing N N 176 
HIS   N   CA   sing N N 177 
HIS   N   H    sing N N 178 
HIS   N   H2   sing N N 179 
HIS   CA  C    sing N N 180 
HIS   CA  CB   sing N N 181 
HIS   CA  HA   sing N N 182 
HIS   C   O    doub N N 183 
HIS   C   OXT  sing N N 184 
HIS   CB  CG   sing N N 185 
HIS   CB  HB2  sing N N 186 
HIS   CB  HB3  sing N N 187 
HIS   CG  ND1  sing Y N 188 
HIS   CG  CD2  doub Y N 189 
HIS   ND1 CE1  doub Y N 190 
HIS   ND1 HD1  sing N N 191 
HIS   CD2 NE2  sing Y N 192 
HIS   CD2 HD2  sing N N 193 
HIS   CE1 NE2  sing Y N 194 
HIS   CE1 HE1  sing N N 195 
HIS   NE2 HE2  sing N N 196 
HIS   OXT HXT  sing N N 197 
HOH   O   H1   sing N N 198 
HOH   O   H2   sing N N 199 
ILE   N   CA   sing N N 200 
ILE   N   H    sing N N 201 
ILE   N   H2   sing N N 202 
ILE   CA  C    sing N N 203 
ILE   CA  CB   sing N N 204 
ILE   CA  HA   sing N N 205 
ILE   C   O    doub N N 206 
ILE   C   OXT  sing N N 207 
ILE   CB  CG1  sing N N 208 
ILE   CB  CG2  sing N N 209 
ILE   CB  HB   sing N N 210 
ILE   CG1 CD1  sing N N 211 
ILE   CG1 HG12 sing N N 212 
ILE   CG1 HG13 sing N N 213 
ILE   CG2 HG21 sing N N 214 
ILE   CG2 HG22 sing N N 215 
ILE   CG2 HG23 sing N N 216 
ILE   CD1 HD11 sing N N 217 
ILE   CD1 HD12 sing N N 218 
ILE   CD1 HD13 sing N N 219 
ILE   OXT HXT  sing N N 220 
LEU   N   CA   sing N N 221 
LEU   N   H    sing N N 222 
LEU   N   H2   sing N N 223 
LEU   CA  C    sing N N 224 
LEU   CA  CB   sing N N 225 
LEU   CA  HA   sing N N 226 
LEU   C   O    doub N N 227 
LEU   C   OXT  sing N N 228 
LEU   CB  CG   sing N N 229 
LEU   CB  HB2  sing N N 230 
LEU   CB  HB3  sing N N 231 
LEU   CG  CD1  sing N N 232 
LEU   CG  CD2  sing N N 233 
LEU   CG  HG   sing N N 234 
LEU   CD1 HD11 sing N N 235 
LEU   CD1 HD12 sing N N 236 
LEU   CD1 HD13 sing N N 237 
LEU   CD2 HD21 sing N N 238 
LEU   CD2 HD22 sing N N 239 
LEU   CD2 HD23 sing N N 240 
LEU   OXT HXT  sing N N 241 
LYS   N   CA   sing N N 242 
LYS   N   H    sing N N 243 
LYS   N   H2   sing N N 244 
LYS   CA  C    sing N N 245 
LYS   CA  CB   sing N N 246 
LYS   CA  HA   sing N N 247 
LYS   C   O    doub N N 248 
LYS   C   OXT  sing N N 249 
LYS   CB  CG   sing N N 250 
LYS   CB  HB2  sing N N 251 
LYS   CB  HB3  sing N N 252 
LYS   CG  CD   sing N N 253 
LYS   CG  HG2  sing N N 254 
LYS   CG  HG3  sing N N 255 
LYS   CD  CE   sing N N 256 
LYS   CD  HD2  sing N N 257 
LYS   CD  HD3  sing N N 258 
LYS   CE  NZ   sing N N 259 
LYS   CE  HE2  sing N N 260 
LYS   CE  HE3  sing N N 261 
LYS   NZ  HZ1  sing N N 262 
LYS   NZ  HZ2  sing N N 263 
LYS   NZ  HZ3  sing N N 264 
LYS   OXT HXT  sing N N 265 
MET   N   CA   sing N N 266 
MET   N   H    sing N N 267 
MET   N   H2   sing N N 268 
MET   CA  C    sing N N 269 
MET   CA  CB   sing N N 270 
MET   CA  HA   sing N N 271 
MET   C   O    doub N N 272 
MET   C   OXT  sing N N 273 
MET   CB  CG   sing N N 274 
MET   CB  HB2  sing N N 275 
MET   CB  HB3  sing N N 276 
MET   CG  SD   sing N N 277 
MET   CG  HG2  sing N N 278 
MET   CG  HG3  sing N N 279 
MET   SD  CE   sing N N 280 
MET   CE  HE1  sing N N 281 
MET   CE  HE2  sing N N 282 
MET   CE  HE3  sing N N 283 
MET   OXT HXT  sing N N 284 
PHE   N   CA   sing N N 285 
PHE   N   H    sing N N 286 
PHE   N   H2   sing N N 287 
PHE   CA  C    sing N N 288 
PHE   CA  CB   sing N N 289 
PHE   CA  HA   sing N N 290 
PHE   C   O    doub N N 291 
PHE   C   OXT  sing N N 292 
PHE   CB  CG   sing N N 293 
PHE   CB  HB2  sing N N 294 
PHE   CB  HB3  sing N N 295 
PHE   CG  CD1  doub Y N 296 
PHE   CG  CD2  sing Y N 297 
PHE   CD1 CE1  sing Y N 298 
PHE   CD1 HD1  sing N N 299 
PHE   CD2 CE2  doub Y N 300 
PHE   CD2 HD2  sing N N 301 
PHE   CE1 CZ   doub Y N 302 
PHE   CE1 HE1  sing N N 303 
PHE   CE2 CZ   sing Y N 304 
PHE   CE2 HE2  sing N N 305 
PHE   CZ  HZ   sing N N 306 
PHE   OXT HXT  sing N N 307 
PRO   N   CA   sing N N 308 
PRO   N   CD   sing N N 309 
PRO   N   H    sing N N 310 
PRO   CA  C    sing N N 311 
PRO   CA  CB   sing N N 312 
PRO   CA  HA   sing N N 313 
PRO   C   O    doub N N 314 
PRO   C   OXT  sing N N 315 
PRO   CB  CG   sing N N 316 
PRO   CB  HB2  sing N N 317 
PRO   CB  HB3  sing N N 318 
PRO   CG  CD   sing N N 319 
PRO   CG  HG2  sing N N 320 
PRO   CG  HG3  sing N N 321 
PRO   CD  HD2  sing N N 322 
PRO   CD  HD3  sing N N 323 
PRO   OXT HXT  sing N N 324 
SER   N   CA   sing N N 325 
SER   N   H    sing N N 326 
SER   N   H2   sing N N 327 
SER   CA  C    sing N N 328 
SER   CA  CB   sing N N 329 
SER   CA  HA   sing N N 330 
SER   C   O    doub N N 331 
SER   C   OXT  sing N N 332 
SER   CB  OG   sing N N 333 
SER   CB  HB2  sing N N 334 
SER   CB  HB3  sing N N 335 
SER   OG  HG   sing N N 336 
SER   OXT HXT  sing N N 337 
THR   N   CA   sing N N 338 
THR   N   H    sing N N 339 
THR   N   H2   sing N N 340 
THR   CA  C    sing N N 341 
THR   CA  CB   sing N N 342 
THR   CA  HA   sing N N 343 
THR   C   O    doub N N 344 
THR   C   OXT  sing N N 345 
THR   CB  OG1  sing N N 346 
THR   CB  CG2  sing N N 347 
THR   CB  HB   sing N N 348 
THR   OG1 HG1  sing N N 349 
THR   CG2 HG21 sing N N 350 
THR   CG2 HG22 sing N N 351 
THR   CG2 HG23 sing N N 352 
THR   OXT HXT  sing N N 353 
TRP   N   CA   sing N N 354 
TRP   N   H    sing N N 355 
TRP   N   H2   sing N N 356 
TRP   CA  C    sing N N 357 
TRP   CA  CB   sing N N 358 
TRP   CA  HA   sing N N 359 
TRP   C   O    doub N N 360 
TRP   C   OXT  sing N N 361 
TRP   CB  CG   sing N N 362 
TRP   CB  HB2  sing N N 363 
TRP   CB  HB3  sing N N 364 
TRP   CG  CD1  doub Y N 365 
TRP   CG  CD2  sing Y N 366 
TRP   CD1 NE1  sing Y N 367 
TRP   CD1 HD1  sing N N 368 
TRP   CD2 CE2  doub Y N 369 
TRP   CD2 CE3  sing Y N 370 
TRP   NE1 CE2  sing Y N 371 
TRP   NE1 HE1  sing N N 372 
TRP   CE2 CZ2  sing Y N 373 
TRP   CE3 CZ3  doub Y N 374 
TRP   CE3 HE3  sing N N 375 
TRP   CZ2 CH2  doub Y N 376 
TRP   CZ2 HZ2  sing N N 377 
TRP   CZ3 CH2  sing Y N 378 
TRP   CZ3 HZ3  sing N N 379 
TRP   CH2 HH2  sing N N 380 
TRP   OXT HXT  sing N N 381 
TYR   N   CA   sing N N 382 
TYR   N   H    sing N N 383 
TYR   N   H2   sing N N 384 
TYR   CA  C    sing N N 385 
TYR   CA  CB   sing N N 386 
TYR   CA  HA   sing N N 387 
TYR   C   O    doub N N 388 
TYR   C   OXT  sing N N 389 
TYR   CB  CG   sing N N 390 
TYR   CB  HB2  sing N N 391 
TYR   CB  HB3  sing N N 392 
TYR   CG  CD1  doub Y N 393 
TYR   CG  CD2  sing Y N 394 
TYR   CD1 CE1  sing Y N 395 
TYR   CD1 HD1  sing N N 396 
TYR   CD2 CE2  doub Y N 397 
TYR   CD2 HD2  sing N N 398 
TYR   CE1 CZ   doub Y N 399 
TYR   CE1 HE1  sing N N 400 
TYR   CE2 CZ   sing Y N 401 
TYR   CE2 HE2  sing N N 402 
TYR   CZ  OH   sing N N 403 
TYR   OH  HH   sing N N 404 
TYR   OXT HXT  sing N N 405 
VAL   N   CA   sing N N 406 
VAL   N   H    sing N N 407 
VAL   N   H2   sing N N 408 
VAL   CA  C    sing N N 409 
VAL   CA  CB   sing N N 410 
VAL   CA  HA   sing N N 411 
VAL   C   O    doub N N 412 
VAL   C   OXT  sing N N 413 
VAL   CB  CG1  sing N N 414 
VAL   CB  CG2  sing N N 415 
VAL   CB  HB   sing N N 416 
VAL   CG1 HG11 sing N N 417 
VAL   CG1 HG12 sing N N 418 
VAL   CG1 HG13 sing N N 419 
VAL   CG2 HG21 sing N N 420 
VAL   CG2 HG22 sing N N 421 
VAL   CG2 HG23 sing N N 422 
VAL   OXT HXT  sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HYO 
_atom_sites.fract_transf_matrix[1][1]   0.011520 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000963 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017448 
_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]   0.015474 
_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   ? 17.499 8.242   24.729 1.00 17.35  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.742 8.318   23.951 1.00 17.03  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.872 7.113   23.040 1.00 16.65  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.154 6.113   23.231 1.00 17.12  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 19.941 8.425   24.895 1.00 20.29  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.043 7.249   25.675 1.00 23.62  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.813 7.163   22.089 1.00 14.81  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.098 6.029   21.205 1.00 13.43  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.490 6.488   19.822 1.00 13.05  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.196 7.608   19.414 1.00 14.15  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.212 5.637   19.140 1.00 11.45  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.718 5.970   17.800 1.00 11.57  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.698 4.739   16.918 1.00 11.59  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.595 3.595   17.394 1.00 13.37  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.164 6.508   17.929 1.00 13.89  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.791 4.970   15.610 1.00 10.77  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.025 3.911   14.598 1.00 10.94  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.502 3.997   14.238 1.00 11.67  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 23.993 5.107   13.942 1.00 11.83  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.182 4.095   13.335 1.00 11.15  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.661 4.271   13.650 1.00 12.63  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.403 2.902   12.355 1.00 12.66  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.894 4.809   12.446 1.00 13.75  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.226 2.851   14.235 1.00 11.25  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.648 2.850   13.858 1.00 12.28  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.749 1.995   12.585 1.00 12.84  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.767 0.759   12.657 1.00 13.30  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.474 2.236   15.006 1.00 14.08  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.524 3.137   16.221 1.00 13.09  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.389 4.232   16.268 1.00 13.41  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.682 2.932   17.306 1.00 14.47  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.392 5.107   17.356 1.00 14.97  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.686 3.795   18.397 1.00 14.99  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.520 4.894   18.403 1.00 15.65  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.516 5.765   19.495 1.00 18.18  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.817 2.647   11.430 1.00 12.85  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.913 1.992   10.128 1.00 13.02  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.159 2.506   9.445  1.00 13.93  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.396 3.721   9.395  1.00 13.56  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.624 2.279   9.274  1.00 14.05  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.261 3.781   9.214  1.00 15.74  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.791 1.711   7.874  1.00 16.09  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.028 1.601   8.987  1.00 15.98  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.267 2.030   8.338  1.00 15.70  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.098 2.907   9.271  1.00 14.96  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.204 2.613   10.474 1.00 15.25  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.545 4.068   8.748  1.00 14.44  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.227 5.050   9.598  1.00 14.09  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.318 6.239   9.876  1.00 13.94  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.812 7.381   10.025 1.00 14.67  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.573 5.491   9.021  1.00 16.29  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.649 4.437   9.182  1.00 20.24  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.373 4.375   10.191 1.00 23.93  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.718 3.542   8.232  1.00 18.41  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.046 5.941   10.142 1.00 13.18  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.063 6.983   10.470 1.00 12.53  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.373 6.661   11.779 1.00 12.26  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.106 5.482   12.101 1.00 12.61  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.982 7.068   9.370  1.00 12.50  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.492 7.474   7.999  1.00 13.39  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.188 8.658   7.811  1.00 15.20  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.303 6.653   6.907  1.00 15.20  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.638 9.043   6.552  1.00 16.26  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.744 7.025   5.636  1.00 16.60  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.403 8.228   5.465  1.00 17.22  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.859 8.635   4.211  1.00 20.91  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.036 7.736   12.519 1.00 12.23  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.224 7.673   13.741 1.00 11.86  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 24.994 8.530   13.475 1.00 11.93  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.160 9.743   13.175 1.00 12.25  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.040 8.233   14.958 1.00 12.75  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.231 8.551   16.211 1.00 13.81  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.145 8.936   17.399 1.00 13.94  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.561 9.999   18.222 1.00 14.94  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.853 9.802   19.334 1.00 17.64  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.563 8.570   19.735 1.00 17.80  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.404 10.837  20.030 1.00 16.82  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.805 7.920   13.507 1.00 11.20  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.547 8.657   13.247 1.00 10.76  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.843 8.858   14.562 1.00 11.65  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.503 7.860   15.260 1.00 11.84  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.612 7.842   12.307 1.00 11.52  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.386 8.713   11.896 1.00 12.73  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.327 7.312   11.058 1.00 12.74  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.575 10.117  14.907 1.00 10.74  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 20.906 10.464  16.184 0.50 10.42  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 20.959 10.453  16.202 0.50 12.77  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.800 11.447  15.961 1.00 11.72  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.675 12.064  14.890 1.00 12.79  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 21.896 11.056  17.242 0.50 10.06  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.095 11.086  17.106 0.50 17.05  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.810 9.959   17.768 0.50 11.14  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.636 11.373  18.520 0.50 18.99  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.647 12.301  16.702 0.50 8.02   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.324 10.196  17.159 0.50 19.13  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 18.940 11.650  16.988 1.00 12.28  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 17.926 12.717  16.921 1.00 12.42  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.734 14.037  16.944 1.00 12.49  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.651 14.208  17.781 1.00 12.83  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.057 12.711  18.185 1.00 12.97  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.207 11.479  18.294 1.00 12.35  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.618 10.488  18.935 1.00 14.97  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.055 11.535  17.626 1.00 14.06  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.395 14.962  16.033 1.00 11.76  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.149 16.257  16.005 1.00 12.70  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.048 16.938  17.357 1.00 15.06  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.025 17.490  17.826 1.00 15.49  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.567 17.146  14.908 1.00 13.15  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.384 18.442  14.627 1.00 14.30  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.619 19.341  13.670 1.00 14.54  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.383 20.517  13.227 1.00 15.94  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.355 21.690  13.845 1.00 18.45  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.780 21.806  15.032 1.00 19.27  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.985 22.742  13.317 1.00 19.38  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 17.880 16.838  18.015 1.00 13.98  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.681 17.541  19.290 1.00 16.01  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.495 16.944  20.446 1.00 17.71  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.576 17.581  21.500 1.00 19.17  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.183 17.692  19.650 1.00 16.96  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.513 16.448  20.164 1.00 16.46  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 14.892 15.550  19.299 1.00 16.43  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.197 16.086  21.441 1.00 17.68  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.348 14.589  20.069 1.00 18.18  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.501 14.868  21.372 1.00 18.73  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.066 15.732  20.284 1.00 16.18  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 19.914 15.085  21.295 1.00 15.53  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.402 15.011  20.884 1.00 17.06  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.211 14.376  21.548 1.00 17.87  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.396 13.686  21.629 1.00 16.21  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 17.975 13.666  22.148 1.00 17.10  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.581 12.231  22.470 1.00 16.98  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 17.778 14.501  23.444 1.00 19.67  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.767 15.631  19.723 1.00 16.08  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.156 15.586  19.277 1.00 16.35  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.099 16.215  20.285 1.00 16.66  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.776 17.255  20.880 1.00 18.10  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.303 16.281  17.914 1.00 15.74  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.281 15.613  20.442 1.00 15.55  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.326 16.137  21.336 1.00 16.80  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.231 17.150  20.627 1.00 18.17  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.221 17.281  19.377 1.00 16.83  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.194 14.963  21.849 1.00 19.63  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 27.972 14.426  20.763 1.00 19.92  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.372 13.878  22.510 1.00 21.04  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.135 17.827  21.403 1.00 18.70  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.121 18.689  20.794 1.00 17.96  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.019 17.888  19.846 1.00 17.44  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.343 18.361  18.768 1.00 16.80  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.018 19.401  21.854 1.00 19.46  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.220 20.124  21.243 1.00 28.01  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.094 21.358  20.617 1.00 33.87  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.490 19.680  21.059 1.00 31.75  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.305 21.687  20.191 1.00 33.61  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.183 20.703  20.410 1.00 34.74  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.414 16.653  20.248 1.00 16.76  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.254 15.847  19.375 1.00 16.70  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.530 15.532  18.038 1.00 15.49  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.167 15.541  16.996 1.00 16.05  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.711 14.521  20.019 1.00 19.15  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.706 13.802  19.145 1.00 27.45  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 33.845 14.280  18.939 1.00 31.10  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.275 12.705  18.519 1.00 30.37  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.197 15.321  18.067 1.00 14.61  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.437 15.109  16.835 1.00 13.58  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.503 16.352  15.926 1.00 12.87  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.807 16.221  14.731 1.00 13.88  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 26.968 14.808  17.146 1.00 14.12  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.714 13.452  17.751 1.00 14.94  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.385 12.470  17.320 1.00 14.84  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.843 13.361  18.648 1.00 15.25  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.309 17.555  16.489 1.00 13.56  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.380 18.784  15.687 1.00 13.81  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.779 19.063  15.158 1.00 14.49  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.908 19.642  14.075 1.00 14.84  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.906 19.989  16.557 1.00 14.54  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.389 20.053  16.663 1.00 15.10  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.600 19.721  17.736 1.00 16.25  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.492 20.501  15.635 1.00 15.20  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.281 19.951  17.440 1.00 15.69  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.177 20.385  16.136 1.00 15.60  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.676 20.899  14.301 1.00 16.78  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.063 20.789  15.378 1.00 17.57  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.583 21.240  13.545 1.00 17.25  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.303 21.215  14.081 1.00 17.37  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.820 18.641  15.907 1.00 13.75  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.202 18.876  15.476 1.00 14.86  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.663 17.839  14.435 1.00 16.18  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.707 17.998  13.821 1.00 17.49  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.118 18.839  16.708 1.00 16.73  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.849 16.778  14.190 1.00 14.58  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.164 15.710  13.200 1.00 15.51  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.942 15.531  12.298 1.00 14.30  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.562 14.404  11.963 1.00 14.42  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.541 14.388  13.961 1.00 15.66  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.888 14.595  14.623 1.00 19.50  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.931 14.544  13.961 1.00 22.67  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.884 14.935  15.926 1.00 20.02  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.307 16.623  11.914 1.00 13.82  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.027 16.584  11.240 1.00 12.67  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.096 16.127  9.817  1.00 14.49  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.966 16.612  9.042  1.00 16.50  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.424 18.026  11.299 1.00 13.78  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.049 18.161  10.655 1.00 14.11  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.964 17.386  11.439 1.00 13.23  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.595 19.617  10.611 1.00 16.88  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.182 15.246  9.405  1.00 13.31  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.033 14.829  8.015  1.00 13.79  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.802 15.536  7.394  1.00 14.58  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.858 16.077  6.275  1.00 15.68  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.911 13.303  7.907  1.00 13.24  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.562 12.896  6.456  1.00 15.59  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.195 12.623  8.398  1.00 15.26  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.634 15.485  8.086  1.00 13.27  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.387 16.012  7.571  1.00 13.89  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.419 16.255  8.712  1.00 13.73  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.441 15.476  9.677  1.00 13.49  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.796 15.016  6.533  1.00 15.07  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.412 15.292  6.071  1.00 16.18  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 22.030 16.120  5.048  1.00 18.63  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.205 14.656  6.545  1.00 16.01  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.663 16.055  4.875  1.00 19.84  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.132 15.164  5.783  1.00 17.99  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.926 13.730  7.561  1.00 16.19  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.808 14.701  5.950  1.00 18.79  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.627 13.270  7.711  1.00 16.98  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.582 13.777  6.947  1.00 18.05  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.564 17.258  8.608  1.00 14.87  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.535 17.468  9.611  1.00 14.70  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.336 18.068  8.953  1.00 15.86  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.467 18.868  8.002  1.00 16.06  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.020 18.312  10.773 1.00 15.45  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.624 19.667  10.404 1.00 16.19  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.675 20.835  10.159 1.00 17.17  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.047 21.782  9.411  1.00 19.30  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.546 20.830  10.706 1.00 18.22  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.161 17.796  9.505  1.00 14.68  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.919 18.362  8.953  1.00 14.88  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.914 18.538  10.083 1.00 14.68  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.392 17.552  10.659 1.00 14.63  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.381 17.435  7.838  1.00 17.10  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.145 17.909  7.123  1.00 20.81  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.292 18.499  7.777  1.00 25.04  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 16.006 17.608  5.909  1.00 25.29  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.683 19.800  10.478 1.00 16.12  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.767 20.113  11.562 0.50 16.72  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.780 20.058  11.591 0.50 17.03  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.336 19.653  11.248 1.00 16.95  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.622 19.182  12.150 1.00 17.74  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.773 21.625  11.808 0.50 18.60  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.870 21.523  12.021 0.50 20.23  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.787 21.994  12.754 0.50 21.58  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.570 22.349  10.914 0.50 24.61  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.918 19.770  9.977  1.00 16.97  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.541 19.349  9.597  1.00 17.51  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.308 17.853  9.750  1.00 17.22  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.165 17.460  9.944  1.00 19.17  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.181 19.765  8.181  1.00 20.37  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.785 18.984  7.163  1.00 26.44  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.366 17.039  9.793  1.00 15.49  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.259 15.590  10.021 1.00 14.73  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.661 15.165  11.456 1.00 14.37  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.569 13.981  11.797 1.00 14.11  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.117 14.843  9.008  1.00 15.39  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.588 15.028  7.570  1.00 15.89  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.471 14.319  6.566  1.00 15.74  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.378 12.856  6.731  1.00 14.52  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.529 11.981  5.746  1.00 15.91  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.765 12.398  4.501  1.00 17.95  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.416 10.680  5.983  1.00 15.39  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.241 16.091  12.284 1.00 13.68  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.822 15.787  13.589 1.00 12.69  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 15.960 14.786  13.472 1.00 13.02  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.178 13.968  14.369 1.00 13.30  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.791 15.309  14.629 1.00 14.31  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.354 15.111  16.015 1.00 14.43  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.186 15.946  16.465 1.00 15.69  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 13.969 14.118  16.687 1.00 15.20  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.798 14.901  12.407 1.00 12.28  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.913 13.947  12.235 1.00 11.66  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.256 14.659  12.145 1.00 11.87  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.344 15.759  11.547 1.00 12.67  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.741 13.126  10.948 1.00 12.22  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.619 12.020  10.994 1.00 12.66  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.578 11.291  9.675  1.00 14.90  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.827 11.013  12.144 1.00 13.59  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.283 13.994  12.643 1.00 11.72  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.683 14.456  12.481 1.00 11.53  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.523 13.240  12.350 1.00 11.69  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.324 12.215  13.039 1.00 11.88  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.115 15.308  13.681 1.00 12.54  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.553 15.906  13.635 1.00 12.25  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.626 17.257  14.328 1.00 13.33  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.578 14.953  14.251 1.00 12.76  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.528 13.320  11.456 1.00 11.70  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.475 12.229  11.211 1.00 11.28  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.880 12.736  11.387 1.00 11.13  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.226 13.790  10.797 1.00 12.13  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.288 11.621  9.790  1.00 10.99  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.293 10.508  9.541  1.00 13.12  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.851 11.084  9.620  1.00 12.40  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.667 12.058  12.215 1.00 11.45  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.083 12.398  12.416 1.00 11.59  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.957 11.243  11.979 1.00 12.13  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.499 10.101  11.773 1.00 12.49  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.335 12.746  13.884 1.00 13.58  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 27.978 11.676  14.752 1.00 14.00  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.245 11.520  11.800 1.00 13.41  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.195 10.483  11.380 1.00 14.72  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.813 9.755   12.586 1.00 16.70  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 31.968 10.349  13.673 1.00 18.86  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.278 11.106  10.508 1.00 18.16  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.004 12.064  11.266 1.00 19.50  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.160 8.461   12.407 1.00 16.28  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.726 7.628   13.471 1.00 17.69  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.085 7.057   13.045 1.00 19.71  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.341 6.828   11.846 1.00 19.80  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.791 6.437   13.829 1.00 18.06  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.699 5.548   12.722 1.00 20.17  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.367 6.903   14.218 1.00 17.50  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.921 6.764   14.040 1.00 21.10  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.200 6.126   13.731 1.00 22.97  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 35.975 4.607   13.524 1.00 23.16  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.513 4.031   12.564 1.00 26.14  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.207 6.437   14.850 1.00 26.80  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.724 5.900   16.065 1.00 32.16  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.400 7.915   15.033 1.00 27.25  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.153 3.986   14.387 1.00 21.76  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.883 2.542   14.277 1.00 23.43  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.690 2.241   13.362 1.00 22.17  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.758 3.059   13.281 1.00 22.19  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.596 1.962   15.660 1.00 26.43  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.707 1.099   12.680 1.00 20.53  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.597 0.682   11.824 1.00 20.67  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.479 0.109   12.672 1.00 20.19  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.738 -0.655  13.604 1.00 22.00  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 33.058 -0.340  10.784 1.00 23.70  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.856 0.313   9.639  1.00 29.63  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.303 -0.714  8.625  1.00 35.00  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.119 -1.586  8.918  1.00 35.38  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.763 -0.630  7.415  1.00 36.05  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.236 0.452   12.344 1.00 16.54  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.081 -0.073  13.048 1.00 15.84  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.478 -1.314  12.427 1.00 15.91  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.804 -1.707  11.278 1.00 16.93  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.530 -1.897  13.191 1.00 15.09  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.943 -3.171  12.792 1.00 16.20  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.511 -3.134  12.362 1.00 16.12  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.970 -4.193  11.989 1.00 16.63  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.117 -4.212  13.896 1.00 16.90  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.847 -4.630  14.237 1.00 20.91  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.845 -1.985  12.446 1.00 14.04  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.452 -1.895  12.034 1.00 13.81  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.363 -1.842  10.518 1.00 14.99  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.254 -1.285  9.849  1.00 16.77  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.805 -0.646  12.658 1.00 13.46  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.688 -0.698  14.169 1.00 15.30  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.346 -1.812  14.721 1.00 15.30  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.876 0.367   14.822 1.00 15.17  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.324 -2.407  9.966  1.00 16.06  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.065 -2.364  8.508  1.00 17.29  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.735 -1.619  8.287  1.00 15.39  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.821 -1.752  9.110  1.00 16.76  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.883 -3.812  7.986  1.00 23.84  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 23.182 -4.481  8.035  1.00 28.09  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 21.301 -3.876  6.574  1.00 28.25  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.637 -0.754  7.266  1.00 15.16  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.402 0.008   7.036  1.00 14.06  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.451 -0.798  6.130  1.00 14.11  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.843 -1.357  5.061  1.00 15.51  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.738 1.358   6.369  1.00 14.19  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.829 2.136   7.143  1.00 15.16  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.462 2.238   6.226  1.00 14.73  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.399 2.450   8.637  1.00 16.10  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.200 -0.854  6.511  1.00 12.91  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.145 -1.476  5.717  1.00 13.80  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.896 -0.640  4.439  1.00 14.41  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.867 0.625   4.461  1.00 14.01  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.849 -1.533  6.509  1.00 12.86  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.694 -1.359  3.300  1.00 15.66  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.375 -0.698  2.025  1.00 16.77  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 14.124 -1.402  1.512  1.00 19.56  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.182 -2.360  0.712  1.00 20.90  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.551 -0.788  1.026  1.00 16.42  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.885 -0.238  1.583  1.00 17.06  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.874 1.289   1.815  1.00 16.57  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.189 1.784   2.273  1.00 15.97  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.374 2.943   2.901  1.00 17.63  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.364 3.792   3.062  1.00 18.05  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.588 3.289   3.334  1.00 19.62  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.994 -0.983  2.028  1.00 18.99  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.747 -1.740  1.877  1.00 19.76  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.528 -0.839  2.060  1.00 20.43  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.620 0.327   2.371  1.00 21.20  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.746 -2.825  2.943  1.00 18.23  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.561 -2.146  4.609  1.00 17.75  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.317  -1.495  1.981  1.00 22.87  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 8.047  -0.823  2.188  1.00 24.93  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.299  -1.342  3.431  1.00 23.53  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 6.063  -1.280  3.464  1.00 24.93  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.118  -0.972  0.951  1.00 31.10  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.778  -2.379  0.525  1.00 43.15  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 7.264  -3.322  1.161  1.00 45.49  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 6.017  -2.539  -0.465 1.00 48.39  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 8.003  -1.917  4.412  1.00 20.84  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.313  -2.428  5.608  1.00 19.49  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.521  -1.327  6.336  1.00 19.60  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.961  -0.186  6.493  1.00 19.93  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.309  -3.124  6.541  1.00 19.79  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 9.030  -4.694  5.905  1.00 19.89  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.357  -1.706  6.853  1.00 17.21  ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.556  -0.883  7.778  1.00 16.79  ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.296  -1.606  9.131  1.00 15.16  ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.430  -1.213  9.909  1.00 15.65  ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.236  -0.401  7.179  1.00 20.81  ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.327  0.744   6.209  1.00 25.89  ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.908  1.202   5.851  1.00 31.41  ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.414  0.979   4.743  1.00 34.38  ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.191  1.866   6.770  1.00 27.58  ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 5.002  -2.709  9.363  1.00 13.75  ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 5.020  -3.391  10.633 1.00 13.52  ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.469  -3.639  11.062 1.00 13.95  ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.343  -3.831  10.207 1.00 15.06  ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.230  -4.667  10.669 1.00 17.05  ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.837  -5.597  9.829  1.00 21.90  ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.817  -4.512  10.253 1.00 17.20  ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.720  -3.558  12.347 1.00 12.37  ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 8.084  -3.780  12.841 1.00 12.74  ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.097  -3.809  14.354 1.00 11.20  ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 7.064  -4.042  14.971 1.00 12.50  ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.260  -3.592  14.966 1.00 11.15  ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.413  -3.663  16.416 1.00 10.26  ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.252 -2.476  16.837 1.00 10.34  ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.259 -2.177  16.160 1.00 11.17  ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.138 -4.996  16.759 1.00 11.67  ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.509 -5.049  18.227 1.00 15.30  ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.242  -6.211  16.396 1.00 12.98  ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.885  -1.793  17.927 1.00 10.13  ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.740 -0.683  18.402 1.00 9.85   ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.164 -0.915  19.843 1.00 11.58  ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.456 -1.553  20.632 1.00 11.67  ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.026 0.705   18.258 1.00 10.80  ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.030  1.058   19.350 1.00 11.40  ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.744  0.526   19.338 1.00 12.83  ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.345  1.979   20.343 1.00 11.77  ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.814  0.856   20.317 1.00 13.92  ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.411  2.320   21.331 1.00 12.54  ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.159  1.750   21.301 1.00 13.70  ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.186  2.024   22.266 1.00 16.04  ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.297 -0.322  20.219 1.00 10.37  ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.767 -0.351  21.611 1.00 10.77  ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.291 0.873   22.401 1.00 11.07  ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.525 2.023   22.014 1.00 11.22  ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.330 -0.380  21.663 1.00 12.01  ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.794 -0.527  23.087 1.00 11.79  ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.482 -1.650  23.810 1.00 11.75  ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.539 0.482   23.716 1.00 13.18  ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.837 -1.763  25.145 1.00 13.54  ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.898 0.383   25.043 1.00 13.36  ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.605 -0.773  25.735 1.00 13.92  ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 15.950 -0.882  27.088 1.00 16.69  ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.688 0.571   23.538 1.00 10.50  ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.123 1.550   24.477 1.00 11.58  ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 11.955 1.521   25.779 1.00 11.95  ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.774 0.634   26.635 1.00 12.16  ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.658  1.221   24.742 1.00 11.29  ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 8.910  2.324   25.993 1.00 13.35  ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.868 2.512   25.949 1.00 12.30  ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.748 2.509   27.139 1.00 13.14  ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 12.986 2.686   28.471 1.00 13.65  ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.389 2.122   29.484 1.00 14.68  ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 14.844 3.562   27.003 1.00 15.43  ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.361 4.894   27.059 1.00 16.93  ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 11.838 3.419   28.451 1.00 12.34  ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.041 3.628   29.661 1.00 12.42  ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.271 2.400   30.110 1.00 12.69  ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.619  2.421   31.135 1.00 13.42  ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.105 4.821   29.460 1.00 13.96  ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.101  4.573   28.490 1.00 14.57  ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.335 1.311   29.330 1.00 12.66  ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.773  -0.004  29.708 1.00 12.58  ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.812 -1.117  29.652 1.00 14.09  ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.475 -2.286  29.937 1.00 15.71  ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.586  -0.357  28.788 1.00 14.11  ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.408  0.628   28.919 1.00 14.03  ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.648  0.296   30.176 1.00 14.13  ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.490  1.191   30.358 1.00 16.51  ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.522  2.346   31.010 1.00 15.65  ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.656  2.786   31.543 1.00 16.61  ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.401  3.058   31.179 1.00 16.76  ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.031 -0.826  29.164 1.00 14.39  ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.070 -1.851  28.892 1.00 16.38  ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.467 -3.008  28.049 1.00 17.26  ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.685 -4.208  28.333 1.00 18.80  ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.642 -2.432  30.176 1.00 19.91  ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.662 -1.567  30.764 1.00 20.95  ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.442 -2.409  31.779 1.00 20.34  ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.205 -1.461  32.562 1.00 21.47  ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.877 -1.054  33.783 1.00 17.44  ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.806 -1.567  34.405 1.00 19.50  ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.607 -0.126  34.392 1.00 20.96  ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.722 -2.659  27.008 1.00 14.76  ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.035 -3.644  26.215 1.00 15.20  ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 10.988 -3.261  24.781 1.00 14.48  ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.923 -2.072  24.425 1.00 14.23  ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.591  -3.770  26.762 1.00 17.75  ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.463  -4.718  27.959 1.00 26.89  ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 8.023  -4.959  28.338 1.00 35.82  ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.937  -5.787  29.605 1.00 42.97  ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.488  -5.046  30.777 1.00 46.91  ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 10.961 -4.289  23.937 1.00 13.62  ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.756 -4.146  22.498 1.00 12.75  ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.289  -4.488  22.182 1.00 14.36  ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.797  -5.546  22.590 1.00 17.92  ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.677 -5.096  21.714 1.00 12.64  ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.149 -4.777  21.831 1.00 13.68  ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.855 -4.108  20.838 1.00 16.43  ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.998 -5.073  22.843 1.00 13.96  ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.127 -4.054  21.268 1.00 15.60  ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.251 -4.609  22.443 1.00 17.11  ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.595  -3.601  21.457 1.00 12.09  ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.162  -3.807  21.177 1.00 12.56  ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.912  -3.908  19.688 1.00 11.53  ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.413  -3.082  18.920 1.00 11.84  ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.350  -2.562  21.674 1.00 13.50  ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.280  -2.407  23.172 1.00 13.44  ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.505  -3.269  23.949 1.00 15.26  ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 6.989  -1.410  23.815 1.00 13.68  ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.392  -3.103  25.323 1.00 16.52  ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.878  -1.228  25.202 1.00 14.71  ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.076  -2.077  25.940 1.00 15.92  ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 6.001  -1.923  27.325 1.00 19.15  ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.110  -4.892  19.271 1.00 12.30  ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.677  -4.921  17.863 1.00 12.62  ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.665  -3.815  17.583 1.00 13.24  ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.742  -3.615  18.405 1.00 15.67  ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.032  -6.305  17.681 1.00 14.91  ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.624  -6.721  19.082 1.00 16.71  ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.519  -5.976  20.088 1.00 13.90  ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.780  -3.196  16.447 1.00 12.39  ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.862  -2.076  16.080 1.00 14.40  ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.546  -2.097  14.603 1.00 13.26  ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.340  -2.492  13.766 1.00 13.37  ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.435  -0.702  16.456 1.00 17.66  ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.345  -0.505  17.973 1.00 20.00  ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.849  -0.513  15.905 1.00 18.66  ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.371  -1.537  14.269 1.00 13.27  ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.964  -1.138  12.933 1.00 13.95  ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.200  0.380   12.865 1.00 13.20  ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.784  1.097   13.817 1.00 14.11  ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.468  -1.390  12.742 1.00 18.06  ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.261  -2.792  12.748 1.00 26.39  ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.777  0.889   11.789 1.00 13.61  ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.083  2.304   11.698 1.00 13.79  ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.669  2.865   10.352 1.00 14.52  ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.617  2.141   9.342  1.00 16.46  ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.582  2.585   12.050 1.00 14.10  ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.618  1.781   11.280 1.00 12.63  ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.046  0.544   11.734 1.00 12.90  ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.189  2.288   10.131 1.00 13.58  ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.980  -0.187  11.003 1.00 13.86  ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.151  1.551   9.414  1.00 14.68  ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.502  0.312   9.839  1.00 13.79  ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.354  4.161   10.322 1.00 15.21  ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 1.955  4.836   9.110  1.00 16.12  ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.124  5.095   8.166  1.00 15.63  ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.285  4.995   8.561  1.00 15.57  ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.216  6.144   9.462  1.00 18.27  ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.068  7.072   10.125 1.00 19.57  ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.834  5.391   6.919  1.00 16.09  ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.880  5.695   5.940  1.00 16.62  ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.497  7.044   6.240  1.00 17.65  ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.815  7.914   6.806  1.00 19.03  ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.298  5.668   4.514  1.00 18.55  ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.914  4.281   4.085  1.00 23.14  ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.533  4.271   2.584  1.00 30.21  ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.274  2.867   2.111  1.00 37.51  ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.534  2.726   0.654  1.00 42.32  ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.768  7.271   5.905  1.00 16.44  ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.399  8.555   6.225  1.00 16.33  ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.616  9.740   5.648  1.00 18.35  ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.233  9.710   4.472  1.00 20.25  ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.825  8.402   5.618  1.00 18.27  ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 7.658  7.250   4.501  1.00 20.51  ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.703  6.341   5.207  1.00 17.22  ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.349  10.728  6.495  1.00 17.80  ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.477  11.832  6.102  1.00 19.71  ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.860  13.109  6.832  1.00 18.68  ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.686  13.126  7.732  1.00 17.99  ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.008  11.486  6.415  1.00 26.18  ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.640  10.269  5.779  1.00 37.45  ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.188  14.207  6.419  1.00 21.24  ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.388  15.519  6.996  1.00 22.35  ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.304  15.683  8.063  1.00 23.52  ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.084  15.702  7.746  1.00 25.71  ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.216  16.545  5.858  1.00 23.40  ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.599  17.967  6.129  1.00 28.16  ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.075  18.106  6.374  1.00 28.99  ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.217  18.852  4.942  1.00 29.41  ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.686  15.679  9.327  1.00 22.66  ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.810  15.710  10.499 1.00 22.82  ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.086  16.951  11.354 1.00 23.86  ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.251  17.346  11.529 1.00 23.52  ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 3.079  14.424  11.345 1.00 23.40  ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 2.873  13.115  10.491 1.00 27.01  ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 2.304  14.425  12.688 1.00 24.96  ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 1.473  12.773  10.205 1.00 30.60  ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 2.024  17.618  11.837 1.00 25.22  ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.201  18.775  12.682 1.00 26.39  ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.649  18.304  14.049 1.00 27.20  ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 2.093  17.382  14.646 1.00 28.71  ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.876  19.560  12.822 1.00 26.93  ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.134  20.851  13.565 1.00 29.30  ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.847  21.879  12.971 1.00 30.30  ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.736  21.002  14.885 1.00 31.69  ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 2.124  23.050  13.664 1.00 32.71  ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.953  22.216  15.557 1.00 32.30  ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.658  23.219  14.941 1.00 33.04  ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.770  18.904  14.509 1.00 25.22  ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 4.333  18.630  15.808 1.00 25.99  ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 4.336  19.965  16.605 1.00 26.02  ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.860  21.006  16.184 1.00 27.78  ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.731  18.035  15.720 1.00 25.82  ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 6.186  17.665  17.118 1.00 25.81  ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.696  16.777  14.827 1.00 25.81  ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.736  19.875  17.715 1.00 28.34  ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.472  20.989  18.616 1.00 30.30  ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.779  21.695  19.022 1.00 31.14  ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.788  20.992  19.111 1.00 30.09  ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.815  20.345  19.853 1.00 35.25  ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 2.541  21.278  21.008 1.00 43.47  ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 1.453  22.279  20.711 1.00 50.40  ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 1.778  23.385  20.223 1.00 50.20  ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? 0.269  21.944  20.945 1.00 54.91  ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.803  23.041  19.339 1.00 32.27  ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 6.029  23.664  19.899 1.00 32.04  ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.434  22.891  21.146 1.00 32.47  ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.590  22.363  21.867 1.00 34.00  ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.776  25.094  20.316 1.00 32.62  ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.695  22.697  21.296 1.00 30.19  ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.238  21.920  22.411 1.00 28.90  ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.449  22.695  22.955 1.00 27.72  ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.745  23.768  22.440 1.00 28.35  ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 8.683  20.553  21.907 1.00 28.03  ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 9.823  20.608  21.054 1.00 26.15  ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.154 22.153  23.953 1.00 27.45  ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.418 22.793  24.399 1.00 28.81  ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.564 22.603  23.368 1.00 28.73  ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.635 23.180  23.554 1.00 29.55  ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 11.872 22.238  25.756 1.00 32.00  ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 12.225 20.769  25.711 1.00 37.71  ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 12.928 20.260  26.953 1.00 45.88  ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 12.353 19.390  27.647 1.00 48.15  ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 14.054 20.731  27.232 1.00 49.64  ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.348 21.823  22.274 1.00 26.46  ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.393 21.575  21.287 1.00 23.16  ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.140 22.244  19.976 1.00 23.81  ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 14.089 22.512  19.279 1.00 24.79  ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 13.557 20.060  21.033 1.00 22.62  ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.012 19.309  22.253 1.00 22.00  ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 15.275 19.501  22.774 1.00 23.28  ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 13.145 18.462  22.932 1.00 24.49  ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 15.716 18.798  23.877 1.00 24.54  ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 13.565 17.756  24.051 1.00 25.29  ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 14.848 17.952  24.538 1.00 26.44  ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 15.316 17.280  25.645 1.00 30.28  ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.827 22.533  19.605 1.00 24.68  ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.546 23.151  18.298 1.00 24.73  ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 10.357 24.110  18.400 1.00 27.93  ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.490  23.825  19.204 1.00 26.12  ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 11.108 22.002  17.329 1.00 23.31  ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.220 21.038  16.945 1.00 20.40  ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 13.251 21.448  16.129 1.00 20.99  ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.256 19.732  17.449 1.00 19.99  ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.258 20.579  15.764 1.00 19.28  ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.266 18.845  17.084 1.00 19.12  ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.270 19.290  16.263 1.00 18.50  ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.309 18.487  15.887 1.00 16.63  ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 10.201 25.084  17.486 1.00 29.49  ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.919  25.822  17.427 1.00 31.15  ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.815  24.899  16.840 1.00 31.62  ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 8.138  23.809  16.304 1.00 31.19  ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 9.228  26.955  16.438 1.00 32.36  ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 10.205 26.323  15.462 1.00 32.50  ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 11.091 25.441  16.355 1.00 30.17  ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 6.546  25.350  16.826 1.00 32.05  ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.429  24.601  16.219 1.00 31.47  ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.717  24.469  14.752 1.00 31.91  ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 6.129  25.468  14.123 1.00 34.41  ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 4.121  25.356  16.427 1.00 32.26  ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.712  23.197  14.244 1.00 30.47  ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 6.093  23.041  12.846 1.00 29.33  ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.599  21.689  12.347 1.00 27.55  ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 5.173  20.854  13.093 1.00 30.12  ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.657  23.125  12.699 1.00 27.70  ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.352  21.824  13.192 1.00 27.27  ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.799  21.953  13.519 1.00 26.61  ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 10.630 20.735  13.397 1.00 24.57  ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 10.513 19.610  14.103 1.00 24.33  ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 9.479  19.428  14.914 1.00 25.10  ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.373 18.613  13.928 1.00 18.68  ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.720  21.526  11.049 1.00 27.06  ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.480  20.285  10.403 1.00 26.54  ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.837  19.569  10.384 1.00 23.76  ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 7.857  20.117  9.953  1.00 24.19  ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.955  20.541  8.986  1.00 27.73  ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.458  20.767  9.011  1.00 27.82  ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.575  19.694  9.036  1.00 28.33  ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.930  22.043  9.160  1.00 28.24  ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.206  19.890  9.117  1.00 29.85  ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 1.559  22.254  9.247  1.00 28.53  ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.700  21.175  9.258  1.00 30.20  ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.654 21.411  9.368  1.00 32.76  ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.833  18.299  10.810 1.00 21.03  ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.992  17.413  10.757 1.00 19.42  ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.788  16.482  9.588  1.00 18.49  ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.706  15.879  9.497  1.00 17.86  ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.200  16.652  12.061 1.00 18.75  ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.442  15.741  11.980 1.00 17.59  ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 9.959  15.244  13.301 1.00 17.56  ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 9.962  15.937  14.287 1.00 17.61  ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.447 13.983  13.369 1.00 16.15  ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.761  16.336  8.725  1.00 17.05  ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.650  15.502  7.561  1.00 17.40  ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.233  14.108  7.839  1.00 16.30  ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 9.994  13.915  8.810  1.00 17.15  ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.340  16.185  6.388  1.00 20.11  ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.739 16.266  6.652  1.00 23.10  ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.820  13.155  6.961  1.00 16.45  ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.309  11.770  6.973  1.00 14.92  ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.024  11.116  8.338  1.00 14.60  ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.842  10.281  8.777  1.00 15.07  ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.835 11.722  6.591  1.00 16.18  ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.131 12.265  5.214  1.00 17.69  ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.216 11.433  4.127  1.00 20.80  ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.317 13.539  4.807  1.00 20.70  ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.501 12.224  3.089  1.00 21.08  ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.561 13.491  3.447  1.00 20.99  ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 7.912  11.460  8.967  1.00 13.70  ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.558  10.935  10.297 1.00 14.64  ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.488  9.863   10.135 1.00 14.18  ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.556  10.018  9.359  1.00 15.08  ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.021  12.104  11.175 1.00 17.09  ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.687  11.766  12.615 1.00 17.14  ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 7.919  11.424  13.392 1.00 18.15  ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.036  12.995  13.346 1.00 19.65  ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.614  8.780   10.911 1.00 14.69  ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.662  7.638   10.892 1.00 13.83  ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.086  7.494   12.306 1.00 14.48  ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.830  7.541   13.277 1.00 15.47  ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.459  6.379   10.535 1.00 14.15  ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.101  6.492   9.153  1.00 15.88  ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.162  5.092   8.632  1.00 18.25  ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.398  5.222   9.907  1.00 22.63  ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.756  7.334   12.436 1.00 13.61  ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.156  7.229   13.762 1.00 15.32  ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.652  5.827   14.045 1.00 14.64  ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.205  5.112   13.122 1.00 15.30  ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 1.941  8.197   13.890 1.00 18.00  ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.231  9.680   13.803 1.00 21.62  ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 0.992  10.501  14.101 1.00 24.41  ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.317  10.122  14.771 1.00 23.88  ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.693  5.440   15.314 1.00 13.88  ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.159  4.159   15.760 1.00 13.01  ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.563  4.314   17.152 1.00 12.65  ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.825  5.309   17.862 1.00 13.68  ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.300  3.107   15.869 1.00 15.12  ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.742  3.340   17.560 1.00 12.24  ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.230  3.318   18.922 1.00 12.40  ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.266  2.552   19.764 1.00 15.58  ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.592  1.399   19.473 1.00 17.16  ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.121 2.580   18.943 1.00 13.34  ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.595 2.382   20.389 1.00 15.13  ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -2.148 3.384   18.121 1.00 13.59  ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.754  3.227   20.776 1.00 14.99  ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.782  2.624   21.629 1.00 16.01  ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.172  3.577   22.712 1.00 16.40  ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 2.986  4.794   22.622 1.00 17.95  ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.675  2.972   23.827 1.00 17.82  ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.105  3.808   24.904 1.00 18.83  ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.387  4.532   24.541 1.00 17.30  ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.340  3.926   23.985 1.00 17.09  ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.343  2.990   26.209 1.00 18.75  ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 4.762  3.883   27.351 1.00 19.36  ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 3.864  4.744   27.930 1.00 20.31  ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 5.984  4.091   27.921 1.00 19.59  ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 4.556  5.458   28.826 1.00 20.96  ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 5.837  5.076   28.865 1.00 20.65  ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.483  5.761   24.887 1.00 18.25  ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 6.680  6.516   24.787 1.00 16.22  ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 6.694  7.696   25.793 1.00 18.18  ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 5.623  8.211   26.133 1.00 20.94  ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.014  6.883   23.334 1.00 19.00  ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 6.077  7.835   22.860 1.00 20.41  ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 7.920  8.117   26.196 1.00 17.39  ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.301  9.230   27.082 1.00 18.18  ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.456  9.988   26.445 1.00 18.65  ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.121 9.477   25.531 1.00 17.85  ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 8.706  8.731   28.497 1.00 19.41  ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 7.526  8.053   29.155 1.00 20.56  ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 7.768  7.409   30.515 1.00 22.81  ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 8.606  7.937   31.280 1.00 25.93  ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.114  6.395   30.818 1.00 21.98  ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 9.704  11.245  26.814 1.00 19.69  ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 10.680 12.067  26.049 1.00 19.68  ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.077 11.409  25.847 1.00 18.94  ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 12.674 11.398  24.731 1.00 18.69  ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 10.675 13.406  26.848 1.00 20.87  ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 9.281  13.459  27.408 1.00 21.42  ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 8.922  12.052  27.779 1.00 20.50  ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 12.575 10.758  26.888 1.00 17.50  ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 13.875 10.086  26.888 1.00 16.38  ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 13.893 8.787   26.082 1.00 15.27  ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 14.958 8.190   25.919 1.00 15.85  ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 12.766 8.340   25.552 1.00 13.60  ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 12.719 7.195   24.648 1.00 13.60  ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.222 7.561   23.240 1.00 13.15  ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.497 6.654   22.435 1.00 13.15  ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.291 6.617   24.535 1.00 13.19  ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 10.933 5.882   25.806 1.00 14.28  ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 9.730  5.913   26.213 1.00 14.59  ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 11.807 5.251   26.369 1.00 13.80  ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.395 8.861   22.937 1.00 13.10  ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 13.935 9.249   21.609 1.00 13.11  ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.288 8.579   21.403 1.00 13.39  ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.128 8.477   22.274 1.00 14.12  ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.047 10.770  21.515 1.00 15.22  ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.455 11.606  21.268 1.00 16.25  ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.472 8.048   20.201 1.00 12.11  ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.694 7.365   19.816 1.00 11.82  ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.554 5.856   19.744 1.00 11.93  ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.404 5.153   19.185 1.00 12.15  ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.462 5.332   20.340 1.00 11.77  ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.226 3.891   20.276 1.00 11.18  ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.017 3.466   18.818 1.00 10.56  ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.321 4.154   18.057 1.00 10.82  ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.523 2.308   18.423 1.00 10.67  ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.386 1.848   17.026 1.00 10.40  ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.071 1.174   16.749 1.00 10.55  ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.597 0.360   17.555 1.00 10.96  ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.568 0.868   16.730 1.00 10.54  ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.810 1.737   16.455 1.00 12.91  ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.313 -0.060  15.523 1.00 12.21  ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.118 0.905   16.331 1.00 15.13  ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.488 1.506   15.586 1.00 9.94   ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.392 0.766   14.957 1.00 10.18  ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 13.046 -0.095  13.851 1.00 10.13  ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.814 0.455   13.032 1.00 10.18  ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.401 1.785   14.319 1.00 10.64  ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.315 1.129   13.441 1.00 11.17  ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.325  0.316   14.288 1.00 12.57  ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.493  2.219   12.658 1.00 12.55  ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.734 -1.375  13.810 1.00 10.73  ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.316 -2.298  12.809 1.00 10.73  ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.268 -3.215  12.271 1.00 11.17  ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.230 -3.484  12.905 1.00 11.52  ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.464 -3.089  13.455 1.00 12.40  ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 14.003 -4.087  14.526 1.00 12.56  ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.255 -4.820  15.071 1.00 14.14  ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 16.035 -3.939  15.927 1.00 15.05  ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.335 -3.744  15.819 1.00 14.83  ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 18.002 -4.198  14.753 1.00 16.04  ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.975 -2.991  16.703 1.00 16.68  ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.561 -3.737  11.087 1.00 12.84  ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.689 -4.740  10.409 1.00 15.74  ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.589 -5.919  10.035 1.00 18.50  ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.755 -5.961  10.393 1.00 17.91  ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.993 -4.121  9.196  1.00 16.03  ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 12.149 -3.703  7.835  1.00 15.73  ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 12.029 -6.929  9.293  1.00 21.70  ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.856 -8.054  8.872  1.00 24.14  ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 14.051 -7.691  7.972  1.00 24.14  ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.998 -8.454  7.879  1.00 27.13  ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 12.028 -9.157  8.162  1.00 27.89  ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.408 -8.646  6.877  1.00 33.54  ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.510 -9.644  6.196  1.00 42.35  ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 9.278  -9.557  6.290  1.00 45.41  ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 11.096 -10.585 5.480  1.00 43.03  ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 14.050 -6.491  7.374  1.00 20.37  ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 15.108 -6.031  6.446  1.00 19.22  ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 16.229 -5.236  7.113  1.00 18.32  ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.240 -4.942  6.494  1.00 20.70  ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.461 -5.214  5.314  1.00 19.02  ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.374 -5.981  4.614  1.00 20.65  ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 12.057 -5.645  4.758  1.00 20.89  ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.466 -7.023  3.731  1.00 23.29  ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.365 -6.523  4.028  1.00 24.12  ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 12.187 -7.343  3.365  1.00 25.11  ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.987 -4.759  8.341  1.00 16.68  ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.979 -3.960  9.030  1.00 16.04  ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.335 -2.792  9.772  1.00 13.41  ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.138 -2.806  10.092 1.00 13.25  ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.163 -1.763  10.026 1.00 12.40  ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.693 -0.579  10.772 1.00 11.78  ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.852 0.339   9.893  1.00 10.73  ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.282 0.689   8.775  1.00 11.44  ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.906 0.196   11.338 1.00 11.58  ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.457 1.492   12.002 1.00 13.28  ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.650 -0.687  12.340 1.00 13.06  ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.699 0.742   10.382 1.00 10.45  ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.754 1.556   9.672  1.00 11.58  ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.880 3.018   10.086 1.00 11.31  ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.731 3.942   9.246  1.00 12.30  ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.292 1.059   9.927  1.00 12.54  ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.216 2.028   9.339  1.00 14.27  ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.092 -0.359  9.392  1.00 14.98  ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.063 3.284   11.377 1.00 11.48  ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.147 4.649   11.883 1.00 12.25  ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.352 4.694   13.372 1.00 10.59  ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.682 3.649   13.981 1.00 10.73  ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.208 5.888   13.978 1.00 10.55  ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.412 6.054   15.428 1.00 10.41  ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.260 6.823   16.024 1.00 10.61  ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.646 7.664   15.359 1.00 11.59  ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.756 6.749   15.792 1.00 11.57  ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 15.905 8.074   15.047 1.00 12.98  ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 16.906 5.803   15.609 1.00 12.79  ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.158 8.895   15.562 1.00 14.07  ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 12.943 6.552   17.287 1.00 10.07  ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 11.879 7.308   17.980 1.00 11.02  ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.250 8.803   17.995 1.00 11.82  ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.410 9.135   18.296 1.00 12.08  ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.758 6.821   19.453 1.00 11.70  ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.746 7.656   20.238 1.00 13.06  ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.315 5.342   19.501 1.00 11.90  ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.307 9.666   17.643 1.00 12.10  ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.524 11.129  17.553 1.00 13.04  ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.424 11.890  18.271 1.00 15.77  ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 10.667 13.011  18.695 1.00 16.66  ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.648 11.501  16.073 1.00 15.11  ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.673 12.904  15.816 1.00 15.53  ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.182  11.355  18.372 1.00 14.44  ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.074  12.099  19.062 1.00 16.63  ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.182  11.132  19.826 1.00 17.45  ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.302  9.906   19.637 1.00 16.77  ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.212  12.847  18.035 1.00 18.65  ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 6.438  13.845  18.759 1.00 28.94  ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 6.358  11.908  17.214 1.00 14.98  ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.264  11.643  20.661 1.00 18.29  ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.327  10.741  21.335 1.00 19.13  ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.391  11.462  22.282 1.00 21.01  ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.441  12.682  22.350 1.00 22.00  ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.703  10.652  23.088 1.00 22.55  ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.750  11.126  24.091 1.00 23.43  ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.385  10.488  23.893 1.00 23.51  ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 1.000  10.169  22.755 1.00 23.58  ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.625  10.338  24.987 1.00 22.26  ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -0.756 9.842   24.992 1.00 23.40  ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -0.965 8.566   24.229 1.00 22.34  ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.046 8.385   23.627 1.00 22.96  ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.659 10.948  24.474 1.00 26.50  ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.689 12.089  25.428 1.00 29.63  ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.979 11.901  26.618 1.00 34.29  ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.424 13.282  24.904 1.00 30.74  ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? -0.027 7.625   24.379 1.00 18.92  ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? -0.140 6.321   23.772 1.00 17.83  ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.180  6.316   22.305 1.00 15.94  ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? -0.005 5.275   21.696 1.00 17.56  ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.850  7.384   21.797 1.00 16.41  ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.400  7.390   20.429 1.00 15.72  ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.924  7.408   20.509 1.00 17.46  ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.511  7.867   21.504 1.00 19.47  ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.944  8.631   19.653 1.00 17.05  ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.574 8.668   19.411 1.00 18.68  ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.025 10.067  19.010 1.00 21.56  ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -0.995 7.604   18.355 1.00 19.28  ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.550  6.931   19.459 1.00 14.06  ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.007  7.047   19.303 1.00 14.04  ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.260  7.406   17.809 1.00 13.90  ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.645  6.831   16.923 1.00 14.84  ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.704  5.772   19.794 1.00 13.17  ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.212  4.551   19.070 1.00 14.18  ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.232  5.904   19.656 1.00 13.48  ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.147  8.362   17.553 1.00 13.71  ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.498  8.753   16.180 1.00 13.30  ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 7.955  8.431   15.899 1.00 12.85  ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 8.820  8.608   16.771 1.00 14.30  ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.207  7.959   14.679 1.00 11.76  ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.574  7.555   14.275 1.00 12.08  ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.042 8.325   13.073 1.00 12.62  ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.275  8.518   12.105 1.00 12.60  ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.531  6.068   13.841 1.00 12.05  ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 8.917  5.161   14.899 1.00 12.23  ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.670  4.680   15.973 1.00 11.22  ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.592  4.752   14.790 1.00 13.38  ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.107  3.818   16.922 1.00 11.64  ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.038  3.890   15.742 1.00 13.23  ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.813  3.407   16.786 1.00 11.82  ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.283 8.814   13.148 1.00 11.75  ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 11.938 9.470   12.002 1.00 12.39  ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.442 8.408   11.060 1.00 12.26  ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.302 7.595   11.438 1.00 12.32  ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.056 10.354  12.527 1.00 12.88  ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.893 8.319   9.849  1.00 12.45  ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.307 7.310   8.868  1.00 13.28  ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.728 7.624   8.385  1.00 12.94  ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.079 8.797   8.193  1.00 13.54  ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.363 7.340   7.630  1.00 15.14  ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.636 6.308   6.578  1.00 24.24  ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.841 5.144   6.936  1.00 18.73  ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.770 6.698   5.379  1.00 32.24  ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.497 6.589   8.098  1.00 11.76  ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.836 6.735   7.468  1.00 12.41  ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.955 5.907   6.181  1.00 13.53  ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.036 5.920   5.579  1.00 13.10  ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.011 6.390   8.430  1.00 12.49  ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.012 7.316   9.669  1.00 13.31  ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.017 4.906   8.845  1.00 13.53  ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.907 5.166   5.747  1.00 13.28  ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 15.020 4.244   4.628  1.00 13.62  ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.313 4.934   3.307  1.00 14.25  ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.791 4.264   2.350  1.00 15.94  ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.760 3.371   4.503  1.00 13.45  ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.615 2.419   5.715  1.00 13.08  ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.331 1.623   5.588  1.00 15.24  ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.174 2.494   5.779  1.00 14.04  ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.915  2.080   5.866  1.00 15.49  ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.603  0.816   5.581  1.00 16.59  ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.941  2.960   6.135  1.00 17.21  ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.981 6.240   3.183  1.00 14.33  ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.241 6.927   1.903  1.00 15.12  ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.674 7.456   1.808  1.00 15.20  ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 17.068 7.958   0.735  1.00 16.63  ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.225 8.072   1.735  1.00 15.81  ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.416 9.129   2.799  1.00 20.30  ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.437 8.777   4.011  1.00 20.18  ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.544 10.309  2.456  1.00 23.56  ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.452 7.438   2.917  1.00 14.50  ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.814 7.991   2.971  1.00 13.55  ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.795 6.973   2.445  1.00 13.71  ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.479 6.275   3.197  1.00 14.22  ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.148 8.408   4.419  1.00 14.36  ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.161 9.461   5.008  1.00 15.73  ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.528 9.745   6.456  1.00 16.80  ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.168 10.738  4.190  1.00 17.17  ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.844 6.851   1.110  1.00 14.07  ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.606 5.767   0.487  1.00 15.00  ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 22.082 5.880   0.718  1.00 14.75  ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.786 4.863   0.781  1.00 15.71  ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.302 5.646   -1.036 1.00 16.39  ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.782 5.605   -1.375 1.00 18.17  ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.592 5.307   -2.874 1.00 20.44  ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.987 4.544   -0.570 1.00 19.47  ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.568 7.119   0.872  1.00 13.86  ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.982 7.371   1.077  1.00 15.05  ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.516 6.799   2.394  1.00 15.45  ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.734 6.673   2.558  1.00 16.81  ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.276 8.881   0.955  1.00 15.17  ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.463 9.714   1.891  1.00 14.15  ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.321 10.399  1.588  1.00 15.67  ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.775 10.031  3.271  1.00 14.69  ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.870 11.074  2.713  1.00 16.28  ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.771 10.898  3.734  1.00 14.72  ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.839 9.724   4.121  1.00 15.41  ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.792 11.433  5.038  1.00 16.48  ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.854 10.278  5.402  1.00 17.02  ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.830 11.090  5.841  1.00 16.66  ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.634 6.449   3.354  1.00 13.78  ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.121 5.817   4.600  1.00 15.19  ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.824 4.481   4.296  1.00 17.54  ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.640 4.035   5.115  1.00 18.95  ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.963 5.557   5.566  1.00 14.96  ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.391 6.774   6.234  1.00 15.23  ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.122 6.408   7.013  1.00 16.68  ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.439 7.425   7.213  1.00 16.01  ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.539 3.858   3.123  1.00 20.16  ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 25.106 2.545   2.759  1.00 24.01  ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.455 2.619   2.063  1.00 28.88  ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.998 1.564   1.693  1.00 30.12  ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 24.160 1.771   1.809  1.00 24.97  ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.811 1.417   2.352  1.00 28.72  ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.625 1.511   3.581  1.00 30.64  ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.911 1.052   1.549  1.00 34.55  ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.995 3.825   1.822  1.00 30.64  ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.261 3.954   1.088  1.00 34.41  ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.206 4.979   1.730  1.00 36.99  ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.796 5.690   2.643  1.00 36.38  ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.931 4.352   -0.356 1.00 38.69  ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.185 5.669   -0.440 1.00 45.27  ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.434 5.930   -1.734 1.00 53.48  ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 26.057 7.103   -1.970 1.00 53.51  ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 26.223 4.970   -2.513 1.00 56.96  ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.455 5.066   1.223  1.00 40.02  ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.537 5.983   1.614  1.00 43.17  ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 32.346 5.449   2.791  1.00 44.99  ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 33.575 5.384   2.695  1.00 45.92  ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 31.036 7.419   1.844  1.00 47.03  ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.999 8.361   2.556  1.00 54.05  ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.913 9.160   1.649  1.00 63.20  ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 32.625 10.360  1.438  1.00 65.53  ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.912 8.593   1.149  1.00 65.28  ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.854 -21.342 7.698  1.00 21.16  ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.729 -21.131 8.632  1.00 19.58  ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.704 -22.222 9.709  1.00 17.72  ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.377 -23.256 9.551  1.00 19.56  ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.405 -21.151 7.861  1.00 22.88  ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.238 -22.412 7.233  1.00 26.79  ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.959 -21.990 10.804 1.00 17.52  ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.770 -22.982 11.857 1.00 17.02  ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.532 -22.357 13.213 1.00 15.76  ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.920 -21.224 13.456 1.00 16.58  ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.848 -23.092 14.081 1.00 14.67  ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.539 -22.595 15.421 1.00 14.56  ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.663 -23.726 16.438 1.00 13.46  ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.720 -24.897 16.059 1.00 15.16  ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 17.105 -22.020 15.452 1.00 17.70  ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.726 -23.346 17.721 1.00 13.44  ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.647 -24.278 18.849 1.00 13.54  ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.252 -24.082 19.465 1.00 14.53  ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.830 -22.927 19.672 1.00 14.82  ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.694 -23.976 19.904 1.00 14.06  ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 21.133 -23.848 19.326 1.00 14.41  ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.625 -25.026 21.029 1.00 15.30  ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 22.133 -23.184 20.319 1.00 15.20  ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.540 -25.170 19.747 1.00 13.90  ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 15.211 -25.118 20.347 1.00 15.36  ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.277 -25.806 21.697 1.00 15.26  ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.324 -27.031 21.759 1.00 16.93  ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 14.173 -25.826 19.436 1.00 16.28  ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.958 -25.070 18.141 1.00 16.04  ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 13.113 -23.952 18.087 1.00 16.56  ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.653 -25.414 16.984 1.00 17.11  ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.958 -23.231 16.909 1.00 17.77  ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.499 -24.697 15.800 1.00 18.85  ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.659 -23.608 15.776 1.00 19.32  ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.553 -22.842 14.627 1.00 22.35  ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.343 -25.053 22.790 1.00 15.31  ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.439 -25.603 24.151 1.00 16.97  ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.308 -24.995 24.978 1.00 17.36  ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 14.115 -23.787 24.973 1.00 16.21  ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.853 -25.309 24.757 1.00 17.36  ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 17.233 -23.815 24.621 1.00 17.75  ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.895 -25.759 26.214 1.00 19.16  ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.510 -25.833 25.675 1.00 17.66  ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.392 -25.294 26.446 1.00 17.33  ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.456 -24.464 25.584 1.00 17.75  ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 11.158 -24.856 24.446 1.00 19.19  ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 11.130 -23.273 26.035 1.00 17.02  ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 10.357 -22.349 25.217 1.00 17.84  ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 11.220 -21.229 24.676 1.00 17.86  ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.751 -20.114 24.505 1.00 17.86  ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 9.101  -21.800 25.954 1.00 20.32  ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 8.010  -22.863 26.097 1.00 26.54  ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 7.124  -22.993 25.231 1.00 29.42  ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 8.140  -23.696 27.116 1.00 27.74  ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.429 -21.603 24.253 1.00 15.84  ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.378 -20.625 23.652 1.00 15.76  ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.855 -21.112 22.288 1.00 15.00  ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 14.021 -22.314 22.059 1.00 15.73  ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.619 -20.475 24.554 1.00 16.91  ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 14.331 -19.954 25.959 1.00 17.26  ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.738 -18.716 26.153 1.00 19.55  ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.635 -20.717 27.087 1.00 19.07  ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.481 -18.230 27.437 1.00 22.29  ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 14.390 -20.233 28.379 1.00 21.84  ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.850 -18.979 28.540 1.00 24.29  ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.620 -18.499 29.818 1.00 28.89  ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 14.074 -20.146 21.388 1.00 13.93  ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.679 -20.351 20.062 1.00 14.02  ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.952 -19.489 20.034 1.00 13.50  ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.857 -18.280 20.282 1.00 14.19  ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.693 -19.900 18.945 1.00 14.90  ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.305 -19.760 17.535 1.00 17.66  ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 13.230 -19.464 16.485 1.00 16.35  ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.682 -18.510 15.464 1.00 17.53  ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 14.197 -18.817 14.270 1.00 17.62  ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.465 -20.089 13.951 1.00 20.18  ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.533 -17.856 13.420 1.00 17.96  ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 17.130 -20.107 19.820 1.00 13.19  ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.411 -19.392 19.783 1.00 12.74  ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.871 -19.344 18.349 1.00 12.25  ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 19.037 -20.433 17.717 1.00 13.44  ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.484 -20.136 20.635 1.00 13.06  ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.737 -19.254 20.737 1.00 14.82  ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.941 -20.514 22.041 1.00 14.21  ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 19.109 -18.128 17.807 1.00 12.15  ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.573 -17.966 16.423 0.50 12.18  ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.516 -17.978 16.414 0.50 13.85  ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.709 -16.979 16.341 1.00 12.91  ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.947 -16.207 17.290 1.00 13.36  ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.417 -17.461 15.500 0.50 12.27  ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.242 -17.410 15.666 0.50 17.23  ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.435 -18.583 15.245 0.50 14.39  ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.457 -17.291 14.173 0.50 17.33  ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.781 -16.131 15.993 0.50 8.80   ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 17.027 -18.289 15.912 0.50 20.88  ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.392 -16.928 15.184 1.00 12.43  ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.389 -15.883 14.957 1.00 12.06  ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.574 -14.537 14.899 1.00 12.46  ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.553 -14.453 14.212 1.00 12.83  ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 23.058 -16.041 13.567 1.00 12.29  ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.891 -17.319 13.492 1.00 12.80  ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.419 -18.391 13.064 1.00 13.91  ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 25.129 -17.207 13.960 1.00 13.26  ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 22.086 -13.507 15.608 1.00 12.97  ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.344 -12.227 15.629 1.00 12.16  ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 21.179 -11.674 14.197 1.00 13.96  ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 20.127 -11.145 13.865 1.00 14.51  ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 22.103 -11.222 16.498 1.00 12.09  ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.320 -9.879  16.723 1.00 13.31  ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 22.173 -8.916  17.499 1.00 14.73  ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.485 -7.667  17.929 1.00 14.93  ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.385 -6.581  17.192 1.00 15.58  ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.742 -6.602  15.914 1.00 16.72  ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.862 -5.472  17.707 1.00 15.25  ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 22.192 -11.867 13.344 1.00 14.29  ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 22.124 -11.337 11.973 1.00 14.20  ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 21.107 -12.070 11.080 1.00 15.21  ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.801 -11.558 10.001 1.00 17.68  ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.522 -11.271 11.277 1.00 15.27  ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 24.072 -12.605 10.833 1.00 14.14  ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.794 -13.419 11.711 1.00 15.01  ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 24.096 -13.162 9.593  1.00 15.10  ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 25.187 -14.475 10.983 1.00 16.00  ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.791 -14.364 9.708  1.00 15.35  ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.569 -13.223 11.506 1.00 14.05  ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.522 -13.971 10.778 1.00 15.56  ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 18.150 -13.892 11.465 1.00 16.55  ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.228 -14.625 11.062 1.00 17.12  ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 19.978 -15.432 10.608 1.00 15.46  ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.293 -15.577 9.788  1.00 16.05  ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.697 -17.066 9.683  1.00 16.22  ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 21.169 -14.945 8.392  1.00 16.22  ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 18.029 -13.119 12.569 1.00 16.18  ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.744 -13.047 13.286 1.00 16.04  ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.634 -12.497 12.417 1.00 17.02  ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.851 -11.551 11.628 1.00 17.56  ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.880 -12.216 14.551 1.00 17.21  ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.444 -13.089 12.561 1.00 17.13  ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.266 -12.659 11.795 1.00 17.35  ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.480 -11.587 12.560 1.00 17.16  ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.699 -11.286 13.747 1.00 17.87  ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.339 -13.903 11.568 1.00 18.89  ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.825 -14.315 12.821 1.00 19.10  ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 13.070 -15.081 10.882 1.00 20.63  ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.414 -11.018 11.876 1.00 18.63  ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.497 -10.099 12.570 1.00 20.27  ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.839  -10.826 13.723 1.00 18.95  ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.749  -10.252 14.804 1.00 19.89  ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.372  -9.599  11.620 1.00 21.29  ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.229  -8.888  12.332 1.00 24.83  ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.362  -7.597  12.803 1.00 28.09  ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 7.047  -9.381  12.760 1.00 26.88  ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.189  -7.275  13.345 1.00 27.79  ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.369  -8.335  13.388 1.00 27.52  ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.395  -12.092 13.519 1.00 18.88  ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.795  -12.835 14.620 1.00 19.87  ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.725  -12.992 15.824 1.00 18.67  ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.293  -12.913 16.956 1.00 18.50  ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.248  -14.210 14.190 1.00 21.55  ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.452  -14.878 15.293 1.00 26.89  ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.359  -14.401 15.651 1.00 28.56  ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 8.013  -15.920 15.919 1.00 29.64  ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 11.042 -13.178 15.567 1.00 17.37  ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 12.014 -13.263 16.657 1.00 17.56  ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 12.067 -11.956 17.451 1.00 17.27  ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 11.980 -11.963 18.682 1.00 18.14  ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.404 -13.603 16.123 1.00 16.86  ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.584 -15.018 15.631 1.00 17.01  ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 13.024 -15.939 16.264 1.00 18.76  ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.290 -15.202 14.626 1.00 16.58  ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 12.145 -10.813 16.753 1.00 17.38  ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 12.172 -9.510  17.435 1.00 18.14  ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.843 -9.168  18.144 1.00 18.09  ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.868 -8.504  19.188 1.00 18.58  ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.534 -8.409  16.434 1.00 17.79  ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 14.011 -8.381  16.155 1.00 17.05  ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.641 -8.841  15.029 1.00 18.34  ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 15.028 -7.783  16.971 1.00 15.42  ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 16.000 -8.589  15.108 1.00 17.58  ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.264 -7.944  16.297 1.00 15.84  ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 15.024 -7.117  18.205 1.00 18.33  ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.452 -7.407  16.779 1.00 16.76  ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 16.231 -6.650  18.718 1.00 19.54  ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.426 -6.800  17.996 1.00 18.38  ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.725  -9.666  17.623 1.00 18.14  ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.400  -9.410  18.235 1.00 20.08  ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 8.171  -10.318 19.473 1.00 20.56  ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 7.194  -10.154 20.200 1.00 21.94  ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.305  -9.674  17.212 1.00 20.64  ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 9.050  -11.336 19.685 1.00 19.49  ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.940  -12.267 20.820 1.00 18.67  ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 10.313 -12.334 21.509 1.00 18.59  ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.751 -13.394 21.922 1.00 18.14  ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.485  -13.647 20.293 1.00 20.06  ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 7.040  -13.569 19.849 1.00 22.73  ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 6.107  -13.599 20.696 1.00 23.61  ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.836  -13.440 18.534 1.00 23.29  ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 11.010 -11.201 21.616 1.00 19.11  ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.401 -11.172 22.074 1.00 18.08  ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.552 -11.492 23.550 1.00 19.57  ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.777 -10.989 24.403 1.00 20.83  ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.948 -9.772  21.787 1.00 18.13  ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.426 -9.611  22.133 1.00 18.55  ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.335 -10.471 21.239 1.00 18.95  ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.833 -8.173  21.987 1.00 20.19  ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.541 -12.329 23.873 1.00 18.70  ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.904 -12.602 25.248 1.00 19.34  ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 15.234 -11.893 25.580 1.00 19.36  ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 15.361 -11.212 26.612 1.00 19.97  ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 14.053 -14.125 25.481 1.00 18.80  ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.609 -14.405 26.878 1.00 21.23  ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.713 -14.852 25.278 1.00 18.55  ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 16.236 -12.027 24.692 1.00 16.76  ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.555 -11.457 24.945 1.00 17.40  ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 18.337 -11.398 23.633 1.00 16.71  ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 18.141 -12.270 22.774 1.00 16.27  ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 18.302 -12.348 25.991 1.00 18.42  ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.774 -12.083 26.179 1.00 18.88  ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 20.357 -11.126 26.966 1.00 21.01  ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.859 -12.794 25.548 1.00 17.10  ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.744 -11.239 26.910 1.00 21.12  ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 22.068 -12.241 26.028 1.00 17.97  ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.924 -13.822 24.585 1.00 16.64  ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 23.325 -12.739 25.646 1.00 18.64  ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 22.170 -14.317 24.230 1.00 17.93  ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 23.341 -13.732 24.713 1.00 17.85  ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 19.203 -10.413 23.479 1.00 15.99  ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 20.070 -10.345 22.292 1.00 16.11  ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 21.364 -9.683  22.637 1.00 16.30  ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 21.402 -8.807  23.525 1.00 16.62  ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 19.378 -9.651  21.120 1.00 16.83  ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.833 -8.272  21.411 1.00 18.79  ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.811 -7.120  21.341 1.00 21.48  ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.563 -6.089  22.012 1.00 22.64  ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.818 -7.234  20.597 1.00 19.36  ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.428 -10.037 21.905 1.00 15.27  ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.712 -9.399  22.140 1.00 15.03  ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.480 -9.370  20.801 1.00 14.98  ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.903 -10.428 20.274 1.00 14.83  ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.454 -10.185 23.227 1.00 16.49  ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.804 -9.624  23.626 1.00 20.99  ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.544 -9.168  22.740 1.00 22.29  ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 26.190 -9.782  24.800 1.00 23.78  ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.648 -8.169  20.232 1.00 15.08  ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 25.334 -7.994  18.956 0.50 15.11  ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 25.313 -8.058  18.941 0.50 15.38  ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.781 -8.467  19.032 1.00 15.30  ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 27.286 -9.053  18.064 1.00 14.83  ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 25.301 -6.525  18.513 0.50 16.32  ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 25.159 -6.660  18.349 0.50 17.49  ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 26.205 -6.266  17.446 0.50 16.84  ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.610 -5.715  19.295 0.50 19.03  ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.463 -8.187  20.163 1.00 15.68  ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.873 -8.594  20.281 1.00 16.70  ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 29.053 -10.109 20.229 1.00 15.11  ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 30.157 -10.543 19.878 1.00 15.44  ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.495 -8.039  21.553 1.00 19.56  ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 29.144 -8.728  22.726 1.00 25.07  ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 28.008 -10.904 20.564 1.00 14.62  ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 28.093 -12.377 20.498 1.00 13.68  ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.451 -12.944 19.226 1.00 12.68  ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.453 -14.152 19.017 1.00 12.91  ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 27.385 -12.979 21.735 1.00 15.16  ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 28.042 -12.595 23.049 1.00 16.30  ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 27.296 -13.159 24.249 1.00 14.31  ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 27.329 -14.643 24.286 1.00 13.53  ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 27.321 -15.371 25.398 1.00 14.43  ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 27.243 -14.783 26.594 1.00 15.73  ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.472 -16.698 25.335 1.00 14.11  ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.755 -12.092 18.411 1.00 11.83  ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.969 -12.541 17.284 1.00 12.03  ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.869 -13.498 17.733 1.00 12.50  ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.551 -14.434 16.984 1.00 12.25  ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.788 -13.139 16.150 1.00 12.50  ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.998 -13.480 14.913 1.00 13.41  ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 25.098 -12.677 14.522 1.00 14.72  ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.309 -14.498 14.267 1.00 13.22  ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 24.213 -13.252 18.917 1.00 11.84  ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 23.135 -14.141 19.372 1.00 12.60  ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.848 -13.389 19.609 1.00 13.09  ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.886 -12.236 20.105 1.00 14.28  ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.487 -14.874 20.675 1.00 13.06  ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.591 -15.952 20.576 1.00 13.65  ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.828 -16.556 21.962 1.00 14.98  ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 24.173 -17.084 19.613 1.00 14.28  ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.728 -14.074 19.381 1.00 12.15  ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.406 -13.554 19.758 1.00 12.81  ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.578 -14.764 20.176 1.00 13.37  ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.647 -15.841 19.571 1.00 14.19  ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.765 -12.826 18.563 1.00 13.73  ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.366 -12.219 18.843 1.00 13.89  ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 17.193 -10.903 18.068 1.00 16.19  ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 16.258 -13.223 18.511 1.00 14.74  ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.784 -14.575 21.243 1.00 13.72  ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.892 -15.603 21.760 1.00 13.94  ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.463 -15.065 21.779 1.00 14.49  ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 15.230 -13.952 22.302 1.00 15.05  ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 17.309 -16.047 23.179 1.00 14.56  ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 16.373 -17.127 23.740 1.00 16.16  ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.769 -16.590 23.166 1.00 15.95  ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.539 -15.845 21.216 1.00 14.89  ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 13.129 -15.478 21.202 1.00 15.01  ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 12.335 -16.571 21.902 1.00 16.10  ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.801 -17.702 22.130 1.00 15.99  ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.634 -15.280 19.776 1.00 16.57  ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.827 -16.434 18.974 1.00 17.05  ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 11.096 -16.242 22.286 1.00 16.67  ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 10.214 -17.210 22.944 1.00 18.57  ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.380  -18.020 21.924 1.00 20.21  ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 9.049  -17.533 20.838 1.00 21.11  ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 9.332  -16.487 23.960 1.00 20.90  ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.450  -15.619 23.270 1.00 24.26  ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 9.028  -19.255 22.286 1.00 20.05  ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 8.266  -20.144 21.401 1.00 21.64  ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.980  -20.613 22.100 1.00 24.21  ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.931  -20.699 23.321 1.00 23.66  ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 9.108  -21.397 21.029 1.00 21.99  ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.360  -22.172 22.190 1.00 22.57  ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.448 -21.049 20.340 1.00 21.19  ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.987  -21.000 21.304 1.00 25.95  ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.764  -21.570 21.856 1.00 27.49  ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.997  -23.047 22.179 1.00 27.72  ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.623  -23.520 23.256 1.00 30.16  ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.600  -21.330 20.892 1.00 31.27  ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.916  -21.931 19.641 1.00 34.79  ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.363  -19.876 20.653 1.00 30.72  ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.634  -23.777 21.254 1.00 25.97  ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.903  -25.202 21.456 1.00 26.31  ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 7.207  -25.441 22.218 1.00 25.24  ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 8.143  -24.641 22.081 1.00 24.69  ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.974  -25.913 20.107 1.00 27.73  ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.302  -26.523 22.974 1.00 24.21  ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.527  -26.878 23.690 1.00 25.29  ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.510  -27.520 22.717 1.00 25.38  ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 9.112  -28.334 21.868 1.00 28.34  ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.220  -27.814 24.864 1.00 30.39  ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.692  -27.044 26.075 1.00 38.78  ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 7.483  -27.989 27.237 1.00 48.60  ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.670  -28.916 27.178 1.00 52.63  ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 8.207  -27.785 28.323 1.00 50.32  ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.776 -27.141 22.837 1.00 21.92  ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.867 -27.685 22.024 1.00 21.20  ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.514 -28.887 22.673 1.00 21.20  ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.287 -29.159 23.864 1.00 23.32  ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.337 -29.560 21.914 1.00 20.08  ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.905 -30.811 22.409 1.00 21.70  ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.403 -30.847 22.527 1.00 21.38  ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.937 -31.880 22.931 1.00 23.46  ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.402 -31.957 21.542 1.00 23.88  ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 11.617 -32.246 21.711 1.00 34.99  ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 16.106 -29.757 22.227 1.00 17.11  ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.568 -29.754 22.286 1.00 16.04  ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.966 -29.534 23.749 1.00 16.72  ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.231 -28.899 24.533 1.00 18.61  ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 18.110 -28.586 21.442 1.00 17.17  ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.940 -28.757 19.942 1.00 20.89  ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 17.964 -29.931 19.446 1.00 21.76  ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.797 -27.729 19.245 1.00 18.07  ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 19.094 -30.135 24.122 1.00 15.57  ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.667 -29.961 25.465 1.00 15.10  ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.954 -29.139 25.310 1.00 15.41  ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.774 -29.448 24.425 1.00 15.96  ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 20.045 -31.316 26.044 1.00 16.94  ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.821 -32.078 26.224 1.00 19.86  ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.788 -31.196 27.387 1.00 19.17  ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 21.150 -28.098 26.121 1.00 14.99  ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.379 -27.289 26.073 1.00 14.90  ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.466 -27.985 26.908 1.00 13.64  ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 23.230 -28.442 28.042 1.00 15.04  ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 22.131 -25.903 26.663 1.00 15.43  ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.945 -25.201 26.026 1.00 15.64  ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.387 -25.042 26.553 1.00 15.79  ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 21.128 -25.071 24.436 1.00 17.40  ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.653 -28.096 26.349 1.00 12.97  ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.785 -28.652 27.090 1.00 12.83  ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 26.167 -27.731 28.253 1.00 13.09  ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 26.181 -26.498 28.114 1.00 13.49  ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.985 -28.768 26.170 1.00 12.37  ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.523 -28.351 29.398 1.00 12.73  ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.997 -27.598 30.579 1.00 13.24  ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.317 -28.265 30.952 1.00 13.17  ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.348 -29.323 31.608 1.00 14.62  ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.971 -27.601 31.728 1.00 13.69  ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.615 -27.066 31.295 1.00 12.69  ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.645 -25.590 30.938 1.00 15.16  ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 23.289 -25.117 30.588 1.00 15.60  ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 23.041 -24.014 29.880 1.00 15.85  ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 24.030 -23.197 29.538 1.00 14.56  ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.792 -23.685 29.560 1.00 17.16  ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.430 -27.690 30.438 1.00 12.56  ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.733 -28.374 30.453 1.00 12.55  ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.788 -27.418 29.920 1.00 12.64  ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.464 -26.299 29.467 1.00 13.82  ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.624 -29.583 29.503 1.00 11.61  ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.521 -29.122 27.728 1.00 13.29  ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 33.045 -27.891 29.921 1.00 14.10  ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 34.173 -27.166 29.324 1.00 14.68  ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.840 -28.018 28.224 1.00 14.70  ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 36.049 -27.851 27.993 1.00 15.66  ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 35.216 -26.742 30.364 1.00 17.16  ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.897 -27.880 31.104 1.00 21.07  ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.561 -29.027 30.857 1.00 20.08  ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.797 -27.591 31.946 1.00 28.47  ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 34.071 -28.876 27.526 1.00 14.33  ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.619 -29.634 26.384 1.00 13.45  ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.290 -28.730 25.373 1.00 13.15  ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.840 -27.602 25.117 1.00 13.48  ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.535 -30.455 25.663 1.00 13.64  ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.913 -31.867 26.609 1.00 14.13  ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.330 -29.259 24.750 1.00 12.36  ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 37.022 -28.656 23.618 1.00 12.61  ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 37.066 -29.572 22.411 1.00 12.66  ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.820 -29.328 21.450 1.00 12.81  ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.441 -28.171 23.964 1.00 13.49  ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.460 -26.915 24.854 1.00 17.28  ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.840 -26.345 24.999 1.00 20.31  ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.416 -26.407 26.093 1.00 22.47  ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.394 -25.796 23.918 1.00 17.66  ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.285 -30.660 22.418 1.00 12.28  ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.135 -31.504 21.224 1.00 13.24  ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.659 -31.747 21.021 1.00 12.81  ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.895 -31.846 21.994 1.00 13.15  ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.898 -32.804 21.272 1.00 15.92  ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.371 -33.557 22.301 1.00 19.32  ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.372 -32.592 21.559 1.00 16.25  ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.248 -31.845 19.747 1.00 11.47  ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.846 -32.093 19.448 1.00 11.37  ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.674 -32.297 17.942 1.00 10.33  ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.643 -32.600 17.242 1.00 12.31  ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.444 -32.169 17.458 1.00 11.06  ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.154 -32.373 16.028 1.00 10.74  ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.255 -31.233 15.610 1.00 11.27  ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.298 -30.893 16.333 1.00 11.88  ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.377 -33.726 15.882 1.00 11.33  ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 29.879 -33.916 14.441 1.00 12.88  ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.276 -34.911 16.301 1.00 12.38  ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.504 -30.661 14.419 1.00 11.12  ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.618 -29.577 13.948 1.00 10.28  ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.030 -29.930 12.580 1.00 10.84  ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.685 -30.623 11.810 1.00 11.96  ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.305 -28.177 13.918 1.00 10.77  ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.155 -27.876 12.690 1.00 10.47  ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.442 -28.361 12.574 1.00 12.77  ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.701 -27.009 11.694 1.00 10.97  ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.240 -28.065 11.464 1.00 13.19  ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.502 -26.707 10.591 1.00 12.22  ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.771 -27.232 10.482 1.00 12.92  ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.609 -26.940 9.398  1.00 14.92  ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.867 -29.343 12.268 1.00 10.95  ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.253 -29.523 10.935 1.00 11.83  ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.632 -28.388 10.020 1.00 11.62  ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.387 -27.205 10.333 1.00 11.95  ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.723 -29.604 11.048 1.00 12.45  ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.127 -29.903 9.674  1.00 13.10  ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.457 -31.068 8.991  1.00 13.53  ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.264 -29.015 9.063  1.00 13.31  ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 24.975 -31.330 7.700  1.00 14.72  ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.755 -29.277 7.782  1.00 14.48  ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.088 -30.454 7.132  1.00 14.64  ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.605 -30.685 5.829  1.00 18.67  ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.166 -28.760 8.862  1.00 11.09  ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.566 -27.833 7.786  1.00 11.87  ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.628 -28.030 6.576  1.00 13.59  ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.780 -28.974 5.791  1.00 14.03  ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.022 -28.067 7.409  1.00 11.37  ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.563 -27.044 6.018  1.00 14.11  ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.637 -27.109 6.434  1.00 14.79  ? 66  SER   C N   1 
ATOM   1558 C  CA  . SER   B 1 60  ? 25.654 -27.300 5.378  1.00 15.69  ? 66  SER   C CA  1 
ATOM   1559 C  C   . SER   B 1 60  ? 26.249 -27.217 3.964  1.00 15.15  ? 66  SER   C C   1 
ATOM   1560 O  O   . SER   B 1 60  ? 25.814 -27.950 3.076  1.00 16.30  ? 66  SER   C O   1 
ATOM   1561 C  CB  . SER   B 1 60  ? 24.527 -26.300 5.538  1.00 18.80  ? 66  SER   C CB  1 
ATOM   1562 O  OG  . SER   B 1 60  ? 24.919 -24.949 5.429  1.00 27.93  ? 66  SER   C OG  1 
ATOM   1563 N  N   . SER   B 1 61  ? 27.274 -26.380 3.761  1.00 14.06  ? 67  SER   C N   1 
ATOM   1564 C  CA  . SER   B 1 61  ? 27.898 -26.238 2.435  1.00 13.95  ? 67  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 61  ? 28.710 -27.454 2.009  1.00 15.94  ? 67  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 61  ? 29.121 -27.555 0.842  1.00 17.94  ? 67  SER   C O   1 
ATOM   1567 C  CB  . SER   B 1 61  ? 28.764 -24.999 2.417  1.00 14.59  ? 67  SER   C CB  1 
ATOM   1568 O  OG  . SER   B 1 61  ? 29.882 -25.078 3.275  1.00 15.67  ? 67  SER   C OG  1 
ATOM   1569 N  N   . ARG   B 1 62  ? 28.926 -28.421 2.911  1.00 14.93  ? 68  ARG   C N   1 
ATOM   1570 C  CA  . ARG   B 1 62  ? 29.554 -29.706 2.554  1.00 15.33  ? 68  ARG   C CA  1 
ATOM   1571 C  C   . ARG   B 1 62  ? 28.620 -30.899 2.798  1.00 15.74  ? 68  ARG   C C   1 
ATOM   1572 O  O   . ARG   B 1 62  ? 29.034 -32.047 2.602  1.00 16.70  ? 68  ARG   C O   1 
ATOM   1573 C  CB  . ARG   B 1 62  ? 30.839 -29.898 3.362  1.00 15.67  ? 68  ARG   C CB  1 
ATOM   1574 C  CG  . ARG   B 1 62  ? 31.897 -28.813 3.106  1.00 20.27  ? 68  ARG   C CG  1 
ATOM   1575 C  CD  . ARG   B 1 62  ? 32.565 -29.072 1.803  1.00 20.86  ? 68  ARG   C CD  1 
ATOM   1576 N  NE  . ARG   B 1 62  ? 33.591 -28.026 1.526  1.00 22.60  ? 68  ARG   C NE  1 
ATOM   1577 C  CZ  . ARG   B 1 62  ? 33.360 -26.903 0.865  1.00 26.05  ? 68  ARG   C CZ  1 
ATOM   1578 N  NH1 . ARG   B 1 62  ? 32.151 -26.647 0.387  1.00 29.28  ? 68  ARG   C NH1 1 
ATOM   1579 N  NH2 . ARG   B 1 62  ? 34.367 -26.061 0.578  1.00 25.26  ? 68  ARG   C NH2 1 
ATOM   1580 N  N   . ARG   B 1 63  ? 27.399 -30.640 3.341  1.00 16.70  ? 69  ARG   C N   1 
ATOM   1581 C  CA  . ARG   B 1 63  ? 26.449 -31.684 3.782  1.00 18.26  ? 69  ARG   C CA  1 
ATOM   1582 C  C   . ARG   B 1 63  ? 27.156 -32.723 4.657  1.00 18.58  ? 69  ARG   C C   1 
ATOM   1583 O  O   . ARG   B 1 63  ? 27.013 -33.938 4.463  1.00 19.94  ? 69  ARG   C O   1 
ATOM   1584 C  CB  . ARG   B 1 63  ? 25.812 -32.382 2.574  1.00 19.57  ? 69  ARG   C CB  1 
ATOM   1585 C  CG  . ARG   B 1 63  ? 24.814 -31.533 1.843  1.00 24.55  ? 69  ARG   C CG  1 
ATOM   1586 C  CD  . ARG   B 1 63  ? 23.820 -32.523 1.305  1.00 35.41  ? 69  ARG   C CD  1 
ATOM   1587 N  NE  . ARG   B 1 63  ? 22.811 -31.866 0.503  1.00 42.96  ? 69  ARG   C NE  1 
ATOM   1588 C  CZ  . ARG   B 1 63  ? 22.776 -31.905 -0.824 1.00 48.46  ? 69  ARG   C CZ  1 
ATOM   1589 N  NH1 . ARG   B 1 63  ? 23.754 -32.497 -1.508 1.00 48.00  ? 69  ARG   C NH1 1 
ATOM   1590 N  NH2 . ARG   B 1 63  ? 21.785 -31.320 -1.483 1.00 48.54  ? 69  ARG   C NH2 1 
ATOM   1591 N  N   . LYS   B 1 64  ? 27.967 -32.236 5.613  1.00 16.30  ? 70  LYS   C N   1 
ATOM   1592 C  CA  . LYS   B 1 64  ? 28.775 -33.129 6.408  1.00 16.27  ? 70  LYS   C CA  1 
ATOM   1593 C  C   . LYS   B 1 64  ? 28.884 -32.661 7.818  1.00 14.76  ? 70  LYS   C C   1 
ATOM   1594 O  O   . LYS   B 1 64  ? 28.878 -31.438 8.097  1.00 15.24  ? 70  LYS   C O   1 
ATOM   1595 C  CB  . LYS   B 1 64  ? 30.185 -33.147 5.792  1.00 19.96  ? 70  LYS   C CB  1 
ATOM   1596 C  CG  . LYS   B 1 64  ? 30.325 -34.192 4.668  1.00 30.27  ? 70  LYS   C CG  1 
ATOM   1597 C  CD  . LYS   B 1 64  ? 31.758 -34.382 4.230  1.00 38.79  ? 70  LYS   C CD  1 
ATOM   1598 C  CE  . LYS   B 1 64  ? 31.844 -35.301 3.040  1.00 43.36  ? 70  LYS   C CE  1 
ATOM   1599 N  NZ  . LYS   B 1 64  ? 31.212 -34.678 1.834  1.00 47.47  ? 70  LYS   C NZ  1 
ATOM   1600 N  N   . HIS   B 1 65  ? 28.987 -33.629 8.716  1.00 13.43  ? 71  HIS   C N   1 
ATOM   1601 C  CA  . HIS   B 1 65  ? 29.274 -33.346 10.130 1.00 13.43  ? 71  HIS   C CA  1 
ATOM   1602 C  C   . HIS   B 1 65  ? 30.752 -33.625 10.342 1.00 15.42  ? 71  HIS   C C   1 
ATOM   1603 O  O   . HIS   B 1 65  ? 31.246 -34.716 9.992  1.00 19.42  ? 71  HIS   C O   1 
ATOM   1604 C  CB  . HIS   B 1 65  ? 28.435 -34.241 11.057 1.00 13.95  ? 71  HIS   C CB  1 
ATOM   1605 C  CG  . HIS   B 1 65  ? 26.971 -33.981 11.007 1.00 12.51  ? 71  HIS   C CG  1 
ATOM   1606 N  ND1 . HIS   B 1 65  ? 26.314 -33.234 11.968 1.00 16.20  ? 71  HIS   C ND1 1 
ATOM   1607 C  CD2 . HIS   B 1 65  ? 26.076 -34.395 10.088 1.00 12.65  ? 71  HIS   C CD2 1 
ATOM   1608 C  CE1 . HIS   B 1 65  ? 25.031 -33.252 11.639 1.00 14.64  ? 71  HIS   C CE1 1 
ATOM   1609 N  NE2 . HIS   B 1 65  ? 24.820 -33.952 10.547 1.00 15.75  ? 71  HIS   C NE2 1 
ATOM   1610 N  N   . TYR   B 1 66  ? 31.508 -32.648 10.881 1.00 12.99  ? 72  TYR   C N   1 
ATOM   1611 C  CA  . TYR   B 1 66  ? 32.953 -32.852 11.034 1.00 12.63  ? 72  TYR   C CA  1 
ATOM   1612 C  C   . TYR   B 1 66  ? 33.326 -32.898 12.518 1.00 12.14  ? 72  TYR   C C   1 
ATOM   1613 O  O   . TYR   B 1 66  ? 32.898 -32.028 13.294 1.00 12.43  ? 72  TYR   C O   1 
ATOM   1614 C  CB  . TYR   B 1 66  ? 33.673 -31.603 10.466 1.00 13.69  ? 72  TYR   C CB  1 
ATOM   1615 C  CG  . TYR   B 1 66  ? 33.650 -31.493 8.947  1.00 13.74  ? 72  TYR   C CG  1 
ATOM   1616 C  CD1 . TYR   B 1 66  ? 34.503 -32.251 8.165  1.00 14.90  ? 72  TYR   C CD1 1 
ATOM   1617 C  CD2 . TYR   B 1 66  ? 32.837 -30.564 8.297  1.00 15.15  ? 72  TYR   C CD2 1 
ATOM   1618 C  CE1 . TYR   B 1 66  ? 34.517 -32.127 6.778  1.00 16.61  ? 72  TYR   C CE1 1 
ATOM   1619 C  CE2 . TYR   B 1 66  ? 32.855 -30.425 6.910  1.00 16.26  ? 72  TYR   C CE2 1 
ATOM   1620 C  CZ  . TYR   B 1 66  ? 33.694 -31.216 6.163  1.00 17.46  ? 72  TYR   C CZ  1 
ATOM   1621 O  OH  . TYR   B 1 66  ? 33.662 -31.020 4.786  1.00 19.03  ? 72  TYR   C OH  1 
ATOM   1622 N  N   . PRO   B 1 67  ? 34.119 -33.876 12.940 1.00 12.44  ? 73  PRO   C N   1 
ATOM   1623 C  CA  . PRO   B 1 67  ? 34.681 -33.833 14.307 1.00 12.53  ? 73  PRO   C CA  1 
ATOM   1624 C  C   . PRO   B 1 67  ? 35.785 -32.779 14.380 1.00 12.83  ? 73  PRO   C C   1 
ATOM   1625 O  O   . PRO   B 1 67  ? 36.631 -32.703 13.463 1.00 15.98  ? 73  PRO   C O   1 
ATOM   1626 C  CB  . PRO   B 1 67  ? 35.283 -35.239 14.498 1.00 14.36  ? 73  PRO   C CB  1 
ATOM   1627 C  CG  . PRO   B 1 67  ? 35.438 -35.812 13.126 1.00 17.40  ? 73  PRO   C CG  1 
ATOM   1628 C  CD  . PRO   B 1 67  ? 34.611 -35.032 12.144 1.00 14.28  ? 73  PRO   C CD  1 
ATOM   1629 N  N   . VAL   B 1 68  ? 35.754 -31.952 15.426 1.00 11.50  ? 74  VAL   C N   1 
ATOM   1630 C  CA  . VAL   B 1 68  ? 36.736 -30.862 15.557 1.00 12.62  ? 74  VAL   C CA  1 
ATOM   1631 C  C   . VAL   B 1 68  ? 37.141 -30.686 16.995 1.00 11.82  ? 74  VAL   C C   1 
ATOM   1632 O  O   . VAL   B 1 68  ? 36.420 -30.973 17.940 1.00 12.11  ? 74  VAL   C O   1 
ATOM   1633 C  CB  . VAL   B 1 68  ? 36.114 -29.500 15.073 1.00 13.52  ? 74  VAL   C CB  1 
ATOM   1634 C  CG1 . VAL   B 1 68  ? 36.005 -29.430 13.529 1.00 15.46  ? 74  VAL   C CG1 1 
ATOM   1635 C  CG2 . VAL   B 1 68  ? 34.758 -29.222 15.773 1.00 14.70  ? 74  VAL   C CG2 1 
ATOM   1636 N  N   . SER   B 1 69  ? 38.355 -30.142 17.165 1.00 12.32  ? 75  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 69  ? 38.845 -29.509 18.390 1.00 12.83  ? 75  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 69  ? 38.568 -28.004 18.268 1.00 11.96  ? 75  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 69  ? 38.691 -27.403 17.184 1.00 11.90  ? 75  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 69  ? 40.356 -29.695 18.491 1.00 14.70  ? 75  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 69  ? 40.606 -31.083 18.638 1.00 20.62  ? 75  SER   C OG  1 
ATOM   1642 N  N   . PHE   B 1 70  ? 38.113 -27.373 19.347 1.00 11.35  ? 76  PHE   C N   1 
ATOM   1643 C  CA  . PHE   B 1 70  ? 37.761 -25.957 19.310 1.00 11.00  ? 76  PHE   C CA  1 
ATOM   1644 C  C   . PHE   B 1 70  ? 38.274 -25.235 20.549 1.00 11.66  ? 76  PHE   C C   1 
ATOM   1645 O  O   . PHE   B 1 70  ? 38.436 -25.845 21.604 1.00 12.04  ? 76  PHE   C O   1 
ATOM   1646 C  CB  . PHE   B 1 70  ? 36.226 -25.719 19.091 1.00 11.53  ? 76  PHE   C CB  1 
ATOM   1647 C  CG  . PHE   B 1 70  ? 35.344 -26.430 20.096 1.00 10.90  ? 76  PHE   C CG  1 
ATOM   1648 C  CD1 . PHE   B 1 70  ? 34.900 -27.725 19.869 1.00 11.44  ? 76  PHE   C CD1 1 
ATOM   1649 C  CD2 . PHE   B 1 70  ? 34.913 -25.776 21.222 1.00 11.39  ? 76  PHE   C CD2 1 
ATOM   1650 C  CE1 . PHE   B 1 70  ? 34.093 -28.365 20.804 1.00 11.44  ? 76  PHE   C CE1 1 
ATOM   1651 C  CE2 . PHE   B 1 70  ? 34.054 -26.414 22.124 1.00 11.39  ? 76  PHE   C CE2 1 
ATOM   1652 C  CZ  . PHE   B 1 70  ? 33.692 -27.705 21.937 1.00 11.73  ? 76  PHE   C CZ  1 
ATOM   1653 N  N   . SER   B 1 71  ? 38.535 -23.949 20.423 1.00 11.33  ? 77  SER   C N   1 
ATOM   1654 C  CA  . SER   B 1 71  ? 39.161 -23.151 21.478 1.00 12.71  ? 77  SER   C CA  1 
ATOM   1655 C  C   . SER   B 1 71  ? 38.170 -22.773 22.568 1.00 13.70  ? 77  SER   C C   1 
ATOM   1656 O  O   . SER   B 1 71  ? 36.960 -23.023 22.478 1.00 14.05  ? 77  SER   C O   1 
ATOM   1657 C  CB  . SER   B 1 71  ? 39.886 -21.949 20.876 1.00 12.25  ? 77  SER   C CB  1 
ATOM   1658 O  OG  . SER   B 1 71  ? 38.971 -21.055 20.248 1.00 14.91  ? 77  SER   C OG  1 
ATOM   1659 N  N   . LYS   B 1 72  ? 38.678 -22.180 23.644 1.00 15.36  ? 78  LYS   C N   1 
ATOM   1660 C  CA  . LYS   B 1 72  ? 37.800 -21.762 24.772 1.00 15.22  ? 78  LYS   C CA  1 
ATOM   1661 C  C   . LYS   B 1 72  ? 37.126 -20.438 24.397 1.00 14.14  ? 78  LYS   C C   1 
ATOM   1662 O  O   . LYS   B 1 72  ? 37.709 -19.640 23.645 1.00 15.89  ? 78  LYS   C O   1 
ATOM   1663 C  CB  . LYS   B 1 72  ? 38.655 -21.543 26.031 1.00 19.45  ? 78  LYS   C CB  1 
ATOM   1664 C  CG  . LYS   B 1 72  ? 39.394 -22.823 26.448 1.00 23.71  ? 78  LYS   C CG  1 
ATOM   1665 C  CD  . LYS   B 1 72  ? 39.873 -22.736 27.891 1.00 35.93  ? 78  LYS   C CD  1 
ATOM   1666 C  CE  . LYS   B 1 72  ? 40.149 -24.107 28.479 1.00 44.14  ? 78  LYS   C CE  1 
ATOM   1667 N  NZ  . LYS   B 1 72  ? 40.129 -24.078 29.969 1.00 47.99  ? 78  LYS   C NZ  1 
ATOM   1668 N  N   . PRO   B 1 73  ? 35.895 -20.183 24.863 1.00 14.09  ? 79  PRO   C N   1 
ATOM   1669 C  CA  . PRO   B 1 73  ? 35.164 -18.957 24.418 1.00 14.20  ? 79  PRO   C CA  1 
ATOM   1670 C  C   . PRO   B 1 73  ? 35.930 -17.699 24.787 1.00 15.56  ? 79  PRO   C C   1 
ATOM   1671 O  O   . PRO   B 1 73  ? 36.379 -17.556 25.965 1.00 17.87  ? 79  PRO   C O   1 
ATOM   1672 C  CB  . PRO   B 1 73  ? 33.837 -18.994 25.156 1.00 15.56  ? 79  PRO   C CB  1 
ATOM   1673 C  CG  . PRO   B 1 73  ? 33.753 -20.358 25.796 1.00 18.24  ? 79  PRO   C CG  1 
ATOM   1674 C  CD  . PRO   B 1 73  ? 35.107 -21.034 25.782 1.00 14.36  ? 79  PRO   C CD  1 
ATOM   1675 N  N   . SER   B 1 74  ? 36.151 -16.798 23.826 1.00 13.89  ? 80  SER   C N   1 
ATOM   1676 C  CA  . SER   B 1 74  ? 37.025 -15.644 24.048 1.00 14.73  ? 80  SER   C CA  1 
ATOM   1677 C  C   . SER   B 1 74  ? 36.641 -14.477 23.129 1.00 14.99  ? 80  SER   C C   1 
ATOM   1678 O  O   . SER   B 1 74  ? 35.761 -14.611 22.295 1.00 14.73  ? 80  SER   C O   1 
ATOM   1679 C  CB  . SER   B 1 74  ? 38.477 -16.037 23.740 1.00 19.45  ? 80  SER   C CB  1 
ATOM   1680 O  OG  . SER   B 1 74  ? 38.879 -17.153 24.503 1.00 26.83  ? 80  SER   C OG  1 
ATOM   1681 N  N   . LEU   B 1 75  ? 37.318 -13.338 23.311 1.00 15.58  ? 81  LEU   C N   1 
ATOM   1682 C  CA  . LEU   B 1 75  ? 37.128 -12.130 22.506 1.00 17.03  ? 81  LEU   C CA  1 
ATOM   1683 C  C   . LEU   B 1 75  ? 38.126 -12.237 21.357 1.00 17.01  ? 81  LEU   C C   1 
ATOM   1684 O  O   . LEU   B 1 75  ? 39.360 -12.172 21.592 1.00 18.81  ? 81  LEU   C O   1 
ATOM   1685 C  CB  . LEU   B 1 75  ? 37.397 -10.875 23.387 1.00 19.54  ? 81  LEU   C CB  1 
ATOM   1686 C  CG  . LEU   B 1 75  ? 37.080 -9.512  22.779 1.00 22.30  ? 81  LEU   C CG  1 
ATOM   1687 C  CD1 . LEU   B 1 75  ? 35.613 -9.345  22.553 1.00 20.77  ? 81  LEU   C CD1 1 
ATOM   1688 C  CD2 . LEU   B 1 75  ? 37.555 -8.407  23.727 1.00 24.55  ? 81  LEU   C CD2 1 
ATOM   1689 N  N   . ILE   B 1 76  ? 37.637 -12.480 20.136 1.00 17.29  ? 82  ILE   C N   1 
ATOM   1690 C  CA  . ILE   B 1 76  ? 38.441 -12.763 18.933 1.00 18.31  ? 82  ILE   C CA  1 
ATOM   1691 C  C   . ILE   B 1 76  ? 38.186 -11.721 17.849 1.00 18.15  ? 82  ILE   C C   1 
ATOM   1692 O  O   . ILE   B 1 76  ? 37.008 -11.326 17.620 1.00 17.68  ? 82  ILE   C O   1 
ATOM   1693 C  CB  . ILE   B 1 76  ? 38.067 -14.163 18.406 1.00 20.04  ? 82  ILE   C CB  1 
ATOM   1694 C  CG1 . ILE   B 1 76  ? 38.311 -15.286 19.425 1.00 22.36  ? 82  ILE   C CG1 1 
ATOM   1695 C  CG2 . ILE   B 1 76  ? 38.751 -14.496 17.065 1.00 22.03  ? 82  ILE   C CG2 1 
ATOM   1696 C  CD1 . ILE   B 1 76  ? 39.714 -15.641 19.672 1.00 25.86  ? 82  ILE   C CD1 1 
ATOM   1697 N  N   . PHE   B 1 77  ? 39.258 -11.246 17.189 1.00 17.57  ? 83  PHE   C N   1 
ATOM   1698 C  CA  . PHE   B 1 77  ? 39.090 -10.298 16.106 1.00 18.47  ? 83  PHE   C CA  1 
ATOM   1699 C  C   . PHE   B 1 77  ? 38.654 -11.114 14.879 1.00 18.65  ? 83  PHE   C C   1 
ATOM   1700 O  O   . PHE   B 1 77  ? 39.292 -12.124 14.490 1.00 20.88  ? 83  PHE   C O   1 
ATOM   1701 C  CB  . PHE   B 1 77  ? 40.434 -9.604  15.788 1.00 18.93  ? 83  PHE   C CB  1 
ATOM   1702 C  CG  . PHE   B 1 77  ? 40.207 -8.509  14.775 1.00 20.57  ? 83  PHE   C CG  1 
ATOM   1703 C  CD1 . PHE   B 1 77  ? 39.548 -7.351  15.123 1.00 22.05  ? 83  PHE   C CD1 1 
ATOM   1704 C  CD2 . PHE   B 1 77  ? 40.574 -8.681  13.445 1.00 22.57  ? 83  PHE   C CD2 1 
ATOM   1705 C  CE1 . PHE   B 1 77  ? 39.263 -6.367  14.166 1.00 23.61  ? 83  PHE   C CE1 1 
ATOM   1706 C  CE2 . PHE   B 1 77  ? 40.337 -7.676  12.508 1.00 23.46  ? 83  PHE   C CE2 1 
ATOM   1707 C  CZ  . PHE   B 1 77  ? 39.676 -6.550  12.863 1.00 23.61  ? 83  PHE   C CZ  1 
ATOM   1708 N  N   . VAL   B 1 78  ? 37.567 -10.665 14.247 1.00 16.38  ? 84  VAL   C N   1 
ATOM   1709 C  CA  . VAL   B 1 78  ? 37.001 -11.354 13.101 1.00 16.36  ? 84  VAL   C CA  1 
ATOM   1710 C  C   . VAL   B 1 78  ? 37.088 -10.403 11.893 1.00 16.23  ? 84  VAL   C C   1 
ATOM   1711 O  O   . VAL   B 1 78  ? 36.621 -9.265  11.992 1.00 16.76  ? 84  VAL   C O   1 
ATOM   1712 C  CB  . VAL   B 1 78  ? 35.511 -11.771 13.393 1.00 16.87  ? 84  VAL   C CB  1 
ATOM   1713 C  CG1 . VAL   B 1 78  ? 34.901 -12.540 12.224 1.00 18.20  ? 84  VAL   C CG1 1 
ATOM   1714 C  CG2 . VAL   B 1 78  ? 35.389 -12.573 14.690 1.00 17.47  ? 84  VAL   C CG2 1 
ATOM   1715 N  N   . GLU   B 1 79  ? 37.568 -10.875 10.726 1.00 15.27  ? 85  GLU   C N   1 
ATOM   1716 C  CA  . GLU   B 1 79  ? 37.589 -10.064 9.517  1.00 16.59  ? 85  GLU   C CA  1 
ATOM   1717 C  C   . GLU   B 1 79  ? 36.196 -9.829  8.999  1.00 16.30  ? 85  GLU   C C   1 
ATOM   1718 O  O   . GLU   B 1 79  ? 35.245 -10.484 9.417  1.00 15.90  ? 85  GLU   C O   1 
ATOM   1719 C  CB  . GLU   B 1 79  ? 38.470 -10.725 8.426  1.00 18.07  ? 85  GLU   C CB  1 
ATOM   1720 C  CG  . GLU   B 1 79  ? 39.938 -10.766 8.806  1.00 20.28  ? 85  GLU   C CG  1 
ATOM   1721 C  CD  . GLU   B 1 79  ? 40.584 -9.415  9.041  1.00 26.38  ? 85  GLU   C CD  1 
ATOM   1722 O  OE1 . GLU   B 1 79  ? 40.171 -8.382  8.447  1.00 28.70  ? 85  GLU   C OE1 1 
ATOM   1723 O  OE2 . GLU   B 1 79  ? 41.549 -9.398  9.835  1.00 30.32  ? 85  GLU   C OE2 1 
ATOM   1724 N  N   . ALA   B 1 80  ? 36.042 -8.813  8.168  1.00 17.18  ? 86  ALA   C N   1 
ATOM   1725 C  CA  . ALA   B 1 80  ? 34.759 -8.456  7.620  1.00 17.99  ? 86  ALA   C CA  1 
ATOM   1726 C  C   . ALA   B 1 80  ? 34.122 -9.622  6.871  1.00 18.70  ? 86  ALA   C C   1 
ATOM   1727 O  O   . ALA   B 1 80  ? 34.816 -10.424 6.229  1.00 19.41  ? 86  ALA   C O   1 
ATOM   1728 C  CB  . ALA   B 1 80  ? 34.951 -7.286  6.651  1.00 19.52  ? 86  ALA   C CB  1 
ATOM   1729 N  N   . SER   B 1 81  ? 32.833 -9.784  7.085  1.00 17.32  ? 87  SER   C N   1 
ATOM   1730 C  CA  . SER   B 1 81  ? 32.105 -10.813 6.388  1.00 18.33  ? 87  SER   C CA  1 
ATOM   1731 C  C   . SER   B 1 81  ? 30.972 -10.163 5.592  1.00 18.81  ? 87  SER   C C   1 
ATOM   1732 O  O   . SER   B 1 81  ? 30.830 -8.918  5.590  1.00 19.25  ? 87  SER   C O   1 
ATOM   1733 C  CB  . SER   B 1 81  ? 31.557 -11.788 7.422  1.00 17.99  ? 87  SER   C CB  1 
ATOM   1734 O  OG  . SER   B 1 81  ? 30.527 -11.131 8.152  1.00 17.84  ? 87  SER   C OG  1 
ATOM   1735 N  N   . GLU   B 1 82  ? 30.151 -10.976 4.923  1.00 20.58  ? 88  GLU   C N   1 
ATOM   1736 C  CA  . GLU   B 1 82  ? 29.037 -10.358 4.205  1.00 21.55  ? 88  GLU   C CA  1 
ATOM   1737 C  C   . GLU   B 1 82  ? 28.002 -9.726  5.147  1.00 21.57  ? 88  GLU   C C   1 
ATOM   1738 O  O   . GLU   B 1 82  ? 27.192 -8.904  4.699  1.00 23.68  ? 88  GLU   C O   1 
ATOM   1739 C  CB  . GLU   B 1 82  ? 28.416 -11.326 3.215  1.00 25.35  ? 88  GLU   C CB  1 
ATOM   1740 C  CG  . GLU   B 1 82  ? 27.693 -12.530 3.751  1.00 32.86  ? 88  GLU   C CG  1 
ATOM   1741 C  CD  . GLU   B 1 82  ? 27.003 -13.244 2.599  1.00 37.96  ? 88  GLU   C CD  1 
ATOM   1742 O  OE1 . GLU   B 1 82  ? 27.640 -13.382 1.528  1.00 39.38  ? 88  GLU   C OE1 1 
ATOM   1743 O  OE2 . GLU   B 1 82  ? 25.822 -13.635 2.757  1.00 40.37  ? 88  GLU   C OE2 1 
ATOM   1744 N  N   . TYR   B 1 83  ? 28.054 -10.022 6.456  1.00 17.73  ? 89  TYR   C N   1 
ATOM   1745 C  CA  . TYR   B 1 83  ? 27.033 -9.551  7.375  1.00 17.75  ? 89  TYR   C CA  1 
ATOM   1746 C  C   . TYR   B 1 83  ? 27.538 -8.710  8.551  1.00 18.50  ? 89  TYR   C C   1 
ATOM   1747 O  O   . TYR   B 1 83  ? 26.699 -8.119  9.228  1.00 19.06  ? 89  TYR   C O   1 
ATOM   1748 C  CB  . TYR   B 1 83  ? 26.169 -10.746 7.876  1.00 18.02  ? 89  TYR   C CB  1 
ATOM   1749 C  CG  . TYR   B 1 83  ? 26.984 -11.958 8.320  1.00 17.12  ? 89  TYR   C CG  1 
ATOM   1750 C  CD1 . TYR   B 1 83  ? 27.367 -12.949 7.405  1.00 18.15  ? 89  TYR   C CD1 1 
ATOM   1751 C  CD2 . TYR   B 1 83  ? 27.438 -12.076 9.627  1.00 16.38  ? 89  TYR   C CD2 1 
ATOM   1752 C  CE1 . TYR   B 1 83  ? 28.142 -14.051 7.811  1.00 16.92  ? 89  TYR   C CE1 1 
ATOM   1753 C  CE2 . TYR   B 1 83  ? 28.186 -13.168 10.046 1.00 16.77  ? 89  TYR   C CE2 1 
ATOM   1754 C  CZ  . TYR   B 1 83  ? 28.535 -14.163 9.135  1.00 17.00  ? 89  TYR   C CZ  1 
ATOM   1755 O  OH  . TYR   B 1 83  ? 29.353 -15.206 9.515  1.00 17.81  ? 89  TYR   C OH  1 
ATOM   1756 N  N   . TYR   B 1 84  ? 28.847 -8.598  8.815  1.00 16.48  ? 90  TYR   C N   1 
ATOM   1757 C  CA  . TYR   B 1 84  ? 29.375 -7.678  9.834  1.00 17.09  ? 90  TYR   C CA  1 
ATOM   1758 C  C   . TYR   B 1 84  ? 30.684 -7.028  9.280  1.00 16.48  ? 90  TYR   C C   1 
ATOM   1759 O  O   . TYR   B 1 84  ? 31.411 -7.675  8.512  1.00 16.29  ? 90  TYR   C O   1 
ATOM   1760 C  CB  . TYR   B 1 84  ? 29.773 -8.434  11.145 1.00 15.87  ? 90  TYR   C CB  1 
ATOM   1761 C  CG  . TYR   B 1 84  ? 28.586 -8.861  12.006 1.00 14.49  ? 90  TYR   C CG  1 
ATOM   1762 C  CD1 . TYR   B 1 84  ? 27.709 -7.918  12.556 1.00 14.83  ? 90  TYR   C CD1 1 
ATOM   1763 C  CD2 . TYR   B 1 84  ? 28.371 -10.180 12.304 1.00 14.17  ? 90  TYR   C CD2 1 
ATOM   1764 C  CE1 . TYR   B 1 84  ? 26.649 -8.303  13.380 1.00 14.79  ? 90  TYR   C CE1 1 
ATOM   1765 C  CE2 . TYR   B 1 84  ? 27.306 -10.576 13.111 1.00 13.54  ? 90  TYR   C CE2 1 
ATOM   1766 C  CZ  . TYR   B 1 84  ? 26.441 -9.638  13.647 1.00 14.09  ? 90  TYR   C CZ  1 
ATOM   1767 O  OH  . TYR   B 1 84  ? 25.372 -10.047 14.435 1.00 14.98  ? 90  TYR   C OH  1 
ATOM   1768 N  N   . PRO   B 1 85  ? 31.080 -5.838  9.767  1.00 16.76  ? 91  PRO   C N   1 
ATOM   1769 C  CA  . PRO   B 1 85  ? 32.422 -5.322  9.450  1.00 16.52  ? 91  PRO   C CA  1 
ATOM   1770 C  C   . PRO   B 1 85  ? 33.469 -6.109  10.264 1.00 16.04  ? 91  PRO   C C   1 
ATOM   1771 O  O   . PRO   B 1 85  ? 33.116 -6.936  11.162 1.00 16.31  ? 91  PRO   C O   1 
ATOM   1772 C  CB  . PRO   B 1 85  ? 32.327 -3.860  9.931  1.00 17.17  ? 91  PRO   C CB  1 
ATOM   1773 C  CG  . PRO   B 1 85  ? 31.415 -3.941  11.111 1.00 17.66  ? 91  PRO   C CG  1 
ATOM   1774 C  CD  . PRO   B 1 85  ? 30.356 -4.986  10.760 1.00 17.01  ? 91  PRO   C CD  1 
ATOM   1775 N  N   . ALA   B 1 86  ? 34.764 -5.814  10.040 1.00 16.59  ? 92  ALA   C N   1 
ATOM   1776 C  CA  . ALA   B 1 86  ? 35.825 -6.408  10.839 1.00 17.65  ? 92  ALA   C CA  1 
ATOM   1777 C  C   . ALA   B 1 86  ? 35.674 -5.844  12.265 1.00 18.26  ? 92  ALA   C C   1 
ATOM   1778 O  O   . ALA   B 1 86  ? 35.456 -4.638  12.442 1.00 20.22  ? 92  ALA   C O   1 
ATOM   1779 C  CB  . ALA   B 1 86  ? 37.188 -6.020  10.264 1.00 17.17  ? 92  ALA   C CB  1 
ATOM   1780 N  N   . ARG   B 1 87  ? 35.671 -6.720  13.272 1.00 16.48  ? 93  ARG   C N   1 
ATOM   1781 C  CA  . ARG   B 1 87  ? 35.401 -6.311  14.646 1.00 16.56  ? 93  ARG   C CA  1 
ATOM   1782 C  C   . ARG   B 1 87  ? 35.809 -7.395  15.623 1.00 16.65  ? 93  ARG   C C   1 
ATOM   1783 O  O   . ARG   B 1 87  ? 36.058 -8.535  15.223 1.00 15.88  ? 93  ARG   C O   1 
ATOM   1784 C  CB  . ARG   B 1 87  ? 33.886 -6.024  14.836 1.00 16.93  ? 93  ARG   C CB  1 
ATOM   1785 C  CG  . ARG   B 1 87  ? 33.038 -7.312  14.812 1.00 15.90  ? 93  ARG   C CG  1 
ATOM   1786 C  CD  . ARG   B 1 87  ? 31.540 -7.022  14.756 1.00 16.55  ? 93  ARG   C CD  1 
ATOM   1787 N  NE  . ARG   B 1 87  ? 30.844 -8.293  14.998 1.00 16.71  ? 93  ARG   C NE  1 
ATOM   1788 C  CZ  . ARG   B 1 87  ? 29.785 -8.469  15.761 1.00 17.70  ? 93  ARG   C CZ  1 
ATOM   1789 N  NH1 . ARG   B 1 87  ? 29.198 -7.431  16.344 1.00 19.08  ? 93  ARG   C NH1 1 
ATOM   1790 N  NH2 . ARG   B 1 87  ? 29.295 -9.692  15.956 1.00 17.93  ? 93  ARG   C NH2 1 
ATOM   1791 N  N   . TYR   B 1 88  ? 35.798 -7.086  16.936 1.00 18.09  ? 94  TYR   C N   1 
ATOM   1792 C  CA  . TYR   B 1 88  ? 35.962 -8.141  17.947 1.00 18.83  ? 94  TYR   C CA  1 
ATOM   1793 C  C   . TYR   B 1 88  ? 34.556 -8.737  18.207 1.00 17.46  ? 94  TYR   C C   1 
ATOM   1794 O  O   . TYR   B 1 88  ? 33.590 -8.010  18.402 1.00 18.74  ? 94  TYR   C O   1 
ATOM   1795 C  CB  . TYR   B 1 88  ? 36.506 -7.570  19.288 1.00 22.04  ? 94  TYR   C CB  1 
ATOM   1796 C  CG  . TYR   B 1 88  ? 38.017 -7.461  19.232 1.00 24.70  ? 94  TYR   C CG  1 
ATOM   1797 C  CD1 . TYR   B 1 88  ? 38.820 -8.571  19.446 1.00 27.07  ? 94  TYR   C CD1 1 
ATOM   1798 C  CD2 . TYR   B 1 88  ? 38.628 -6.297  18.807 1.00 28.77  ? 94  TYR   C CD2 1 
ATOM   1799 C  CE1 . TYR   B 1 88  ? 40.209 -8.503  19.329 1.00 29.58  ? 94  TYR   C CE1 1 
ATOM   1800 C  CE2 . TYR   B 1 88  ? 40.021 -6.209  18.707 1.00 30.24  ? 94  TYR   C CE2 1 
ATOM   1801 C  CZ  . TYR   B 1 88  ? 40.801 -7.325  18.950 1.00 31.64  ? 94  TYR   C CZ  1 
ATOM   1802 O  OH  . TYR   B 1 88  ? 42.183 -7.331  18.852 1.00 34.78  ? 94  TYR   C OH  1 
ATOM   1803 N  N   . GLN   B 1 89  ? 34.492 -10.053 18.280 1.00 16.42  ? 95  GLN   C N   1 
ATOM   1804 C  CA  . GLN   B 1 89  ? 33.259 -10.755 18.665 1.00 15.00  ? 95  GLN   C CA  1 
ATOM   1805 C  C   . GLN   B 1 89  ? 33.580 -11.491 19.978 1.00 14.44  ? 95  GLN   C C   1 
ATOM   1806 O  O   . GLN   B 1 89  ? 34.661 -12.106 20.101 1.00 15.39  ? 95  GLN   C O   1 
ATOM   1807 C  CB  . GLN   B 1 89  ? 32.905 -11.757 17.563 1.00 15.30  ? 95  GLN   C CB  1 
ATOM   1808 C  CG  . GLN   B 1 89  ? 31.588 -12.469 17.870 1.00 16.26  ? 95  GLN   C CG  1 
ATOM   1809 C  CD  . GLN   B 1 89  ? 30.912 -13.062 16.639 1.00 15.08  ? 95  GLN   C CD  1 
ATOM   1810 O  OE1 . GLN   B 1 89  ? 30.867 -12.455 15.551 1.00 15.58  ? 95  GLN   C OE1 1 
ATOM   1811 N  NE2 . GLN   B 1 89  ? 30.351 -14.234 16.818 1.00 14.96  ? 95  GLN   C NE2 1 
ATOM   1812 N  N   . SER   B 1 90  ? 32.691 -11.452 20.946 1.00 13.59  ? 96  SER   C N   1 
ATOM   1813 C  CA  . SER   B 1 90  ? 32.898 -12.069 22.231 1.00 14.33  ? 96  SER   C CA  1 
ATOM   1814 C  C   . SER   B 1 90  ? 32.281 -13.481 22.291 1.00 13.70  ? 96  SER   C C   1 
ATOM   1815 O  O   . SER   B 1 90  ? 31.427 -13.838 21.476 1.00 13.54  ? 96  SER   C O   1 
ATOM   1816 C  CB  . SER   B 1 90  ? 32.378 -11.188 23.368 1.00 16.37  ? 96  SER   C CB  1 
ATOM   1817 O  OG  . SER   B 1 90  ? 30.972 -11.139 23.293 1.00 16.86  ? 96  SER   C OG  1 
ATOM   1818 N  N   . HIS   B 1 91  ? 32.759 -14.286 23.280 1.00 13.46  ? 97  HIS   C N   1 
ATOM   1819 C  CA  . HIS   B 1 91  ? 32.265 -15.637 23.527 1.00 12.86  ? 97  HIS   C CA  1 
ATOM   1820 C  C   . HIS   B 1 91  ? 32.338 -16.500 22.261 1.00 12.71  ? 97  HIS   C C   1 
ATOM   1821 O  O   . HIS   B 1 91  ? 31.434 -17.345 22.024 1.00 13.36  ? 97  HIS   C O   1 
ATOM   1822 C  CB  . HIS   B 1 91  ? 30.829 -15.619 24.115 1.00 13.71  ? 97  HIS   C CB  1 
ATOM   1823 C  CG  . HIS   B 1 91  ? 30.714 -14.864 25.427 1.00 15.60  ? 97  HIS   C CG  1 
ATOM   1824 N  ND1 . HIS   B 1 91  ? 30.738 -15.526 26.643 1.00 17.03  ? 97  HIS   C ND1 1 
ATOM   1825 C  CD2 . HIS   B 1 91  ? 30.589 -13.524 25.654 1.00 17.10  ? 97  HIS   C CD2 1 
ATOM   1826 C  CE1 . HIS   B 1 91  ? 30.576 -14.580 27.579 1.00 17.70  ? 97  HIS   C CE1 1 
ATOM   1827 N  NE2 . HIS   B 1 91  ? 30.515 -13.350 27.030 1.00 18.45  ? 97  HIS   C NE2 1 
ATOM   1828 N  N   . LEU   B 1 92  ? 33.407 -16.349 21.516 1.00 11.86  ? 98  LEU   C N   1 
ATOM   1829 C  CA  . LEU   B 1 92  ? 33.606 -17.067 20.266 1.00 12.01  ? 98  LEU   C CA  1 
ATOM   1830 C  C   . LEU   B 1 92  ? 34.683 -18.144 20.436 1.00 11.69  ? 98  LEU   C C   1 
ATOM   1831 O  O   . LEU   B 1 92  ? 35.663 -17.940 21.148 1.00 13.07  ? 98  LEU   C O   1 
ATOM   1832 C  CB  . LEU   B 1 92  ? 34.040 -16.067 19.146 1.00 13.25  ? 98  LEU   C CB  1 
ATOM   1833 C  CG  . LEU   B 1 92  ? 34.131 -16.611 17.737 1.00 14.33  ? 98  LEU   C CG  1 
ATOM   1834 C  CD1 . LEU   B 1 92  ? 32.794 -16.941 17.192 1.00 15.69  ? 98  LEU   C CD1 1 
ATOM   1835 C  CD2 . LEU   B 1 92  ? 34.783 -15.587 16.772 1.00 15.61  ? 98  LEU   C CD2 1 
ATOM   1836 N  N   . MET   B 1 93  ? 34.470 -19.295 19.798 1.00 11.37  ? 99  MET   C N   1 
ATOM   1837 C  CA  . MET   B 1 93  ? 35.415 -20.422 19.831 1.00 11.12  ? 99  MET   C CA  1 
ATOM   1838 C  C   . MET   B 1 93  ? 35.798 -20.754 18.392 1.00 11.20  ? 99  MET   C C   1 
ATOM   1839 O  O   . MET   B 1 93  ? 34.907 -20.786 17.519 1.00 12.52  ? 99  MET   C O   1 
ATOM   1840 C  CB  . MET   B 1 93  ? 34.677 -21.631 20.419 1.00 13.09  ? 99  MET   C CB  1 
ATOM   1841 C  CG  . MET   B 1 93  ? 34.198 -21.348 21.848 1.00 14.24  ? 99  MET   C CG  1 
ATOM   1842 S  SD  . MET   B 1 93  ? 33.205 -22.671 22.507 1.00 14.73  ? 99  MET   C SD  1 
ATOM   1843 C  CE  . MET   B 1 93  ? 31.802 -22.611 21.463 1.00 16.86  ? 99  MET   C CE  1 
ATOM   1844 N  N   . LEU   B 1 94  ? 37.086 -21.010 18.119 1.00 11.32  ? 100 LEU   C N   1 
ATOM   1845 C  CA  . LEU   B 1 94  ? 37.496 -21.287 16.747 1.00 12.51  ? 100 LEU   C CA  1 
ATOM   1846 C  C   . LEU   B 1 94  ? 37.925 -22.756 16.597 1.00 11.94  ? 100 LEU   C C   1 
ATOM   1847 O  O   . LEU   B 1 94  ? 38.455 -23.349 17.541 1.00 12.68  ? 100 LEU   C O   1 
ATOM   1848 C  CB  . LEU   B 1 94  ? 38.743 -20.444 16.369 1.00 13.56  ? 100 LEU   C CB  1 
ATOM   1849 C  CG  . LEU   B 1 94  ? 38.564 -18.956 16.305 1.00 14.72  ? 100 LEU   C CG  1 
ATOM   1850 C  CD1 . LEU   B 1 94  ? 39.843 -18.306 15.846 1.00 18.02  ? 100 LEU   C CD1 1 
ATOM   1851 C  CD2 . LEU   B 1 94  ? 37.360 -18.533 15.426 1.00 17.69  ? 100 LEU   C CD2 1 
ATOM   1852 N  N   . ALA   B 1 95  ? 37.766 -23.302 15.400 1.00 12.60  ? 101 ALA   C N   1 
ATOM   1853 C  CA  . ALA   B 1 95  ? 38.306 -24.589 14.994 1.00 11.86  ? 101 ALA   C CA  1 
ATOM   1854 C  C   . ALA   B 1 95  ? 38.840 -24.477 13.545 1.00 12.15  ? 101 ALA   C C   1 
ATOM   1855 O  O   . ALA   B 1 95  ? 38.475 -23.556 12.823 1.00 12.44  ? 101 ALA   C O   1 
ATOM   1856 C  CB  . ALA   B 1 95  ? 37.202 -25.667 15.020 1.00 12.89  ? 101 ALA   C CB  1 
ATOM   1857 N  N   . VAL   B 1 96  ? 39.705 -25.394 13.149 1.00 12.17  ? 102 VAL   C N   1 
ATOM   1858 C  CA  . VAL   B 1 96  ? 40.141 -25.502 11.773 1.00 13.28  ? 102 VAL   C CA  1 
ATOM   1859 C  C   . VAL   B 1 96  ? 39.076 -26.246 10.992 1.00 13.32  ? 102 VAL   C C   1 
ATOM   1860 O  O   . VAL   B 1 96  ? 38.774 -27.423 11.281 1.00 15.05  ? 102 VAL   C O   1 
ATOM   1861 C  CB  . VAL   B 1 96  ? 41.507 -26.249 11.719 1.00 14.72  ? 102 VAL   C CB  1 
ATOM   1862 C  CG1 . VAL   B 1 96  ? 41.900 -26.409 10.252 1.00 16.92  ? 102 VAL   C CG1 1 
ATOM   1863 C  CG2 . VAL   B 1 96  ? 42.545 -25.451 12.476 1.00 16.74  ? 102 VAL   C CG2 1 
ATOM   1864 N  N   . GLY   B 1 97  ? 38.471 -25.559 10.024 1.00 14.01  ? 103 GLY   C N   1 
ATOM   1865 C  CA  . GLY   B 1 97  ? 37.389 -26.183 9.282  1.00 15.15  ? 103 GLY   C CA  1 
ATOM   1866 C  C   . GLY   B 1 97  ? 36.712 -25.233 8.344  1.00 15.10  ? 103 GLY   C C   1 
ATOM   1867 O  O   . GLY   B 1 97  ? 36.995 -24.027 8.338  1.00 17.94  ? 103 GLY   C O   1 
ATOM   1868 N  N   . HIS   B 1 98  ? 35.802 -25.759 7.548  1.00 16.37  ? 104 HIS   C N   1 
ATOM   1869 C  CA  . HIS   B 1 98  ? 35.119 -24.964 6.546  1.00 15.94  ? 104 HIS   C CA  1 
ATOM   1870 C  C   . HIS   B 1 98  ? 33.865 -24.261 7.064  1.00 14.20  ? 104 HIS   C C   1 
ATOM   1871 O  O   . HIS   B 1 98  ? 33.068 -24.868 7.799  1.00 14.66  ? 104 HIS   C O   1 
ATOM   1872 C  CB  . HIS   B 1 98  ? 34.786 -25.856 5.357  1.00 18.29  ? 104 HIS   C CB  1 
ATOM   1873 C  CG  . HIS   B 1 98  ? 34.241 -25.072 4.226  1.00 22.25  ? 104 HIS   C CG  1 
ATOM   1874 N  ND1 . HIS   B 1 98  ? 35.006 -24.126 3.565  1.00 24.39  ? 104 HIS   C ND1 1 
ATOM   1875 C  CD2 . HIS   B 1 98  ? 32.978 -25.035 3.755  1.00 24.22  ? 104 HIS   C CD2 1 
ATOM   1876 C  CE1 . HIS   B 1 98  ? 34.194 -23.573 2.668  1.00 26.79  ? 104 HIS   C CE1 1 
ATOM   1877 N  NE2 . HIS   B 1 98  ? 32.967 -24.109 2.734  1.00 26.72  ? 104 HIS   C NE2 1 
ATOM   1878 N  N   . SER   B 1 99  ? 33.658 -22.974 6.663  1.00 14.61  ? 105 SER   C N   1 
ATOM   1879 C  CA  . SER   B 1 99  ? 32.444 -22.201 7.058  1.00 14.66  ? 105 SER   C CA  1 
ATOM   1880 C  C   . SER   B 1 99  ? 32.187 -21.067 6.049  1.00 16.36  ? 105 SER   C C   1 
ATOM   1881 O  O   . SER   B 1 99  ? 33.010 -20.134 5.959  1.00 18.57  ? 105 SER   C O   1 
ATOM   1882 C  CB  . SER   B 1 99  ? 32.683 -21.606 8.445  1.00 16.15  ? 105 SER   C CB  1 
ATOM   1883 O  OG  . SER   B 1 99  ? 31.605 -20.780 8.856  1.00 17.02  ? 105 SER   C OG  1 
ATOM   1884 N  N   . GLU   B 1 100 ? 31.091 -21.179 5.292  1.00 16.45  ? 106 GLU   C N   1 
ATOM   1885 C  CA  . GLU   B 1 100 ? 30.611 -20.139 4.349  1.00 16.34  ? 106 GLU   C CA  1 
ATOM   1886 C  C   . GLU   B 1 100 ? 29.514 -19.371 5.110  1.00 14.85  ? 106 GLU   C C   1 
ATOM   1887 O  O   . GLU   B 1 100 ? 28.952 -19.851 6.115  1.00 14.86  ? 106 GLU   C O   1 
ATOM   1888 C  CB  . GLU   B 1 100 ? 29.970 -20.824 3.122  1.00 20.91  ? 106 GLU   C CB  1 
ATOM   1889 C  CG  . GLU   B 1 100 ? 31.057 -21.444 2.307  1.00 33.89  ? 106 GLU   C CG  1 
ATOM   1890 C  CD  . GLU   B 1 100 ? 30.613 -22.211 1.110  1.00 46.67  ? 106 GLU   C CD  1 
ATOM   1891 O  OE1 . GLU   B 1 100 ? 29.516 -21.923 0.586  1.00 51.84  ? 106 GLU   C OE1 1 
ATOM   1892 O  OE2 . GLU   B 1 100 ? 31.359 -23.132 0.715  1.00 51.73  ? 106 GLU   C OE2 1 
ATOM   1893 N  N   . PRO   B 1 101 ? 29.110 -18.191 4.620  1.00 16.12  ? 107 PRO   C N   1 
ATOM   1894 C  CA  . PRO   B 1 101 ? 28.036 -17.449 5.328  1.00 15.28  ? 107 PRO   C CA  1 
ATOM   1895 C  C   . PRO   B 1 101 ? 26.765 -18.273 5.538  1.00 15.64  ? 107 PRO   C C   1 
ATOM   1896 O  O   . PRO   B 1 101 ? 26.149 -18.189 6.609  1.00 14.97  ? 107 PRO   C O   1 
ATOM   1897 C  CB  . PRO   B 1 101 ? 27.782 -16.209 4.425  1.00 18.12  ? 107 PRO   C CB  1 
ATOM   1898 C  CG  . PRO   B 1 101 ? 28.955 -16.124 3.543  1.00 20.63  ? 107 PRO   C CG  1 
ATOM   1899 C  CD  . PRO   B 1 101 ? 29.720 -17.403 3.511  1.00 17.86  ? 107 PRO   C CD  1 
ATOM   1900 N  N   . GLY   B 1 102 ? 26.390 -19.116 4.577  1.00 14.78  ? 108 GLY   C N   1 
ATOM   1901 C  CA  . GLY   B 1 102 ? 25.161 -19.909 4.710  1.00 15.14  ? 108 GLY   C CA  1 
ATOM   1902 C  C   . GLY   B 1 102 ? 25.256 -21.025 5.744  1.00 13.43  ? 108 GLY   C C   1 
ATOM   1903 O  O   . GLY   B 1 102 ? 24.262 -21.692 6.064  1.00 15.98  ? 108 GLY   C O   1 
ATOM   1904 N  N   . ASP   B 1 103 ? 26.490 -21.325 6.233  1.00 13.13  ? 109 ASP   C N   1 
ATOM   1905 C  CA  . ASP   B 1 103 ? 26.658 -22.361 7.249  1.00 12.51  ? 109 ASP   C CA  1 
ATOM   1906 C  C   . ASP   B 1 103 ? 26.297 -21.829 8.640  1.00 12.47  ? 109 ASP   C C   1 
ATOM   1907 O  O   . ASP   B 1 103 ? 26.202 -22.620 9.597  1.00 12.82  ? 109 ASP   C O   1 
ATOM   1908 C  CB  . ASP   B 1 103 ? 28.111 -22.861 7.265  1.00 13.55  ? 109 ASP   C CB  1 
ATOM   1909 C  CG  . ASP   B 1 103 ? 28.409 -23.650 6.031  1.00 14.86  ? 109 ASP   C CG  1 
ATOM   1910 O  OD1 . ASP   B 1 103 ? 27.541 -24.413 5.586  1.00 15.54  ? 109 ASP   C OD1 1 
ATOM   1911 O  OD2 . ASP   B 1 103 ? 29.550 -23.522 5.496  1.00 15.09  ? 109 ASP   C OD2 1 
ATOM   1912 N  N   . CYS   B 1 104 ? 26.087 -20.501 8.819  1.00 12.06  ? 110 CYS   C N   1 
ATOM   1913 C  CA  . CYS   B 1 104 ? 25.714 -19.948 10.137 1.00 12.11  ? 110 CYS   C CA  1 
ATOM   1914 C  C   . CYS   B 1 104 ? 24.457 -20.634 10.644 1.00 13.05  ? 110 CYS   C C   1 
ATOM   1915 O  O   . CYS   B 1 104 ? 23.521 -20.878 9.890  1.00 13.71  ? 110 CYS   C O   1 
ATOM   1916 C  CB  . CYS   B 1 104 ? 25.501 -18.426 10.040 1.00 13.02  ? 110 CYS   C CB  1 
ATOM   1917 S  SG  . CYS   B 1 104 ? 27.032 -17.462 9.944  1.00 14.63  ? 110 CYS   C SG  1 
ATOM   1918 N  N   . GLY   B 1 105 ? 24.473 -20.963 11.910 1.00 10.81  ? 111 GLY   C N   1 
ATOM   1919 C  CA  . GLY   B 1 105 ? 23.338 -21.644 12.544 1.00 11.95  ? 111 GLY   C CA  1 
ATOM   1920 C  C   . GLY   B 1 105 ? 23.522 -23.146 12.712 1.00 11.87  ? 111 GLY   C C   1 
ATOM   1921 O  O   . GLY   B 1 105 ? 22.755 -23.786 13.439 1.00 13.38  ? 111 GLY   C O   1 
ATOM   1922 N  N   . GLY   B 1 106 ? 24.537 -23.722 12.037 1.00 12.27  ? 112 GLY   C N   1 
ATOM   1923 C  CA  . GLY   B 1 106 ? 24.843 -25.148 12.221 1.00 12.89  ? 112 GLY   C CA  1 
ATOM   1924 C  C   . GLY   B 1 106 ? 25.251 -25.439 13.649 1.00 11.67  ? 112 GLY   C C   1 
ATOM   1925 O  O   . GLY   B 1 106 ? 25.997 -24.661 14.268 1.00 11.65  ? 112 GLY   C O   1 
ATOM   1926 N  N   . ILE   B 1 107 ? 24.804 -26.533 14.171 1.00 11.38  ? 113 ILE   C N   1 
ATOM   1927 C  CA  . ILE   B 1 107 ? 25.099 -26.891 15.571 1.00 11.47  ? 113 ILE   C CA  1 
ATOM   1928 C  C   . ILE   B 1 107 ? 26.447 -27.536 15.760 1.00 11.27  ? 113 ILE   C C   1 
ATOM   1929 O  O   . ILE   B 1 107 ? 26.850 -28.427 14.997 1.00 11.86  ? 113 ILE   C O   1 
ATOM   1930 C  CB  . ILE   B 1 107 ? 23.946 -27.819 16.123 1.00 14.16  ? 113 ILE   C CB  1 
ATOM   1931 C  CG1 . ILE   B 1 107 ? 22.749 -26.858 16.563 1.00 18.14  ? 113 ILE   C CG1 1 
ATOM   1932 C  CG2 . ILE   B 1 107 ? 24.395 -28.672 17.346 1.00 14.90  ? 113 ILE   C CG2 1 
ATOM   1933 C  CD1 . ILE   B 1 107 ? 21.410 -27.543 16.970 1.00 21.92  ? 113 ILE   C CD1 1 
ATOM   1934 N  N   . LEU   B 1 108 ? 27.150 -27.087 16.842 1.00 11.04  ? 114 LEU   C N   1 
ATOM   1935 C  CA  . LEU   B 1 108 ? 28.304 -27.789 17.390 1.00 10.44  ? 114 LEU   C CA  1 
ATOM   1936 C  C   . LEU   B 1 108 ? 27.816 -28.532 18.658 1.00 10.68  ? 114 LEU   C C   1 
ATOM   1937 O  O   . LEU   B 1 108 ? 27.189 -27.912 19.528 1.00 10.60  ? 114 LEU   C O   1 
ATOM   1938 C  CB  . LEU   B 1 108 ? 29.374 -26.739 17.771 1.00 10.58  ? 114 LEU   C CB  1 
ATOM   1939 C  CG  . LEU   B 1 108 ? 30.569 -27.262 18.570 1.00 10.78  ? 114 LEU   C CG  1 
ATOM   1940 C  CD1 . LEU   B 1 108 ? 31.447 -28.215 17.715 1.00 11.86  ? 114 LEU   C CD1 1 
ATOM   1941 C  CD2 . LEU   B 1 108 ? 31.445 -26.098 19.089 1.00 11.41  ? 114 LEU   C CD2 1 
ATOM   1942 N  N   . ARG   B 1 109 ? 28.105 -29.828 18.737 1.00 10.35  ? 115 ARG   C N   1 
ATOM   1943 C  CA  . ARG   B 1 109 ? 27.646 -30.641 19.888 1.00 11.40  ? 115 ARG   C CA  1 
ATOM   1944 C  C   . ARG   B 1 109 ? 28.768 -31.476 20.433 1.00 12.09  ? 115 ARG   C C   1 
ATOM   1945 O  O   . ARG   B 1 109 ? 29.693 -31.881 19.706 1.00 12.52  ? 115 ARG   C O   1 
ATOM   1946 C  CB  . ARG   B 1 109 ? 26.469 -31.547 19.426 1.00 15.08  ? 115 ARG   C CB  1 
ATOM   1947 C  CG  . ARG   B 1 109 ? 26.850 -32.570 18.420 1.00 20.24  ? 115 ARG   C CG  1 
ATOM   1948 C  CD  . ARG   B 1 109 ? 25.616 -33.396 18.003 1.00 28.34  ? 115 ARG   C CD  1 
ATOM   1949 N  NE  . ARG   B 1 109 ? 24.698 -32.674 17.108 1.00 34.78  ? 115 ARG   C NE  1 
ATOM   1950 C  CZ  . ARG   B 1 109 ? 23.446 -32.327 17.430 1.00 43.45  ? 115 ARG   C CZ  1 
ATOM   1951 N  NH1 . ARG   B 1 109 ? 22.968 -32.578 18.651 1.00 44.10  ? 115 ARG   C NH1 1 
ATOM   1952 N  NH2 . ARG   B 1 109 ? 22.685 -31.677 16.556 1.00 45.60  ? 115 ARG   C NH2 1 
ATOM   1953 N  N   . CYS   B 1 110 ? 28.682 -31.735 21.735 1.00 11.96  ? 116 CYS   C N   1 
ATOM   1954 C  CA  . CYS   B 1 110 ? 29.626 -32.627 22.423 1.00 13.02  ? 116 CYS   C CA  1 
ATOM   1955 C  C   . CYS   B 1 110 ? 28.775 -33.711 23.111 1.00 14.42  ? 116 CYS   C C   1 
ATOM   1956 O  O   . CYS   B 1 110 ? 27.544 -33.794 22.929 1.00 14.22  ? 116 CYS   C O   1 
ATOM   1957 C  CB  . CYS   B 1 110 ? 30.439 -31.830 23.441 1.00 12.48  ? 116 CYS   C CB  1 
ATOM   1958 S  SG  . CYS   B 1 110 ? 29.444 -31.164 24.821 1.00 12.37  ? 116 CYS   C SG  1 
ATOM   1959 N  N   . GLN   B 1 111 ? 29.407 -34.563 23.967 1.00 15.34  ? 117 GLN   C N   1 
ATOM   1960 C  CA  . GLN   B 1 111 ? 28.627 -35.604 24.668 1.00 17.28  ? 117 GLN   C CA  1 
ATOM   1961 C  C   . GLN   B 1 111 ? 27.570 -35.047 25.619 1.00 17.33  ? 117 GLN   C C   1 
ATOM   1962 O  O   . GLN   B 1 111 ? 26.630 -35.770 25.992 1.00 19.43  ? 117 GLN   C O   1 
ATOM   1963 C  CB  . GLN   B 1 111 ? 29.520 -36.597 25.451 1.00 18.47  ? 117 GLN   C CB  1 
ATOM   1964 C  CG  . GLN   B 1 111 ? 30.260 -35.911 26.579 1.00 21.05  ? 117 GLN   C CG  1 
ATOM   1965 C  CD  . GLN   B 1 111 ? 31.205 -36.836 27.314 1.00 32.09  ? 117 GLN   C CD  1 
ATOM   1966 O  OE1 . GLN   B 1 111 ? 32.416 -36.825 27.065 1.00 36.20  ? 117 GLN   C OE1 1 
ATOM   1967 N  NE2 . GLN   B 1 111 ? 30.663 -37.605 28.243 1.00 31.66  ? 117 GLN   C NE2 1 
ATOM   1968 N  N   . HIS   B 1 112 ? 27.675 -33.755 25.998 1.00 14.95  ? 118 HIS   C N   1 
ATOM   1969 C  CA  . HIS   B 1 112 ? 26.733 -33.174 26.961 1.00 14.25  ? 118 HIS   C CA  1 
ATOM   1970 C  C   . HIS   B 1 112 ? 25.558 -32.467 26.302 1.00 15.19  ? 118 HIS   C C   1 
ATOM   1971 O  O   . HIS   B 1 112 ? 24.631 -32.053 26.998 1.00 15.56  ? 118 HIS   C O   1 
ATOM   1972 C  CB  . HIS   B 1 112 ? 27.479 -32.189 27.894 1.00 14.81  ? 118 HIS   C CB  1 
ATOM   1973 C  CG  . HIS   B 1 112 ? 28.661 -32.832 28.567 1.00 14.35  ? 118 HIS   C CG  1 
ATOM   1974 N  ND1 . HIS   B 1 112 ? 29.971 -32.569 28.165 1.00 13.79  ? 118 HIS   C ND1 1 
ATOM   1975 C  CD2 . HIS   B 1 112 ? 28.699 -33.682 29.643 1.00 16.68  ? 118 HIS   C CD2 1 
ATOM   1976 C  CE1 . HIS   B 1 112 ? 30.744 -33.309 28.953 1.00 14.64  ? 118 HIS   C CE1 1 
ATOM   1977 N  NE2 . HIS   B 1 112 ? 30.022 -33.951 29.880 1.00 16.85  ? 118 HIS   C NE2 1 
ATOM   1978 N  N   . GLY   B 1 113 ? 25.639 -32.208 24.990 1.00 14.11  ? 119 GLY   C N   1 
ATOM   1979 C  CA  . GLY   B 1 113 ? 24.568 -31.508 24.291 1.00 13.46  ? 119 GLY   C CA  1 
ATOM   1980 C  C   . GLY   B 1 113 ? 25.093 -30.453 23.336 1.00 12.06  ? 119 GLY   C C   1 
ATOM   1981 O  O   . GLY   B 1 113 ? 26.213 -30.575 22.806 1.00 12.00  ? 119 GLY   C O   1 
ATOM   1982 N  N   . VAL   B 1 114 ? 24.247 -29.454 23.061 1.00 12.72  ? 120 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 114 ? 24.593 -28.375 22.119 1.00 12.16  ? 120 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 114 ? 25.542 -27.394 22.780 1.00 11.63  ? 120 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 114 ? 25.256 -26.833 23.856 1.00 12.37  ? 120 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 114 ? 23.303 -27.665 21.650 1.00 13.32  ? 120 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 114 ? 23.679 -26.461 20.799 1.00 14.79  ? 120 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 114 ? 22.389 -28.649 20.898 1.00 15.90  ? 120 VAL   C CG2 1 
ATOM   1989 N  N   . VAL   B 1 115 ? 26.704 -27.172 22.151 1.00 10.77  ? 121 VAL   C N   1 
ATOM   1990 C  CA  . VAL   B 1 115 ? 27.708 -26.239 22.637 1.00 10.83  ? 121 VAL   C CA  1 
ATOM   1991 C  C   . VAL   B 1 115 ? 27.490 -24.809 22.127 1.00 11.61  ? 121 VAL   C C   1 
ATOM   1992 O  O   . VAL   B 1 115 ? 27.754 -23.819 22.837 1.00 11.61  ? 121 VAL   C O   1 
ATOM   1993 C  CB  . VAL   B 1 115 ? 29.111 -26.763 22.249 1.00 10.95  ? 121 VAL   C CB  1 
ATOM   1994 C  CG1 . VAL   B 1 115 ? 30.199 -25.757 22.609 1.00 12.85  ? 121 VAL   C CG1 1 
ATOM   1995 C  CG2 . VAL   B 1 115 ? 29.345 -28.140 22.875 1.00 13.02  ? 121 VAL   C CG2 1 
ATOM   1996 N  N   . GLY   B 1 116 ? 27.146 -24.716 20.848 1.00 11.10  ? 122 GLY   C N   1 
ATOM   1997 C  CA  . GLY   B 1 116 ? 26.937 -23.410 20.232 1.00 12.59  ? 122 GLY   C CA  1 
ATOM   1998 C  C   . GLY   B 1 116 ? 26.569 -23.571 18.779 1.00 11.23  ? 122 GLY   C C   1 
ATOM   1999 O  O   . GLY   B 1 116 ? 26.261 -24.692 18.323 1.00 11.50  ? 122 GLY   C O   1 
ATOM   2000 N  N   . ILE   B 1 117 ? 26.574 -22.418 18.036 1.00 10.53  ? 123 ILE   C N   1 
ATOM   2001 C  CA  . ILE   B 1 117 ? 26.195 -22.450 16.630 1.00 10.76  ? 123 ILE   C CA  1 
ATOM   2002 C  C   . ILE   B 1 117 ? 27.235 -21.718 15.802 1.00 10.78  ? 123 ILE   C C   1 
ATOM   2003 O  O   . ILE   B 1 117 ? 27.893 -20.772 16.262 1.00 11.65  ? 123 ILE   C O   1 
ATOM   2004 C  CB  . ILE   B 1 117 ? 24.787 -21.811 16.362 1.00 12.05  ? 123 ILE   C CB  1 
ATOM   2005 C  CG1 . ILE   B 1 117 ? 24.706 -20.411 16.989 1.00 12.93  ? 123 ILE   C CG1 1 
ATOM   2006 C  CG2 . ILE   B 1 117 ? 23.681 -22.763 16.795 1.00 14.45  ? 123 ILE   C CG2 1 
ATOM   2007 C  CD1 . ILE   B 1 117 ? 23.353 -19.619 16.572 1.00 14.11  ? 123 ILE   C CD1 1 
ATOM   2008 N  N   . VAL   B 1 118 ? 27.400 -22.161 14.545 1.00 10.85  ? 124 VAL   C N   1 
ATOM   2009 C  CA  . VAL   B 1 118 ? 28.330 -21.469 13.619 1.00 11.02  ? 124 VAL   C CA  1 
ATOM   2010 C  C   . VAL   B 1 118 ? 27.977 -19.997 13.464 1.00 11.06  ? 124 VAL   C C   1 
ATOM   2011 O  O   . VAL   B 1 118 ? 26.775 -19.649 13.294 1.00 11.47  ? 124 VAL   C O   1 
ATOM   2012 C  CB  . VAL   B 1 118 ? 28.308 -22.140 12.222 1.00 10.90  ? 124 VAL   C CB  1 
ATOM   2013 C  CG1 . VAL   B 1 118 ? 29.173 -21.379 11.215 1.00 11.94  ? 124 VAL   C CG1 1 
ATOM   2014 C  CG2 . VAL   B 1 118 ? 28.767 -23.596 12.312 1.00 11.88  ? 124 VAL   C CG2 1 
ATOM   2015 N  N   . SER   B 1 119 ? 29.002 -19.123 13.598 1.00 11.22  ? 125 SER   C N   1 
ATOM   2016 C  CA  . SER   B 1 119 ? 28.791 -17.662 13.466 1.00 12.15  ? 125 SER   C CA  1 
ATOM   2017 C  C   . SER   B 1 119 ? 29.800 -16.975 12.561 1.00 12.73  ? 125 SER   C C   1 
ATOM   2018 O  O   . SER   B 1 119 ? 29.490 -15.899 12.007 1.00 13.23  ? 125 SER   C O   1 
ATOM   2019 C  CB  . SER   B 1 119 ? 28.858 -17.038 14.864 1.00 12.63  ? 125 SER   C CB  1 
ATOM   2020 O  OG  . SER   B 1 119 ? 28.739 -15.608 14.832 1.00 13.53  ? 125 SER   C OG  1 
ATOM   2021 N  N   . THR   B 1 120 ? 31.027 -17.547 12.416 1.00 11.73  ? 126 THR   C N   1 
ATOM   2022 C  CA  . THR   B 1 120 ? 32.062 -16.874 11.594 1.00 12.14  ? 126 THR   C CA  1 
ATOM   2023 C  C   . THR   B 1 120 ? 32.746 -17.888 10.693 1.00 11.78  ? 126 THR   C C   1 
ATOM   2024 O  O   . THR   B 1 120 ? 32.676 -19.116 10.941 1.00 11.89  ? 126 THR   C O   1 
ATOM   2025 C  CB  . THR   B 1 120 ? 33.148 -16.133 12.474 1.00 12.16  ? 126 THR   C CB  1 
ATOM   2026 O  OG1 . THR   B 1 120 ? 34.009 -17.118 13.113 1.00 14.28  ? 126 THR   C OG1 1 
ATOM   2027 C  CG2 . THR   B 1 120 ? 32.548 -15.214 13.492 1.00 13.89  ? 126 THR   C CG2 1 
ATOM   2028 N  N   . GLY   B 1 121 ? 33.452 -17.406 9.685  1.00 12.93  ? 127 GLY   C N   1 
ATOM   2029 C  CA  . GLY   B 1 121 ? 34.217 -18.285 8.805  1.00 15.29  ? 127 GLY   C CA  1 
ATOM   2030 C  C   . GLY   B 1 121 ? 35.263 -17.494 8.050  1.00 17.45  ? 127 GLY   C C   1 
ATOM   2031 O  O   . GLY   B 1 121 ? 35.147 -16.291 7.881  1.00 20.58  ? 127 GLY   C O   1 
ATOM   2032 N  N   . GLY   B 1 122 ? 36.148 -18.201 7.389  1.00 21.17  ? 128 GLY   C N   1 
ATOM   2033 C  CA  . GLY   B 1 122 ? 37.197 -17.594 6.562  1.00 24.15  ? 128 GLY   C CA  1 
ATOM   2034 C  C   . GLY   B 1 122 ? 38.591 -17.970 7.020  1.00 24.80  ? 128 GLY   C C   1 
ATOM   2035 O  O   . GLY   B 1 122 ? 38.802 -18.374 8.155  1.00 23.88  ? 128 GLY   C O   1 
ATOM   2036 N  N   . ASN   B 1 123 ? 39.581 -17.818 6.137  1.00 24.43  ? 129 ASN   C N   1 
ATOM   2037 C  CA  . ASN   B 1 123 ? 40.979 -18.192 6.412  1.00 25.67  ? 129 ASN   C CA  1 
ATOM   2038 C  C   . ASN   B 1 123 ? 41.122 -19.641 6.913  1.00 22.10  ? 129 ASN   C C   1 
ATOM   2039 O  O   . ASN   B 1 123 ? 42.067 -19.939 7.640  1.00 23.40  ? 129 ASN   C O   1 
ATOM   2040 C  CB  . ASN   B 1 123 ? 41.697 -17.204 7.341  1.00 31.05  ? 129 ASN   C CB  1 
ATOM   2041 C  CG  . ASN   B 1 123 ? 42.590 -16.229 6.572  1.00 38.80  ? 129 ASN   C CG  1 
ATOM   2042 O  OD1 . ASN   B 1 123 ? 42.534 -16.123 5.338  1.00 40.78  ? 129 ASN   C OD1 1 
ATOM   2043 N  ND2 . ASN   B 1 123 ? 43.423 -15.480 7.276  1.00 41.06  ? 129 ASN   C ND2 1 
ATOM   2044 N  N   . GLY   B 1 124 ? 40.214 -20.524 6.510  1.00 19.20  ? 130 GLY   C N   1 
ATOM   2045 C  CA  . GLY   B 1 124 ? 40.293 -21.931 6.922  1.00 17.95  ? 130 GLY   C CA  1 
ATOM   2046 C  C   . GLY   B 1 124 ? 39.874 -22.207 8.358  1.00 16.51  ? 130 GLY   C C   1 
ATOM   2047 O  O   . GLY   B 1 124 ? 40.116 -23.309 8.858  1.00 16.19  ? 130 GLY   C O   1 
ATOM   2048 N  N   . LEU   B 1 125 ? 39.215 -21.237 9.007  1.00 15.34  ? 131 LEU   C N   1 
ATOM   2049 C  CA  . LEU   B 1 125 ? 38.725 -21.373 10.365 1.00 14.24  ? 131 LEU   C CA  1 
ATOM   2050 C  C   . LEU   B 1 125 ? 37.217 -21.236 10.399 1.00 14.74  ? 131 LEU   C C   1 
ATOM   2051 O  O   . LEU   B 1 125 ? 36.601 -20.552 9.536  1.00 16.57  ? 131 LEU   C O   1 
ATOM   2052 C  CB  . LEU   B 1 125 ? 39.324 -20.301 11.278 1.00 16.83  ? 131 LEU   C CB  1 
ATOM   2053 C  CG  . LEU   B 1 125 ? 40.869 -20.333 11.319 1.00 19.42  ? 131 LEU   C CG  1 
ATOM   2054 C  CD1 . LEU   B 1 125 ? 41.447 -19.079 11.961 1.00 24.46  ? 131 LEU   C CD1 1 
ATOM   2055 C  CD2 . LEU   B 1 125 ? 41.355 -21.614 11.958 1.00 20.64  ? 131 LEU   C CD2 1 
ATOM   2056 N  N   . VAL   B 1 126 ? 36.611 -21.907 11.341 1.00 12.22  ? 132 VAL   C N   1 
ATOM   2057 C  CA  . VAL   B 1 126 ? 35.174 -21.779 11.582 1.00 11.69  ? 132 VAL   C CA  1 
ATOM   2058 C  C   . VAL   B 1 126 ? 35.032 -21.318 13.052 1.00 10.84  ? 132 VAL   C C   1 
ATOM   2059 O  O   . VAL   B 1 126 ? 35.697 -21.833 13.944 1.00 11.25  ? 132 VAL   C O   1 
ATOM   2060 C  CB  . VAL   B 1 126 ? 34.410 -23.127 11.345 1.00 11.31  ? 132 VAL   C CB  1 
ATOM   2061 C  CG1 . VAL   B 1 126 ? 35.030 -24.322 12.072 1.00 13.72  ? 132 VAL   C CG1 1 
ATOM   2062 C  CG2 . VAL   B 1 126 ? 32.919 -23.024 11.701 1.00 12.14  ? 132 VAL   C CG2 1 
ATOM   2063 N  N   . GLY   B 1 127 ? 34.186 -20.318 13.282 1.00 11.38  ? 133 GLY   C N   1 
ATOM   2064 C  CA  . GLY   B 1 127 ? 33.935 -19.797 14.635 1.00 10.76  ? 133 GLY   C CA  1 
ATOM   2065 C  C   . GLY   B 1 127 ? 32.508 -20.111 15.070 1.00 11.07  ? 133 GLY   C C   1 
ATOM   2066 O  O   . GLY   B 1 127 ? 31.543 -19.983 14.296 1.00 11.29  ? 133 GLY   C O   1 
ATOM   2067 N  N   . PHE   B 1 128 ? 32.404 -20.497 16.353 1.00 10.17  ? 134 PHE   C N   1 
ATOM   2068 C  CA  . PHE   B 1 128 ? 31.100 -20.867 16.966 1.00 10.25  ? 134 PHE   C CA  1 
ATOM   2069 C  C   . PHE   B 1 128 ? 30.778 -19.926 18.122 1.00 10.46  ? 134 PHE   C C   1 
ATOM   2070 O  O   . PHE   B 1 128 ? 31.634 -19.676 18.980 1.00 11.27  ? 134 PHE   C O   1 
ATOM   2071 C  CB  . PHE   B 1 128 ? 31.205 -22.303 17.580 1.00 10.53  ? 134 PHE   C CB  1 
ATOM   2072 C  CG  . PHE   B 1 128 ? 31.695 -23.312 16.562 1.00 10.67  ? 134 PHE   C CG  1 
ATOM   2073 C  CD1 . PHE   B 1 128 ? 30.818 -23.902 15.660 1.00 10.81  ? 134 PHE   C CD1 1 
ATOM   2074 C  CD2 . PHE   B 1 128 ? 33.032 -23.700 16.542 1.00 11.31  ? 134 PHE   C CD2 1 
ATOM   2075 C  CE1 . PHE   B 1 128 ? 31.282 -24.874 14.783 1.00 11.79  ? 134 PHE   C CE1 1 
ATOM   2076 C  CE2 . PHE   B 1 128 ? 33.498 -24.666 15.645 1.00 11.99  ? 134 PHE   C CE2 1 
ATOM   2077 C  CZ  . PHE   B 1 128 ? 32.626 -25.253 14.782 1.00 12.00  ? 134 PHE   C CZ  1 
ATOM   2078 N  N   . ALA   B 1 129 ? 29.529 -19.418 18.141 1.00 10.58  ? 135 ALA   C N   1 
ATOM   2079 C  CA  . ALA   B 1 129 ? 29.050 -18.632 19.268 1.00 10.63  ? 135 ALA   C CA  1 
ATOM   2080 C  C   . ALA   B 1 129 ? 28.656 -19.592 20.411 1.00 11.21  ? 135 ALA   C C   1 
ATOM   2081 O  O   . ALA   B 1 129 ? 27.764 -20.438 20.251 1.00 11.31  ? 135 ALA   C O   1 
ATOM   2082 C  CB  . ALA   B 1 129 ? 27.828 -17.810 18.818 1.00 12.02  ? 135 ALA   C CB  1 
ATOM   2083 N  N   . ASP   B 1 130 ? 29.370 -19.508 21.532 1.00 11.29  ? 136 ASP   C N   1 
ATOM   2084 C  CA  . ASP   B 1 130 ? 29.091 -20.385 22.674 1.00 11.41  ? 136 ASP   C CA  1 
ATOM   2085 C  C   . ASP   B 1 130 ? 27.751 -20.036 23.289 1.00 11.83  ? 136 ASP   C C   1 
ATOM   2086 O  O   . ASP   B 1 130 ? 27.365 -18.848 23.381 1.00 12.84  ? 136 ASP   C O   1 
ATOM   2087 C  CB  . ASP   B 1 130 ? 30.182 -20.174 23.744 1.00 12.60  ? 136 ASP   C CB  1 
ATOM   2088 C  CG  . ASP   B 1 130 ? 30.099 -21.103 24.942 1.00 15.56  ? 136 ASP   C CG  1 
ATOM   2089 O  OD1 . ASP   B 1 130 ? 29.905 -22.312 24.749 1.00 15.48  ? 136 ASP   C OD1 1 
ATOM   2090 O  OD2 . ASP   B 1 130 ? 30.121 -20.590 26.103 1.00 18.97  ? 136 ASP   C OD2 1 
ATOM   2091 N  N   . VAL   B 1 131 ? 27.051 -21.043 23.800 1.00 11.62  ? 137 VAL   C N   1 
ATOM   2092 C  CA  . VAL   B 1 131 ? 25.807 -20.845 24.586 1.00 12.07  ? 137 VAL   C CA  1 
ATOM   2093 C  C   . VAL   B 1 131 ? 25.898 -21.488 25.965 1.00 13.27  ? 137 VAL   C C   1 
ATOM   2094 O  O   . VAL   B 1 131 ? 24.912 -21.435 26.739 1.00 13.95  ? 137 VAL   C O   1 
ATOM   2095 C  CB  . VAL   B 1 131 ? 24.522 -21.290 23.858 1.00 12.87  ? 137 VAL   C CB  1 
ATOM   2096 C  CG1 . VAL   B 1 131 ? 24.359 -20.463 22.563 1.00 13.07  ? 137 VAL   C CG1 1 
ATOM   2097 C  CG2 . VAL   B 1 131 ? 24.561 -22.793 23.543 1.00 13.03  ? 137 VAL   C CG2 1 
ATOM   2098 N  N   . ARG   B 1 132 ? 27.000 -22.188 26.289 1.00 12.14  ? 138 ARG   C N   1 
ATOM   2099 C  CA  . ARG   B 1 132 ? 27.080 -22.978 27.548 1.00 12.11  ? 138 ARG   C CA  1 
ATOM   2100 C  C   . ARG   B 1 132 ? 27.035 -22.131 28.811 1.00 12.69  ? 138 ARG   C C   1 
ATOM   2101 O  O   . ARG   B 1 132 ? 26.732 -22.690 29.893 1.00 14.78  ? 138 ARG   C O   1 
ATOM   2102 C  CB  . ARG   B 1 132 ? 28.339 -23.836 27.552 1.00 12.18  ? 138 ARG   C CB  1 
ATOM   2103 C  CG  . ARG   B 1 132 ? 28.321 -24.877 26.416 1.00 12.00  ? 138 ARG   C CG  1 
ATOM   2104 C  CD  . ARG   B 1 132 ? 29.615 -25.655 26.450 1.00 11.98  ? 138 ARG   C CD  1 
ATOM   2105 N  NE  . ARG   B 1 132 ? 30.716 -24.778 26.030 1.00 11.84  ? 138 ARG   C NE  1 
ATOM   2106 C  CZ  . ARG   B 1 132 ? 31.963 -25.181 25.841 1.00 12.66  ? 138 ARG   C CZ  1 
ATOM   2107 N  NH1 . ARG   B 1 132 ? 32.334 -26.416 26.181 1.00 12.33  ? 138 ARG   C NH1 1 
ATOM   2108 N  NH2 . ARG   B 1 132 ? 32.870 -24.336 25.375 1.00 12.86  ? 138 ARG   C NH2 1 
ATOM   2109 N  N   . ASP   B 1 133 ? 27.364 -20.841 28.731 1.00 13.34  ? 139 ASP   C N   1 
ATOM   2110 C  CA  . ASP   B 1 133 ? 27.328 -19.970 29.914 1.00 13.87  ? 139 ASP   C CA  1 
ATOM   2111 C  C   . ASP   B 1 133 ? 25.915 -19.421 30.180 1.00 14.93  ? 139 ASP   C C   1 
ATOM   2112 O  O   . ASP   B 1 133 ? 25.720 -18.798 31.237 1.00 15.84  ? 139 ASP   C O   1 
ATOM   2113 C  CB  . ASP   B 1 133 ? 28.307 -18.792 29.747 1.00 15.29  ? 139 ASP   C CB  1 
ATOM   2114 C  CG  . ASP   B 1 133 ? 27.930 -17.873 28.606 1.00 17.57  ? 139 ASP   C CG  1 
ATOM   2115 O  OD1 . ASP   B 1 133 ? 27.624 -18.380 27.528 1.00 17.08  ? 139 ASP   C OD1 1 
ATOM   2116 O  OD2 . ASP   B 1 133 ? 27.884 -16.618 28.818 1.00 20.14  ? 139 ASP   C OD2 1 
ATOM   2117 N  N   . LEU   B 1 134 ? 24.964 -19.601 29.237 1.00 14.18  ? 140 LEU   C N   1 
ATOM   2118 C  CA  . LEU   B 1 134 ? 23.616 -19.027 29.356 1.00 14.06  ? 140 LEU   C CA  1 
ATOM   2119 C  C   . LEU   B 1 134 ? 22.732 -19.985 30.142 1.00 14.65  ? 140 LEU   C C   1 
ATOM   2120 O  O   . LEU   B 1 134 ? 21.902 -20.737 29.577 1.00 14.07  ? 140 LEU   C O   1 
ATOM   2121 C  CB  . LEU   B 1 134 ? 23.041 -18.803 27.953 1.00 13.41  ? 140 LEU   C CB  1 
ATOM   2122 C  CG  . LEU   B 1 134 ? 23.892 -17.829 27.072 1.00 14.86  ? 140 LEU   C CG  1 
ATOM   2123 C  CD1 . LEU   B 1 134 ? 23.298 -17.709 25.643 1.00 15.37  ? 140 LEU   C CD1 1 
ATOM   2124 C  CD2 . LEU   B 1 134 ? 24.034 -16.430 27.729 1.00 16.99  ? 140 LEU   C CD2 1 
ATOM   2125 N  N   . LEU   B 1 135 ? 22.948 -20.012 31.468 1.00 14.74  ? 141 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 135 ? 22.307 -21.048 32.301 1.00 15.72  ? 141 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 135 ? 20.797 -20.955 32.357 1.00 16.39  ? 141 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 135 ? 20.121 -21.968 32.541 1.00 17.45  ? 141 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 135 ? 22.889 -21.103 33.727 1.00 15.71  ? 141 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 135 ? 24.437 -21.098 33.809 1.00 16.31  ? 141 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 135 ? 24.911 -21.134 35.288 1.00 17.47  ? 141 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 135 ? 25.095 -22.246 32.992 1.00 17.33  ? 141 LEU   C CD2 1 
ATOM   2133 N  N   . TRP   B 1 136 ? 20.288 -19.734 32.160 1.00 16.94  ? 142 TRP   C N   1 
ATOM   2134 C  CA  . TRP   B 1 136 ? 18.848 -19.459 32.187 1.00 17.37  ? 142 TRP   C CA  1 
ATOM   2135 C  C   . TRP   B 1 136 ? 18.103 -20.157 31.047 1.00 17.24  ? 142 TRP   C C   1 
ATOM   2136 O  O   . TRP   B 1 136 ? 16.877 -20.260 31.115 1.00 18.61  ? 142 TRP   C O   1 
ATOM   2137 C  CB  . TRP   B 1 136 ? 18.574 -17.947 32.180 1.00 17.61  ? 142 TRP   C CB  1 
ATOM   2138 C  CG  . TRP   B 1 136 ? 19.259 -17.213 31.072 1.00 16.21  ? 142 TRP   C CG  1 
ATOM   2139 C  CD1 . TRP   B 1 136 ? 20.430 -16.510 31.155 1.00 17.74  ? 142 TRP   C CD1 1 
ATOM   2140 C  CD2 . TRP   B 1 136 ? 18.751 -16.999 29.736 1.00 16.83  ? 142 TRP   C CD2 1 
ATOM   2141 N  NE1 . TRP   B 1 136 ? 20.729 -15.934 29.919 1.00 18.17  ? 142 TRP   C NE1 1 
ATOM   2142 C  CE2 . TRP   B 1 136 ? 19.686 -16.188 29.049 1.00 17.56  ? 142 TRP   C CE2 1 
ATOM   2143 C  CE3 . TRP   B 1 136 ? 17.579 -17.394 29.082 1.00 17.39  ? 142 TRP   C CE3 1 
ATOM   2144 C  CZ2 . TRP   B 1 136 ? 19.486 -15.789 27.711 1.00 18.08  ? 142 TRP   C CZ2 1 
ATOM   2145 C  CZ3 . TRP   B 1 136 ? 17.361 -16.951 27.786 1.00 18.54  ? 142 TRP   C CZ3 1 
ATOM   2146 C  CH2 . TRP   B 1 136 ? 18.324 -16.203 27.107 1.00 18.10  ? 142 TRP   C CH2 1 
ATOM   2147 N  N   . LEU   B 1 137 ? 18.793 -20.630 29.996 1.00 16.57  ? 143 LEU   C N   1 
ATOM   2148 C  CA  . LEU   B 1 137 ? 18.100 -21.384 28.938 1.00 16.88  ? 143 LEU   C CA  1 
ATOM   2149 C  C   . LEU   B 1 137 ? 17.495 -22.682 29.503 1.00 19.12  ? 143 LEU   C C   1 
ATOM   2150 O  O   . LEU   B 1 137 ? 16.599 -23.237 28.894 1.00 20.89  ? 143 LEU   C O   1 
ATOM   2151 C  CB  . LEU   B 1 137 ? 19.052 -21.720 27.791 1.00 16.66  ? 143 LEU   C CB  1 
ATOM   2152 C  CG  . LEU   B 1 137 ? 19.478 -20.547 26.911 1.00 15.93  ? 143 LEU   C CG  1 
ATOM   2153 C  CD1 . LEU   B 1 137 ? 20.630 -20.971 25.975 1.00 16.77  ? 143 LEU   C CD1 1 
ATOM   2154 C  CD2 . LEU   B 1 137 ? 18.335 -20.021 26.057 1.00 16.86  ? 143 LEU   C CD2 1 
ATOM   2155 N  N   . ASP   B 1 138 ? 17.992 -23.168 30.664 1.00 17.79  ? 144 ASP   C N   1 
ATOM   2156 C  CA  . ASP   B 1 138 ? 17.518 -24.444 31.231 1.00 19.93  ? 144 ASP   C CA  1 
ATOM   2157 C  C   . ASP   B 1 138 ? 16.281 -24.291 32.111 1.00 22.93  ? 144 ASP   C C   1 
ATOM   2158 O  O   . ASP   B 1 138 ? 15.812 -25.309 32.624 1.00 24.55  ? 144 ASP   C O   1 
ATOM   2159 C  CB  . ASP   B 1 138 ? 18.617 -25.120 32.077 1.00 19.60  ? 144 ASP   C CB  1 
ATOM   2160 C  CG  . ASP   B 1 138 ? 19.846 -25.561 31.290 1.00 21.28  ? 144 ASP   C CG  1 
ATOM   2161 O  OD1 . ASP   B 1 138 ? 19.785 -25.587 30.039 1.00 20.98  ? 144 ASP   C OD1 1 
ATOM   2162 O  OD2 . ASP   B 1 138 ? 20.875 -25.890 31.930 1.00 23.15  ? 144 ASP   C OD2 1 
ATOM   2163 N  N   . GLU   B 1 139 ? 15.777 -23.070 32.317 1.00 24.90  ? 145 GLU   C N   1 
ATOM   2164 C  CA  . GLU   B 1 139 ? 14.645 -22.859 33.226 1.00 28.88  ? 145 GLU   C CA  1 
ATOM   2165 C  C   . GLU   B 1 139 ? 13.608 -21.882 32.648 1.00 32.70  ? 145 GLU   C C   1 
ATOM   2166 O  O   . GLU   B 1 139 ? 13.850 -21.268 31.621 1.00 32.96  ? 145 GLU   C O   1 
ATOM   2167 C  CB  . GLU   B 1 139 ? 15.226 -22.318 34.548 1.00 33.63  ? 145 GLU   C CB  1 
ATOM   2168 C  CG  . GLU   B 1 139 ? 15.956 -20.999 34.374 1.00 41.64  ? 145 GLU   C CG  1 
ATOM   2169 C  CD  . GLU   B 1 139 ? 16.899 -20.601 35.495 1.00 51.24  ? 145 GLU   C CD  1 
ATOM   2170 O  OE1 . GLU   B 1 139 ? 17.310 -19.416 35.534 1.00 52.49  ? 145 GLU   C OE1 1 
ATOM   2171 O  OE2 . GLU   B 1 139 ? 17.219 -21.471 36.338 1.00 53.23  ? 145 GLU   C OE2 1 
ATOM   2172 N  N   . GLU   B 1 140 ? 12.466 -21.704 33.353 1.00 36.05  ? 146 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 140 ? 11.366 -20.763 33.072 1.00 40.03  ? 146 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 140 ? 10.329 -21.356 32.140 1.00 43.89  ? 146 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 140 ? 9.140  -21.335 32.493 1.00 45.86  ? 146 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 140 ? 11.852 -19.383 32.607 1.00 42.08  ? 146 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 140 ? 10.814 -18.444 32.020 1.00 47.93  ? 146 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 140 ? 10.170 -17.524 33.042 1.00 54.67  ? 146 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 140 ? 10.581 -16.344 33.119 1.00 56.84  ? 146 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 140 ? 9.259  -17.984 33.768 1.00 56.60  ? 146 GLU   C OE2 1 
HETATM 2181 N  N1  . A1BO5 C 2 .   ? 8.967  16.274  21.290 1.00 24.81  ? 201 A1BO5 A N1  1 
HETATM 2182 C  C4  . A1BO5 C 2 .   ? 7.105  13.289  24.391 1.00 23.49  ? 201 A1BO5 A C4  1 
HETATM 2183 C  C5  . A1BO5 C 2 .   ? 8.056  13.471  23.391 1.00 23.89  ? 201 A1BO5 A C5  1 
HETATM 2184 C  C6  . A1BO5 C 2 .   ? 9.182  15.544  24.009 1.00 27.14  ? 201 A1BO5 A C6  1 
HETATM 2185 C  C7  . A1BO5 C 2 .   ? 9.364  16.996  23.601 1.00 27.80  ? 201 A1BO5 A C7  1 
HETATM 2186 C  C8  . A1BO5 C 2 .   ? 9.779  17.136  22.152 1.00 26.70  ? 201 A1BO5 A C8  1 
HETATM 2187 C  C10 . A1BO5 C 2 .   ? 10.268 16.309  19.211 1.00 20.01  ? 201 A1BO5 A C10 1 
HETATM 2188 C  C13 . A1BO5 C 2 .   ? 8.654  12.368  22.785 1.00 22.53  ? 201 A1BO5 A C13 1 
HETATM 2189 O  O1  . A1BO5 C 2 .   ? 7.499  14.615  20.937 1.00 22.94  ? 201 A1BO5 A O1  1 
HETATM 2190 C  C12 . A1BO5 C 2 .   ? 8.297  15.150  21.671 1.00 24.59  ? 201 A1BO5 A C12 1 
HETATM 2191 C  C9  . A1BO5 C 2 .   ? 8.957  16.650  19.873 1.00 22.28  ? 201 A1BO5 A C9  1 
HETATM 2192 C  C11 . A1BO5 C 2 .   ? 10.258 16.535  17.723 1.00 19.96  ? 201 A1BO5 A C11 1 
HETATM 2193 O  O   . A1BO5 C 2 .   ? 9.860  17.606  17.250 1.00 20.65  ? 201 A1BO5 A O   1 
HETATM 2194 N  N2  . A1BO5 C 2 .   ? 10.667 15.514  16.988 1.00 18.59  ? 201 A1BO5 A N2  1 
HETATM 2195 N  N   . A1BO5 C 2 .   ? 8.444  14.777  22.986 1.00 25.68  ? 201 A1BO5 A N   1 
HETATM 2196 C  C3  . A1BO5 C 2 .   ? 6.767  12.002  24.770 1.00 22.51  ? 201 A1BO5 A C3  1 
HETATM 2197 C  C2  . A1BO5 C 2 .   ? 7.341  10.912  24.130 1.00 21.48  ? 201 A1BO5 A C2  1 
HETATM 2198 C  C1  . A1BO5 C 2 .   ? 8.291  11.078  23.138 1.00 21.39  ? 201 A1BO5 A C1  1 
HETATM 2199 C  C   . A1BO5 C 2 .   ? 8.979  9.888   22.514 1.00 21.76  ? 201 A1BO5 A C   1 
HETATM 2200 ZN ZN  . ZN    D 3 .   ? 11.258 -4.144  5.882  1.00 18.89  2 202 ZN    A ZN  1 
HETATM 2201 S  S   . DMS   E 4 .   ? 19.187 -2.072  24.183 1.00 83.62  ? 203 DMS   A S   1 
HETATM 2202 O  O   . DMS   E 4 .   ? 18.265 -2.706  23.184 1.00 83.42  ? 203 DMS   A O   1 
HETATM 2203 C  C1  . DMS   E 4 .   ? 19.542 -3.292  25.474 1.00 83.64  ? 203 DMS   A C1  1 
HETATM 2204 C  C2  . DMS   E 4 .   ? 20.867 -2.093  23.492 1.00 83.65  ? 203 DMS   A C2  1 
HETATM 2205 ZN ZN  . ZN    F 3 .   ? 30.681 -31.236 26.760 1.00 13.30  2 201 ZN    C ZN  1 
HETATM 2206 S  S   . DMS   G 4 .   ? 20.917 -32.443 9.881  1.00 73.30  ? 202 DMS   C S   1 
HETATM 2207 O  O   . DMS   G 4 .   ? 21.569 -32.424 8.534  1.00 73.29  ? 202 DMS   C O   1 
HETATM 2208 C  C1  . DMS   G 4 .   ? 22.171 -32.545 11.181 1.00 73.30  ? 202 DMS   C C1  1 
HETATM 2209 C  C2  . DMS   G 4 .   ? 20.456 -30.723 10.238 1.00 73.21  ? 202 DMS   C C2  1 
HETATM 2210 S  S   . DMS   H 4 .   ? 27.341 -4.218  6.810  1.00 80.02  ? 203 DMS   C S   1 
HETATM 2211 O  O   . DMS   H 4 .   ? 27.309 -4.260  8.307  1.00 79.77  ? 203 DMS   C O   1 
HETATM 2212 C  C1  . DMS   H 4 .   ? 28.913 -3.471  6.297  1.00 80.07  ? 203 DMS   C C1  1 
HETATM 2213 C  C2  . DMS   H 4 .   ? 27.756 -5.879  6.229  1.00 80.05  ? 203 DMS   C C2  1 
HETATM 2214 O  O   . HOH   I 5 .   ? 21.718 -0.403  -0.294 1.00 31.73  ? 301 HOH   A O   1 
HETATM 2215 O  O   . HOH   I 5 .   ? 8.275  -2.797  31.835 1.00 28.08  ? 302 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 37.361 15.072  14.253 1.00 48.93  ? 303 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 35.339 -3.867  7.883  1.00 22.03  ? 304 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 5.742  18.978  20.619 1.00 32.36  ? 305 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? -0.356 15.919  8.386  1.00 40.41  ? 306 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 14.351 17.321  4.014  1.00 34.53  ? 307 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 14.038 2.822   1.182  1.00 26.52  ? 308 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? -0.094 16.058  14.951 1.00 40.88  ? 309 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 27.949 7.996   1.832  1.00 32.40  ? 310 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 2.973  9.439   8.725  1.00 25.88  ? 311 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 0.382  -0.892  19.346 1.00 25.69  ? 312 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 2.560  -2.920  20.651 1.00 28.74  ? 313 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 30.383 10.531  15.777 1.00 30.50  ? 314 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 21.214 19.810  18.268 1.00 37.05  ? 315 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 3.859  9.239   27.821 1.00 36.97  ? 316 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 7.671  -5.148  3.037  1.00 41.89  ? 317 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 4.659  -3.645  28.830 1.00 29.15  ? 318 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 33.826 14.133  9.825  1.00 33.61  ? 319 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 23.469 21.651  7.176  1.00 24.56  ? 320 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 12.829 -5.732  30.500 1.00 37.77  ? 321 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 8.819  19.886  18.702 1.00 24.50  ? 322 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 14.951 11.213  -0.010 1.00 28.64  ? 323 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 9.796  21.928  9.764  1.00 37.75  ? 324 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 28.176 3.223   5.080  1.00 30.21  ? 325 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 35.240 11.059  12.362 1.00 46.59  ? 326 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 21.877 2.314   -0.822 1.00 33.83  ? 327 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 19.202 10.143  19.603 1.00 13.51  ? 328 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 11.317 12.552  10.724 1.00 16.72  ? 329 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 22.557 0.924   17.453 1.00 16.76  ? 330 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 9.185  2.608   2.649  1.00 29.66  ? 331 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 18.421 21.884  9.397  1.00 19.07  ? 332 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 13.638 4.039   23.443 1.00 13.35  ? 333 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 12.030 15.273  1.458  1.00 48.65  ? 334 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 11.725 17.913  4.734  1.00 30.44  ? 335 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 7.654  21.139  16.382 1.00 25.74  ? 336 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 29.741 11.728  18.588 1.00 30.49  ? 337 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 0.981  8.127   5.980  1.00 42.05  ? 338 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 17.370 1.174   28.164 1.00 23.41  ? 339 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 13.615 15.228  26.204 1.00 40.00  ? 340 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? -0.148 1.290   15.739 1.00 13.26  ? 341 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 16.482 3.989   23.631 1.00 17.85  ? 342 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 31.494 20.051  11.882 1.00 23.08  ? 343 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 33.975 -2.239  13.597 1.00 34.73  ? 344 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 24.793 5.192   21.550 1.00 30.13  ? 345 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 33.704 11.060  15.676 1.00 40.90  ? 346 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 26.851 -1.206  8.961  1.00 25.65  ? 347 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 19.813 20.230  5.705  1.00 47.15  ? 348 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 20.962 -4.143  14.244 1.00 16.64  ? 349 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 3.730  -8.119  9.953  1.00 54.61  ? 350 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 36.811 2.404   10.355 1.00 39.97  ? 351 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 19.827 17.908  23.939 1.00 36.62  ? 352 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 20.825 -2.545  16.913 1.00 15.60  ? 353 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 21.621 5.170   24.753 1.00 42.07  ? 354 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 34.977 8.183   9.516  1.00 42.44  ? 355 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 29.202 12.023  21.422 1.00 34.59  ? 356 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 36.344 18.216  14.671 1.00 33.27  ? 357 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 28.900 3.402   12.804 1.00 16.65  ? 358 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 5.316  5.391   32.693 1.00 23.65  ? 359 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 13.702 13.842  23.836 1.00 20.99  ? 360 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 18.157 17.756  4.134  1.00 33.72  ? 361 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 10.328 10.134  31.377 1.00 22.18  ? 362 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 15.180 -4.955  0.427  1.00 44.50  ? 363 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 11.995 11.138  29.603 1.00 21.08  ? 364 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 13.247 11.343  9.021  1.00 13.91  ? 365 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 32.756 16.630  9.334  1.00 31.62  ? 366 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 11.624 -6.902  24.720 1.00 28.34  ? 367 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 6.648  -6.891  23.807 1.00 25.80  ? 368 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 22.581 19.605  19.883 1.00 30.56  ? 369 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 30.936 -2.176  15.844 1.00 46.02  ? 370 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 16.951 -3.437  27.774 1.00 33.11  ? 371 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 16.596 21.215  19.089 1.00 23.48  ? 372 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 24.180 -3.443  16.132 1.00 31.88  ? 373 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 1.193  5.091   27.036 1.00 28.32  ? 374 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 38.070 4.715   10.292 1.00 44.65  ? 375 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 4.893  7.998   2.226  1.00 32.99  ? 376 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 27.167 -1.335  15.957 1.00 26.51  ? 377 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 17.544 20.013  16.866 1.00 15.86  ? 378 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 19.323 3.059   19.400 1.00 18.49  ? 379 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 9.504  4.046   33.474 1.00 14.13  ? 380 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 3.234  0.179   28.937 1.00 34.77  ? 381 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 5.548  20.002  23.471 1.00 43.96  ? 382 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 30.422 4.584   5.943  1.00 21.98  ? 383 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 30.441 2.936   14.947 1.00 21.28  ? 384 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 3.099  7.679   24.333 1.00 23.63  ? 385 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 25.289 17.880  4.689  1.00 34.83  ? 386 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 32.291 2.098   6.205  1.00 35.12  ? 387 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 5.274  16.426  21.093 1.00 47.60  ? 388 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 22.906 -0.683  5.425  1.00 23.19  ? 389 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 36.252 -0.248  12.634 1.00 31.93  ? 390 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 6.137  2.352   5.400  1.00 21.70  ? 391 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 3.980  0.111   24.034 1.00 21.07  ? 392 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 4.139  -4.193  6.042  1.00 29.18  ? 393 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 30.375 15.848  23.019 1.00 27.70  ? 394 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 32.064 8.819   7.848  1.00 23.23  ? 395 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 16.422 9.457   -1.657 1.00 20.66  ? 396 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 27.724 17.651  24.270 1.00 26.25  ? 397 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 17.212 -5.478  12.271 1.00 38.62  ? 398 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 1.830  11.261  27.461 1.00 42.06  ? 399 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 30.215 -1.318  8.770  1.00 30.47  ? 400 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 6.007  27.962  18.003 1.00 34.50  ? 401 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 17.484 10.845  26.042 1.00 23.65  ? 402 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 29.174 15.893  4.513  1.00 33.08  ? 403 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 0.100  5.570   5.885  1.00 25.31  ? 404 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 16.930 6.338   27.045 1.00 28.37  ? 405 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 14.458 -2.413  17.951 1.00 18.21  ? 406 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 6.000  -3.664  31.491 1.00 29.53  ? 407 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 12.282 22.417  11.279 1.00 30.51  ? 408 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 15.161 14.929  3.049  1.00 28.87  ? 409 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 23.343 -6.651  12.000 1.00 28.61  ? 410 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 0.675  -0.740  8.973  1.00 31.73  ? 411 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 8.600  -6.471  9.810  1.00 31.64  ? 412 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 8.162  6.510   33.828 1.00 19.03  ? 413 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 23.573 3.693   -2.218 1.00 41.63  ? 414 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 34.594 16.819  20.257 1.00 46.23  ? 415 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 7.282  13.546  4.444  1.00 26.42  ? 416 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 15.258 24.359  17.260 1.00 38.61  ? 417 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 6.016  3.088   6.679  1.00 37.67  ? 418 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 16.818 -4.083  2.865  1.00 26.07  ? 419 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 17.753 24.325  10.406 1.00 40.66  ? 420 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 17.445 0.914   20.241 1.00 18.68  ? 421 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 19.895 13.255  2.147  1.00 32.22  ? 422 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 33.838 18.764  10.912 1.00 27.15  ? 423 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 7.329  -8.833  8.471  1.00 51.91  ? 424 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 23.346 19.121  6.360  1.00 20.27  ? 425 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 24.762 10.632  22.977 1.00 39.78  ? 426 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 36.578 15.986  16.812 1.00 38.49  ? 427 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 33.880 5.225   16.848 1.00 29.87  ? 428 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 0.491  -1.216  16.622 1.00 19.33  ? 429 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 1.198  -5.015  17.499 1.00 38.28  ? 430 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 35.886 15.343  11.176 1.00 46.30  ? 431 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 25.273 19.779  21.728 1.00 32.51  ? 432 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 3.314  -0.378  21.272 1.00 28.96  ? 433 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 22.602 3.534   20.875 1.00 21.63  ? 434 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 34.071 7.797   16.799 1.00 34.79  ? 435 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 19.365 -0.314  33.049 1.00 32.16  ? 436 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 20.833 10.058  21.871 1.00 17.82  ? 437 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 23.200 8.330   21.698 1.00 25.31  ? 438 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 15.618 21.564  7.488  1.00 34.70  ? 439 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 10.488 4.882   3.173  1.00 27.31  ? 440 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 17.161 -2.358  19.662 1.00 22.75  ? 441 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 19.830 9.246   -0.942 1.00 29.62  ? 442 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? 20.982 -4.794  11.536 1.00 29.84  ? 443 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 2.736  16.939  18.662 1.00 37.19  ? 444 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? 0.861  7.814   27.542 1.00 38.85  ? 445 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 19.051 -3.233  33.719 1.00 35.22  ? 446 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 12.028 10.700  -0.085 1.00 37.33  ? 447 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 2.723  -0.633  26.510 1.00 37.87  ? 448 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 35.246 4.523   19.089 1.00 43.04  ? 449 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 13.830 -6.486  25.711 1.00 44.57  ? 450 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 2.294  14.327  16.683 1.00 50.11  ? 451 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 31.852 6.944   5.626  1.00 30.40  ? 452 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 3.211  11.927  18.307 1.00 53.44  ? 453 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 15.789 13.198  26.003 1.00 37.09  ? 454 HOH   A O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 16.857 -4.870  34.297 1.00 32.25  ? 455 HOH   A O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 33.431 -4.195  5.845  1.00 41.32  ? 456 HOH   A O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 18.315 3.307   25.976 1.00 38.14  ? 457 HOH   A O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 29.713 0.732   16.674 1.00 34.79  ? 458 HOH   A O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 29.152 0.597   4.926  1.00 51.42  ? 459 HOH   A O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 23.627 1.126   19.887 1.00 28.71  ? 460 HOH   A O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? 18.501 2.083   22.856 1.00 36.92  ? 461 HOH   A O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 0.139  0.113   23.116 1.00 29.40  ? 462 HOH   A O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 30.177 7.138   17.995 1.00 31.36  ? 463 HOH   A O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 9.860  8.064   1.895  1.00 38.06  ? 464 HOH   A O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 1.513  4.398   -3.084 1.00 49.49  ? 465 HOH   A O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 21.152 3.073   23.196 1.00 36.37  ? 466 HOH   A O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 8.430  12.274  31.625 1.00 35.14  ? 467 HOH   A O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 3.465  8.743   30.441 1.00 59.71  ? 468 HOH   A O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 12.329 -4.996  33.148 1.00 30.28  ? 469 HOH   A O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 21.065 -0.882  19.057 1.00 27.76  ? 470 HOH   A O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 31.149 4.569   17.117 1.00 25.06  ? 471 HOH   A O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 35.418 9.175   18.852 1.00 52.34  ? 472 HOH   A O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 39.136 -2.284  10.877 1.00 39.48  ? 473 HOH   A O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 37.749 -4.618  6.722  1.00 28.11  ? 474 HOH   A O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 5.273  12.569  27.910 1.00 46.33  ? 475 HOH   A O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 28.812 1.528   19.127 1.00 50.92  ? 476 HOH   A O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 4.074  -6.833  23.401 1.00 44.57  ? 477 HOH   A O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 31.142 -24.012 -1.244 1.00 22.55  ? 301 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 26.610 -5.489  10.090 1.00 22.23  ? 302 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 23.465 -26.540 4.355  1.00 22.33  ? 303 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 17.665 -33.182 24.038 1.00 38.24  ? 304 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 22.671 -29.568 -3.139 1.00 27.61  ? 305 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 30.899 -18.233 26.882 1.00 18.84  ? 306 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 19.829 -4.175  20.263 1.00 22.67  ? 307 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 38.816 -18.695 21.480 1.00 28.22  ? 308 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 38.276 -7.424  6.919  1.00 20.05  ? 309 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 17.929 -27.522 16.634 1.00 17.63  ? 310 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 20.769 -18.790 12.915 1.00 14.37  ? 311 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 36.281 -2.496  11.130 1.00 30.33  ? 312 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 24.724 -5.882  15.285 1.00 27.72  ? 313 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 23.072 -5.980  21.208 1.00 19.03  ? 314 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 21.818 -26.290 34.379 1.00 24.99  ? 315 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 10.317 -17.547 18.500 1.00 27.24  ? 316 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 17.882 -6.067  24.077 1.00 27.65  ? 317 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 37.412 -18.828 28.070 1.00 24.87  ? 318 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 22.033 -28.787 4.801  1.00 26.09  ? 319 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 26.676 -15.279 30.809 1.00 28.44  ? 320 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 16.237 -15.996 8.974  1.00 39.83  ? 321 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 14.735 -23.760 12.390 1.00 34.90  ? 322 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 14.742 -28.741 25.577 1.00 35.69  ? 323 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 37.291 -32.000 10.935 1.00 23.20  ? 324 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 28.425 -5.351  18.696 1.00 40.13  ? 325 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 31.148 -21.571 28.409 1.00 17.30  ? 326 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 7.102  -9.343  22.789 1.00 39.38  ? 327 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 24.809 -15.785 7.389  1.00 19.59  ? 328 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 37.117 -10.494 4.780  1.00 38.19  ? 329 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 24.006 -8.120  9.624  1.00 21.52  ? 330 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 41.152 -10.591 22.896 1.00 40.86  ? 331 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 36.197 -26.363 34.302 1.00 35.67  ? 332 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 35.140 -32.783 3.325  1.00 33.24  ? 333 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 5.917  -16.429 22.660 1.00 57.65  ? 334 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 10.019 -8.942  23.985 1.00 31.37  ? 335 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 18.725 -8.795  13.930 1.00 28.04  ? 336 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 35.887 -28.646 2.893  1.00 44.30  ? 337 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 42.723 -11.638 10.900 1.00 28.57  ? 338 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 40.536 -27.367 15.150 1.00 12.88  ? 339 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 14.119 -24.318 29.450 1.00 31.38  ? 340 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 39.189 -33.745 13.606 1.00 47.22  ? 341 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 10.542 -16.872 15.316 1.00 34.69  ? 342 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 13.377 -11.185 28.544 1.00 38.81  ? 343 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 32.628 -23.798 29.153 1.00 16.98  ? 344 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 26.009 -25.325 8.824  1.00 13.63  ? 345 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 37.711 -23.727 4.065  1.00 40.25  ? 346 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 10.650 -16.835 12.695 1.00 33.23  ? 347 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 32.051 -10.496 13.772 1.00 18.25  ? 348 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 30.354 -10.700 27.908 1.00 43.31  ? 349 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 31.294 -6.174  5.869  1.00 36.50  ? 350 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 25.802 -37.899 24.377 1.00 33.04  ? 351 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 29.997 -15.326 19.586 1.00 15.95  ? 352 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 24.606 -9.712  27.112 1.00 40.17  ? 353 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 35.185 -13.198 8.712  1.00 19.94  ? 354 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 19.289 -27.709 28.270 1.00 18.80  ? 355 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 19.684 -32.118 19.820 1.00 45.10  ? 356 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 23.567 -33.588 29.100 1.00 29.87  ? 357 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 12.010 -24.266 21.821 1.00 18.64  ? 358 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 33.812 -33.973 23.838 1.00 35.40  ? 359 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 41.937 -24.853 7.346  1.00 35.05  ? 360 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 23.995 -3.406  19.036 1.00 43.41  ? 361 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 41.663 -12.815 13.101 1.00 38.79  ? 362 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 9.456  -8.162  21.621 1.00 27.82  ? 363 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 4.367  -10.287 19.974 1.00 31.97  ? 364 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 22.980 -8.552  14.108 1.00 15.81  ? 365 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 20.718 -25.716 13.932 1.00 21.57  ? 366 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 36.599 -16.275 12.248 1.00 29.11  ? 367 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 37.805 -31.465 25.820 1.00 26.37  ? 368 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 27.031 -35.645 20.807 1.00 28.15  ? 369 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 31.311 -12.217 10.688 1.00 15.70  ? 370 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 33.030 -9.866  11.135 1.00 15.20  ? 371 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 36.296 -21.377 6.801  1.00 23.33  ? 372 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 29.816 -13.146 12.967 1.00 15.92  ? 373 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 10.109 -24.818 19.988 1.00 22.66  ? 374 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 17.521 -24.195 8.700  1.00 43.47  ? 375 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 8.782  -13.328 10.985 1.00 26.70  ? 376 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 28.266 -16.422 22.102 1.00 14.17  ? 377 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 32.720 -17.305 5.430  1.00 36.00  ? 378 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 10.974 -6.459  13.303 1.00 24.52  ? 379 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 36.311 -32.486 24.991 1.00 34.00  ? 380 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 38.797 -14.738 13.346 1.00 29.82  ? 381 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 32.181 -34.729 24.782 1.00 29.82  ? 382 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 23.200 -25.441 9.013  1.00 20.55  ? 383 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 6.137  -18.550 25.099 1.00 48.40  ? 384 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 26.692 -6.064  21.986 1.00 30.00  ? 385 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 31.455 -13.521 4.399  1.00 33.39  ? 386 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 35.667 -24.739 24.683 1.00 17.71  ? 387 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 33.416 -33.047 0.855  1.00 45.47  ? 388 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 15.342 -30.146 18.194 1.00 36.70  ? 389 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 22.205 -23.794 6.162  1.00 37.39  ? 390 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 43.287 -25.695 23.566 1.00 22.46  ? 391 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 30.203 -15.930 30.451 1.00 32.08  ? 392 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 14.711 -18.278 10.536 1.00 35.91  ? 393 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 21.730 -18.956 6.018  1.00 28.17  ? 394 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 10.726 -11.981 9.204  1.00 29.46  ? 395 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 22.897 -28.160 12.668 1.00 22.57  ? 396 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 28.863 -36.438 7.914  1.00 20.90  ? 397 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 36.906 -29.370 10.149 1.00 21.36  ? 398 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 11.695 -22.587 28.835 1.00 27.66  ? 399 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 32.003 -34.845 31.865 1.00 34.35  ? 400 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 23.323 -28.279 1.535  1.00 31.66  ? 401 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 34.534 -13.537 25.511 1.00 20.20  ? 402 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 22.854 -33.515 5.481  1.00 30.95  ? 403 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 7.039  -17.142 18.713 1.00 47.58  ? 404 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 27.007 -12.036 27.652 1.00 27.32  ? 405 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 35.698 -28.703 7.771  1.00 19.48  ? 406 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 3.777  -8.366  14.806 1.00 28.77  ? 407 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 41.862 -12.422 17.943 1.00 24.66  ? 408 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 37.834 -20.516 4.753  1.00 37.89  ? 409 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 30.276 -18.172 8.425  1.00 26.00  ? 410 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 26.047 -31.055 30.918 1.00 18.46  ? 411 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 33.093 -30.451 31.691 1.00 19.81  ? 412 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 26.345 -31.355 14.898 1.00 20.62  ? 413 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 10.974 -21.555 13.893 1.00 44.31  ? 414 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 4.105  -12.849 17.514 1.00 42.41  ? 415 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 20.523 -23.719 34.913 1.00 28.75  ? 416 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 22.781 -13.776 29.976 1.00 33.50  ? 417 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? 35.397 -4.242  17.728 1.00 31.51  ? 418 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 39.904 -25.571 6.924  1.00 37.54  ? 419 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 34.805 -35.181 18.220 1.00 29.94  ? 420 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 31.104 -37.602 9.165  1.00 46.48  ? 421 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 39.038 -13.168 25.773 1.00 26.17  ? 422 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 10.089 -18.345 26.860 1.00 33.24  ? 423 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 9.788  -24.664 29.458 1.00 41.06  ? 424 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 4.859  -28.307 23.183 1.00 48.16  ? 425 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 18.726 -8.306  25.612 1.00 21.08  ? 426 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 16.406 -20.568 11.665 1.00 26.00  ? 427 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 17.193 -25.324 12.851 1.00 25.47  ? 428 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 40.004 -30.063 14.589 1.00 17.12  ? 429 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 32.819 -14.420 9.435  1.00 15.28  ? 430 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 20.486 -32.220 22.356 1.00 30.49  ? 431 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 37.837 -13.900 10.226 1.00 33.68  ? 432 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 34.204 -15.781 27.234 1.00 36.37  ? 433 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 23.592 -17.639 33.369 1.00 20.53  ? 434 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 18.812 -19.101 10.938 1.00 19.22  ? 435 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 36.675 -24.890 27.251 1.00 31.30  ? 436 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 35.160 -13.661 6.090  1.00 32.88  ? 437 HOH   C O   1 
HETATM 2528 O  O   . HOH   J 5 .   ? 34.787 -23.292 -0.942 1.00 35.72  ? 438 HOH   C O   1 
HETATM 2529 O  O   . HOH   J 5 .   ? 6.633  -22.975 18.328 1.00 32.36  ? 439 HOH   C O   1 
HETATM 2530 O  O   . HOH   J 5 .   ? 31.538 -15.788 7.194  1.00 28.94  ? 440 HOH   C O   1 
HETATM 2531 O  O   . HOH   J 5 .   ? 6.593  -20.043 18.266 1.00 33.52  ? 441 HOH   C O   1 
HETATM 2532 O  O   . HOH   J 5 .   ? 33.906 -36.229 8.837  1.00 46.08  ? 442 HOH   C O   1 
HETATM 2533 O  O   . HOH   J 5 .   ? 12.333 -29.001 18.812 1.00 59.43  ? 443 HOH   C O   1 
HETATM 2534 O  O   . HOH   J 5 .   ? 37.202 -31.127 28.870 1.00 41.09  ? 444 HOH   C O   1 
HETATM 2535 O  O   . HOH   J 5 .   ? 43.645 -25.593 26.128 1.00 36.03  ? 445 HOH   C O   1 
HETATM 2536 O  O   . HOH   J 5 .   ? 41.984 -31.625 15.648 1.00 30.81  ? 446 HOH   C O   1 
HETATM 2537 O  O   . HOH   J 5 .   ? 9.134  -12.795 25.397 1.00 48.74  ? 447 HOH   C O   1 
HETATM 2538 O  O   . HOH   J 5 .   ? 24.261 -16.575 3.276  1.00 43.60  ? 448 HOH   C O   1 
HETATM 2539 O  O   . HOH   J 5 .   ? 8.906  -19.013 17.124 1.00 35.03  ? 449 HOH   C O   1 
HETATM 2540 O  O   . HOH   J 5 .   ? 34.297 -31.959 29.544 1.00 24.49  ? 450 HOH   C O   1 
HETATM 2541 O  O   . HOH   J 5 .   ? 41.522 -13.945 9.763  1.00 40.41  ? 451 HOH   C O   1 
HETATM 2542 O  O   . HOH   J 5 .   ? 24.047 -15.620 31.641 1.00 31.48  ? 452 HOH   C O   1 
HETATM 2543 O  O   . HOH   J 5 .   ? 21.413 -17.482 34.791 1.00 25.77  ? 453 HOH   C O   1 
HETATM 2544 O  O   . HOH   J 5 .   ? 38.564 -25.996 5.137  1.00 44.25  ? 454 HOH   C O   1 
HETATM 2545 O  O   . HOH   J 5 .   ? 10.356 -20.053 29.076 1.00 33.88  ? 455 HOH   C O   1 
HETATM 2546 O  O   . HOH   J 5 .   ? 22.880 -16.774 5.417  1.00 43.13  ? 456 HOH   C O   1 
HETATM 2547 O  O   . HOH   J 5 .   ? 21.349 -24.990 4.161  1.00 41.33  ? 457 HOH   C O   1 
HETATM 2548 O  O   . HOH   J 5 .   ? 10.386 -27.059 18.446 1.00 41.01  ? 458 HOH   C O   1 
HETATM 2549 O  O   . HOH   J 5 .   ? 16.326 -27.606 14.330 1.00 34.26  ? 459 HOH   C O   1 
HETATM 2550 O  O   . HOH   J 5 .   ? 18.541 -26.006 10.399 1.00 38.23  ? 460 HOH   C O   1 
HETATM 2551 O  O   . HOH   J 5 .   ? 28.469 -12.662 30.461 1.00 45.01  ? 461 HOH   C O   1 
HETATM 2552 O  O   . HOH   J 5 .   ? 32.672 -19.421 29.059 1.00 30.60  ? 462 HOH   C O   1 
HETATM 2553 O  O   . HOH   J 5 .   ? 38.653 -13.808 5.801  1.00 47.26  ? 463 HOH   C O   1 
HETATM 2554 O  O   . HOH   J 5 .   ? 41.558 -15.443 13.381 1.00 34.77  ? 464 HOH   C O   1 
HETATM 2555 O  O   . HOH   J 5 .   ? 18.173 -17.945 8.569  1.00 34.35  ? 465 HOH   C O   1 
HETATM 2556 O  O   . HOH   J 5 .   ? 33.744 -19.487 0.610  1.00 235.05 ? 466 HOH   C O   1 
HETATM 2557 O  O   . HOH   J 5 .   ? 16.962 -28.830 28.949 1.00 38.69  ? 467 HOH   C O   1 
HETATM 2558 O  O   . HOH   J 5 .   ? 9.246  -23.411 17.913 1.00 32.92  ? 468 HOH   C O   1 
HETATM 2559 O  O   . HOH   J 5 .   ? 35.297 -23.124 28.959 1.00 29.45  ? 469 HOH   C O   1 
HETATM 2560 O  O   . HOH   J 5 .   ? 39.569 -11.180 4.942  1.00 41.21  ? 470 HOH   C O   1 
HETATM 2561 O  O   . HOH   J 5 .   ? 3.123  -8.742  21.919 1.00 43.82  ? 471 HOH   C O   1 
HETATM 2562 O  O   . HOH   J 5 .   ? 34.581 -10.754 26.434 1.00 42.52  ? 472 HOH   C O   1 
HETATM 2563 O  O   . HOH   J 5 .   ? 19.260 -17.603 6.092  1.00 41.37  ? 473 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   ? 0.2417 0.2101 0.2076 -0.0096 0.0079  -0.0172 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2352 0.2047 0.2072 -0.0086 0.0037  -0.0146 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2260 0.2000 0.2068 -0.0041 0.0005  -0.0093 7   SER   A C   
4    O O   . SER   A 1   ? 0.2311 0.2076 0.2119 -0.0030 0.0002  -0.0072 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2776 0.2495 0.2437 -0.0160 -0.0009 -0.0137 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3185 0.2966 0.2824 -0.0191 -0.0056 -0.0087 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1999 0.1748 0.1880 -0.0021 -0.0014 -0.0076 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1784 0.1566 0.1751 0.0013  -0.0032 -0.0038 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1718 0.1492 0.1749 0.0043  -0.0016 -0.0045 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1871 0.1615 0.1889 0.0050  0.0011  -0.0071 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1481 0.1281 0.1586 0.0056  -0.0028 -0.0021 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1479 0.1280 0.1639 0.0073  -0.0011 -0.0029 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1456 0.1273 0.1677 0.0090  0.0006  -0.0021 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1670 0.1494 0.1914 0.0092  -0.0001 -0.0002 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1756 0.1569 0.1951 0.0055  -0.0035 -0.0019 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1343 0.1163 0.1587 0.0095  0.0032  -0.0037 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1343 0.1172 0.1642 0.0096  0.0062  -0.0045 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1404 0.1247 0.1781 0.0096  0.0064  -0.0041 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1426 0.1276 0.1794 0.0088  0.0057  -0.0045 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1379 0.1217 0.1641 0.0084  0.0091  -0.0065 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1587 0.1428 0.1785 0.0086  0.0086  -0.0057 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1558 0.1397 0.1856 0.0068  0.0133  -0.0088 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1727 0.1599 0.1899 0.0068  0.0101  -0.0055 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1319 0.1165 0.1788 0.0104  0.0080  -0.0031 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1409 0.1276 0.1980 0.0107  0.0091  -0.0023 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1468 0.1322 0.2088 0.0104  0.0160  -0.0061 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1509 0.1342 0.2200 0.0115  0.0190  -0.0061 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1598 0.1487 0.2264 0.0119  0.0056  0.0033  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1488 0.1397 0.2089 0.0101  -0.0008 0.0064  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1520 0.1454 0.2119 0.0084  -0.0031 0.0069  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1688 0.1590 0.2218 0.0092  -0.0039 0.0080  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1742 0.1682 0.2262 0.0053  -0.0081 0.0083  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1778 0.1692 0.2228 0.0062  -0.0085 0.0094  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1858 0.1787 0.2299 0.0040  -0.0103 0.0090  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2209 0.2140 0.2558 -0.0004 -0.0140 0.0092  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1480 0.1343 0.2061 0.0082  0.0188  -0.0095 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1497 0.1353 0.2096 0.0058  0.0260  -0.0144 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1582 0.1467 0.2244 0.0050  0.0284  -0.0152 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1539 0.1450 0.2162 0.0043  0.0248  -0.0136 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1669 0.1530 0.2138 0.0018  0.0268  -0.0171 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1898 0.1788 0.2293 0.0011  0.0221  -0.0146 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1931 0.1792 0.2391 -0.0029 0.0343  -0.0227 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1806 0.1683 0.2582 0.0054  0.0349  -0.0175 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1735 0.1645 0.2586 0.0048  0.0381  -0.0183 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1611 0.1559 0.2515 0.0073  0.0312  -0.0121 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1628 0.1579 0.2587 0.0102  0.0264  -0.0070 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1547 0.1528 0.2411 0.0050  0.0298  -0.0122 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1485 0.1498 0.2371 0.0059  0.0230  -0.0071 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1519 0.1515 0.2263 0.0043  0.0175  -0.0066 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1612 0.1624 0.2339 0.0029  0.0140  -0.0048 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1716 0.1778 0.2694 0.0049  0.0253  -0.0066 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2145 0.2233 0.3311 0.0078  0.0294  -0.0046 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2566 0.2692 0.3834 0.0098  0.0246  0.0018  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1902 0.1972 0.3122 0.0076  0.0386  -0.0096 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1462 0.1423 0.2122 0.0047  0.0166  -0.0076 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1423 0.1364 0.1972 0.0040  0.0125  -0.0069 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1408 0.1323 0.1927 0.0059  0.0089  -0.0052 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1444 0.1352 0.1995 0.0074  0.0101  -0.0051 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1447 0.1386 0.1917 0.0018  0.0153  -0.0092 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1548 0.1521 0.2018 -0.0018 0.0188  -0.0106 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1768 0.1758 0.2247 -0.0029 0.0168  -0.0087 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1777 0.1765 0.2233 -0.0049 0.0243  -0.0142 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1892 0.1919 0.2365 -0.0068 0.0198  -0.0096 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1946 0.1974 0.2385 -0.0096 0.0278  -0.0158 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2014 0.2064 0.2463 -0.0104 0.0252  -0.0130 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2473 0.2570 0.2903 -0.0156 0.0284  -0.0139 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1432 0.1328 0.1888 0.0054  0.0050  -0.0041 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1412 0.1282 0.1813 0.0060  0.0023  -0.0034 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1456 0.1297 0.1780 0.0061  0.0032  -0.0047 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1505 0.1333 0.1815 0.0050  0.0030  -0.0047 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1523 0.1397 0.1924 0.0042  -0.0021 -0.0014 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1696 0.1539 0.2011 0.0030  -0.0043 -0.0018 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1711 0.1572 0.2015 -0.0010 -0.0087 0.0001  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1888 0.1699 0.2088 -0.0040 -0.0088 -0.0029 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2261 0.2057 0.2387 -0.0059 -0.0095 -0.0037 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2263 0.2093 0.2407 -0.0047 -0.0110 -0.0008 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2204 0.1947 0.2240 -0.0092 -0.0080 -0.0076 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1377 0.1210 0.1666 0.0072  0.0043  -0.0051 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1342 0.1162 0.1585 0.0077  0.0053  -0.0050 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1480 0.1267 0.1680 0.0085  0.0044  -0.0054 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1507 0.1298 0.1693 0.0089  0.0037  -0.0054 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1432 0.1280 0.1665 0.0074  0.0074  -0.0048 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1589 0.1447 0.1801 0.0076  0.0079  -0.0026 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1566 0.1446 0.1827 0.0051  0.0096  -0.0059 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1382 0.1134 0.1563 0.0084  0.0049  -0.0059 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1371 0.1082 0.1504 0.0083  0.0056  -0.0076 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1669 0.1380 0.1802 0.0082  0.0055  -0.0076 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1542 0.1226 0.1686 0.0101  0.0090  -0.0073 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1658 0.1354 0.1848 0.0111  0.0098  -0.0049 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1347 0.1027 0.1446 0.0050  0.0040  -0.0096 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2229 0.1913 0.2336 0.0049  0.0036  -0.0094 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1469 0.1192 0.1573 0.0032  0.0001  -0.0081 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2512 0.2157 0.2547 0.0025  0.0045  -0.0122 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1089 0.0744 0.1214 0.0038  0.0045  -0.0101 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2467 0.2198 0.2604 0.0034  0.0000  -0.0076 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1636 0.1285 0.1746 0.0105  0.0113  -0.0093 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1652 0.1266 0.1800 0.0127  0.0158  -0.0090 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1676 0.1229 0.1839 0.0112  0.0172  -0.0109 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1750 0.1269 0.1854 0.0074  0.0161  -0.0147 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1747 0.1326 0.1853 0.0126  0.0194  -0.0124 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1657 0.1290 0.1747 0.0137  0.0183  -0.0106 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.2002 0.1654 0.2033 0.0114  0.0153  -0.0116 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1841 0.1507 0.1994 0.0169  0.0203  -0.0070 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1559 0.1105 0.1802 0.0134  0.0192  -0.0075 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1693 0.1172 0.1959 0.0118  0.0208  -0.0090 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2039 0.1425 0.2258 0.0097  0.0255  -0.0155 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2125 0.1462 0.2299 0.0055  0.0252  -0.0193 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1711 0.1197 0.2087 0.0148  0.0228  -0.0030 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1865 0.1287 0.2281 0.0133  0.0240  -0.0030 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1849 0.1279 0.2395 0.0165  0.0262  0.0044  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2027 0.1406 0.2623 0.0150  0.0269  0.0058  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2369 0.1633 0.3009 0.0151  0.0326  0.0027  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2506 0.1692 0.3122 0.0157  0.0384  -0.0039 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2481 0.1702 0.3180 0.0138  0.0331  0.0051  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1909 0.1275 0.2129 0.0117  0.0301  -0.0171 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2214 0.1485 0.2385 0.0089  0.0363  -0.0244 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2476 0.1748 0.2506 0.0022  0.0333  -0.0298 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2709 0.1904 0.2670 -0.0026 0.0380  -0.0366 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2321 0.1573 0.2550 0.0128  0.0434  -0.0248 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2256 0.1573 0.2426 0.0130  0.0417  -0.0247 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2202 0.1615 0.2425 0.0169  0.0377  -0.0178 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2450 0.1745 0.2524 0.0095  0.0446  -0.0305 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2436 0.1881 0.2592 0.0159  0.0375  -0.0195 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2556 0.1937 0.2622 0.0116  0.0414  -0.0268 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2266 0.1625 0.2256 0.0014  0.0260  -0.0266 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2212 0.1595 0.2095 -0.0049 0.0217  -0.0289 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2391 0.1811 0.2278 -0.0077 0.0155  -0.0265 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2498 0.1963 0.2328 -0.0123 0.0106  -0.0259 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2283 0.1737 0.2138 -0.0038 0.0187  -0.0264 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2407 0.1838 0.2252 -0.0018 0.0245  -0.0286 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2379 0.1882 0.2193 -0.0015 0.0208  -0.0256 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2787 0.2141 0.2544 -0.0075 0.0307  -0.0362 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2243 0.1656 0.2212 -0.0048 0.0155  -0.0240 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2260 0.1711 0.2243 -0.0072 0.0104  -0.0217 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2335 0.1753 0.2242 -0.0149 0.0094  -0.0256 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2562 0.1891 0.2426 -0.0180 0.0145  -0.0310 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2154 0.1600 0.2227 -0.0038 0.0113  -0.0187 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2173 0.1663 0.2073 -0.0184 0.0032  -0.0227 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2356 0.1841 0.2186 -0.0271 0.0006  -0.0247 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2523 0.1983 0.2398 -0.0285 0.0005  -0.0247 24  THR   A C   
141  O O   . THR   A 18  ? 0.2320 0.1787 0.2286 -0.0228 0.0013  -0.0218 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2679 0.2274 0.2507 -0.0302 -0.0068 -0.0194 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2654 0.2317 0.2597 -0.0257 -0.0100 -0.0139 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2858 0.2485 0.2651 -0.0289 -0.0074 -0.0183 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2618 0.2063 0.2424 -0.0374 -0.0012 -0.0272 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2515 0.1948 0.2363 -0.0397 -0.0022 -0.0265 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2376 0.1921 0.2330 -0.0358 -0.0076 -0.0192 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2272 0.1811 0.2300 -0.0328 -0.0066 -0.0176 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2743 0.2159 0.2491 -0.0515 -0.0041 -0.0300 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3805 0.3235 0.3603 -0.0546 -0.0066 -0.0279 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4572 0.3898 0.4398 -0.0537 -0.0013 -0.0313 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4223 0.3768 0.4073 -0.0572 -0.0135 -0.0218 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4511 0.3885 0.4377 -0.0573 -0.0054 -0.0280 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4600 0.4110 0.4487 -0.0592 -0.0126 -0.0223 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2250 0.1897 0.2220 -0.0361 -0.0127 -0.0146 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2171 0.1915 0.2259 -0.0321 -0.0161 -0.0083 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1999 0.1728 0.2159 -0.0233 -0.0121 -0.0079 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2030 0.1796 0.2271 -0.0212 -0.0121 -0.0054 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2435 0.2283 0.2558 -0.0329 -0.0214 -0.0026 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3407 0.3347 0.3674 -0.0292 -0.0235 0.0033  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3839 0.3823 0.4155 -0.0327 -0.0258 0.0057  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3746 0.3708 0.4087 -0.0222 -0.0216 0.0052  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1916 0.1595 0.2040 -0.0193 -0.0085 -0.0103 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1770 0.1443 0.1948 -0.0128 -0.0052 -0.0095 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1687 0.1314 0.1891 -0.0126 -0.0025 -0.0100 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1779 0.1447 0.2046 -0.0103 -0.0023 -0.0073 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1865 0.1498 0.2001 -0.0095 -0.0022 -0.0114 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1957 0.1639 0.2082 -0.0085 -0.0043 -0.0100 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1899 0.1650 0.2090 -0.0071 -0.0067 -0.0065 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2028 0.1679 0.2088 -0.0092 -0.0031 -0.0122 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1817 0.1359 0.1975 -0.0158 -0.0003 -0.0135 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1854 0.1344 0.2051 -0.0158 0.0023  -0.0132 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1911 0.1448 0.2146 -0.0191 -0.0008 -0.0109 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1937 0.1474 0.2226 -0.0178 0.0004  -0.0084 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2003 0.1374 0.2149 -0.0189 0.0066  -0.0183 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2090 0.1405 0.2243 -0.0141 0.0117  -0.0196 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2267 0.1550 0.2356 -0.0146 0.0141  -0.0237 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2078 0.1377 0.2318 -0.0086 0.0149  -0.0158 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2193 0.1437 0.2332 -0.0092 0.0191  -0.0230 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2143 0.1403 0.2380 -0.0053 0.0192  -0.0175 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2241 0.1571 0.2562 -0.0066 0.0141  -0.0101 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2365 0.1614 0.2696 0.0001  0.0227  -0.0132 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2277 0.1603 0.2676 -0.0019 0.0169  -0.0056 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2300 0.1587 0.2712 0.0015  0.0210  -0.0067 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1808 0.1396 0.2021 -0.0237 -0.0049 -0.0108 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1912 0.1558 0.2175 -0.0271 -0.0079 -0.0081 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2016 0.1763 0.2368 -0.0228 -0.0089 -0.0038 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2144 0.1944 0.2556 -0.0245 -0.0100 -0.0014 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2154 0.1832 0.2371 -0.0343 -0.0123 -0.0085 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1802 0.1571 0.2165 -0.0177 -0.0075 -0.0034 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1868 0.1716 0.2308 -0.0141 -0.0067 -0.0009 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1728 0.1553 0.2154 -0.0101 -0.0031 -0.0015 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1724 0.1585 0.2169 -0.0072 -0.0018 -0.0014 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1855 0.1764 0.2331 -0.0133 -0.0092 0.0009  30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2310 0.2273 0.2825 -0.0180 -0.0134 0.0037  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2661 0.2686 0.3265 -0.0184 -0.0133 0.0062  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2407 0.2350 0.2851 -0.0227 -0.0169 0.0032  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1694 0.1463 0.2095 -0.0103 -0.0014 -0.0017 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1557 0.1311 0.1947 -0.0073 0.0011  -0.0009 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1754 0.1575 0.2176 -0.0071 0.0025  0.0013  31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1988 0.1840 0.2441 -0.0096 0.0026  0.0029  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1726 0.1400 0.2108 -0.0077 0.0026  -0.0004 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1767 0.1434 0.2162 -0.0046 0.0048  0.0024  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1670 0.1323 0.2032 -0.0016 0.0056  0.0003  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2130 0.1723 0.2560 -0.0046 0.0068  0.0043  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1602 0.1448 0.2009 -0.0050 0.0039  0.0014  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1639 0.1548 0.2052 -0.0065 0.0058  0.0029  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1745 0.1650 0.2143 -0.0065 0.0060  0.0069  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1867 0.1814 0.2275 -0.0095 0.0062  0.0106  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1559 0.1503 0.1967 -0.0056 0.0077  0.0003  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1844 0.1847 0.2233 -0.0087 0.0104  0.0008  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1793 0.1752 0.2253 -0.0052 0.0078  -0.0018 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1597 0.1465 0.1980 -0.0035 0.0059  0.0072  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1668 0.1547 0.2064 -0.0029 0.0061  0.0121  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1667 0.1481 0.2068 0.0010  0.0068  0.0113  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1657 0.1446 0.2022 0.0025  0.0068  0.0067  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1798 0.1761 0.2165 -0.0053 0.0064  0.0136  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1922 0.1921 0.2303 -0.0053 0.0058  0.0196  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2203 0.2257 0.2619 -0.0081 0.0045  0.0273  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1903 0.1906 0.2273 -0.0029 0.0060  0.0198  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2335 0.2431 0.2772 -0.0075 0.0037  0.0328  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2121 0.2185 0.2528 -0.0042 0.0048  0.0279  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1948 0.1914 0.2287 0.0000  0.0068  0.0147  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2210 0.2307 0.2623 -0.0029 0.0046  0.0306  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2042 0.2032 0.2377 0.0012  0.0068  0.0167  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2143 0.2197 0.2518 0.0000  0.0059  0.0244  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1803 0.1593 0.2255 0.0026  0.0076  0.0159  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1795 0.1527 0.2263 0.0063  0.0098  0.0149  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1905 0.1668 0.2452 0.0079  0.0105  0.0227  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1901 0.1694 0.2506 0.0063  0.0096  0.0291  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1926 0.1551 0.2392 0.0069  0.0119  0.0100  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2018 0.1597 0.2538 0.0054  0.0126  0.0124  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2121 0.1659 0.2746 0.0080  0.0158  0.0180  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2370 0.1904 0.3059 0.0066  0.0155  0.0230  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2251 0.1762 0.2910 0.0115  0.0189  0.0182  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1751 0.1509 0.2317 0.0111  0.0123  0.0231  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1728 0.1529 0.2398 0.0132  0.0131  0.0320  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1710 0.1447 0.2421 0.0178  0.0175  0.0298  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1716 0.1470 0.2371 0.0187  0.0177  0.0262  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1973 0.1905 0.2618 0.0099  0.0094  0.0375  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2380 0.2393 0.3133 0.0105  0.0086  0.0488  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2898 0.2868 0.3748 0.0154  0.0119  0.0511  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2915 0.3043 0.3653 0.0054  0.0048  0.0554  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1887 0.1541 0.2699 0.0207  0.0219  0.0311  36  SER   A N   
245  C CA  A SER   A 30  ? 0.1970 0.1551 0.2833 0.0249  0.0280  0.0281  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2011 0.1592 0.2867 0.0248  0.0279  0.0278  36  SER   A CA  
247  C C   . SER   A 30  ? 0.1941 0.1615 0.2882 0.0277  0.0280  0.0354  36  SER   A C   
248  O O   . SER   A 30  ? 0.2055 0.1710 0.2977 0.0299  0.0313  0.0312  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2204 0.1677 0.3187 0.0271  0.0339  0.0291  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2424 0.1884 0.3381 0.0268  0.0342  0.0269  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2581 0.1983 0.3636 0.0312  0.0414  0.0265  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.2915 0.2420 0.4018 0.0280  0.0332  0.0384  36  SER   A OG  
253  N N   . SER   A 31  ? 0.1880 0.1665 0.2903 0.0268  0.0240  0.0468  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1885 0.1781 0.2989 0.0283  0.0231  0.0554  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1871 0.1831 0.2842 0.0258  0.0200  0.0509  37  SER   A C   
256  O O   . SER   A 31  ? 0.2083 0.2098 0.3103 0.0278  0.0210  0.0544  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2170 0.2191 0.3379 0.0260  0.0184  0.0696  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2948 0.3065 0.4035 0.0192  0.0119  0.0706  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1708 0.1650 0.2526 0.0221  0.0173  0.0429  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1638 0.1620 0.2338 0.0198  0.0152  0.0379  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1654 0.1535 0.2270 0.0216  0.0181  0.0272  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1642 0.1544 0.2173 0.0203  0.0168  0.0233  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1734 0.1776 0.2339 0.0140  0.0106  0.0373  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1737 0.1905 0.2393 0.0099  0.0071  0.0480  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1736 0.1956 0.2286 0.0031  0.0041  0.0458  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1611 0.1847 0.2058 0.0006  0.0040  0.0395  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1790 0.2099 0.2156 -0.0063 0.0023  0.0390  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.2023 0.2411 0.2386 -0.0123 0.0002  0.0446  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1752 0.2055 0.2039 -0.0081 0.0032  0.0329  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1600 0.1371 0.2228 0.0234  0.0218  0.0222  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1535 0.1221 0.2067 0.0229  0.0237  0.0126  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1605 0.1312 0.2029 0.0193  0.0191  0.0087  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1674 0.1363 0.2018 0.0184  0.0186  0.0034  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1748 0.1424 0.2267 0.0249  0.0272  0.0098  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1824 0.1420 0.2239 0.0231  0.0291  0.0007  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2018 0.1532 0.2413 0.0215  0.0310  -0.0037 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1936 0.1554 0.2285 0.0224  0.0286  -0.0018 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1499 0.1241 0.1927 0.0170  0.0159  0.0113  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1438 0.1201 0.1790 0.0140  0.0127  0.0077  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1479 0.1203 0.1828 0.0121  0.0119  0.0058  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1564 0.1277 0.1972 0.0121  0.0126  0.0094  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1481 0.1337 0.1826 0.0115  0.0103  0.0115  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1528 0.1434 0.1850 0.0116  0.0102  0.0124  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1791 0.1780 0.2090 0.0073  0.0084  0.0149  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1679 0.1545 0.1941 0.0124  0.0104  0.0065  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1481 0.1196 0.1776 0.0104  0.0102  0.0014  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1462 0.1162 0.1758 0.0080  0.0088  0.0001  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1474 0.1219 0.1747 0.0066  0.0068  -0.0015 41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1507 0.1257 0.1751 0.0072  0.0062  -0.0033 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1624 0.1244 0.1898 0.0070  0.0099  -0.0037 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1592 0.1196 0.1867 0.0038  0.0082  -0.0049 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1760 0.1274 0.2031 0.0022  0.0107  -0.0074 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1657 0.1293 0.1896 0.0016  0.0050  -0.0069 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1457 0.1235 0.1754 0.0045  0.0060  -0.0006 42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1388 0.1207 0.1692 0.0034  0.0054  -0.0021 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1361 0.1177 0.1692 0.0016  0.0041  -0.0026 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1485 0.1295 0.1831 0.0001  0.0042  -0.0012 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1329 0.1207 0.1640 0.0018  0.0071  -0.0010 42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1581 0.1486 0.1918 0.0009  0.0084  -0.0035 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1512 0.1405 0.1793 0.0026  0.0078  0.0001  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1395 0.1218 0.1738 0.0014  0.0025  -0.0037 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1394 0.1234 0.1776 -0.0008 0.0007  -0.0033 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1419 0.1317 0.1873 -0.0003 0.0015  -0.0026 43  SER   A C   
304  O O   . SER   A 37  ? 0.1456 0.1366 0.1923 0.0016  0.0035  -0.0033 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1667 0.1477 0.2015 -0.0026 -0.0024 -0.0038 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1721 0.1543 0.2056 -0.0015 -0.0036 -0.0035 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1550 0.1482 0.2063 -0.0020 0.0008  -0.0015 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1665 0.1653 0.2277 -0.0012 0.0027  -0.0006 44  SER   A CA  
309  C C   . SER   A 38  ? 0.1886 0.1901 0.2560 -0.0006 -0.0006 0.0024  44  SER   A C   
310  O O   . SER   A 38  ? 0.2174 0.2182 0.2808 -0.0029 -0.0053 0.0040  44  SER   A O   
311  C CB  . SER   A 38  ? 0.2071 0.2097 0.2734 -0.0034 0.0041  -0.0002 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2240 0.2267 0.2903 -0.0060 -0.0002 0.0019  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1788 0.1836 0.2561 0.0018  0.0020  0.0034  45  THR   A N   
314  C CA  . THR   A 39  ? 0.1925 0.2010 0.2786 0.0027  -0.0012 0.0083  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2101 0.2253 0.3134 0.0038  0.0013  0.0115  45  THR   A C   
316  O O   . THR   A 39  ? 0.2097 0.2249 0.3179 0.0049  0.0077  0.0081  45  THR   A O   
317  C CB  . THR   A 39  ? 0.1983 0.2041 0.2839 0.0055  0.0001  0.0081  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2234 0.2279 0.3151 0.0078  0.0071  0.0049  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.1983 0.1982 0.2684 0.0048  -0.0014 0.0050  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2225 0.2438 0.3354 0.0033  -0.0036 0.0183  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2371 0.2657 0.3701 0.0051  -0.0011 0.0228  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2360 0.2630 0.3811 0.0099  0.0046  0.0233  46  THR   A C   
323  O O   . THR   A 40  ? 0.2693 0.2969 0.4270 0.0124  0.0124  0.0212  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2802 0.3177 0.4204 0.0019  -0.0091 0.0315  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3487 0.3869 0.4863 0.0011  -0.0145 0.0362  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2901 0.3275 0.4176 -0.0037 -0.0136 0.0299  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2206 0.2449 0.3614 0.0107  0.0015  0.0253  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2388 0.2605 0.3910 0.0149  0.0066  0.0260  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2298 0.2424 0.3703 0.0157  0.0133  0.0167  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2374 0.2462 0.3594 0.0133  0.0111  0.0122  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2754 0.2995 0.4293 0.0147  -0.0003 0.0337  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2065 0.2157 0.3580 0.0185  0.0217  0.0140  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2145 0.2159 0.3549 0.0178  0.0281  0.0055  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2121 0.2097 0.3454 0.0183  0.0244  0.0072  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2306 0.2299 0.3754 0.0206  0.0216  0.0141  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2494 0.2477 0.4035 0.0192  0.0396  0.0008  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3231 0.3242 0.4785 0.0171  0.0451  -0.0038 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.3880 0.3855 0.5563 0.0176  0.0581  -0.0098 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.3852 0.3835 0.5754 0.0217  0.0623  -0.0058 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4069 0.4006 0.5620 0.0129  0.0649  -0.0193 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1733 0.1665 0.2886 0.0161  0.0242  0.0017  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1682 0.1579 0.2759 0.0163  0.0215  0.0025  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1702 0.1539 0.2805 0.0166  0.0290  -0.0020 49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1824 0.1636 0.2972 0.0156  0.0375  -0.0078 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1622 0.1433 0.2679 0.0169  0.0261  0.0000  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1772 0.1521 0.2861 0.0169  0.0326  -0.0035 50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1829 0.1546 0.2748 0.0135  0.0333  -0.0088 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1908 0.1571 0.2838 0.0122  0.0389  -0.0124 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1820 0.1562 0.3040 0.0199  0.0305  0.0040  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2224 0.2011 0.3709 0.0240  0.0315  0.0119  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1604 0.1353 0.2378 0.0118  0.0280  -0.0091 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1626 0.1362 0.2257 0.0086  0.0282  -0.0127 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1793 0.1525 0.2376 0.0043  0.0345  -0.0194 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2003 0.1755 0.2615 0.0036  0.0367  -0.0210 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1606 0.1379 0.2130 0.0088  0.0211  -0.0099 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1834 0.1613 0.2366 0.0111  0.0154  -0.0044 51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1829 0.1586 0.2399 0.0117  0.0158  -0.0025 51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1821 0.1627 0.2315 0.0114  0.0106  -0.0022 51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.1963 0.1675 0.2466 0.0003  0.0374  -0.0230 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2142 0.1862 0.2567 -0.0062 0.0428  -0.0292 52  THR   A CA  
361  C C   . THR   A 46  ? 0.1930 0.1701 0.2217 -0.0096 0.0379  -0.0274 52  THR   A C   
362  O O   . THR   A 46  ? 0.2113 0.1884 0.2371 -0.0078 0.0338  -0.0242 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2984 0.2641 0.3432 -0.0099 0.0512  -0.0351 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3485 0.3095 0.4094 -0.0065 0.0574  -0.0366 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3578 0.3250 0.3905 -0.0191 0.0563  -0.0417 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1908 0.1732 0.2121 -0.0141 0.0379  -0.0283 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1781 0.1666 0.1895 -0.0169 0.0330  -0.0247 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1811 0.1711 0.1839 -0.0252 0.0363  -0.0281 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2001 0.1892 0.1999 -0.0319 0.0428  -0.0342 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1786 0.1729 0.1877 -0.0183 0.0306  -0.0222 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1888 0.1812 0.2059 -0.0117 0.0281  -0.0199 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1853 0.1864 0.1879 -0.0200 0.0253  -0.0164 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2007 0.1910 0.2200 -0.0054 0.0227  -0.0156 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1665 0.1593 0.1647 -0.0257 0.0325  -0.0246 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1796 0.1759 0.1687 -0.0343 0.0340  -0.0262 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1868 0.1926 0.1682 -0.0421 0.0328  -0.0243 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1792 0.1907 0.1622 -0.0392 0.0278  -0.0180 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1673 0.1662 0.1550 -0.0322 0.0292  -0.0211 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2050 0.2125 0.1775 -0.0530 0.0376  -0.0296 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2185 0.2368 0.1819 -0.0629 0.0360  -0.0271 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2554 0.2791 0.2088 -0.0730 0.0356  -0.0270 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2759 0.2973 0.2209 -0.0833 0.0421  -0.0350 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2157 0.2320 0.1762 -0.0687 0.0429  -0.0343 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2220 0.2326 0.1937 -0.0587 0.0439  -0.0348 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2123 0.2298 0.1876 -0.0535 0.0361  -0.0255 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2032 0.2156 0.1878 -0.0458 0.0372  -0.0266 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2219 0.2356 0.2123 -0.0387 0.0315  -0.0202 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2257 0.2454 0.2148 -0.0378 0.0252  -0.0123 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2459 0.2552 0.2442 -0.0329 0.0326  -0.0215 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2454 0.2758 0.2004 -0.0703 0.0287  -0.0184 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2558 0.2908 0.2041 -0.0777 0.0275  -0.0173 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2592 0.3069 0.2102 -0.0763 0.0191  -0.0050 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2652 0.3165 0.2240 -0.0691 0.0148  0.0021  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2389 0.2620 0.1918 -0.0716 0.0309  -0.0226 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2295 0.2500 0.1949 -0.0558 0.0252  -0.0154 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2898 0.3432 0.2359 -0.0830 0.0172  -0.0027 57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3102 0.3763 0.2608 -0.0819 0.0100  0.0093  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.2920 0.3537 0.2484 -0.0744 0.0093  0.0102  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3057 0.3780 0.2635 -0.0772 0.0051  0.0180  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.3865 0.4680 0.3272 -0.0976 0.0069  0.0144  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5442 0.6229 0.4725 -0.1096 0.0111  0.0060  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5788 0.6427 0.5071 -0.1054 0.0172  -0.0039 57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.6094 0.7011 0.5280 -0.1240 0.0084  0.0099  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2615 0.3089 0.2214 -0.0661 0.0134  0.0028  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2441 0.2878 0.2085 -0.0599 0.0128  0.0039  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2399 0.2911 0.2137 -0.0518 0.0077  0.0139  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2417 0.2936 0.2220 -0.0453 0.0063  0.0174  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2520 0.2803 0.2196 -0.0526 0.0173  -0.0040 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2594 0.2765 0.2199 -0.0610 0.0253  -0.0159 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2075 0.2635 0.1829 -0.0521 0.0059  0.0179  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.1971 0.2581 0.1827 -0.0436 0.0033  0.0257  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1786 0.2316 0.1657 -0.0378 0.0051  0.0225  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.1811 0.2386 0.1749 -0.0329 0.0040  0.0278  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2411 0.3189 0.2307 -0.0485 -0.0010 0.0366  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.3008 0.3884 0.2943 -0.0508 -0.0041 0.0440  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.3622 0.4675 0.3637 -0.0541 -0.0087 0.0571  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3975 0.5153 0.3937 -0.0657 -0.0122 0.0622  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.3084 0.4161 0.3234 -0.0447 -0.0087 0.0634  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.1663 0.2082 0.1479 -0.0392 0.0083  0.0142  60  THR   A N   
420  C CA  . THR   A 54  ? 0.1658 0.1993 0.1488 -0.0339 0.0098  0.0115  60  THR   A CA  
421  C C   . THR   A 54  ? 0.1751 0.1960 0.1588 -0.0293 0.0126  0.0049  60  THR   A C   
422  O O   . THR   A 54  ? 0.1914 0.2085 0.1724 -0.0328 0.0148  0.0004  60  THR   A O   
423  C CB  . THR   A 54  ? 0.2119 0.2455 0.1904 -0.0402 0.0106  0.0102  60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.2775 0.3049 0.2495 -0.0476 0.0138  0.0034  60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.2093 0.2566 0.1877 -0.0455 0.0076  0.0172  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.1557 0.1711 0.1433 -0.0220 0.0124  0.0051  61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.1630 0.1684 0.1528 -0.0178 0.0140  0.0008  61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.1437 0.1456 0.1361 -0.0120 0.0130  0.0024  61  GLY   A C   
429  O O   . GLY   A 55  ? 0.1593 0.1647 0.1509 -0.0122 0.0122  0.0052  61  GLY   A O   
430  N N   . VAL   A 56  ? 0.1441 0.1400 0.1395 -0.0076 0.0129  0.0009  62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.1334 0.1266 0.1299 -0.0038 0.0115  0.0026  62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.1342 0.1266 0.1323 0.0004  0.0104  0.0025  62  VAL   A C   
433  O O   . VAL   A 56  ? 0.1446 0.1348 0.1449 0.0008  0.0109  0.0005  62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.1525 0.1387 0.1520 -0.0046 0.0123  0.0016  62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.1986 0.1833 0.1995 -0.0017 0.0099  0.0046  62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.1700 0.1557 0.1677 -0.0094 0.0140  0.0012  62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1314 0.1253 0.1281 0.0028  0.0095  0.0041  63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1284 0.1204 0.1255 0.0056  0.0089  0.0032  63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.1518 0.1416 0.1467 0.0057  0.0073  0.0040  63  TYR   A C   
440  O O   . TYR   A 57  ? 0.1533 0.1443 0.1456 0.0043  0.0071  0.0056  63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.1392 0.1347 0.1367 0.0075  0.0104  0.0036  63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.1468 0.1441 0.1424 0.0084  0.0121  0.0043  63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.1632 0.1654 0.1590 0.0073  0.0130  0.0066  63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.1530 0.1476 0.1466 0.0096  0.0134  0.0024  63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.1765 0.1809 0.1715 0.0081  0.0155  0.0071  63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.1630 0.1589 0.1546 0.0097  0.0165  0.0019  63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.1756 0.1765 0.1684 0.0093  0.0177  0.0044  63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.2050 0.2079 0.1966 0.0094  0.0215  0.0039  63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.1371 0.1245 0.1324 0.0065  0.0059  0.0032  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.1434 0.1303 0.1354 0.0050  0.0038  0.0045  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.1491 0.1364 0.1352 0.0046  0.0057  0.0022  64  TYR   A C   
452  O O   . TYR   A 58  ? 0.1511 0.1371 0.1380 0.0061  0.0073  -0.0003 64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.1584 0.1435 0.1544 0.0049  0.0009  0.0056  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.1564 0.1430 0.1487 0.0018  -0.0024 0.0085  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.1553 0.1435 0.1476 -0.0002 -0.0043 0.0127  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.1751 0.1620 0.1636 -0.0002 -0.0039 0.0075  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.1784 0.1696 0.1664 -0.0044 -0.0079 0.0164  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.1783 0.1678 0.1614 -0.0050 -0.0072 0.0103  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.1845 0.1768 0.1677 -0.0071 -0.0096 0.0154  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2202 0.2167 0.1973 -0.0132 -0.0136 0.0193  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.1431 0.1320 0.1238 0.0022  0.0058  0.0030  65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.1590 0.1479 0.1332 0.0007  0.0091  -0.0001 65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.1660 0.1550 0.1330 -0.0045 0.0063  0.0004  65  CYS   A C   
464  O O   . CYS   A 59  ? 0.1690 0.1609 0.1322 -0.0080 0.0040  0.0036  65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.1546 0.1467 0.1277 0.0008  0.0124  0.0003  65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.1833 0.1748 0.1492 -0.0015 0.0186  -0.0045 65  CYS   A SG  
467  N N   . SER   A 60  ? 0.1720 0.1585 0.1367 -0.0059 0.0061  -0.0023 66  SER   A N   
468  C CA  . SER   A 60  ? 0.1846 0.1727 0.1419 -0.0124 0.0024  -0.0012 66  SER   A CA  
469  C C   . SER   A 60  ? 0.1944 0.1839 0.1403 -0.0183 0.0053  -0.0037 66  SER   A C   
470  O O   . SER   A 60  ? 0.2082 0.2018 0.1477 -0.0246 0.0011  0.0000  66  SER   A O   
471  C CB  . SER   A 60  ? 0.2147 0.2000 0.1715 -0.0136 0.0018  -0.0039 66  SER   A CB  
472  O OG  . SER   A 60  ? 0.2366 0.2172 0.1895 -0.0135 0.0081  -0.0108 66  SER   A OG  
473  N N   . SER   A 61  ? 0.1791 0.1661 0.1235 -0.0163 0.0128  -0.0091 67  SER   A N   
474  C CA  . SER   A 61  ? 0.1833 0.1713 0.1174 -0.0218 0.0174  -0.0127 67  SER   A CA  
475  C C   . SER   A 61  ? 0.1853 0.1787 0.1179 -0.0232 0.0157  -0.0080 67  SER   A C   
476  O O   . SER   A 61  ? 0.1969 0.1922 0.1206 -0.0284 0.0192  -0.0103 67  SER   A O   
477  C CB  . SER   A 61  ? 0.2037 0.1868 0.1399 -0.0184 0.0271  -0.0197 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.2073 0.1920 0.1544 -0.0110 0.0293  -0.0174 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.1814 0.1769 0.1226 -0.0191 0.0108  -0.0018 68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.1790 0.1790 0.1199 -0.0208 0.0080  0.0037  68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.1959 0.1978 0.1415 -0.0219 0.0001  0.0113  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.2151 0.2199 0.1620 -0.0233 -0.0026 0.0169  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.1957 0.1961 0.1442 -0.0150 0.0114  0.0038  68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.1952 0.1953 0.1424 -0.0135 0.0196  -0.0018 68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.1982 0.2021 0.1366 -0.0191 0.0221  -0.0021 68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2282 0.2321 0.1672 -0.0175 0.0313  -0.0075 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.2203 0.2207 0.1538 -0.0199 0.0379  -0.0144 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.2362 0.2334 0.1613 -0.0250 0.0356  -0.0169 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.2333 0.2335 0.1701 -0.0179 0.0474  -0.0188 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.1989 0.1988 0.1492 -0.0204 -0.0032 0.0121  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.2206 0.2218 0.1800 -0.0197 -0.0095 0.0195  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.2292 0.2289 0.1976 -0.0152 -0.0088 0.0222  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.2465 0.2478 0.2200 -0.0164 -0.0125 0.0291  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.2649 0.2719 0.2199 -0.0271 -0.0153 0.0267  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.2792 0.2883 0.2285 -0.0322 -0.0180 0.0262  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.2689 0.2856 0.2185 -0.0391 -0.0259 0.0367  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.2854 0.3055 0.2250 -0.0468 -0.0282 0.0354  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.2383 0.2625 0.1618 -0.0566 -0.0279 0.0336  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.2661 0.2923 0.1827 -0.0595 -0.0258 0.0339  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.2854 0.3118 0.1990 -0.0645 -0.0294 0.0311  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.1977 0.1944 0.1686 -0.0105 -0.0042 0.0172  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.2017 0.1973 0.1786 -0.0079 -0.0030 0.0186  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.1917 0.1845 0.1740 -0.0035 -0.0003 0.0147  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.1893 0.1817 0.1698 -0.0017 0.0021  0.0105  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.2351 0.2338 0.2057 -0.0098 -0.0002 0.0179  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.3509 0.3528 0.3179 -0.0147 -0.0033 0.0235  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.4646 0.4696 0.4267 -0.0163 -0.0001 0.0229  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.5555 0.5644 0.5127 -0.0221 -0.0033 0.0287  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.6077 0.6195 0.5552 -0.0274 -0.0046 0.0283  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.1793 0.1700 0.1682 -0.0024 -0.0001 0.0161  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.1676 0.1566 0.1602 -0.0001 0.0026  0.0126  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.1880 0.1796 0.1781 -0.0012 0.0049  0.0122  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.2330 0.2248 0.2230 -0.0034 0.0043  0.0149  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.1649 0.1495 0.1657 0.0004  0.0025  0.0133  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.1769 0.1600 0.1828 0.0019  0.0005  0.0143  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2113 0.1929 0.2201 0.0038  0.0020  0.0109  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.1792 0.1631 0.1880 0.0010  -0.0031 0.0193  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.1990 0.1803 0.2132 0.0044  -0.0005 0.0136  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.2175 0.2006 0.2322 0.0027  -0.0038 0.0190  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.1585 0.1530 0.1477 0.0001  0.0072  0.0099  72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.1633 0.1626 0.1514 -0.0012 0.0089  0.0107  72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.1489 0.1495 0.1396 -0.0022 0.0098  0.0098  72  TYR   A C   
523  O O   . TYR   A 66  ? 0.1522 0.1528 0.1447 -0.0007 0.0101  0.0083  72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.1742 0.1779 0.1608 0.0007  0.0113  0.0103  72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.1751 0.1787 0.1568 -0.0002 0.0118  0.0103  72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.1983 0.2046 0.1770 -0.0029 0.0118  0.0126  72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.1799 0.1811 0.1589 0.0007  0.0125  0.0078  72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.2159 0.2231 0.1886 -0.0050 0.0126  0.0124  72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.1949 0.1966 0.1673 -0.0019 0.0135  0.0070  72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2103 0.2153 0.1793 -0.0048 0.0136  0.0094  72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.2535 0.2597 0.2146 -0.0087 0.0146  0.0086  72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.1583 0.1606 0.1485 -0.0058 0.0102  0.0108  73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.1610 0.1667 0.1516 -0.0088 0.0109  0.0102  73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.1655 0.1801 0.1576 -0.0077 0.0112  0.0129  73  PRO   A C   
535  O O   . PRO   A 67  ? 0.1946 0.2136 0.1873 -0.0065 0.0118  0.0154  73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.1908 0.1959 0.1797 -0.0140 0.0114  0.0105  73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.2140 0.2188 0.2021 -0.0128 0.0106  0.0131  73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.1791 0.1812 0.1677 -0.0082 0.0098  0.0130  73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.1531 0.1708 0.1467 -0.0086 0.0110  0.0131  74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.1739 0.2010 0.1721 -0.0072 0.0110  0.0175  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.1573 0.1911 0.1554 -0.0126 0.0096  0.0198  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.1611 0.1913 0.1556 -0.0162 0.0095  0.0164  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.2146 0.2395 0.2168 -0.0014 0.0121  0.0171  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.2457 0.2671 0.2472 0.0023  0.0140  0.0157  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.2300 0.2485 0.2305 -0.0011 0.0113  0.0135  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.1520 0.1969 0.1552 -0.0134 0.0088  0.0261  75  SER   A N   
547  C CA  . SER   A 69  ? 0.1566 0.2115 0.1618 -0.0183 0.0066  0.0311  75  SER   A CA  
548  C C   . SER   A 69  ? 0.1436 0.2006 0.1574 -0.0123 0.0069  0.0346  75  SER   A C   
549  O O   . SER   A 69  ? 0.1528 0.2095 0.1737 -0.0057 0.0093  0.0364  75  SER   A O   
550  C CB  . SER   A 69  ? 0.2033 0.2709 0.2120 -0.0223 0.0051  0.0381  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.3124 0.3774 0.3129 -0.0287 0.0050  0.0346  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1482 0.2072 0.1617 -0.0148 0.0053  0.0358  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1474 0.2071 0.1693 -0.0094 0.0057  0.0392  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1511 0.2232 0.1774 -0.0144 0.0024  0.0476  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1764 0.2539 0.1950 -0.0235 -0.0001 0.0479  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1570 0.2040 0.1750 -0.0056 0.0073  0.0317  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1430 0.1853 0.1517 -0.0111 0.0066  0.0260  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1512 0.1858 0.1531 -0.0127 0.0078  0.0195  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1543 0.1995 0.1623 -0.0145 0.0053  0.0273  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1671 0.1968 0.1628 -0.0174 0.0087  0.0141  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1724 0.2131 0.1724 -0.0198 0.0061  0.0211  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1655 0.1985 0.1601 -0.0211 0.0082  0.0145  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1541 0.2310 0.1929 -0.0094 0.0026  0.0548  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1591 0.2488 0.2047 -0.0137 -0.0011 0.0651  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1560 0.2428 0.1948 -0.0176 -0.0027 0.0625  77  SER   A C   
566  O O   . SER   A 71  ? 0.1618 0.2358 0.1941 -0.0148 -0.0003 0.0532  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1783 0.2732 0.2427 -0.0060 0.0006  0.0744  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1976 0.2802 0.2659 0.0020  0.0046  0.0695  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1572 0.2567 0.1974 -0.0249 -0.0069 0.0710  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1664 0.2649 0.2003 -0.0297 -0.0083 0.0694  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1778 0.2705 0.2222 -0.0211 -0.0068 0.0715  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1897 0.2843 0.2491 -0.0138 -0.0056 0.0783  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.1857 0.3015 0.2175 -0.0415 -0.0137 0.0793  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.2474 0.3670 0.2650 -0.0524 -0.0145 0.0749  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.3330 0.4697 0.3450 -0.0667 -0.0198 0.0833  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.4303 0.5688 0.4260 -0.0791 -0.0195 0.0767  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4922 0.6403 0.4753 -0.0944 -0.0220 0.0779  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1672 0.2521 0.2053 -0.0217 -0.0060 0.0655  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1648 0.2432 0.2123 -0.0141 -0.0043 0.0669  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.1812 0.2713 0.2446 -0.0133 -0.0070 0.0815  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.2009 0.3051 0.2636 -0.0220 -0.0117 0.0904  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.1951 0.2674 0.2317 -0.0182 -0.0042 0.0595  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2249 0.3060 0.2484 -0.0306 -0.0065 0.0584  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.1834 0.2650 0.2059 -0.0298 -0.0058 0.0568  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1712 0.2560 0.2492 -0.0037 -0.0036 0.0842  80  SER   A N   
586  C CA  . SER   A 74  ? 0.1854 0.2806 0.2828 -0.0013 -0.0048 0.0989  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1719 0.2554 0.2824 0.0084  0.0004  0.0981  80  SER   A C   
588  O O   . SER   A 74  ? 0.1705 0.2389 0.2742 0.0128  0.0047  0.0862  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2607 0.3663 0.3677 -0.0003 -0.0049 0.1063  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.4046 0.5201 0.4983 -0.0103 -0.0095 0.1062  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.1949 0.2865 0.3257 0.0112  0.0000  0.1121  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.2072 0.2884 0.3537 0.0199  0.0057  0.1131  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.2180 0.2970 0.3786 0.0277  0.0122  0.1136  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2361 0.3293 0.4116 0.0278  0.0107  0.1263  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.2114 0.3037 0.3740 0.0180  0.0016  0.1295  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2696 0.3516 0.4486 0.0253  0.0067  0.1320  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2905 0.3569 0.4542 0.0248  0.0083  0.1187  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2747 0.3710 0.4719 0.0227  0.0016  0.1514  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.2143 0.2773 0.3694 0.0331  0.0192  0.1002  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.2149 0.2735 0.3787 0.0395  0.0268  0.0969  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2293 0.2724 0.4047 0.0470  0.0363  0.0921  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2323 0.2631 0.3984 0.0466  0.0372  0.0837  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2314 0.2840 0.3736 0.0370  0.0270  0.0832  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2770 0.3428 0.4064 0.0287  0.0186  0.0863  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2512 0.2980 0.3990 0.0426  0.0354  0.0778  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.3138 0.3949 0.4538 0.0276  0.0168  0.0970  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2391 0.2831 0.4361 0.0536  0.0437  0.0977  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2553 0.2836 0.4637 0.0601  0.0544  0.0919  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2765 0.2905 0.4663 0.0599  0.0604  0.0740  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.2972 0.3147 0.4790 0.0589  0.0609  0.0699  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2504 0.2837 0.4891 0.0673  0.0622  0.1029  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2820 0.2975 0.5337 0.0735  0.0744  0.0967  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.2940 0.3034 0.5540 0.0742  0.0740  0.1009  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3157 0.3194 0.5689 0.0774  0.0867  0.0853  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.3268 0.3182 0.5977 0.0790  0.0858  0.0941  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3253 0.3116 0.5904 0.0820  0.0992  0.0786  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.3341 0.3138 0.6076 0.0827  0.0986  0.0828  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2596 0.2578 0.4407 0.0595  0.0638  0.0636  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2798 0.2644 0.4434 0.0579  0.0692  0.0474  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.2813 0.2503 0.4570 0.0622  0.0819  0.0415  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.3027 0.2649 0.4878 0.0636  0.0836  0.0439  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.2869 0.2673 0.4269 0.0519  0.0618  0.0394  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2962 0.2654 0.4190 0.0495  0.0664  0.0247  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2851 0.2798 0.4156 0.0477  0.0509  0.0452  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.3127 0.2763 0.4878 0.0636  0.0908  0.0337  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.3384 0.2876 0.5252 0.0671  0.1053  0.0266  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.3587 0.2913 0.5330 0.0632  0.1078  0.0154  85  GLU   A C   
628  O O   . GLU   A 79  ? 0.3532 0.2856 0.5045 0.0572  0.0996  0.0094  85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.4046 0.3523 0.5824 0.0660  0.1123  0.0171  85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.5119 0.4439 0.6959 0.0674  0.1288  0.0059  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.5883 0.5207 0.8058 0.0759  0.1394  0.0150  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.5833 0.5079 0.8161 0.0790  0.1429  0.0187  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.6386 0.5795 0.8682 0.0796  0.1441  0.0193  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.3730 0.2912 0.5618 0.0661  0.1196  0.0119  86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.3805 0.2823 0.5547 0.0607  0.1228  -0.0007 86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.3964 0.2936 0.5437 0.0535  0.1238  -0.0155 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.4154 0.3156 0.5610 0.0540  0.1289  -0.0189 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.3871 0.2727 0.5797 0.0641  0.1382  -0.0049 86  ALA   A CB  
639  N N   . SER   A 81  ? 0.3757 0.2687 0.5026 0.0468  0.1173  -0.0221 87  SER   A N   
640  C CA  . SER   A 81  ? 0.3689 0.2596 0.4697 0.0388  0.1158  -0.0340 87  SER   A CA  
641  C C   . SER   A 81  ? 0.3628 0.2393 0.4511 0.0318  0.1186  -0.0447 87  SER   A C   
642  O O   . SER   A 81  ? 0.3693 0.2378 0.4700 0.0340  0.1222  -0.0427 87  SER   A O   
643  C CB  . SER   A 81  ? 0.3576 0.2624 0.4448 0.0366  0.1009  -0.0285 87  SER   A CB  
644  O OG  . SER   A 81  ? 0.3347 0.2410 0.4178 0.0349  0.0913  -0.0247 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.3682 0.2424 0.4325 0.0229  0.1165  -0.0548 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.3935 0.2569 0.4443 0.0147  0.1168  -0.0636 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.3911 0.2606 0.4398 0.0144  0.1036  -0.0562 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.4069 0.2687 0.4472 0.0083  0.1029  -0.0615 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.4427 0.3045 0.4685 0.0039  0.1170  -0.0749 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.5147 0.3910 0.5272 0.0019  0.1034  -0.0697 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.6262 0.5025 0.6146 -0.0098 0.1011  -0.0782 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.6557 0.5381 0.6359 -0.0118 0.1009  -0.0794 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.6792 0.5500 0.6570 -0.0175 0.0989  -0.0830 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3554 0.2385 0.4114 0.0203  0.0937  -0.0443 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.3124 0.2017 0.3660 0.0196  0.0823  -0.0379 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.3132 0.2047 0.3865 0.0262  0.0815  -0.0274 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.3258 0.2177 0.3983 0.0246  0.0757  -0.0245 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.3042 0.2076 0.3479 0.0189  0.0712  -0.0334 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3028 0.2060 0.3271 0.0117  0.0696  -0.0415 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3248 0.2236 0.3359 0.0041  0.0667  -0.0473 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3344 0.2423 0.3539 0.0118  0.0711  -0.0428 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.3460 0.2466 0.3399 -0.0035 0.0640  -0.0527 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3501 0.2589 0.3519 0.0044  0.0690  -0.0488 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.3700 0.2753 0.3592 -0.0034 0.0654  -0.0536 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4234 0.3313 0.3957 -0.0117 0.0623  -0.0579 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.3171 0.2111 0.4094 0.0334  0.0872  -0.0206 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.3096 0.2081 0.4220 0.0391  0.0852  -0.0081 90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.3443 0.2371 0.4798 0.0455  0.0969  -0.0047 90  TYR   A C   
669  O O   . TYR   A 84  ? 0.3215 0.2135 0.4575 0.0469  0.1037  -0.0091 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2854 0.2019 0.3986 0.0412  0.0748  0.0027  90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2522 0.1754 0.3476 0.0361  0.0637  0.0017  90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2598 0.1829 0.3548 0.0340  0.0585  0.0047  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2500 0.1792 0.3302 0.0333  0.0592  -0.0023 90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2407 0.1701 0.3218 0.0298  0.0496  0.0038  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2414 0.1764 0.3087 0.0293  0.0501  -0.0027 90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.2335 0.1682 0.3014 0.0277  0.0458  -0.0001 90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.2115 0.1515 0.2688 0.0240  0.0382  -0.0007 90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.3574 0.2493 0.5137 0.0500  0.0983  0.0052  91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.3701 0.2605 0.5530 0.0575  0.1083  0.0122  91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.3671 0.2761 0.5581 0.0615  0.1024  0.0240  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.3622 0.2840 0.5389 0.0582  0.0904  0.0273  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3802 0.2675 0.5819 0.0601  0.1080  0.0223  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.3829 0.2814 0.5704 0.0555  0.0931  0.0276  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.3643 0.2594 0.5225 0.0486  0.0899  0.0130  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.3636 0.2749 0.5793 0.0684  0.1104  0.0316  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.3465 0.2765 0.5729 0.0719  0.1050  0.0446  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.3460 0.2901 0.5765 0.0707  0.0921  0.0594  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.3747 0.3145 0.6181 0.0719  0.0924  0.0659  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.3467 0.2758 0.6034 0.0798  0.1169  0.0514  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.3277 0.2870 0.5431 0.0667  0.0806  0.0628  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.3089 0.2811 0.5245 0.0636  0.0688  0.0750  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2839 0.2735 0.4894 0.0601  0.0594  0.0800  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.3193 0.3096 0.5154 0.0599  0.0612  0.0731  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.2975 0.2611 0.4939 0.0581  0.0642  0.0666  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.3013 0.2654 0.4694 0.0526  0.0589  0.0545  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.3023 0.2552 0.4534 0.0482  0.0577  0.0436  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.2821 0.2403 0.4111 0.0427  0.0493  0.0382  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.2832 0.2432 0.3981 0.0410  0.0482  0.0311  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.2917 0.2510 0.4109 0.0440  0.0541  0.0291  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2160 0.1796 0.3141 0.0363  0.0412  0.0271  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2726 0.2758 0.4796 0.0565  0.0497  0.0920  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2650 0.2837 0.4596 0.0510  0.0404  0.0958  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2404 0.2536 0.4086 0.0450  0.0353  0.0840  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2488 0.2569 0.4137 0.0429  0.0334  0.0831  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2693 0.3058 0.4784 0.0486  0.0330  0.1147  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.2590 0.3062 0.4920 0.0534  0.0359  0.1273  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.2628 0.3224 0.4911 0.0511  0.0327  0.1294  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.2564 0.2994 0.5174 0.0607  0.0434  0.1358  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.2709 0.3410 0.5221 0.0555  0.0356  0.1410  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.2485 0.3014 0.5342 0.0659  0.0471  0.1476  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.2668 0.3334 0.5473 0.0634  0.0432  0.1500  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.2871 0.3642 0.5936 0.0687  0.0472  0.1622  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.2110 0.2262 0.3618 0.0420  0.0330  0.0760  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1991 0.2115 0.3274 0.0365  0.0282  0.0663  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1842 0.2120 0.3062 0.0302  0.0200  0.0733  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1717 0.2095 0.2972 0.0297  0.0187  0.0787  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1983 0.2015 0.3126 0.0370  0.0317  0.0529  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.1911 0.1919 0.2854 0.0318  0.0267  0.0445  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.1984 0.1889 0.2800 0.0319  0.0296  0.0322  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2015 0.1821 0.2856 0.0346  0.0358  0.0269  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.1845 0.1772 0.2519 0.0282  0.0254  0.0274  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1684 0.1982 0.2810 0.0249  0.0150  0.0730  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1708 0.2143 0.2759 0.0174  0.0082  0.0784  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1644 0.2049 0.2499 0.0135  0.0070  0.0669  96  SER   A C   
725  O O   . SER   A 90  ? 0.1818 0.2101 0.2596 0.0162  0.0101  0.0559  96  SER   A O   
726  C CB  . SER   A 90  ? 0.2030 0.2511 0.3100 0.0131  0.0044  0.0852  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2482 0.2848 0.3446 0.0128  0.0056  0.0748  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1646 0.2171 0.2431 0.0064  0.0025  0.0704  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1514 0.2022 0.2131 0.0016  0.0016  0.0609  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1512 0.1938 0.2098 0.0065  0.0051  0.0529  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1633 0.1984 0.2107 0.0057  0.0059  0.0431  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1728 0.2172 0.2248 -0.0012 0.0014  0.0537  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.1886 0.2420 0.2417 -0.0074 -0.0020 0.0612  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.2285 0.2907 0.2711 -0.0169 -0.0045 0.0613  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2229 0.2775 0.2860 -0.0060 -0.0028 0.0688  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2288 0.2981 0.2741 -0.0215 -0.0072 0.0688  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2246 0.2899 0.2829 -0.0149 -0.0066 0.0742  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1357 0.1801 0.2047 0.0112  0.0073  0.0574  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1509 0.1882 0.2172 0.0153  0.0111  0.0503  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1426 0.1897 0.2064 0.0118  0.0091  0.0534  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1473 0.2067 0.2190 0.0093  0.0065  0.0635  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1791 0.2112 0.2593 0.0228  0.0166  0.0523  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.1832 0.2077 0.2605 0.0265  0.0215  0.0447  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.2043 0.2172 0.2681 0.0258  0.0222  0.0335  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2114 0.2312 0.3039 0.0330  0.0287  0.0466  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1544 0.1960 0.2078 0.0113  0.0101  0.0452  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1424 0.1913 0.1919 0.0076  0.0086  0.0465  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1517 0.1954 0.2031 0.0128  0.0128  0.0429  99  MET   A C   
749  O O   . MET   A 93  ? 0.1694 0.2022 0.2160 0.0158  0.0154  0.0351  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1522 0.1980 0.1873 0.0017  0.0067  0.0394  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1739 0.2242 0.2054 -0.0044 0.0038  0.0414  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.2106 0.2558 0.2272 -0.0114 0.0038  0.0318  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.2712 0.3016 0.2871 -0.0039 0.0067  0.0234  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1353 0.1877 0.1939 0.0131  0.0133  0.0489  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1577 0.2060 0.2183 0.0175  0.0180  0.0455  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1511 0.2024 0.2028 0.0134  0.0164  0.0434  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1571 0.2176 0.2065 0.0075  0.0123  0.0478  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1832 0.2387 0.2619 0.0223  0.0218  0.0540  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2264 0.2777 0.3175 0.0275  0.0253  0.0566  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2530 0.3103 0.3642 0.0329  0.0306  0.0645  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2627 0.2982 0.3464 0.0304  0.0296  0.0456  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1457 0.1896 0.1922 0.0157  0.0197  0.0368  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1364 0.1823 0.1758 0.0124  0.0187  0.0352  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1320 0.1751 0.1735 0.0162  0.0240  0.0327  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1459 0.1827 0.1912 0.0207  0.0287  0.0296  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1704 0.2079 0.1963 0.0089  0.0162  0.0280  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1263 0.1739 0.1649 0.0137  0.0238  0.0335  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1293 0.1744 0.1674 0.0159  0.0288  0.0304  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1776 0.2127 0.2017 0.0137  0.0275  0.0228  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.2003 0.2347 0.2169 0.0096  0.0231  0.0223  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1365 0.1921 0.1782 0.0136  0.0286  0.0356  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1610 0.2139 0.1999 0.0147  0.0338  0.0317  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1302 0.1977 0.1884 0.0157  0.0295  0.0450  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1735 0.2011 0.1951 0.0160  0.0315  0.0176  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.1931 0.2128 0.2025 0.0135  0.0297  0.0120  103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.2011 0.2142 0.2079 0.0148  0.0347  0.0066  103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2186 0.2303 0.2330 0.0182  0.0396  0.0059  103 GLY   A O   
778  N N   . HIS   A 98  ? 0.2240 0.2333 0.2198 0.0111  0.0338  0.0030  104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2406 0.2439 0.2310 0.0101  0.0383  -0.0028 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.2237 0.2207 0.2131 0.0107  0.0363  -0.0053 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.2220 0.2181 0.2092 0.0097  0.0299  -0.0036 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2440 0.2466 0.2220 0.0045  0.0369  -0.0048 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2560 0.2533 0.2263 0.0013  0.0419  -0.0113 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.2674 0.2641 0.2400 0.0020  0.0512  -0.0154 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.2636 0.2561 0.2247 -0.0029 0.0392  -0.0144 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.2809 0.2713 0.2443 -0.0023 0.0545  -0.0220 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.2801 0.2687 0.2358 -0.0058 0.0467  -0.0212 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2367 0.2289 0.2278 0.0118  0.0420  -0.0095 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2140 0.1996 0.2027 0.0113  0.0409  -0.0127 105 SER   A CA  
790  C C   . SER   A 99  ? 0.2423 0.2211 0.2276 0.0095  0.0490  -0.0199 105 SER   A C   
791  O O   . SER   A 99  ? 0.2752 0.2541 0.2661 0.0114  0.0571  -0.0216 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2458 0.2322 0.2440 0.0154  0.0379  -0.0088 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.2591 0.2467 0.2696 0.0199  0.0437  -0.0069 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2369 0.2098 0.2140 0.0056  0.0472  -0.0241 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.2516 0.2165 0.2225 0.0017  0.0537  -0.0319 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.2586 0.2185 0.2317 0.0023  0.0509  -0.0326 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.2463 0.2094 0.2226 0.0044  0.0432  -0.0274 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.2728 0.2380 0.2269 -0.0074 0.0526  -0.0359 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.2864 0.2566 0.2383 -0.0084 0.0562  -0.0355 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3195 0.2923 0.2550 -0.0179 0.0544  -0.0376 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.3640 0.3328 0.2882 -0.0253 0.0549  -0.0427 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3074 0.2866 0.2411 -0.0188 0.0524  -0.0337 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.2747 0.2261 0.2471 0.0006  0.0578  -0.0390 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.2747 0.2212 0.2516 0.0021  0.0557  -0.0389 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.2668 0.2164 0.2366 -0.0015 0.0452  -0.0360 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.2606 0.2119 0.2376 0.0022  0.0402  -0.0315 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.2943 0.2302 0.2684 -0.0015 0.0660  -0.0481 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.3001 0.2360 0.2777 0.0002  0.0753  -0.0507 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.2877 0.2331 0.2582 -0.0016 0.0695  -0.0467 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2521 0.2040 0.2089 -0.0087 0.0417  -0.0376 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.2382 0.1941 0.1899 -0.0125 0.0322  -0.0340 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.2195 0.1828 0.1777 -0.0081 0.0251  -0.0262 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.2260 0.1924 0.1838 -0.0097 0.0180  -0.0224 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.1954 0.1613 0.1602 -0.0028 0.0272  -0.0237 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.1914 0.1630 0.1624 0.0009  0.0218  -0.0174 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.1829 0.1539 0.1629 0.0053  0.0201  -0.0152 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1803 0.1550 0.1643 0.0069  0.0158  -0.0112 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1838 0.1591 0.1581 0.0037  0.0246  -0.0154 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.2000 0.1776 0.1651 -0.0011 0.0245  -0.0160 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.2034 0.1823 0.1685 -0.0005 0.0297  -0.0172 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.1953 0.1743 0.1545 -0.0055 0.0192  -0.0144 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1828 0.1489 0.1660 0.0065  0.0238  -0.0180 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1802 0.1465 0.1713 0.0097  0.0218  -0.0153 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1839 0.1520 0.1730 0.0075  0.0155  -0.0137 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.1954 0.1628 0.1785 0.0032  0.0131  -0.0151 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.2079 0.1679 0.2025 0.0105  0.0266  -0.0183 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.2180 0.1768 0.2226 0.0155  0.0345  -0.0175 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1645 0.1361 0.1596 0.0100  0.0130  -0.0103 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1598 0.1333 0.1562 0.0089  0.0085  -0.0086 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1596 0.1368 0.1568 0.0089  0.0061  -0.0060 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1605 0.1392 0.1618 0.0089  0.0038  -0.0044 111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1583 0.1366 0.1524 0.0088  0.0074  -0.0057 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1495 0.1305 0.1447 0.0086  0.0056  -0.0031 112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1394 0.1221 0.1397 0.0102  0.0064  -0.0023 112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1418 0.1258 0.1436 0.0114  0.0085  -0.0023 112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1396 0.1226 0.1431 0.0096  0.0052  -0.0012 113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1349 0.1190 0.1415 0.0093  0.0069  -0.0017 113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1366 0.1231 0.1412 0.0082  0.0082  -0.0010 113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1424 0.1285 0.1454 0.0077  0.0076  0.0001  113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1354 0.1175 0.1474 0.0089  0.0067  -0.0019 113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1645 0.1462 0.1797 0.0096  0.0060  -0.0025 113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1560 0.1380 0.1699 0.0071  0.0098  -0.0036 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.1904 0.1709 0.2137 0.0098  0.0062  -0.0019 113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1277 0.1175 0.1323 0.0071  0.0095  -0.0009 114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1301 0.1234 0.1331 0.0044  0.0104  -0.0001 114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1299 0.1217 0.1334 0.0009  0.0121  -0.0027 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1300 0.1220 0.1347 0.0003  0.0127  -0.0039 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1338 0.1333 0.1373 0.0042  0.0105  0.0029  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1391 0.1447 0.1408 -0.0003 0.0107  0.0049  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1570 0.1634 0.1573 -0.0005 0.0107  0.0059  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1527 0.1665 0.1575 -0.0009 0.0099  0.0100  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1383 0.1284 0.1410 -0.0017 0.0134  -0.0039 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1391 0.1261 0.1425 -0.0056 0.0169  -0.0078 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1455 0.1342 0.1446 -0.0110 0.0185  -0.0087 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1498 0.1407 0.1470 -0.0110 0.0169  -0.0060 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1603 0.1404 0.1705 -0.0029 0.0181  -0.0089 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1628 0.1402 0.1743 -0.0020 0.0172  -0.0067 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.1814 0.1533 0.2025 0.0006  0.0181  -0.0060 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.1916 0.1654 0.2150 0.0043  0.0142  -0.0029 115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.1868 0.1593 0.2174 0.0062  0.0145  -0.0027 115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.2013 0.1709 0.2374 0.0052  0.0194  -0.0064 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.2091 0.1840 0.2408 0.0083  0.0104  0.0005  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.1677 0.1552 0.1648 -0.0166 0.0223  -0.0130 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2061 0.1941 0.1977 -0.0241 0.0248  -0.0153 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.2431 0.2217 0.2379 -0.0265 0.0312  -0.0218 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2350 0.2080 0.2376 -0.0216 0.0328  -0.0229 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.2092 0.2065 0.1936 -0.0310 0.0238  -0.0143 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.2060 0.2031 0.1884 -0.0354 0.0275  -0.0190 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.2862 0.2627 0.2756 -0.0347 0.0354  -0.0262 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.3192 0.2853 0.3128 -0.0373 0.0434  -0.0334 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3190 0.2834 0.3147 -0.0384 0.0481  -0.0383 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.3572 0.3125 0.3610 -0.0373 0.0550  -0.0432 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.3701 0.3335 0.3561 -0.0476 0.0481  -0.0386 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.4428 0.4155 0.4160 -0.0578 0.0477  -0.0403 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.5579 0.5297 0.5217 -0.0696 0.0514  -0.0450 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.5959 0.5760 0.5534 -0.0735 0.0462  -0.0401 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.5702 0.5320 0.5329 -0.0761 0.0610  -0.0547 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.2703 0.2434 0.2603 -0.0397 0.0446  -0.0363 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.2556 0.2287 0.2460 -0.0417 0.0487  -0.0405 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2411 0.2135 0.2416 -0.0322 0.0462  -0.0371 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.2706 0.2422 0.2738 -0.0327 0.0499  -0.0404 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.2535 0.2374 0.2319 -0.0502 0.0462  -0.0394 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.2769 0.2633 0.2444 -0.0613 0.0481  -0.0422 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.2787 0.2744 0.2407 -0.0637 0.0414  -0.0355 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.3142 0.2951 0.2757 -0.0714 0.0564  -0.0513 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.3225 0.3188 0.2751 -0.0751 0.0447  -0.0398 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.3387 0.3258 0.2896 -0.0806 0.0540  -0.0499 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2183 0.1924 0.2229 -0.0245 0.0395  -0.0304 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2076 0.1816 0.2200 -0.0170 0.0365  -0.0271 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.1734 0.1535 0.1827 -0.0131 0.0290  -0.0206 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.1719 0.1553 0.1762 -0.0141 0.0261  -0.0179 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1589 0.1404 0.1718 -0.0089 0.0265  -0.0186 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1503 0.1358 0.1614 -0.0051 0.0208  -0.0135 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1367 0.1292 0.1418 -0.0086 0.0193  -0.0115 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1454 0.1405 0.1487 -0.0125 0.0210  -0.0130 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1463 0.1303 0.1632 -0.0006 0.0190  -0.0123 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.1678 0.1545 0.1822 0.0022  0.0147  -0.0087 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.1642 0.1436 0.1885 0.0027  0.0191  -0.0118 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1327 0.1288 0.1355 -0.0075 0.0163  -0.0075 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1453 0.1492 0.1454 -0.0102 0.0144  -0.0034 121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1402 0.1453 0.1442 -0.0054 0.0120  0.0004  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1507 0.1612 0.1554 -0.0073 0.0109  0.0039  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1569 0.1650 0.1546 -0.0120 0.0133  -0.0006 121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.1753 0.1933 0.1735 -0.0138 0.0107  0.0062  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.1898 0.1965 0.1828 -0.0182 0.0161  -0.0047 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1431 0.1434 0.1496 0.0001  0.0112  0.0003  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1520 0.1517 0.1618 0.0040  0.0101  0.0026  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1328 0.1270 0.1427 0.0079  0.0098  0.0010  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1360 0.1273 0.1444 0.0077  0.0097  -0.0011 122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1321 0.1246 0.1439 0.0107  0.0100  0.0020  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1326 0.1202 0.1425 0.0126  0.0102  -0.0002 123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1346 0.1225 0.1459 0.0147  0.0126  0.0011  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1445 0.1350 0.1609 0.0159  0.0138  0.0043  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1489 0.1320 0.1588 0.0128  0.0094  -0.0024 123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1655 0.1484 0.1792 0.0135  0.0104  -0.0011 123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1643 0.1472 0.1746 0.0114  0.0077  -0.0034 123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1811 0.1591 0.1943 0.0131  0.0098  -0.0036 123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1299 0.1153 0.1374 0.0149  0.0135  -0.0009 124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1416 0.1264 0.1508 0.0168  0.0173  -0.0008 124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1520 0.1321 0.1649 0.0183  0.0200  -0.0021 124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1580 0.1335 0.1675 0.0168  0.0188  -0.0051 124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1534 0.1356 0.1557 0.0153  0.0182  -0.0040 124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1706 0.1512 0.1743 0.0167  0.0238  -0.0055 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1554 0.1417 0.1551 0.0138  0.0158  -0.0021 124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1524 0.1339 0.1735 0.0211  0.0236  0.0008  125 SER   A N   
926  C CA  . SER   A 119 ? 0.1640 0.1403 0.1913 0.0229  0.0271  0.0005  125 SER   A CA  
927  C C   . SER   A 119 ? 0.1973 0.1711 0.2309 0.0257  0.0340  -0.0002 125 SER   A C   
928  O O   . SER   A 119 ? 0.2102 0.1764 0.2466 0.0265  0.0388  -0.0034 125 SER   A O   
929  C CB  . SER   A 119 ? 0.1860 0.1673 0.2208 0.0236  0.0244  0.0066  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.1896 0.1671 0.2334 0.0258  0.0277  0.0085  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1772 0.1570 0.2144 0.0272  0.0355  0.0029  126 THR   A N   
932  C CA  . THR   A 120 ? 0.2029 0.1806 0.2485 0.0303  0.0436  0.0024  126 THR   A CA  
933  C C   . THR   A 120 ? 0.2134 0.1953 0.2544 0.0295  0.0447  0.0014  126 THR   A C   
934  O O   . THR   A 120 ? 0.2056 0.1926 0.2390 0.0269  0.0388  0.0026  126 THR   A O   
935  C CB  . THR   A 120 ? 0.2208 0.2042 0.2837 0.0346  0.0451  0.0114  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.3493 0.3275 0.4229 0.0383  0.0547  0.0097  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.1690 0.1652 0.2351 0.0341  0.0403  0.0193  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2230 0.2025 0.2692 0.0315  0.0528  -0.0008 127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2331 0.2179 0.2760 0.0305  0.0542  -0.0010 127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.2559 0.2372 0.3053 0.0326  0.0649  -0.0046 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.2678 0.2421 0.3259 0.0352  0.0717  -0.0067 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.2762 0.2611 0.3196 0.0306  0.0665  -0.0063 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.2866 0.2692 0.3345 0.0316  0.0773  -0.0106 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.2806 0.2746 0.3380 0.0340  0.0780  -0.0037 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.2753 0.2786 0.3422 0.0364  0.0720  0.0058  128 GLY   A O   
946  N N   . ASN   A 123 ? 0.2656 0.2596 0.3206 0.0326  0.0855  -0.0082 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.2731 0.2778 0.3381 0.0348  0.0881  -0.0024 129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.2571 0.2727 0.3190 0.0331  0.0772  0.0055  129 ASN   A C   
949  O O   . ASN   A 123 ? 0.2568 0.2832 0.3324 0.0359  0.0769  0.0140  129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.3033 0.3105 0.3931 0.0420  0.0961  0.0033  129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.3456 0.3412 0.4391 0.0432  0.1098  -0.0060 129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.4088 0.4012 0.4930 0.0395  0.1171  -0.0142 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.3570 0.3463 0.4645 0.0477  0.1139  -0.0048 129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.2205 0.2336 0.2647 0.0279  0.0691  0.0026  130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.2057 0.2267 0.2452 0.0253  0.0599  0.0082  130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.1784 0.2033 0.2241 0.0267  0.0528  0.0149  130 GLY   A C   
957  O O   . GLY   A 124 ? 0.1976 0.2291 0.2403 0.0240  0.0463  0.0193  130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1841 0.2038 0.2354 0.0295  0.0538  0.0144  131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1734 0.1961 0.2276 0.0294  0.0467  0.0197  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.2027 0.2158 0.2449 0.0273  0.0432  0.0135  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2334 0.2375 0.2691 0.0268  0.0472  0.0063  131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1832 0.2091 0.2555 0.0342  0.0498  0.0263  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.1945 0.2324 0.2827 0.0366  0.0525  0.0350  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.2235 0.2628 0.3328 0.0425  0.0581  0.0411  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.1985 0.2490 0.2850 0.0323  0.0437  0.0429  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1598 0.1752 0.1992 0.0253  0.0363  0.0164  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1647 0.1726 0.1963 0.0239  0.0330  0.0120  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1592 0.1715 0.1974 0.0241  0.0292  0.0177  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1673 0.1885 0.2082 0.0222  0.0259  0.0235  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1588 0.1641 0.1773 0.0198  0.0288  0.0082  132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1696 0.1820 0.1871 0.0172  0.0245  0.0123  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1669 0.1656 0.1797 0.0186  0.0257  0.0047  132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1581 0.1647 0.1981 0.0254  0.0297  0.0162  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1497 0.1605 0.1950 0.0249  0.0261  0.0214  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1490 0.1544 0.1848 0.0222  0.0223  0.0169  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1722 0.1692 0.2020 0.0224  0.0235  0.0106  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1337 0.1447 0.1683 0.0189  0.0180  0.0202  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1415 0.1485 0.1688 0.0163  0.0151  0.0161  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1461 0.1559 0.1776 0.0152  0.0136  0.0198  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1410 0.1597 0.1779 0.0135  0.0122  0.0268  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1423 0.1528 0.1628 0.0119  0.0126  0.0152  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1462 0.1555 0.1630 0.0122  0.0135  0.0131  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1376 0.1399 0.1489 0.0128  0.0137  0.0080  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1576 0.1741 0.1767 0.0112  0.0137  0.0172  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1442 0.1461 0.1518 0.0123  0.0141  0.0071  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1572 0.1729 0.1727 0.0110  0.0145  0.0155  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1438 0.1521 0.1533 0.0114  0.0147  0.0104  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1379 0.1412 0.1674 0.0156  0.0135  0.0160  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1444 0.1499 0.1765 0.0138  0.0119  0.0189  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1436 0.1531 0.1691 0.0087  0.0095  0.0176  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1479 0.1525 0.1676 0.0079  0.0095  0.0118  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1534 0.1504 0.1857 0.0159  0.0131  0.0150  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1427 0.1612 0.1691 0.0044  0.0077  0.0230  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1545 0.1766 0.1735 -0.0021 0.0067  0.0207  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1521 0.1704 0.1693 -0.0033 0.0071  0.0172  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1581 0.1762 0.1802 -0.0016 0.0066  0.0204  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1739 0.2082 0.1933 -0.0083 0.0044  0.0281  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2909 0.3291 0.3010 -0.0169 0.0044  0.0250  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2247 0.2578 0.2292 -0.0179 0.0065  0.0182  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.3903 0.4360 0.3988 -0.0231 0.0029  0.0289  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1399 0.1558 0.1513 -0.0066 0.0085  0.0113  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1491 0.1631 0.1594 -0.0087 0.0096  0.0080  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1637 0.1827 0.1678 -0.0169 0.0113  0.0058  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1590 0.1768 0.1620 -0.0193 0.0133  0.0024  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1525 0.1577 0.1643 -0.0044 0.0110  0.0022  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1632 0.1636 0.1788 0.0016  0.0096  0.0036  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1676 0.1695 0.1771 -0.0049 0.0130  -0.0024 137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1603 0.1846 0.1597 -0.0220 0.0112  0.0069  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1662 0.1937 0.1578 -0.0311 0.0140  0.0029  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.1726 0.2080 0.1608 -0.0383 0.0133  0.0059  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.1961 0.2325 0.1770 -0.0465 0.0172  0.0004  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1642 0.1961 0.1508 -0.0361 0.0135  0.0039  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1616 0.1850 0.1502 -0.0305 0.0151  -0.0004 138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.1891 0.2172 0.1730 -0.0356 0.0144  0.0011  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1696 0.2064 0.1575 -0.0337 0.0096  0.0104  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.1863 0.2292 0.1732 -0.0365 0.0078  0.0143  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.2029 0.2450 0.1824 -0.0433 0.0100  0.0096  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.2031 0.2537 0.1970 -0.0331 0.0042  0.0233  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1700 0.2112 0.1634 -0.0363 0.0090  0.0147  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.1780 0.2280 0.1687 -0.0439 0.0077  0.0191  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.1801 0.2247 0.1729 -0.0416 0.0099  0.0154  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.1971 0.2482 0.1867 -0.0483 0.0095  0.0180  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.1812 0.2406 0.1788 -0.0431 0.0021  0.0319  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2368 0.2889 0.2458 -0.0319 0.0013  0.0346  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2375 0.2804 0.2488 -0.0245 0.0030  0.0294  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2748 0.3301 0.2902 -0.0311 -0.0009 0.0417  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1729 0.2068 0.1712 -0.0327 0.0116  0.0104  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1614 0.1906 0.1631 -0.0300 0.0131  0.0076  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.1656 0.1923 0.1631 -0.0344 0.0188  -0.0011 140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.1734 0.1924 0.1744 -0.0297 0.0217  -0.0070 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1720 0.1924 0.1811 -0.0201 0.0120  0.0068  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1873 0.2085 0.2018 -0.0155 0.0083  0.0142  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.2026 0.2144 0.2215 -0.0077 0.0084  0.0115  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.2026 0.2293 0.2205 -0.0178 0.0060  0.0217  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.1701 0.2040 0.1603 -0.0443 0.0207  -0.0016 141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.1844 0.2159 0.1698 -0.0499 0.0280  -0.0110 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.1807 0.2066 0.1731 -0.0456 0.0317  -0.0155 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.1941 0.2143 0.1887 -0.0453 0.0383  -0.0234 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.2025 0.2438 0.1765 -0.0636 0.0299  -0.0112 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2244 0.2743 0.1917 -0.0696 0.0251  -0.0045 141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2542 0.3141 0.2083 -0.0853 0.0274  -0.0058 141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2428 0.2871 0.2101 -0.0664 0.0259  -0.0079 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.1674 0.1947 0.1647 -0.0420 0.0278  -0.0102 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.1814 0.2050 0.1856 -0.0384 0.0303  -0.0132 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.1863 0.2014 0.1994 -0.0295 0.0311  -0.0163 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.2019 0.2145 0.2221 -0.0271 0.0342  -0.0194 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.1808 0.2078 0.1877 -0.0374 0.0255  -0.0061 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.1675 0.1922 0.1780 -0.0311 0.0192  0.0005  142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.1856 0.2156 0.1943 -0.0329 0.0149  0.0082  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.1745 0.1917 0.1921 -0.0224 0.0171  0.0004  142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.1930 0.2178 0.2079 -0.0252 0.0115  0.0118  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.1745 0.1914 0.1935 -0.0194 0.0127  0.0067  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.1837 0.1951 0.2069 -0.0177 0.0185  -0.0038 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.1975 0.2073 0.2214 -0.0126 0.0107  0.0071  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.2045 0.2104 0.2318 -0.0117 0.0150  -0.0021 142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.2006 0.2052 0.2272 -0.0095 0.0117  0.0024  142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.1662 0.1778 0.1797 -0.0249 0.0281  -0.0149 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.1838 0.1885 0.2050 -0.0178 0.0284  -0.0170 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.2132 0.2149 0.2383 -0.0192 0.0358  -0.0238 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2291 0.2268 0.2640 -0.0139 0.0368  -0.0245 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.1823 0.1844 0.2016 -0.0142 0.0248  -0.0147 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.1856 0.1882 0.2049 -0.0106 0.0190  -0.0089 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.2052 0.2064 0.2221 -0.0083 0.0169  -0.0073 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.1946 0.1933 0.2203 -0.0057 0.0169  -0.0083 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2480 0.2518 0.2663 -0.0269 0.0414  -0.0284 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.2969 0.2964 0.3192 -0.0290 0.0504  -0.0361 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3563 0.3567 0.3845 -0.0309 0.0569  -0.0400 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3716 0.3680 0.4050 -0.0326 0.0660  -0.0469 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.3124 0.3129 0.3232 -0.0382 0.0549  -0.0409 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.3620 0.3618 0.3674 -0.0377 0.0504  -0.0382 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.3853 0.3820 0.3969 -0.0295 0.0453  -0.0339 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.4383 0.4414 0.4328 -0.0463 0.0519  -0.0401 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3768 0.3824 0.4050 -0.0310 0.0532  -0.0360 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.4221 0.4298 0.4555 -0.0335 0.0594  -0.0395 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.4513 0.4607 0.4936 -0.0276 0.0541  -0.0339 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.4438 0.4526 0.4859 -0.0229 0.0459  -0.0279 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.4786 0.4929 0.4986 -0.0445 0.0619  -0.0414 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5625 0.5830 0.5747 -0.0460 0.0523  -0.0329 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.6685 0.6969 0.6665 -0.0575 0.0524  -0.0321 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.6681 0.7026 0.6625 -0.0590 0.0455  -0.0240 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.7151 0.7437 0.7056 -0.0655 0.0596  -0.0392 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.4864 0.4981 0.5362 -0.0287 0.0596  -0.0363 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.5225 0.5369 0.5810 -0.0251 0.0560  -0.0319 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.5412 0.5526 0.6158 -0.0171 0.0555  -0.0300 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.5480 0.5620 0.6348 -0.0157 0.0595  -0.0303 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.5730 0.5900 0.6239 -0.0252 0.0465  -0.0250 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.6589 0.6768 0.7181 -0.0211 0.0415  -0.0202 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.7726 0.7961 0.8326 -0.0256 0.0436  -0.0198 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.8036 0.8290 0.8574 -0.0279 0.0383  -0.0152 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.7956 0.8214 0.8634 -0.0269 0.0509  -0.0238 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2601 0.2632 0.2806 -0.0042 -0.0100 0.0446  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.2355 0.2421 0.2664 -0.0051 -0.0103 0.0460  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.2137 0.2178 0.2418 -0.0052 -0.0099 0.0423  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2420 0.2414 0.2598 -0.0051 -0.0106 0.0393  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2757 0.2843 0.3094 -0.0078 -0.0153 0.0510  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.3305 0.3344 0.3531 -0.0101 -0.0197 0.0501  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.2073 0.2141 0.2444 -0.0052 -0.0082 0.0427  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.2023 0.2069 0.2373 -0.0054 -0.0076 0.0401  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1828 0.1899 0.2261 -0.0038 -0.0033 0.0392  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.1905 0.1999 0.2394 -0.0021 -0.0003 0.0388  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1690 0.1753 0.2132 -0.0046 -0.0029 0.0390  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1650 0.1727 0.2155 -0.0031 0.0015  0.0381  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1544 0.1585 0.1984 -0.0028 0.0025  0.0355  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1793 0.1802 0.2163 -0.0041 -0.0005 0.0353  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.1993 0.2112 0.2619 -0.0042 0.0021  0.0427  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1535 0.1576 0.1993 -0.0009 0.0068  0.0336  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1575 0.1585 0.1982 -0.0004 0.0084  0.0320  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1665 0.1696 0.2160 -0.0012 0.0113  0.0353  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1663 0.1725 0.2243 -0.0003 0.0143  0.0363  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1666 0.1657 0.2019 0.0022  0.0111  0.0277  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.1730 0.1715 0.2030 0.0033  0.0091  0.0247  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.1857 0.1813 0.2144 0.0028  0.0125  0.0266  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.1838 0.1818 0.2117 0.0056  0.0113  0.0206  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1594 0.1609 0.2079 -0.0027 0.0108  0.0371  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1742 0.1778 0.2317 -0.0034 0.0140  0.0406  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1762 0.1760 0.2275 -0.0020 0.0178  0.0390  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.2005 0.1970 0.2458 -0.0031 0.0159  0.0392  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1833 0.1885 0.2466 -0.0069 0.0097  0.0450  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1769 0.1862 0.2466 -0.0082 0.0059  0.0474  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1774 0.1919 0.2600 -0.0079 0.0080  0.0508  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.1935 0.2010 0.2557 -0.0094 0.0006  0.0463  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.1897 0.2077 0.2777 -0.0089 0.0044  0.0534  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.2130 0.2237 0.2795 -0.0104 -0.0028 0.0486  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.2128 0.2290 0.2923 -0.0102 -0.0011 0.0523  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2488 0.2681 0.3323 -0.0109 -0.0045 0.0551  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.1769 0.1764 0.2283 0.0004  0.0231  0.0372  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.2017 0.1973 0.2456 0.0021  0.0271  0.0357  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.2035 0.2005 0.2555 0.0028  0.0336  0.0380  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.1859 0.1854 0.2447 0.0039  0.0362  0.0376  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2114 0.2039 0.2443 0.0046  0.0271  0.0303  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2140 0.2089 0.2514 0.0058  0.0284  0.0280  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2384 0.2268 0.2629 0.0064  0.0311  0.0290  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2077 0.2032 0.2600 0.0024  0.0366  0.0407  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2003 0.1972 0.2611 0.0033  0.0436  0.0433  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.1982 0.2011 0.2751 0.0020  0.0434  0.0471  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2134 0.2195 0.2963 -0.0008 0.0377  0.0499  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.1865 0.1907 0.2695 0.0041  0.0488  0.0466  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.1897 0.1997 0.2884 0.0035  0.0486  0.0502  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.1902 0.2007 0.2878 0.0046  0.0465  0.0469  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.1856 0.1990 0.2939 0.0056  0.0493  0.0483  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2164 0.2284 0.3272 0.0049  0.0568  0.0537  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.2923 0.3061 0.4100 0.0029  0.0578  0.0590  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3223 0.3417 0.4539 0.0004  0.0545  0.0642  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3126 0.3214 0.4200 0.0036  0.0613  0.0577  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.1691 0.1773 0.2554 0.0041  0.0411  0.0432  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1684 0.1770 0.2535 0.0049  0.0387  0.0402  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1586 0.1691 0.2421 0.0026  0.0311  0.0413  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1706 0.1795 0.2474 0.0010  0.0274  0.0416  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.1890 0.1926 0.2609 0.0069  0.0401  0.0339  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.1952 0.1955 0.2651 0.0093  0.0475  0.0315  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2206 0.2221 0.3003 0.0107  0.0527  0.0320  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2237 0.2193 0.2814 0.0103  0.0495  0.0290  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.2576 0.2550 0.3342 0.0130  0.0599  0.0294  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.2614 0.2532 0.3153 0.0125  0.0564  0.0267  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.2892 0.2816 0.3520 0.0138  0.0616  0.0265  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.3508 0.3384 0.4085 0.0162  0.0688  0.0236  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1422 0.1555 0.2316 0.0026  0.0292  0.0420  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1439 0.1584 0.2305 0.0010  0.0227  0.0426  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1393 0.1523 0.2213 0.0027  0.0232  0.0383  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1454 0.1594 0.2344 0.0042  0.0268  0.0379  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1492 0.1689 0.2482 -0.0007 0.0201  0.0485  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.1847 0.2055 0.2810 -0.0019 0.0143  0.0493  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1626 0.1884 0.2700 -0.0038 0.0109  0.0556  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.1764 0.2040 0.2859 -0.0034 0.0088  0.0569  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.1801 0.2070 0.2826 -0.0048 0.0034  0.0575  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.2170 0.2409 0.3088 -0.0067 -0.0006 0.0560  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.1829 0.2115 0.2880 -0.0042 0.0025  0.0594  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1400 0.1503 0.2110 0.0027  0.0200  0.0349  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1359 0.1451 0.2031 0.0041  0.0201  0.0310  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1291 0.1399 0.1963 0.0030  0.0158  0.0328  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1468 0.1565 0.2073 0.0017  0.0119  0.0334  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1452 0.1504 0.2006 0.0052  0.0198  0.0261  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.1681 0.1729 0.2221 0.0065  0.0202  0.0221  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.1615 0.1643 0.2140 0.0061  0.0236  0.0249  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1249 0.1378 0.1988 0.0036  0.0167  0.0335  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1250 0.1393 0.1984 0.0028  0.0132  0.0356  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1460 0.1604 0.2196 0.0027  0.0132  0.0358  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1340 0.1482 0.2084 0.0041  0.0149  0.0330  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1389 0.1523 0.2166 0.0054  0.0185  0.0300  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1217 0.1397 0.2046 0.0015  0.0119  0.0417  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.1840 0.2023 0.2683 0.0016  0.0124  0.0418  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1489 0.1674 0.2305 -0.0005 0.0086  0.0446  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.1852 0.2048 0.2684 0.0005  0.0085  0.0451  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.0729 0.0932 0.1683 0.0028  0.0163  0.0432  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2293 0.2484 0.3155 0.0001  0.0113  0.0445  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1285 0.1432 0.2004 0.0038  0.0125  0.0342  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1226 0.1377 0.1978 0.0048  0.0143  0.0328  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1228 0.1402 0.2104 0.0051  0.0170  0.0360  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1252 0.1448 0.2175 0.0043  0.0156  0.0411  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1269 0.1421 0.1978 0.0044  0.0119  0.0349  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1380 0.1506 0.1975 0.0044  0.0098  0.0321  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1548 0.1660 0.2078 0.0033  0.0069  0.0334  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1447 0.1566 0.2026 0.0057  0.0112  0.0281  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1278 0.1444 0.2205 0.0063  0.0205  0.0329  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1131 0.1310 0.2179 0.0068  0.0237  0.0356  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1334 0.1539 0.2433 0.0064  0.0221  0.0415  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1367 0.1595 0.2552 0.0065  0.0226  0.0463  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1117 0.1274 0.2201 0.0079  0.0274  0.0307  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1230 0.1388 0.2440 0.0087  0.0316  0.0326  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1411 0.1538 0.2647 0.0093  0.0347  0.0272  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1405 0.1517 0.2751 0.0104  0.0396  0.0277  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1450 0.1571 0.2900 0.0107  0.0412  0.0314  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1581 0.1731 0.3039 0.0101  0.0384  0.0360  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1383 0.1481 0.2929 0.0118  0.0460  0.0309  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1394 0.1597 0.2437 0.0061  0.0202  0.0415  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1367 0.1589 0.2440 0.0059  0.0190  0.0472  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1499 0.1739 0.2540 0.0046  0.0147  0.0524  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.1797 0.2053 0.2869 0.0044  0.0133  0.0578  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1522 0.1734 0.2546 0.0061  0.0190  0.0460  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1426 0.1625 0.2321 0.0055  0.0159  0.0445  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1565 0.1744 0.2396 0.0058  0.0159  0.0389  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1574 0.1769 0.2394 0.0049  0.0132  0.0479  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1729 0.1895 0.2457 0.0054  0.0134  0.0391  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1650 0.1821 0.2362 0.0048  0.0118  0.0441  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1374 0.1607 0.2356 0.0036  0.0123  0.0510  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1567 0.1816 0.2528 0.0019  0.0078  0.0554  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1654 0.1927 0.2709 0.0016  0.0084  0.0576  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.1723 0.2011 0.2771 -0.0001 0.0044  0.0609  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1610 0.1830 0.2434 0.0007  0.0045  0.0525  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1724 0.1920 0.2455 0.0012  0.0042  0.0509  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.1800 0.1961 0.2401 0.0004  0.0015  0.0478  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1739 0.1948 0.2477 0.0009  0.0025  0.0565  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1579 0.1852 0.2716 0.0032  0.0135  0.0554  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1525 0.1817 0.2754 0.0033  0.0153  0.0575  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.1598 0.1934 0.2936 0.0028  0.0132  0.0649  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.1647 0.1995 0.3032 0.0035  0.0132  0.0682  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1659 0.1933 0.2946 0.0053  0.0216  0.0535  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.1587 0.1950 0.2972 0.0017  0.0114  0.0681  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.1559 0.1972 0.3062 0.0010  0.0087  0.0757  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1475 0.1909 0.3137 0.0033  0.0147  0.0777  24  THR   C C   
1231 O O   . THR   B 18  ? 0.1571 0.1977 0.3244 0.0051  0.0209  0.0730  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.1752 0.2187 0.3239 -0.0017 0.0034  0.0782  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.1768 0.2197 0.3290 -0.0013 0.0075  0.0758  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.2039 0.2440 0.3359 -0.0040 -0.0022 0.0755  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.1598 0.2084 0.3394 0.0033  0.0127  0.0854  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.1743 0.2252 0.3706 0.0055  0.0185  0.0881  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.1571 0.2078 0.3551 0.0054  0.0218  0.0857  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.1681 0.2166 0.3713 0.0078  0.0293  0.0828  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.1802 0.2377 0.3911 0.0053  0.0147  0.0975  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.2177 0.2784 0.4474 0.0075  0.0204  0.1011  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2566 0.3153 0.4953 0.0108  0.0276  0.1005  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.2390 0.3038 0.4787 0.0070  0.0208  0.1043  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.2463 0.3084 0.5012 0.0124  0.0318  0.1043  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.2411 0.3071 0.4973 0.0102  0.0281  0.1067  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.1572 0.2096 0.3504 0.0026  0.0166  0.0868  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.1695 0.2215 0.3640 0.0025  0.0201  0.0848  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.1602 0.2057 0.3433 0.0040  0.0259  0.0766  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1572 0.2014 0.3443 0.0056  0.0323  0.0748  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.1913 0.2453 0.3820 -0.0011 0.0134  0.0870  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2573 0.3117 0.4528 -0.0012 0.0176  0.0865  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.2717 0.3303 0.4834 -0.0001 0.0214  0.0911  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.2982 0.3479 0.4802 -0.0021 0.0180  0.0812  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1500 0.1914 0.3187 0.0037  0.0237  0.0716  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1579 0.1934 0.3160 0.0051  0.0282  0.0640  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1523 0.1860 0.3179 0.0080  0.0356  0.0619  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1650 0.1954 0.3289 0.0094  0.0413  0.0580  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1547 0.1872 0.2987 0.0042  0.0243  0.0600  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1604 0.1923 0.2935 0.0017  0.0184  0.0597  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1832 0.2147 0.3147 0.0009  0.0187  0.0593  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1575 0.1890 0.2835 0.0007  0.0138  0.0598  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1504 0.1856 0.3245 0.0090  0.0358  0.0648  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1582 0.1909 0.3402 0.0117  0.0429  0.0629  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1524 0.1869 0.3479 0.0134  0.0488  0.0659  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1595 0.1897 0.3567 0.0156  0.0560  0.0619  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1510 0.1850 0.3397 0.0122  0.0416  0.0660  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1467 0.1773 0.3237 0.0115  0.0395  0.0611  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.1650 0.1970 0.3347 0.0098  0.0333  0.0629  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1295 0.1546 0.3018 0.0126  0.0436  0.0541  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.1593 0.1876 0.3210 0.0099  0.0338  0.0576  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1380 0.1623 0.3015 0.0115  0.0397  0.0522  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.1670 0.1877 0.3416 0.0144  0.0503  0.0491  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.1525 0.1725 0.3117 0.0119  0.0418  0.0461  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.1863 0.2020 0.3543 0.0146  0.0518  0.0423  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.1737 0.1896 0.3350 0.0132  0.0473  0.0411  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1482 0.1884 0.3525 0.0123  0.0458  0.0727  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1671 0.2099 0.3860 0.0139  0.0514  0.0765  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.1765 0.2164 0.3884 0.0139  0.0556  0.0725  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.1903 0.2311 0.4122 0.0156  0.0618  0.0745  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1672 0.2180 0.3989 0.0123  0.0458  0.0855  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.1698 0.2063 0.3644 0.0121  0.0521  0.0674  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.1634 0.1966 0.3495 0.0121  0.0555  0.0638  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.1704 0.1967 0.3392 0.0127  0.0564  0.0553  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1697 0.1936 0.3260 0.0115  0.0544  0.0523  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.1805 0.2174 0.3645 0.0090  0.0491  0.0674  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.2058 0.2496 0.4082 0.0084  0.0488  0.0755  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.2138 0.2585 0.4249 0.0097  0.0553  0.0773  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.2091 0.2580 0.4179 0.0066  0.0416  0.0807  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.1781 0.2012 0.3468 0.0143  0.0590  0.0518  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.1718 0.1893 0.3259 0.0144  0.0583  0.0443  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.1960 0.2077 0.3398 0.0157  0.0636  0.0385  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.2109 0.2205 0.3603 0.0177  0.0710  0.0384  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.1711 0.1870 0.3308 0.0156  0.0601  0.0427  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.1822 0.1931 0.3294 0.0154  0.0587  0.0354  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.1896 0.2026 0.3280 0.0132  0.0509  0.0356  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.2013 0.2101 0.3558 0.0166  0.0615  0.0338  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.1910 0.1998 0.3196 0.0146  0.0600  0.0339  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.2052 0.2079 0.3216 0.0158  0.0639  0.0280  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.2097 0.2079 0.3181 0.0162  0.0632  0.0211  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2205 0.2132 0.3252 0.0178  0.0684  0.0162  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.2021 0.2048 0.3072 0.0145  0.0603  0.0281  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2399 0.2361 0.3305 0.0157  0.0634  0.0219  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.1949 0.2016 0.3084 0.0137  0.0614  0.0346  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.1770 0.1772 0.2826 0.0147  0.0567  0.0206  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.1885 0.1851 0.2876 0.0147  0.0553  0.0145  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.1775 0.1779 0.2795 0.0132  0.0494  0.0165  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1707 0.1751 0.2725 0.0120  0.0452  0.0208  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.2081 0.2007 0.2911 0.0147  0.0538  0.0092  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.2171 0.2073 0.2927 0.0142  0.0503  0.0034  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2466 0.2321 0.3198 0.0147  0.0525  -0.0025 33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.1956 0.1882 0.2660 0.0129  0.0438  0.0031  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2500 0.2352 0.3172 0.0137  0.0473  -0.0064 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.2090 0.1988 0.2749 0.0128  0.0423  -0.0028 33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.1887 0.1852 0.2582 0.0119  0.0393  0.0073  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.2186 0.2100 0.2797 0.0119  0.0367  -0.0043 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.2068 0.2041 0.2703 0.0112  0.0343  0.0053  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.2074 0.2026 0.2680 0.0113  0.0332  0.0000  33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1680 0.1670 0.2724 0.0132  0.0493  0.0134  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.1679 0.1700 0.2742 0.0120  0.0444  0.0151  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1722 0.1714 0.2758 0.0118  0.0439  0.0093  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.1772 0.1722 0.2820 0.0125  0.0477  0.0049  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.1713 0.1774 0.2907 0.0120  0.0448  0.0215  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.1930 0.1972 0.3236 0.0133  0.0505  0.0216  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.2268 0.2284 0.3610 0.0133  0.0513  0.0182  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2410 0.2387 0.3807 0.0144  0.0565  0.0155  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.2002 0.2035 0.3321 0.0121  0.0472  0.0182  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1595 0.1608 0.2601 0.0107  0.0392  0.0092  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1572 0.1567 0.2572 0.0103  0.0382  0.0043  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1540 0.1573 0.2579 0.0094  0.0350  0.0076  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1535 0.1590 0.2509 0.0090  0.0313  0.0090  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.1807 0.1775 0.2683 0.0102  0.0360  -0.0013 35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2386 0.2337 0.3253 0.0095  0.0341  -0.0069 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2520 0.2496 0.3453 0.0087  0.0326  -0.0055 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.2779 0.2695 0.3563 0.0095  0.0335  -0.0123 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1518 0.1553 0.2660 0.0093  0.0369  0.0089  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1497 0.1565 0.2681 0.0086  0.0349  0.0125  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1531 0.1600 0.2711 0.0086  0.0348  0.0126  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1539 0.1610 0.2665 0.0079  0.0317  0.0088  36  SER   C C   
1338 O O   . SER   B 30  ? 0.1477 0.1576 0.2581 0.0077  0.0294  0.0117  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.1610 0.1672 0.2919 0.0087  0.0382  0.0143  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.1756 0.1825 0.3062 0.0087  0.0379  0.0154  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.1656 0.1741 0.3000 0.0080  0.0368  0.0168  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.1954 0.1982 0.3296 0.0085  0.0404  0.0097  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1604 0.1646 0.2708 0.0076  0.0317  0.0023  37  SER   C N   
1344 C CA  . SER   B 31  ? 0.1742 0.1794 0.2809 0.0069  0.0283  -0.0010 37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1571 0.1640 0.2532 0.0074  0.0249  -0.0003 37  SER   C C   
1346 O O   . SER   B 31  ? 0.1610 0.1699 0.2557 0.0073  0.0223  -0.0009 37  SER   C O   
1347 C CB  . SER   B 31  ? 0.2119 0.2136 0.3177 0.0063  0.0280  -0.0081 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.2861 0.2850 0.3814 0.0068  0.0271  -0.0117 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1534 0.1593 0.2428 0.0081  0.0251  0.0010  38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1444 0.1512 0.2240 0.0085  0.0221  0.0019  38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1309 0.1400 0.2107 0.0085  0.0216  0.0079  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1364 0.1457 0.2085 0.0086  0.0193  0.0090  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.1668 0.1707 0.2384 0.0091  0.0226  -0.0005 38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.1834 0.1843 0.2515 0.0091  0.0222  -0.0067 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.1624 0.1598 0.2215 0.0098  0.0234  -0.0086 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.1554 0.1534 0.2053 0.0104  0.0207  -0.0070 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.1710 0.1663 0.2109 0.0111  0.0199  -0.0094 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.1900 0.1814 0.2261 0.0113  0.0216  -0.0138 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.1693 0.1650 0.2020 0.0116  0.0173  -0.0077 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1170 0.1274 0.2051 0.0082  0.0238  0.0120  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1190 0.1312 0.2070 0.0079  0.0229  0.0178  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1270 0.1385 0.2096 0.0078  0.0222  0.0188  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1251 0.1375 0.2030 0.0073  0.0197  0.0219  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1257 0.1394 0.2097 0.0077  0.0205  0.0197  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1372 0.1522 0.2203 0.0072  0.0192  0.0255  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1508 0.1670 0.2413 0.0070  0.0205  0.0293  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1374 0.1521 0.2126 0.0070  0.0168  0.0263  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1190 0.1286 0.2025 0.0083  0.0247  0.0165  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1300 0.1391 0.2096 0.0083  0.0247  0.0179  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1332 0.1426 0.2214 0.0086  0.0284  0.0205  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1467 0.1549 0.2411 0.0093  0.0318  0.0184  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1399 0.1460 0.2102 0.0088  0.0247  0.0132  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1508 0.1563 0.2117 0.0088  0.0209  0.0113  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.1714 0.1739 0.2237 0.0096  0.0210  0.0072  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1595 0.1662 0.2170 0.0080  0.0182  0.0153  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1206 0.1316 0.2096 0.0080  0.0278  0.0245  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1257 0.1374 0.2234 0.0085  0.0316  0.0273  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1344 0.1461 0.2276 0.0080  0.0310  0.0288  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1464 0.1589 0.2340 0.0067  0.0268  0.0305  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1324 0.1479 0.2412 0.0081  0.0310  0.0332  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1301 0.1472 0.2505 0.0089  0.0349  0.0370  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1546 0.1737 0.2869 0.0095  0.0362  0.0406  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1395 0.1596 0.2611 0.0076  0.0324  0.0418  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1385 0.1487 0.2342 0.0090  0.0358  0.0281  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1421 0.1521 0.2353 0.0086  0.0365  0.0299  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1439 0.1566 0.2502 0.0090  0.0404  0.0346  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1493 0.1608 0.2619 0.0107  0.0456  0.0334  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1552 0.1604 0.2376 0.0098  0.0392  0.0247  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.1764 0.1812 0.2565 0.0095  0.0406  0.0271  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1774 0.1806 0.2482 0.0096  0.0349  0.0204  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1464 0.1625 0.2569 0.0075  0.0379  0.0398  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1422 0.1618 0.2664 0.0077  0.0411  0.0451  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1567 0.1759 0.2791 0.0071  0.0427  0.0465  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1599 0.1767 0.2711 0.0060  0.0400  0.0444  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1569 0.1819 0.2908 0.0061  0.0361  0.0512  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.1651 0.1909 0.2919 0.0035  0.0293  0.0524  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1590 0.1806 0.2936 0.0078  0.0476  0.0504  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1828 0.2046 0.3182 0.0072  0.0500  0.0526  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.1991 0.2262 0.3425 0.0041  0.0440  0.0589  44  SER   C C   
1400 O O   . SER   B 38  ? 0.2058 0.2376 0.3588 0.0031  0.0400  0.0629  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.2096 0.2307 0.3538 0.0098  0.0591  0.0535  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2445 0.2712 0.4063 0.0101  0.0598  0.0589  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.1988 0.2250 0.3381 0.0025  0.0433  0.0598  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.2154 0.2458 0.3612 -0.0010 0.0373  0.0650  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2436 0.2762 0.4000 -0.0013 0.0420  0.0694  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2392 0.2681 0.3915 0.0007  0.0492  0.0673  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2259 0.2526 0.3569 -0.0032 0.0309  0.0621  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2382 0.2599 0.3594 -0.0023 0.0350  0.0592  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2201 0.2445 0.3403 -0.0027 0.0267  0.0579  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2596 0.2978 0.4285 -0.0043 0.0375  0.0754  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2744 0.3153 0.4547 -0.0053 0.0411  0.0801  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.2825 0.3191 0.4516 -0.0075 0.0390  0.0785  46  THR   C C   
1413 O O   . THR   B 40  ? 0.3143 0.3487 0.4830 -0.0066 0.0455  0.0787  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3131 0.3623 0.5129 -0.0076 0.0368  0.0874  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3590 0.4090 0.5537 -0.0113 0.0262  0.0878  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.3010 0.3541 0.5122 -0.0049 0.0395  0.0894  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.2640 0.2990 0.4238 -0.0104 0.0304  0.0768  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.2733 0.3036 0.4226 -0.0126 0.0279  0.0752  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.2686 0.2915 0.3990 -0.0100 0.0305  0.0687  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2643 0.2860 0.3877 -0.0078 0.0304  0.0648  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.2917 0.3228 0.4392 -0.0168 0.0176  0.0762  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.2596 0.2780 0.3822 -0.0103 0.0325  0.0677  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.2814 0.2930 0.3863 -0.0080 0.0341  0.0622  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2871 0.2960 0.3813 -0.0098 0.0261  0.0592  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.3235 0.3329 0.4205 -0.0134 0.0203  0.0615  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3488 0.3564 0.4495 -0.0076 0.0394  0.0630  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4536 0.4615 0.5584 -0.0044 0.0490  0.0638  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.5816 0.5849 0.6800 -0.0037 0.0544  0.0647  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6301 0.6342 0.7354 -0.0063 0.0542  0.0690  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.6096 0.6077 0.6946 -0.0002 0.0593  0.0607  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2483 0.2540 0.3306 -0.0073 0.0258  0.0541  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2438 0.2464 0.3152 -0.0082 0.0195  0.0509  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2501 0.2465 0.3091 -0.0077 0.0197  0.0486  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2783 0.2725 0.3351 -0.0061 0.0251  0.0489  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2397 0.2331 0.2903 -0.0086 0.0144  0.0464  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2657 0.2531 0.3057 -0.0083 0.0141  0.0448  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2669 0.2508 0.2946 -0.0056 0.0131  0.0401  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.2978 0.2767 0.3169 -0.0049 0.0127  0.0390  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.2935 0.2788 0.3349 -0.0121 0.0092  0.0468  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.4281 0.4169 0.4846 -0.0155 0.0107  0.0529  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.2121 0.1985 0.2394 -0.0039 0.0128  0.0376  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.2027 0.1867 0.2200 -0.0015 0.0115  0.0333  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2136 0.1960 0.2258 0.0015  0.0159  0.0315  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2354 0.2196 0.2523 0.0021  0.0203  0.0326  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.2148 0.2024 0.2351 -0.0010 0.0099  0.0317  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2609 0.2494 0.2834 -0.0035 0.0053  0.0331  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.2748 0.2595 0.2924 -0.0051 0.0022  0.0333  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2219 0.2144 0.2505 -0.0039 0.0046  0.0339  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.2035 0.1824 0.2058 0.0034  0.0146  0.0288  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.2004 0.1775 0.1958 0.0062  0.0175  0.0267  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.2048 0.1834 0.1975 0.0080  0.0156  0.0226  52  THR   C C   
1452 O O   . THR   B 46  ? 0.2122 0.1907 0.2033 0.0079  0.0120  0.0215  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2284 0.2004 0.2150 0.0071  0.0168  0.0272  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.2647 0.2351 0.2547 0.0051  0.0189  0.0312  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.2602 0.2302 0.2379 0.0101  0.0185  0.0250  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.1991 0.1789 0.1915 0.0096  0.0181  0.0204  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.1980 0.1793 0.1888 0.0111  0.0163  0.0164  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.1864 0.1647 0.1670 0.0132  0.0145  0.0144  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2074 0.1827 0.1814 0.0142  0.0164  0.0148  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.2029 0.1859 0.1973 0.0116  0.0196  0.0145  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.2010 0.1870 0.2062 0.0100  0.0220  0.0172  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.2071 0.1917 0.2012 0.0126  0.0174  0.0105  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2201 0.2092 0.2317 0.0084  0.0183  0.0185  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.1781 0.1572 0.1576 0.0139  0.0109  0.0125  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.1795 0.1568 0.1511 0.0161  0.0086  0.0108  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.1838 0.1615 0.1522 0.0173  0.0093  0.0076  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.1863 0.1665 0.1599 0.0168  0.0103  0.0054  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.1724 0.1515 0.1460 0.0167  0.0051  0.0095  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.1834 0.1580 0.1424 0.0191  0.0087  0.0074  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.1919 0.1659 0.1452 0.0202  0.0085  0.0040  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.1930 0.1667 0.1405 0.0221  0.0036  0.0031  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2151 0.1856 0.1548 0.0235  0.0030  0.0053  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.2012 0.1713 0.1477 0.0206  0.0130  0.0049  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.1856 0.1566 0.1399 0.0189  0.0180  0.0066  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2134 0.1873 0.1752 0.0181  0.0189  0.0035  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2161 0.1908 0.1859 0.0168  0.0239  0.0058  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.2150 0.1928 0.1946 0.0158  0.0250  0.0050  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.1971 0.1769 0.1793 0.0158  0.0221  0.0016  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2286 0.2075 0.2161 0.0148  0.0291  0.0079  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.1824 0.1598 0.1352 0.0222  0.0001  0.0006  56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.1824 0.1609 0.1335 0.0239  -0.0046 0.0005  56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.1794 0.1626 0.1385 0.0236  -0.0073 -0.0026 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.1915 0.1766 0.1570 0.0219  -0.0053 -0.0043 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.1703 0.1477 0.1233 0.0242  -0.0044 0.0040  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.1867 0.1674 0.1511 0.0224  -0.0032 0.0042  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.1970 0.1822 0.1567 0.0252  -0.0116 -0.0027 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.1996 0.1897 0.1684 0.0250  -0.0141 -0.0048 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.1976 0.1893 0.1718 0.0262  -0.0147 -0.0024 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2064 0.2020 0.1867 0.0271  -0.0175 -0.0033 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2311 0.2230 0.1979 0.0257  -0.0190 -0.0077 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.2832 0.2741 0.2434 0.0281  -0.0229 -0.0058 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.2726 0.2609 0.2296 0.0295  -0.0215 -0.0023 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.3768 0.3696 0.3354 0.0287  -0.0278 -0.0078 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.1945 0.1831 0.1669 0.0261  -0.0118 0.0005  58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.1819 0.1708 0.1584 0.0272  -0.0116 0.0022  58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.1733 0.1667 0.1595 0.0265  -0.0112 0.0009  58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.1755 0.1707 0.1658 0.0245  -0.0097 -0.0005 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.1867 0.1713 0.1602 0.0263  -0.0086 0.0047  58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.1983 0.1769 0.1617 0.0274  -0.0086 0.0074  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1615 0.1565 0.1517 0.0284  -0.0120 0.0017  59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.1605 0.1590 0.1595 0.0282  -0.0107 0.0013  59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1623 0.1580 0.1606 0.0292  -0.0082 0.0032  59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1613 0.1593 0.1659 0.0299  -0.0067 0.0034  59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.1673 0.1712 0.1740 0.0295  -0.0136 -0.0001 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2135 0.2204 0.2227 0.0277  -0.0159 -0.0030 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2468 0.2594 0.2656 0.0282  -0.0189 -0.0043 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.2741 0.2881 0.2914 0.0289  -0.0234 -0.0054 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2089 0.2248 0.2374 0.0279  -0.0165 -0.0040 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1620 0.1522 0.1526 0.0294  -0.0074 0.0048  60  THR   C N   
1510 C CA  . THR   B 54  ? 0.1761 0.1622 0.1646 0.0297  -0.0050 0.0061  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1741 0.1559 0.1568 0.0272  -0.0038 0.0070  60  THR   C C   
1512 O O   . THR   B 54  ? 0.1801 0.1606 0.1589 0.0263  -0.0047 0.0074  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2119 0.1949 0.1981 0.0328  -0.0054 0.0073  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2582 0.2379 0.2381 0.0331  -0.0070 0.0083  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2120 0.2001 0.2055 0.0355  -0.0069 0.0069  60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1581 0.1375 0.1400 0.0259  -0.0019 0.0075  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1595 0.1352 0.1371 0.0231  -0.0014 0.0086  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1479 0.1208 0.1238 0.0221  0.0001  0.0089  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1732 0.1452 0.1492 0.0240  0.0012  0.0084  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1583 0.1295 0.1324 0.0191  -0.0001 0.0098  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1563 0.1243 0.1273 0.0176  0.0005  0.0102  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1606 0.1323 0.1354 0.0149  0.0002  0.0113  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1669 0.1404 0.1442 0.0132  -0.0005 0.0122  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1686 0.1293 0.1325 0.0163  -0.0005 0.0107  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1911 0.1478 0.1503 0.0140  -0.0008 0.0108  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1846 0.1410 0.1449 0.0193  0.0001  0.0100  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1582 0.1308 0.1335 0.0145  0.0011  0.0115  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1452 0.1211 0.1243 0.0120  0.0007  0.0132  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1556 0.1275 0.1288 0.0099  -0.0003 0.0143  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1734 0.1408 0.1402 0.0111  0.0005  0.0133  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1468 0.1287 0.1337 0.0130  0.0024  0.0131  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1433 0.1251 0.1293 0.0140  0.0043  0.0133  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1733 0.1540 0.1581 0.0168  0.0061  0.0119  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1488 0.1320 0.1361 0.0125  0.0046  0.0154  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1788 0.1593 0.1631 0.0180  0.0087  0.0123  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1652 0.1481 0.1511 0.0136  0.0069  0.0159  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1750 0.1565 0.1594 0.0163  0.0093  0.0143  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.2009 0.1819 0.1841 0.0177  0.0125  0.0150  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1555 0.1294 0.1313 0.0071  -0.0020 0.0165  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1695 0.1402 0.1397 0.0048  -0.0038 0.0179  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1651 0.1390 0.1374 0.0052  -0.0025 0.0192  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1645 0.1442 0.1454 0.0050  -0.0019 0.0208  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1765 0.1477 0.1489 0.0014  -0.0070 0.0201  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1881 0.1557 0.1539 -0.0013 -0.0100 0.0213  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1998 0.1597 0.1547 -0.0015 -0.0108 0.0193  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1882 0.1595 0.1580 -0.0035 -0.0121 0.0245  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.2189 0.1746 0.1658 -0.0040 -0.0139 0.0199  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.2066 0.1744 0.1692 -0.0060 -0.0156 0.0257  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.2153 0.1751 0.1660 -0.0064 -0.0166 0.0232  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2706 0.2263 0.2125 -0.0091 -0.0204 0.0240  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1625 0.1321 0.1266 0.0057  -0.0019 0.0187  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1720 0.1432 0.1357 0.0061  -0.0003 0.0204  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1977 0.1653 0.1534 0.0032  -0.0036 0.0223  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.2094 0.1700 0.1537 0.0029  -0.0042 0.0208  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1676 0.1367 0.1278 0.0093  0.0038  0.0185  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.2025 0.1726 0.1610 0.0100  0.0067  0.0209  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.2093 0.1815 0.1711 0.0010  -0.0060 0.0257  66  SER   C N   
1558 C CA  . SER   B 60  ? 0.2239 0.1933 0.1789 -0.0021 -0.0103 0.0279  66  SER   C CA  
1559 C C   . SER   B 60  ? 0.2221 0.1873 0.1663 -0.0014 -0.0093 0.0284  66  SER   C C   
1560 O O   . SER   B 60  ? 0.2425 0.2017 0.1753 -0.0035 -0.0125 0.0280  66  SER   C O   
1561 C CB  . SER   B 60  ? 0.2578 0.2336 0.2230 -0.0040 -0.0129 0.0319  66  SER   C CB  
1562 O OG  . SER   B 60  ? 0.3691 0.3502 0.3418 -0.0024 -0.0100 0.0343  66  SER   C OG  
1563 N N   . SER   B 61  ? 0.2064 0.1743 0.1535 0.0014  -0.0046 0.0289  67  SER   C N   
1564 C CA  . SER   B 61  ? 0.2098 0.1738 0.1466 0.0023  -0.0024 0.0298  67  SER   C CA  
1565 C C   . SER   B 61  ? 0.2419 0.1976 0.1661 0.0038  -0.0002 0.0259  67  SER   C C   
1566 O O   . SER   B 61  ? 0.2727 0.2233 0.1855 0.0044  0.0016  0.0261  67  SER   C O   
1567 C CB  . SER   B 61  ? 0.2132 0.1826 0.1586 0.0048  0.0024  0.0318  67  SER   C CB  
1568 O OG  . SER   B 61  ? 0.2241 0.1953 0.1760 0.0077  0.0068  0.0290  67  SER   C OG  
1569 N N   . ARG   B 62  ? 0.2295 0.1831 0.1548 0.0045  0.0000  0.0224  68  ARG   C N   
1570 C CA  . ARG   B 62  ? 0.2413 0.1862 0.1549 0.0058  0.0018  0.0187  68  ARG   C CA  
1571 C C   . ARG   B 62  ? 0.2503 0.1896 0.1582 0.0029  -0.0030 0.0167  68  ARG   C C   
1572 O O   . ARG   B 62  ? 0.2682 0.1995 0.1669 0.0038  -0.0018 0.0134  68  ARG   C O   
1573 C CB  . ARG   B 62  ? 0.2429 0.1895 0.1629 0.0098  0.0070  0.0166  68  ARG   C CB  
1574 C CG  . ARG   B 62  ? 0.2974 0.2491 0.2238 0.0126  0.0122  0.0183  68  ARG   C CG  
1575 C CD  . ARG   B 62  ? 0.3110 0.2562 0.2253 0.0142  0.0161  0.0180  68  ARG   C CD  
1576 N NE  . ARG   B 62  ? 0.3290 0.2793 0.2503 0.0168  0.0217  0.0202  68  ARG   C NE  
1577 C CZ  . ARG   B 62  ? 0.3711 0.3247 0.2939 0.0160  0.0220  0.0238  68  ARG   C CZ  
1578 N NH1 . ARG   B 62  ? 0.4140 0.3668 0.3317 0.0127  0.0169  0.0260  68  ARG   C NH1 
1579 N NH2 . ARG   B 62  ? 0.3578 0.3151 0.2868 0.0184  0.0277  0.0257  68  ARG   C NH2 
1580 N N   . ARG   B 63  ? 0.2586 0.2023 0.1736 -0.0002 -0.0080 0.0187  69  ARG   C N   
1581 C CA  . ARG   B 63  ? 0.2802 0.2201 0.1935 -0.0032 -0.0125 0.0174  69  ARG   C CA  
1582 C C   . ARG   B 63  ? 0.2854 0.2216 0.1987 -0.0009 -0.0096 0.0140  69  ARG   C C   
1583 O O   . ARG   B 63  ? 0.3082 0.2363 0.2129 -0.0019 -0.0110 0.0115  69  ARG   C O   
1584 C CB  . ARG   B 63  ? 0.3041 0.2360 0.2036 -0.0064 -0.0168 0.0167  69  ARG   C CB  
1585 C CG  . ARG   B 63  ? 0.3656 0.3012 0.2658 -0.0096 -0.0215 0.0206  69  ARG   C CG  
1586 C CD  . ARG   B 63  ? 0.5084 0.4373 0.3997 -0.0140 -0.0279 0.0195  69  ARG   C CD  
1587 N NE  . ARG   B 63  ? 0.6033 0.5350 0.4941 -0.0174 -0.0337 0.0233  69  ARG   C NE  
1588 C CZ  . ARG   B 63  ? 0.6796 0.6056 0.5561 -0.0188 -0.0362 0.0233  69  ARG   C CZ  
1589 N NH1 . ARG   B 63  ? 0.6817 0.5988 0.5434 -0.0167 -0.0324 0.0195  69  ARG   C NH1 
1590 N NH2 . ARG   B 63  ? 0.6794 0.6087 0.5564 -0.0220 -0.0424 0.0273  69  ARG   C NH2 
1591 N N   . LYS   B 64  ? 0.2515 0.1935 0.1744 0.0024  -0.0058 0.0140  70  LYS   C N   
1592 C CA  . LYS   B 64  ? 0.2519 0.1910 0.1750 0.0052  -0.0031 0.0114  70  LYS   C CA  
1593 C C   . LYS   B 64  ? 0.2264 0.1728 0.1617 0.0065  -0.0023 0.0122  70  LYS   C C   
1594 O O   . LYS   B 64  ? 0.2271 0.1811 0.1710 0.0068  -0.0018 0.0141  70  LYS   C O   
1595 C CB  . LYS   B 64  ? 0.3011 0.2377 0.2198 0.0090  0.0021  0.0099  70  LYS   C CB  
1596 C CG  . LYS   B 64  ? 0.4402 0.3660 0.3441 0.0088  0.0027  0.0074  70  LYS   C CG  
1597 C CD  . LYS   B 64  ? 0.5502 0.4730 0.4506 0.0131  0.0089  0.0058  70  LYS   C CD  
1598 C CE  . LYS   B 64  ? 0.6172 0.5286 0.5018 0.0129  0.0100  0.0032  70  LYS   C CE  
1599 N NZ  . LYS   B 64  ? 0.6726 0.5827 0.5486 0.0101  0.0077  0.0046  70  LYS   C NZ  
1600 N N   . HIS   B 65  ? 0.2104 0.1540 0.1458 0.0074  -0.0023 0.0107  71  HIS   C N   
1601 C CA  . HIS   B 65  ? 0.2054 0.1548 0.1502 0.0092  -0.0014 0.0110  71  HIS   C CA  
1602 C C   . HIS   B 65  ? 0.2307 0.1794 0.1757 0.0135  0.0022  0.0093  71  HIS   C C   
1603 O O   . HIS   B 65  ? 0.2861 0.2278 0.2241 0.0149  0.0035  0.0076  71  HIS   C O   
1604 C CB  . HIS   B 65  ? 0.2128 0.1596 0.1578 0.0076  -0.0037 0.0112  71  HIS   C CB  
1605 C CG  . HIS   B 65  ? 0.1933 0.1416 0.1405 0.0035  -0.0071 0.0132  71  HIS   C CG  
1606 N ND1 . HIS   B 65  ? 0.2349 0.1898 0.1910 0.0027  -0.0075 0.0152  71  HIS   C ND1 
1607 C CD2 . HIS   B 65  ? 0.1982 0.1422 0.1401 0.0000  -0.0102 0.0137  71  HIS   C CD2 
1608 C CE1 . HIS   B 65  ? 0.2147 0.1695 0.1719 -0.0010 -0.0105 0.0171  71  HIS   C CE1 
1609 N NE2 . HIS   B 65  ? 0.2335 0.1821 0.1826 -0.0029 -0.0127 0.0163  71  HIS   C NE2 
1610 N N   . TYR   B 66  ? 0.1946 0.1506 0.1481 0.0156  0.0040  0.0098  72  TYR   C N   
1611 C CA  . TYR   B 66  ? 0.1893 0.1457 0.1448 0.0195  0.0072  0.0086  72  TYR   C CA  
1612 C C   . TYR   B 66  ? 0.1795 0.1400 0.1418 0.0212  0.0064  0.0084  72  TYR   C C   
1613 O O   . TYR   B 66  ? 0.1793 0.1454 0.1477 0.0200  0.0049  0.0091  72  TYR   C O   
1614 C CB  . TYR   B 66  ? 0.1990 0.1610 0.1601 0.0205  0.0097  0.0094  72  TYR   C CB  
1615 C CG  . TYR   B 66  ? 0.2033 0.1615 0.1573 0.0199  0.0115  0.0098  72  TYR   C CG  
1616 C CD1 . TYR   B 66  ? 0.2221 0.1745 0.1695 0.0223  0.0149  0.0085  72  TYR   C CD1 
1617 C CD2 . TYR   B 66  ? 0.2205 0.1809 0.1743 0.0171  0.0102  0.0117  72  TYR   C CD2 
1618 C CE1 . TYR   B 66  ? 0.2479 0.1962 0.1871 0.0219  0.0170  0.0088  72  TYR   C CE1 
1619 C CE2 . TYR   B 66  ? 0.2383 0.1950 0.1844 0.0167  0.0117  0.0124  72  TYR   C CE2 
1620 C CZ  . TYR   B 66  ? 0.2582 0.2087 0.1963 0.0190  0.0151  0.0108  72  TYR   C CZ  
1621 O OH  . TYR   B 66  ? 0.2826 0.2290 0.2116 0.0184  0.0168  0.0116  72  TYR   C OH  
1622 N N   . PRO   B 67  ? 0.1847 0.1422 0.1457 0.0241  0.0073  0.0075  73  PRO   C N   
1623 C CA  . PRO   B 67  ? 0.1823 0.1442 0.1495 0.0261  0.0063  0.0076  73  PRO   C CA  
1624 C C   . PRO   B 67  ? 0.1807 0.1499 0.1568 0.0280  0.0076  0.0075  73  PRO   C C   
1625 O O   . PRO   B 67  ? 0.2205 0.1894 0.1975 0.0297  0.0106  0.0073  73  PRO   C O   
1626 C CB  . PRO   B 67  ? 0.2087 0.1648 0.1720 0.0289  0.0070  0.0071  73  PRO   C CB  
1627 C CG  . PRO   B 67  ? 0.2516 0.2011 0.2082 0.0292  0.0097  0.0062  73  PRO   C CG  
1628 C CD  . PRO   B 67  ? 0.2130 0.1627 0.1667 0.0258  0.0095  0.0064  73  PRO   C CD  
1629 N N   . VAL   B 68  ? 0.1598 0.1350 0.1423 0.0275  0.0057  0.0075  74  VAL   C N   
1630 C CA  . VAL   B 68  ? 0.1684 0.1507 0.1603 0.0286  0.0064  0.0072  74  VAL   C CA  
1631 C C   . VAL   B 68  ? 0.1554 0.1419 0.1520 0.0295  0.0036  0.0066  74  VAL   C C   
1632 O O   . VAL   B 68  ? 0.1607 0.1458 0.1536 0.0286  0.0013  0.0066  74  VAL   C O   
1633 C CB  . VAL   B 68  ? 0.1775 0.1633 0.1729 0.0258  0.0069  0.0077  74  VAL   C CB  
1634 C CG1 . VAL   B 68  ? 0.2043 0.1872 0.1960 0.0253  0.0097  0.0086  74  VAL   C CG1 
1635 C CG2 . VAL   B 68  ? 0.1932 0.1788 0.1865 0.0231  0.0045  0.0078  74  VAL   C CG2 
1636 N N   . SER   B 69  ? 0.1571 0.1490 0.1622 0.0313  0.0037  0.0062  75  SER   C N   
1637 C CA  . SER   B 69  ? 0.1597 0.1570 0.1709 0.0315  0.0007  0.0052  75  SER   C CA  
1638 C C   . SER   B 69  ? 0.1452 0.1468 0.1624 0.0290  0.0010  0.0045  75  SER   C C   
1639 O O   . SER   B 69  ? 0.1429 0.1456 0.1636 0.0284  0.0039  0.0052  75  SER   C O   
1640 C CB  . SER   B 69  ? 0.1794 0.1806 0.1985 0.0345  0.0005  0.0054  75  SER   C CB  
1641 O OG  . SER   B 69  ? 0.2576 0.2544 0.2717 0.0372  0.0003  0.0064  75  SER   C OG  
1642 N N   . PHE   B 70  ? 0.1368 0.1402 0.1544 0.0275  -0.0016 0.0032  76  PHE   C N   
1643 C CA  . PHE   B 70  ? 0.1294 0.1360 0.1525 0.0251  -0.0011 0.0022  76  PHE   C CA  
1644 C C   . PHE   B 70  ? 0.1350 0.1453 0.1627 0.0248  -0.0043 -0.0001 76  PHE   C C   
1645 O O   . PHE   B 70  ? 0.1415 0.1511 0.1650 0.0259  -0.0073 -0.0008 76  PHE   C O   
1646 C CB  . PHE   B 70  ? 0.1390 0.1424 0.1567 0.0227  0.0001  0.0030  76  PHE   C CB  
1647 C CG  . PHE   B 70  ? 0.1348 0.1347 0.1447 0.0224  -0.0016 0.0028  76  PHE   C CG  
1648 C CD1 . PHE   B 70  ? 0.1457 0.1409 0.1481 0.0231  -0.0014 0.0042  76  PHE   C CD1 
1649 C CD2 . PHE   B 70  ? 0.1406 0.1415 0.1505 0.0214  -0.0029 0.0012  76  PHE   C CD2 
1650 C CE1 . PHE   B 70  ? 0.1488 0.1409 0.1448 0.0228  -0.0026 0.0045  76  PHE   C CE1 
1651 C CE2 . PHE   B 70  ? 0.1443 0.1417 0.1466 0.0213  -0.0036 0.0014  76  PHE   C CE2 
1652 C CZ  . PHE   B 70  ? 0.1521 0.1455 0.1481 0.0220  -0.0035 0.0032  76  PHE   C CZ  
1653 N N   . SER   B 71  ? 0.1268 0.1408 0.1628 0.0233  -0.0037 -0.0012 77  SER   C N   
1654 C CA  . SER   B 71  ? 0.1414 0.1589 0.1828 0.0226  -0.0070 -0.0039 77  SER   C CA  
1655 C C   . SER   B 71  ? 0.1568 0.1717 0.1919 0.0211  -0.0083 -0.0060 77  SER   C C   
1656 O O   . SER   B 71  ? 0.1648 0.1760 0.1932 0.0204  -0.0064 -0.0049 77  SER   C O   
1657 C CB  . SER   B 71  ? 0.1300 0.1519 0.1835 0.0215  -0.0056 -0.0043 77  SER   C CB  
1658 O OG  . SER   B 71  ? 0.1638 0.1845 0.2183 0.0196  -0.0024 -0.0037 77  SER   C OG  
1659 N N   . LYS   B 72  ? 0.1765 0.1932 0.2137 0.0205  -0.0117 -0.0089 78  LYS   C N   
1660 C CA  . LYS   B 72  ? 0.1781 0.1917 0.2083 0.0192  -0.0126 -0.0114 78  LYS   C CA  
1661 C C   . LYS   B 72  ? 0.1627 0.1762 0.1982 0.0170  -0.0095 -0.0124 78  LYS   C C   
1662 O O   . LYS   B 72  ? 0.1805 0.1971 0.2261 0.0162  -0.0084 -0.0123 78  LYS   C O   
1663 C CB  . LYS   B 72  ? 0.2314 0.2465 0.2611 0.0192  -0.0178 -0.0146 78  LYS   C CB  
1664 C CG  . LYS   B 72  ? 0.2866 0.3023 0.3121 0.0217  -0.0213 -0.0131 78  LYS   C CG  
1665 C CD  . LYS   B 72  ? 0.4429 0.4587 0.4636 0.0216  -0.0269 -0.0159 78  LYS   C CD  
1666 C CE  . LYS   B 72  ? 0.5498 0.5644 0.5627 0.0243  -0.0299 -0.0137 78  LYS   C CE  
1667 N NZ  . LYS   B 72  ? 0.6026 0.6150 0.6058 0.0241  -0.0344 -0.0161 78  LYS   C NZ  
1668 N N   . PRO   B 73  ? 0.1653 0.1750 0.1949 0.0161  -0.0075 -0.0130 79  PRO   C N   
1669 C CA  . PRO   B 73  ? 0.1649 0.1743 0.2004 0.0143  -0.0040 -0.0133 79  PRO   C CA  
1670 C C   . PRO   B 73  ? 0.1788 0.1901 0.2222 0.0129  -0.0053 -0.0168 79  PRO   C C   
1671 O O   . PRO   B 73  ? 0.2096 0.2199 0.2494 0.0126  -0.0087 -0.0206 79  PRO   C O   
1672 C CB  . PRO   B 73  ? 0.1862 0.1913 0.2138 0.0140  -0.0020 -0.0136 79  PRO   C CB  
1673 C CG  . PRO   B 73  ? 0.2243 0.2274 0.2415 0.0156  -0.0039 -0.0128 79  PRO   C CG  
1674 C CD  . PRO   B 73  ? 0.1739 0.1796 0.1919 0.0169  -0.0079 -0.0128 79  PRO   C CD  
1675 N N   . SER   B 74  ? 0.1534 0.1670 0.2073 0.0118  -0.0030 -0.0158 80  SER   C N   
1676 C CA  . SER   B 74  ? 0.1603 0.1759 0.2236 0.0103  -0.0044 -0.0189 80  SER   C CA  
1677 C C   . SER   B 74  ? 0.1601 0.1762 0.2331 0.0090  -0.0002 -0.0174 80  SER   C C   
1678 O O   . SER   B 74  ? 0.1574 0.1727 0.2295 0.0094  0.0032  -0.0138 80  SER   C O   
1679 C CB  . SER   B 74  ? 0.2163 0.2368 0.2860 0.0109  -0.0074 -0.0184 80  SER   C CB  
1680 O OG  . SER   B 74  ? 0.3124 0.3328 0.3742 0.0125  -0.0113 -0.0190 80  SER   C OG  
1681 N N   . LEU   B 75  ? 0.1641 0.1813 0.2465 0.0073  -0.0008 -0.0202 81  LEU   C N   
1682 C CA  . LEU   B 75  ? 0.1789 0.1964 0.2719 0.0060  0.0030  -0.0188 81  LEU   C CA  
1683 C C   . LEU   B 75  ? 0.1740 0.1963 0.2759 0.0064  0.0037  -0.0153 81  LEU   C C   
1684 O O   . LEU   B 75  ? 0.1936 0.2192 0.3018 0.0058  0.0007  -0.0171 81  LEU   C O   
1685 C CB  . LEU   B 75  ? 0.2096 0.2250 0.3080 0.0038  0.0020  -0.0240 81  LEU   C CB  
1686 C CG  . LEU   B 75  ? 0.2412 0.2556 0.3504 0.0024  0.0061  -0.0231 81  LEU   C CG  
1687 C CD1 . LEU   B 75  ? 0.2243 0.2353 0.3296 0.0031  0.0104  -0.0208 81  LEU   C CD1 
1688 C CD2 . LEU   B 75  ? 0.2688 0.2807 0.3831 0.0000  0.0043  -0.0291 81  LEU   C CD2 
1689 N N   . ILE   B 76  ? 0.1775 0.2003 0.2793 0.0073  0.0073  -0.0103 82  ILE   C N   
1690 C CA  . ILE   B 76  ? 0.1874 0.2138 0.2947 0.0082  0.0089  -0.0065 82  ILE   C CA  
1691 C C   . ILE   B 76  ? 0.1825 0.2092 0.2982 0.0074  0.0134  -0.0030 82  ILE   C C   
1692 O O   . ILE   B 76  ? 0.1781 0.2021 0.2914 0.0072  0.0155  -0.0013 82  ILE   C O   
1693 C CB  . ILE   B 76  ? 0.2130 0.2386 0.3097 0.0103  0.0091  -0.0035 82  ILE   C CB  
1694 C CG1 . ILE   B 76  ? 0.2454 0.2705 0.3338 0.0114  0.0050  -0.0062 82  ILE   C CG1 
1695 C CG2 . ILE   B 76  ? 0.2364 0.2644 0.3364 0.0115  0.0118  0.0005  82  ILE   C CG2 
1696 C CD1 . ILE   B 76  ? 0.2868 0.3156 0.3802 0.0121  0.0023  -0.0074 82  ILE   C CD1 
1697 N N   . PHE   B 77  ? 0.1704 0.2005 0.2967 0.0071  0.0148  -0.0014 83  PHE   C N   
1698 C CA  . PHE   B 77  ? 0.1792 0.2095 0.3131 0.0066  0.0193  0.0026  83  PHE   C CA  
1699 C C   . PHE   B 77  ? 0.1842 0.2141 0.3103 0.0084  0.0218  0.0077  83  PHE   C C   
1700 O O   . PHE   B 77  ? 0.2134 0.2447 0.3354 0.0100  0.0216  0.0087  83  PHE   C O   
1701 C CB  . PHE   B 77  ? 0.1790 0.2131 0.3270 0.0057  0.0205  0.0029  83  PHE   C CB  
1702 C CG  . PHE   B 77  ? 0.1973 0.2310 0.3534 0.0050  0.0253  0.0071  83  PHE   C CG  
1703 C CD1 . PHE   B 77  ? 0.2152 0.2462 0.3765 0.0033  0.0262  0.0060  83  PHE   C CD1 
1704 C CD2 . PHE   B 77  ? 0.2216 0.2569 0.3790 0.0063  0.0293  0.0126  83  PHE   C CD2 
1705 C CE1 . PHE   B 77  ? 0.2327 0.2631 0.4013 0.0030  0.0307  0.0106  83  PHE   C CE1 
1706 C CE2 . PHE   B 77  ? 0.2310 0.2656 0.3950 0.0058  0.0338  0.0171  83  PHE   C CE2 
1707 C CZ  . PHE   B 77  ? 0.2316 0.2640 0.4013 0.0042  0.0343  0.0163  83  PHE   C CZ  
1708 N N   . VAL   B 78  ? 0.1569 0.1845 0.2810 0.0082  0.0242  0.0110  84  VAL   C N   
1709 C CA  . VAL   B 78  ? 0.1598 0.1865 0.2755 0.0095  0.0258  0.0156  84  VAL   C CA  
1710 C C   . VAL   B 78  ? 0.1556 0.1829 0.2782 0.0093  0.0300  0.0207  84  VAL   C C   
1711 O O   . VAL   B 78  ? 0.1601 0.1867 0.2901 0.0081  0.0313  0.0214  84  VAL   C O   
1712 C CB  . VAL   B 78  ? 0.1703 0.1940 0.2767 0.0094  0.0242  0.0158  84  VAL   C CB  
1713 C CG1 . VAL   B 78  ? 0.1907 0.2130 0.2878 0.0103  0.0248  0.0203  84  VAL   C CG1 
1714 C CG2 . VAL   B 78  ? 0.1804 0.2030 0.2804 0.0095  0.0206  0.0111  84  VAL   C CG2 
1715 N N   . GLU   B 79  ? 0.1444 0.1721 0.2636 0.0106  0.0325  0.0245  85  GLU   C N   
1716 C CA  . GLU   B 79  ? 0.1597 0.1875 0.2832 0.0107  0.0367  0.0299  85  GLU   C CA  
1717 C C   . GLU   B 79  ? 0.1586 0.1840 0.2765 0.0104  0.0364  0.0335  85  GLU   C C   
1718 O O   . GLU   B 79  ? 0.1568 0.1806 0.2665 0.0103  0.0333  0.0321  85  GLU   C O   
1719 C CB  . GLU   B 79  ? 0.1797 0.2080 0.2990 0.0124  0.0398  0.0328  85  GLU   C CB  
1720 C CG  . GLU   B 79  ? 0.2034 0.2351 0.3320 0.0128  0.0408  0.0304  85  GLU   C CG  
1721 C CD  . GLU   B 79  ? 0.2743 0.3086 0.4194 0.0112  0.0428  0.0306  85  GLU   C CD  
1722 O OE1 . GLU   B 79  ? 0.3023 0.3357 0.4523 0.0104  0.0456  0.0343  85  GLU   C OE1 
1723 O OE2 . GLU   B 79  ? 0.3203 0.3576 0.4740 0.0107  0.0413  0.0269  85  GLU   C OE2 
1724 N N   . ALA   B 80  ? 0.1679 0.1933 0.2917 0.0101  0.0396  0.0383  86  ALA   C N   
1725 C CA  . ALA   B 80  ? 0.1798 0.2035 0.3002 0.0099  0.0392  0.0426  86  ALA   C CA  
1726 C C   . ALA   B 80  ? 0.1945 0.2164 0.2997 0.0106  0.0372  0.0447  86  ALA   C C   
1727 O O   . ALA   B 80  ? 0.2061 0.2274 0.3039 0.0117  0.0382  0.0451  86  ALA   C O   
1728 C CB  . ALA   B 80  ? 0.1964 0.2205 0.3249 0.0099  0.0434  0.0483  86  ALA   C CB  
1729 N N   . SER   B 81  ? 0.1787 0.1995 0.2799 0.0100  0.0342  0.0453  87  SER   C N   
1730 C CA  . SER   B 81  ? 0.1966 0.2155 0.2844 0.0102  0.0315  0.0474  87  SER   C CA  
1731 C C   . SER   B 81  ? 0.2025 0.2213 0.2907 0.0097  0.0309  0.0534  87  SER   C C   
1732 O O   . SER   B 81  ? 0.2040 0.2240 0.3033 0.0096  0.0331  0.0561  87  SER   C O   
1733 C CB  . SER   B 81  ? 0.1942 0.2125 0.2768 0.0098  0.0278  0.0427  87  SER   C CB  
1734 O OG  . SER   B 81  ? 0.1898 0.2089 0.2792 0.0089  0.0267  0.0427  87  SER   C OG  
1735 N N   . GLU   B 82  ? 0.2294 0.2465 0.3062 0.0094  0.0277  0.0557  88  GLU   C N   
1736 C CA  . GLU   B 82  ? 0.2411 0.2587 0.3191 0.0088  0.0262  0.0618  88  GLU   C CA  
1737 C C   . GLU   B 82  ? 0.2372 0.2567 0.3258 0.0082  0.0249  0.0615  88  GLU   C C   
1738 O O   . GLU   B 82  ? 0.2616 0.2823 0.3560 0.0081  0.0246  0.0668  88  GLU   C O   
1739 C CB  . GLU   B 82  ? 0.2948 0.3101 0.3583 0.0083  0.0224  0.0645  88  GLU   C CB  
1740 C CG  . GLU   B 82  ? 0.3927 0.4070 0.4489 0.0072  0.0179  0.0611  88  GLU   C CG  
1741 C CD  . GLU   B 82  ? 0.4625 0.4743 0.5056 0.0062  0.0138  0.0646  88  GLU   C CD  
1742 O OE1 . GLU   B 82  ? 0.4844 0.4936 0.5183 0.0069  0.0154  0.0666  88  GLU   C OE1 
1743 O OE2 . GLU   B 82  ? 0.4930 0.5055 0.5352 0.0047  0.0092  0.0656  88  GLU   C OE2 
1744 N N   . TYR   B 83  ? 0.1873 0.2071 0.2792 0.0080  0.0246  0.0557  89  TYR   C N   
1745 C CA  . TYR   B 83  ? 0.1845 0.2054 0.2846 0.0076  0.0239  0.0551  89  TYR   C CA  
1746 C C   . TYR   B 83  ? 0.1903 0.2115 0.3012 0.0078  0.0270  0.0506  89  TYR   C C   
1747 O O   . TYR   B 83  ? 0.1948 0.2162 0.3133 0.0078  0.0276  0.0505  89  TYR   C O   
1748 C CB  . TYR   B 83  ? 0.1906 0.2111 0.2831 0.0068  0.0200  0.0530  89  TYR   C CB  
1749 C CG  . TYR   B 83  ? 0.1830 0.2017 0.2659 0.0069  0.0191  0.0476  89  TYR   C CG  
1750 C CD1 . TYR   B 83  ? 0.2006 0.2174 0.2715 0.0068  0.0174  0.0483  89  TYR   C CD1 
1751 C CD2 . TYR   B 83  ? 0.1728 0.1913 0.2583 0.0072  0.0200  0.0418  89  TYR   C CD2 
1752 C CE1 . TYR   B 83  ? 0.1882 0.2033 0.2513 0.0073  0.0169  0.0436  89  TYR   C CE1 
1753 C CE2 . TYR   B 83  ? 0.1809 0.1980 0.2583 0.0075  0.0190  0.0374  89  TYR   C CE2 
1754 C CZ  . TYR   B 83  ? 0.1878 0.2033 0.2546 0.0076  0.0176  0.0384  89  TYR   C CZ  
1755 O OH  . TYR   B 83  ? 0.2009 0.2148 0.2608 0.0083  0.0170  0.0344  89  TYR   C OH  
1756 N N   . TYR   B 84  ? 0.1644 0.1852 0.2767 0.0081  0.0291  0.0469  90  TYR   C N   
1757 C CA  . TYR   B 84  ? 0.1686 0.1893 0.2915 0.0079  0.0316  0.0427  90  TYR   C CA  
1758 C C   . TYR   B 84  ? 0.1588 0.1800 0.2873 0.0081  0.0346  0.0435  90  TYR   C C   
1759 O O   . TYR   B 84  ? 0.1585 0.1801 0.2803 0.0085  0.0346  0.0447  90  TYR   C O   
1760 C CB  . TYR   B 84  ? 0.1547 0.1746 0.2735 0.0077  0.0299  0.0355  90  TYR   C CB  
1761 C CG  . TYR   B 84  ? 0.1385 0.1576 0.2543 0.0076  0.0282  0.0339  90  TYR   C CG  
1762 C CD1 . TYR   B 84  ? 0.1402 0.1586 0.2645 0.0076  0.0300  0.0342  90  TYR   C CD1 
1763 C CD2 . TYR   B 84  ? 0.1382 0.1568 0.2435 0.0076  0.0253  0.0320  90  TYR   C CD2 
1764 C CE1 . TYR   B 84  ? 0.1408 0.1584 0.2629 0.0077  0.0293  0.0328  90  TYR   C CE1 
1765 C CE2 . TYR   B 84  ? 0.1311 0.1489 0.2343 0.0075  0.0243  0.0308  90  TYR   C CE2 
1766 C CZ  . TYR   B 84  ? 0.1354 0.1529 0.2471 0.0075  0.0264  0.0313  90  TYR   C CZ  
1767 O OH  . TYR   B 84  ? 0.1474 0.1643 0.2574 0.0076  0.0261  0.0305  90  TYR   C OH  
1768 N N   . PRO   B 85  ? 0.1583 0.1793 0.2990 0.0076  0.0373  0.0420  91  PRO   C N   
1769 C CA  . PRO   B 85  ? 0.1529 0.1747 0.3001 0.0074  0.0400  0.0418  91  PRO   C CA  
1770 C C   . PRO   B 85  ? 0.1476 0.1701 0.2916 0.0071  0.0382  0.0355  91  PRO   C C   
1771 O O   . PRO   B 85  ? 0.1536 0.1755 0.2906 0.0071  0.0351  0.0311  91  PRO   C O   
1772 C CB  . PRO   B 85  ? 0.1569 0.1774 0.3182 0.0066  0.0426  0.0413  91  PRO   C CB  
1773 C CG  . PRO   B 85  ? 0.1640 0.1829 0.3242 0.0064  0.0409  0.0369  91  PRO   C CG  
1774 C CD  . PRO   B 85  ? 0.1593 0.1787 0.3082 0.0072  0.0381  0.0396  91  PRO   C CD  
1775 N N   . ALA   B 86  ? 0.1521 0.1761 0.3023 0.0068  0.0402  0.0350  92  ALA   C N   
1776 C CA  . ALA   B 86  ? 0.1651 0.1904 0.3151 0.0065  0.0383  0.0293  92  ALA   C CA  
1777 C C   . ALA   B 86  ? 0.1714 0.1954 0.3269 0.0051  0.0365  0.0233  92  ALA   C C   
1778 O O   . ALA   B 86  ? 0.1934 0.2160 0.3589 0.0041  0.0385  0.0234  92  ALA   C O   
1779 C CB  . ALA   B 86  ? 0.1553 0.1830 0.3140 0.0064  0.0412  0.0308  92  ALA   C CB  
1780 N N   . ARG   B 87  ? 0.1514 0.1751 0.2996 0.0052  0.0329  0.0182  93  ARG   C N   
1781 C CA  . ARG   B 87  ? 0.1526 0.1741 0.3026 0.0041  0.0310  0.0123  93  ARG   C CA  
1782 C C   . ARG   B 87  ? 0.1563 0.1783 0.2979 0.0044  0.0270  0.0073  93  ARG   C C   
1783 O O   . ARG   B 87  ? 0.1486 0.1722 0.2824 0.0056  0.0257  0.0087  93  ARG   C O   
1784 C CB  . ARG   B 87  ? 0.1592 0.1779 0.3064 0.0045  0.0320  0.0136  93  ARG   C CB  
1785 C CG  . ARG   B 87  ? 0.1504 0.1690 0.2846 0.0057  0.0298  0.0147  93  ARG   C CG  
1786 C CD  . ARG   B 87  ? 0.1594 0.1763 0.2930 0.0060  0.0311  0.0175  93  ARG   C CD  
1787 N NE  . ARG   B 87  ? 0.1654 0.1820 0.2874 0.0067  0.0286  0.0173  93  ARG   C NE  
1788 C CZ  . ARG   B 87  ? 0.1796 0.1945 0.2985 0.0069  0.0284  0.0160  93  ARG   C CZ  
1789 N NH1 . ARG   B 87  ? 0.1953 0.2082 0.3213 0.0067  0.0308  0.0149  93  ARG   C NH1 
1790 N NH2 . ARG   B 87  ? 0.1858 0.2006 0.2947 0.0073  0.0261  0.0160  93  ARG   C NH2 
1791 N N   . TYR   B 88  ? 0.1752 0.1951 0.3171 0.0033  0.0249  0.0014  94  TYR   C N   
1792 C CA  . TYR   B 88  ? 0.1879 0.2076 0.3200 0.0038  0.0209  -0.0029 94  TYR   C CA  
1793 C C   . TYR   B 88  ? 0.1749 0.1919 0.2966 0.0048  0.0211  -0.0020 94  TYR   C C   
1794 O O   . TYR   B 88  ? 0.1914 0.2057 0.3152 0.0045  0.0233  -0.0017 94  TYR   C O   
1795 C CB  . TYR   B 88  ? 0.2281 0.2461 0.3631 0.0021  0.0182  -0.0096 94  TYR   C CB  
1796 C CG  . TYR   B 88  ? 0.2579 0.2795 0.4010 0.0011  0.0161  -0.0110 94  TYR   C CG  
1797 C CD1 . TYR   B 88  ? 0.2885 0.3132 0.4269 0.0020  0.0126  -0.0118 94  TYR   C CD1 
1798 C CD2 . TYR   B 88  ? 0.3045 0.3271 0.4614 -0.0005 0.0182  -0.0104 94  TYR   C CD2 
1799 C CE1 . TYR   B 88  ? 0.3159 0.3448 0.4635 0.0013  0.0108  -0.0123 94  TYR   C CE1 
1800 C CE2 . TYR   B 88  ? 0.3188 0.3453 0.4849 -0.0016 0.0165  -0.0112 94  TYR   C CE2 
1801 C CZ  . TYR   B 88  ? 0.3369 0.3669 0.4985 -0.0005 0.0128  -0.0119 94  TYR   C CZ  
1802 O OH  . TYR   B 88  ? 0.3717 0.4065 0.5434 -0.0012 0.0110  -0.0122 94  TYR   C OH  
1803 N N   . GLN   B 89  ? 0.1650 0.1826 0.2765 0.0060  0.0188  -0.0016 95  GLN   C N   
1804 C CA  . GLN   B 89  ? 0.1510 0.1662 0.2528 0.0068  0.0186  -0.0012 95  GLN   C CA  
1805 C C   . GLN   B 89  ? 0.1470 0.1609 0.2408 0.0070  0.0152  -0.0061 95  GLN   C C   
1806 O O   . GLN   B 89  ? 0.1589 0.1748 0.2512 0.0073  0.0124  -0.0075 95  GLN   C O   
1807 C CB  . GLN   B 89  ? 0.1562 0.1727 0.2523 0.0078  0.0186  0.0038  95  GLN   C CB  
1808 C CG  . GLN   B 89  ? 0.1718 0.1863 0.2597 0.0082  0.0183  0.0049  95  GLN   C CG  
1809 C CD  . GLN   B 89  ? 0.1579 0.1729 0.2423 0.0085  0.0187  0.0103  95  GLN   C CD  
1810 O OE1 . GLN   B 89  ? 0.1621 0.1783 0.2517 0.0083  0.0204  0.0142  95  GLN   C OE1 
1811 N NE2 . GLN   B 89  ? 0.1597 0.1735 0.2351 0.0089  0.0170  0.0106  95  GLN   C NE2 
1812 N N   . SER   B 90  ? 0.1391 0.1497 0.2277 0.0070  0.0156  -0.0085 96  SER   C N   
1813 C CA  . SER   B 90  ? 0.1520 0.1607 0.2319 0.0073  0.0127  -0.0129 96  SER   C CA  
1814 C C   . SER   B 90  ? 0.1477 0.1558 0.2169 0.0086  0.0118  -0.0107 96  SER   C C   
1815 O O   . SER   B 90  ? 0.1458 0.1543 0.2144 0.0090  0.0136  -0.0064 96  SER   C O   
1816 C CB  . SER   B 90  ? 0.1794 0.1838 0.2587 0.0066  0.0141  -0.0173 96  SER   C CB  
1817 O OG  . SER   B 90  ? 0.1869 0.1893 0.2646 0.0072  0.0178  -0.0148 96  SER   C OG  
1818 N N   . HIS   B 91  ? 0.1478 0.1550 0.2087 0.0092  0.0086  -0.0137 97  HIS   C N   
1819 C CA  . HIS   B 91  ? 0.1440 0.1500 0.1945 0.0104  0.0076  -0.0121 97  HIS   C CA  
1820 C C   . HIS   B 91  ? 0.1413 0.1495 0.1921 0.0111  0.0075  -0.0076 97  HIS   C C   
1821 O O   . HIS   B 91  ? 0.1519 0.1587 0.1969 0.0115  0.0082  -0.0048 97  HIS   C O   
1822 C CB  . HIS   B 91  ? 0.1576 0.1600 0.2033 0.0105  0.0105  -0.0117 97  HIS   C CB  
1823 C CG  . HIS   B 91  ? 0.1836 0.1825 0.2267 0.0102  0.0112  -0.0166 97  HIS   C CG  
1824 N ND1 . HIS   B 91  ? 0.2062 0.2023 0.2384 0.0109  0.0095  -0.0192 97  HIS   C ND1 
1825 C CD2 . HIS   B 91  ? 0.2010 0.1984 0.2504 0.0092  0.0135  -0.0192 97  HIS   C CD2 
1826 C CE1 . HIS   B 91  ? 0.2163 0.2089 0.2474 0.0104  0.0109  -0.0235 97  HIS   C CE1 
1827 N NE2 . HIS   B 91  ? 0.2221 0.2151 0.2637 0.0093  0.0133  -0.0239 97  HIS   C NE2 
1828 N N   . LEU   B 92  ? 0.1276 0.1388 0.1842 0.0111  0.0066  -0.0070 98  LEU   C N   
1829 C CA  . LEU   B 92  ? 0.1290 0.1418 0.1854 0.0118  0.0071  -0.0031 98  LEU   C CA  
1830 C C   . LEU   B 92  ? 0.1260 0.1397 0.1786 0.0133  0.0043  -0.0039 98  LEU   C C   
1831 O O   . LEU   B 92  ? 0.1420 0.1573 0.1972 0.0134  0.0020  -0.0068 98  LEU   C O   
1832 C CB  . LEU   B 92  ? 0.1405 0.1558 0.2070 0.0112  0.0093  -0.0011 98  LEU   C CB  
1833 C CG  . LEU   B 92  ? 0.1543 0.1703 0.2197 0.0118  0.0107  0.0031  98  LEU   C CG  
1834 C CD1 . LEU   B 92  ? 0.1739 0.1879 0.2344 0.0114  0.0116  0.0062  98  LEU   C CD1 
1835 C CD2 . LEU   B 92  ? 0.1663 0.1850 0.2417 0.0114  0.0131  0.0049  98  LEU   C CD2 
1836 N N   . MET   B 93  ? 0.1243 0.1368 0.1707 0.0143  0.0044  -0.0013 99  MET   C N   
1837 C CA  . MET   B 93  ? 0.1223 0.1351 0.1652 0.0161  0.0024  -0.0014 99  MET   C CA  
1838 C C   . MET   B 93  ? 0.1226 0.1360 0.1670 0.0168  0.0045  0.0016  99  MET   C C   
1839 O O   . MET   B 93  ? 0.1408 0.1525 0.1826 0.0161  0.0064  0.0041  99  MET   C O   
1840 C CB  . MET   B 93  ? 0.1520 0.1611 0.1843 0.0168  0.0012  -0.0010 99  MET   C CB  
1841 C CG  . MET   B 93  ? 0.1681 0.1759 0.1971 0.0163  -0.0002 -0.0037 99  MET   C CG  
1842 S SD  . MET   B 93  ? 0.1796 0.1829 0.1971 0.0169  -0.0006 -0.0025 99  MET   C SD  
1843 C CE  . MET   B 93  ? 0.2070 0.2089 0.2249 0.0154  0.0024  0.0008  99  MET   C CE  
1844 N N   . LEU   B 94  ? 0.1219 0.1378 0.1704 0.0183  0.0043  0.0015  100 LEU   C N   
1845 C CA  . LEU   B 94  ? 0.1368 0.1526 0.1861 0.0192  0.0072  0.0042  100 LEU   C CA  
1846 C C   . LEU   B 94  ? 0.1326 0.1460 0.1750 0.0215  0.0067  0.0046  100 LEU   C C   
1847 O O   . LEU   B 94  ? 0.1420 0.1561 0.1837 0.0227  0.0041  0.0031  100 LEU   C O   
1848 C CB  . LEU   B 94  ? 0.1447 0.1651 0.2055 0.0195  0.0087  0.0042  100 LEU   C CB  
1849 C CG  . LEU   B 94  ? 0.1558 0.1784 0.2252 0.0175  0.0099  0.0041  100 LEU   C CG  
1850 C CD1 . LEU   B 94  ? 0.1923 0.2192 0.2732 0.0178  0.0116  0.0046  100 LEU   C CD1 
1851 C CD2 . LEU   B 94  ? 0.1952 0.2154 0.2614 0.0162  0.0123  0.0068  100 LEU   C CD2 
1852 N N   . ALA   B 95  ? 0.1434 0.1540 0.1811 0.0221  0.0093  0.0068  101 ALA   C N   
1853 C CA  . ALA   B 95  ? 0.1368 0.1446 0.1691 0.0244  0.0101  0.0073  101 ALA   C CA  
1854 C C   . ALA   B 95  ? 0.1403 0.1476 0.1736 0.0253  0.0144  0.0093  101 ALA   C C   
1855 O O   . ALA   B 95  ? 0.1430 0.1512 0.1785 0.0238  0.0163  0.0108  101 ALA   C O   
1856 C CB  . ALA   B 95  ? 0.1557 0.1576 0.1764 0.0239  0.0089  0.0076  101 ALA   C CB  
1857 N N   . VAL   B 96  ? 0.1417 0.1474 0.1733 0.0280  0.0162  0.0096  102 VAL   C N   
1858 C CA  . VAL   B 96  ? 0.1570 0.1607 0.1867 0.0292  0.0209  0.0113  102 VAL   C CA  
1859 C C   . VAL   B 96  ? 0.1645 0.1610 0.1807 0.0283  0.0212  0.0118  102 VAL   C C   
1860 O O   . VAL   B 96  ? 0.1906 0.1824 0.1990 0.0289  0.0196  0.0108  102 VAL   C O   
1861 C CB  . VAL   B 96  ? 0.1737 0.1781 0.2075 0.0328  0.0233  0.0112  102 VAL   C CB  
1862 C CG1 . VAL   B 96  ? 0.2039 0.2050 0.2339 0.0342  0.0291  0.0130  102 VAL   C CG1 
1863 C CG2 . VAL   B 96  ? 0.1918 0.2039 0.2402 0.0332  0.0222  0.0109  102 VAL   C CG2 
1864 N N   . GLY   B 97  ? 0.1745 0.1700 0.1879 0.0265  0.0228  0.0136  103 GLY   C N   
1865 C CA  . GLY   B 97  ? 0.1952 0.1843 0.1961 0.0250  0.0220  0.0141  103 GLY   C CA  
1866 C C   . GLY   B 97  ? 0.1950 0.1843 0.1945 0.0230  0.0227  0.0166  103 GLY   C C   
1867 O O   . GLY   B 97  ? 0.2261 0.2206 0.2349 0.0226  0.0241  0.0180  103 GLY   C O   
1868 N N   . HIS   B 98  ? 0.2167 0.2004 0.2048 0.0215  0.0217  0.0173  104 HIS   C N   
1869 C CA  . HIS   B 98  ? 0.2123 0.1958 0.1976 0.0196  0.0219  0.0201  104 HIS   C CA  
1870 C C   . HIS   B 98  ? 0.1878 0.1743 0.1772 0.0167  0.0179  0.0214  104 HIS   C C   
1871 O O   . HIS   B 98  ? 0.1948 0.1800 0.1822 0.0154  0.0144  0.0201  104 HIS   C O   
1872 C CB  . HIS   B 98  ? 0.2496 0.2253 0.2200 0.0194  0.0222  0.0203  104 HIS   C CB  
1873 C CG  . HIS   B 98  ? 0.3012 0.2764 0.2676 0.0178  0.0225  0.0236  104 HIS   C CG  
1874 N ND1 . HIS   B 98  ? 0.3260 0.3039 0.2967 0.0191  0.0270  0.0260  104 HIS   C ND1 
1875 C CD2 . HIS   B 98  ? 0.3290 0.3022 0.2890 0.0149  0.0184  0.0253  104 HIS   C CD2 
1876 C CE1 . HIS   B 98  ? 0.3586 0.3354 0.3240 0.0172  0.0256  0.0292  104 HIS   C CE1 
1877 N NE2 . HIS   B 98  ? 0.3608 0.3349 0.3196 0.0146  0.0202  0.0288  104 HIS   C NE2 
1878 N N   . SER   B 99  ? 0.1897 0.1800 0.1854 0.0158  0.0189  0.0242  105 SER   C N   
1879 C CA  . SER   B 99  ? 0.1877 0.1809 0.1883 0.0133  0.0158  0.0259  105 SER   C CA  
1880 C C   . SER   B 99  ? 0.2079 0.2028 0.2108 0.0126  0.0172  0.0301  105 SER   C C   
1881 O O   . SER   B 99  ? 0.2321 0.2303 0.2431 0.0137  0.0206  0.0311  105 SER   C O   
1882 C CB  . SER   B 99  ? 0.2010 0.1992 0.2133 0.0136  0.0156  0.0240  105 SER   C CB  
1883 O OG  . SER   B 99  ? 0.2093 0.2101 0.2273 0.0117  0.0137  0.0255  105 SER   C OG  
1884 N N   . GLU   B 100 ? 0.2122 0.2047 0.2081 0.0106  0.0143  0.0327  106 GLU   C N   
1885 C CA  . GLU   B 100 ? 0.2099 0.2039 0.2072 0.0097  0.0145  0.0374  106 GLU   C CA  
1886 C C   . GLU   B 100 ? 0.1862 0.1844 0.1935 0.0080  0.0118  0.0389  106 GLU   C C   
1887 O O   . GLU   B 100 ? 0.1855 0.1843 0.1949 0.0072  0.0094  0.0365  106 GLU   C O   
1888 C CB  . GLU   B 100 ? 0.2744 0.2630 0.2572 0.0084  0.0119  0.0393  106 GLU   C CB  
1889 C CG  . GLU   B 100 ? 0.4437 0.4275 0.4164 0.0104  0.0157  0.0380  106 GLU   C CG  
1890 C CD  . GLU   B 100 ? 0.6133 0.5903 0.5696 0.0093  0.0136  0.0388  106 GLU   C CD  
1891 O OE1 . GLU   B 100 ? 0.6797 0.6568 0.6330 0.0069  0.0092  0.0419  106 GLU   C OE1 
1892 O OE2 . GLU   B 100 ? 0.6825 0.6540 0.6289 0.0108  0.0161  0.0361  106 GLU   C OE2 
1893 N N   . PRO   B 101 ? 0.1993 0.2003 0.2128 0.0075  0.0123  0.0431  107 PRO   C N   
1894 C CA  . PRO   B 101 ? 0.1840 0.1889 0.2078 0.0062  0.0103  0.0447  107 PRO   C CA  
1895 C C   . PRO   B 101 ? 0.1903 0.1940 0.2098 0.0042  0.0055  0.0448  107 PRO   C C   
1896 O O   . PRO   B 101 ? 0.1787 0.1846 0.2055 0.0037  0.0046  0.0435  107 PRO   C O   
1897 C CB  . PRO   B 101 ? 0.2176 0.2245 0.2463 0.0061  0.0115  0.0503  107 PRO   C CB  
1898 C CG  . PRO   B 101 ? 0.2516 0.2567 0.2754 0.0077  0.0152  0.0509  107 PRO   C CG  
1899 C CD  . PRO   B 101 ? 0.2216 0.2226 0.2345 0.0085  0.0157  0.0468  107 PRO   C CD  
1900 N N   . GLY   B 102 ? 0.1847 0.1846 0.1923 0.0030  0.0024  0.0460  108 GLY   C N   
1901 C CA  . GLY   B 102 ? 0.1907 0.1895 0.1951 0.0006  -0.0027 0.0463  108 GLY   C CA  
1902 C C   . GLY   B 102 ? 0.1705 0.1671 0.1726 0.0006  -0.0031 0.0415  108 GLY   C C   
1903 O O   . GLY   B 102 ? 0.2033 0.1993 0.2046 -0.0014 -0.0067 0.0415  108 GLY   C O   
1904 N N   . ASP   B 103 ? 0.1677 0.1630 0.1684 0.0028  0.0004  0.0376  109 ASP   C N   
1905 C CA  . ASP   B 103 ? 0.1611 0.1545 0.1597 0.0032  0.0001  0.0334  109 ASP   C CA  
1906 C C   . ASP   B 103 ? 0.1556 0.1531 0.1652 0.0033  0.0009  0.0325  109 ASP   C C   
1907 O O   . ASP   B 103 ? 0.1608 0.1571 0.1693 0.0034  0.0003  0.0298  109 ASP   C O   
1908 C CB  . ASP   B 103 ? 0.1767 0.1675 0.1706 0.0056  0.0033  0.0301  109 ASP   C CB  
1909 C CG  . ASP   B 103 ? 0.1994 0.1846 0.1806 0.0056  0.0030  0.0302  109 ASP   C CG  
1910 O OD1 . ASP   B 103 ? 0.2119 0.1933 0.1854 0.0035  -0.0007 0.0306  109 ASP   C OD1 
1911 O OD2 . ASP   B 103 ? 0.2035 0.1876 0.1822 0.0078  0.0068  0.0296  109 ASP   C OD2 
1912 N N   . CYS   B 104 ? 0.1454 0.1474 0.1654 0.0035  0.0025  0.0346  110 CYS   C N   
1913 C CA  . CYS   B 104 ? 0.1418 0.1469 0.1714 0.0038  0.0037  0.0333  110 CYS   C CA  
1914 C C   . CYS   B 104 ? 0.1541 0.1586 0.1832 0.0021  0.0011  0.0340  110 CYS   C C   
1915 O O   . CYS   B 104 ? 0.1631 0.1674 0.1905 0.0002  -0.0019 0.0372  110 CYS   C O   
1916 C CB  . CYS   B 104 ? 0.1485 0.1574 0.1889 0.0040  0.0057  0.0360  110 CYS   C CB  
1917 S SG  . CYS   B 104 ? 0.1669 0.1771 0.2119 0.0059  0.0097  0.0345  110 CYS   C SG  
1918 N N   . GLY   B 105 ? 0.1253 0.1296 0.1558 0.0027  0.0021  0.0310  111 GLY   C N   
1919 C CA  . GLY   B 105 ? 0.1398 0.1436 0.1705 0.0013  0.0006  0.0316  111 GLY   C CA  
1920 C C   . GLY   B 105 ? 0.1435 0.1428 0.1646 0.0010  -0.0012 0.0294  111 GLY   C C   
1921 O O   . GLY   B 105 ? 0.1628 0.1613 0.1841 0.0001  -0.0018 0.0295  111 GLY   C O   
1922 N N   . GLY   B 106 ? 0.1523 0.1485 0.1653 0.0018  -0.0016 0.0278  112 GLY   C N   
1923 C CA  . GLY   B 106 ? 0.1648 0.1562 0.1689 0.0019  -0.0028 0.0255  112 GLY   C CA  
1924 C C   . GLY   B 106 ? 0.1490 0.1403 0.1541 0.0036  -0.0010 0.0227  112 GLY   C C   
1925 O O   . GLY   B 106 ? 0.1464 0.1404 0.1559 0.0054  0.0012  0.0210  112 GLY   C O   
1926 N N   . ILE   B 107 ? 0.1477 0.1360 0.1488 0.0029  -0.0022 0.0222  113 ILE   C N   
1927 C CA  . ILE   B 107 ? 0.1491 0.1369 0.1499 0.0045  -0.0007 0.0201  113 ILE   C CA  
1928 C C   . ILE   B 107 ? 0.1492 0.1345 0.1444 0.0069  -0.0003 0.0173  113 ILE   C C   
1929 O O   . ILE   B 107 ? 0.1602 0.1415 0.1490 0.0070  -0.0013 0.0169  113 ILE   C O   
1930 C CB  . ILE   B 107 ? 0.1844 0.1697 0.1839 0.0027  -0.0017 0.0215  113 ILE   C CB  
1931 C CG1 . ILE   B 107 ? 0.2304 0.2200 0.2390 0.0014  -0.0005 0.0239  113 ILE   C CG1 
1932 C CG2 . ILE   B 107 ? 0.1962 0.1787 0.1913 0.0045  -0.0007 0.0196  113 ILE   C CG2 
1933 C CD1 . ILE   B 107 ? 0.2779 0.2666 0.2885 -0.0007 -0.0010 0.0264  113 ILE   C CD1 
1934 N N   . LEU   B 108 ? 0.1448 0.1322 0.1425 0.0089  0.0011  0.0153  114 LEU   C N   
1935 C CA  . LEU   B 108 ? 0.1391 0.1248 0.1327 0.0113  0.0011  0.0130  114 LEU   C CA  
1936 C C   . LEU   B 108 ? 0.1439 0.1274 0.1343 0.0116  0.0008  0.0129  114 LEU   C C   
1937 O O   . LEU   B 108 ? 0.1412 0.1267 0.1347 0.0111  0.0018  0.0130  114 LEU   C O   
1938 C CB  . LEU   B 108 ? 0.1378 0.1276 0.1366 0.0130  0.0020  0.0111  114 LEU   C CB  
1939 C CG  . LEU   B 108 ? 0.1411 0.1306 0.1378 0.0155  0.0014  0.0090  114 LEU   C CG  
1940 C CD1 . LEU   B 108 ? 0.1569 0.1438 0.1499 0.0170  0.0013  0.0090  114 LEU   C CD1 
1941 C CD2 . LEU   B 108 ? 0.1454 0.1395 0.1486 0.0164  0.0017  0.0070  114 LEU   C CD2 
1942 N N   . ARG   B 109 ? 0.1433 0.1224 0.1275 0.0124  0.0000  0.0128  115 ARG   C N   
1943 C CA  . ARG   B 109 ? 0.1587 0.1351 0.1393 0.0127  -0.0001 0.0133  115 ARG   C CA  
1944 C C   . ARG   B 109 ? 0.1697 0.1439 0.1458 0.0155  -0.0007 0.0121  115 ARG   C C   
1945 O O   . ARG   B 109 ? 0.1760 0.1489 0.1508 0.0169  -0.0011 0.0113  115 ARG   C O   
1946 C CB  . ARG   B 109 ? 0.2074 0.1798 0.1857 0.0102  -0.0006 0.0155  115 ARG   C CB  
1947 C CG  . ARG   B 109 ? 0.2761 0.2437 0.2493 0.0101  -0.0019 0.0152  115 ARG   C CG  
1948 C CD  . ARG   B 109 ? 0.3805 0.3441 0.3521 0.0070  -0.0030 0.0172  115 ARG   C CD  
1949 N NE  . ARG   B 109 ? 0.4599 0.4260 0.4356 0.0041  -0.0041 0.0186  115 ARG   C NE  
1950 C CZ  . ARG   B 109 ? 0.5671 0.5357 0.5482 0.0017  -0.0041 0.0209  115 ARG   C CZ  
1951 N NH1 . ARG   B 109 ? 0.5748 0.5434 0.5573 0.0021  -0.0024 0.0219  115 ARG   C NH1 
1952 N NH2 . ARG   B 109 ? 0.5919 0.5632 0.5775 -0.0007 -0.0055 0.0226  115 ARG   C NH2 
1953 N N   . CYS   B 110 ? 0.1691 0.1426 0.1427 0.0165  -0.0006 0.0122  116 CYS   C N   
1954 C CA  . CYS   B 110 ? 0.1847 0.1560 0.1539 0.0193  -0.0017 0.0118  116 CYS   C CA  
1955 C C   . CYS   B 110 ? 0.2058 0.1722 0.1698 0.0188  -0.0012 0.0140  116 CYS   C C   
1956 O O   . CYS   B 110 ? 0.2034 0.1685 0.1682 0.0162  -0.0001 0.0156  116 CYS   C O   
1957 C CB  . CYS   B 110 ? 0.1762 0.1515 0.1466 0.0211  -0.0025 0.0100  116 CYS   C CB  
1958 S SG  . CYS   B 110 ? 0.1752 0.1511 0.1438 0.0201  -0.0012 0.0101  116 CYS   C SG  
1959 N N   . GLN   B 111 ? 0.2199 0.1837 0.1791 0.0213  -0.0020 0.0145  117 GLN   C N   
1960 C CA  . GLN   B 111 ? 0.2478 0.2067 0.2022 0.0210  -0.0011 0.0170  117 GLN   C CA  
1961 C C   . GLN   B 111 ? 0.2482 0.2082 0.2022 0.0196  0.0008  0.0180  117 GLN   C C   
1962 O O   . GLN   B 111 ? 0.2767 0.2331 0.2286 0.0185  0.0023  0.0206  117 GLN   C O   
1963 C CB  . GLN   B 111 ? 0.2656 0.2215 0.2149 0.0242  -0.0023 0.0179  117 GLN   C CB  
1964 C CG  . GLN   B 111 ? 0.2973 0.2571 0.2452 0.0264  -0.0037 0.0169  117 GLN   C CG  
1965 C CD  . GLN   B 111 ? 0.4394 0.3970 0.3829 0.0297  -0.0057 0.0182  117 GLN   C CD  
1966 O OE1 . GLN   B 111 ? 0.4899 0.4497 0.4359 0.0319  -0.0078 0.0171  117 GLN   C OE1 
1967 N NE2 . GLN   B 111 ? 0.4374 0.3908 0.3748 0.0302  -0.0048 0.0209  117 GLN   C NE2 
1968 N N   . HIS   B 112 ? 0.2156 0.1804 0.1722 0.0197  0.0011  0.0161  118 HIS   C N   
1969 C CA  . HIS   B 112 ? 0.2068 0.1722 0.1625 0.0188  0.0037  0.0167  118 HIS   C CA  
1970 C C   . HIS   B 112 ? 0.2156 0.1832 0.1782 0.0160  0.0058  0.0174  118 HIS   C C   
1971 O O   . HIS   B 112 ? 0.2201 0.1879 0.1832 0.0152  0.0087  0.0184  118 HIS   C O   
1972 C CB  . HIS   B 112 ? 0.2136 0.1819 0.1673 0.0206  0.0029  0.0139  118 HIS   C CB  
1973 C CG  . HIS   B 112 ? 0.2102 0.1772 0.1580 0.0234  0.0000  0.0136  118 HIS   C CG  
1974 N ND1 . HIS   B 112 ? 0.2011 0.1712 0.1517 0.0248  -0.0031 0.0114  118 HIS   C ND1 
1975 C CD2 . HIS   B 112 ? 0.2435 0.2069 0.1833 0.0251  -0.0001 0.0155  118 HIS   C CD2 
1976 C CE1 . HIS   B 112 ? 0.2142 0.1827 0.1592 0.0273  -0.0054 0.0122  118 HIS   C CE1 
1977 N NE2 . HIS   B 112 ? 0.2460 0.2104 0.1839 0.0276  -0.0039 0.0146  118 HIS   C NE2 
1978 N N   . GLY   B 113 ? 0.1996 0.1690 0.1675 0.0145  0.0045  0.0169  119 GLY   C N   
1979 C CA  . GLY   B 113 ? 0.1883 0.1601 0.1631 0.0119  0.0057  0.0180  119 GLY   C CA  
1980 C C   . GLY   B 113 ? 0.1674 0.1433 0.1474 0.0116  0.0046  0.0162  119 GLY   C C   
1981 O O   . GLY   B 113 ? 0.1671 0.1431 0.1457 0.0129  0.0028  0.0145  119 GLY   C O   
1982 N N   . VAL   B 114 ? 0.1725 0.1516 0.1592 0.0100  0.0062  0.0170  120 VAL   C N   
1983 C CA  . VAL   B 114 ? 0.1623 0.1452 0.1547 0.0095  0.0055  0.0160  120 VAL   C CA  
1984 C C   . VAL   B 114 ? 0.1546 0.1398 0.1475 0.0114  0.0061  0.0129  120 VAL   C C   
1985 O O   . VAL   B 114 ? 0.1639 0.1494 0.1567 0.0120  0.0081  0.0119  120 VAL   C O   
1986 C CB  . VAL   B 114 ? 0.1735 0.1590 0.1735 0.0073  0.0068  0.0184  120 VAL   C CB  
1987 C CG1 . VAL   B 114 ? 0.1889 0.1781 0.1948 0.0071  0.0065  0.0178  120 VAL   C CG1 
1988 C CG2 . VAL   B 114 ? 0.2069 0.1903 0.2070 0.0048  0.0053  0.0215  120 VAL   C CG2 
1989 N N   . VAL   B 115 ? 0.1430 0.1296 0.1365 0.0123  0.0043  0.0112  121 VAL   C N   
1990 C CA  . VAL   B 115 ? 0.1423 0.1315 0.1379 0.0137  0.0042  0.0082  121 VAL   C CA  
1991 C C   . VAL   B 115 ? 0.1483 0.1409 0.1520 0.0127  0.0056  0.0079  121 VAL   C C   
1992 O O   . VAL   B 115 ? 0.1469 0.1410 0.1532 0.0131  0.0065  0.0056  121 VAL   C O   
1993 C CB  . VAL   B 115 ? 0.1443 0.1336 0.1380 0.0154  0.0019  0.0070  121 VAL   C CB  
1994 C CG1 . VAL   B 115 ? 0.1660 0.1587 0.1637 0.0164  0.0012  0.0042  121 VAL   C CG1 
1995 C CG2 . VAL   B 115 ? 0.1744 0.1600 0.1605 0.0168  0.0007  0.0075  121 VAL   C CG2 
1996 N N   . GLY   B 116 ? 0.1403 0.1340 0.1476 0.0114  0.0055  0.0101  122 GLY   C N   
1997 C CA  . GLY   B 116 ? 0.1554 0.1523 0.1707 0.0105  0.0068  0.0107  122 GLY   C CA  
1998 C C   . GLY   B 116 ? 0.1376 0.1348 0.1543 0.0092  0.0059  0.0137  122 GLY   C C   
1999 O O   . GLY   B 116 ? 0.1436 0.1382 0.1551 0.0085  0.0044  0.0151  122 GLY   C O   
2000 N N   . ILE   B 117 ? 0.1255 0.1256 0.1491 0.0086  0.0068  0.0147  123 ILE   C N   
2001 C CA  . ILE   B 117 ? 0.1280 0.1285 0.1523 0.0074  0.0059  0.0179  123 ILE   C CA  
2002 C C   . ILE   B 117 ? 0.1267 0.1290 0.1538 0.0081  0.0065  0.0176  123 ILE   C C   
2003 O O   . ILE   B 117 ? 0.1353 0.1397 0.1678 0.0090  0.0080  0.0157  123 ILE   C O   
2004 C CB  . ILE   B 117 ? 0.1416 0.1439 0.1722 0.0056  0.0063  0.0213  123 ILE   C CB  
2005 C CG1 . ILE   B 117 ? 0.1490 0.1540 0.1882 0.0062  0.0091  0.0205  123 ILE   C CG1 
2006 C CG2 . ILE   B 117 ? 0.1735 0.1741 0.2015 0.0044  0.0054  0.0227  123 ILE   C CG2 
2007 C CD1 . ILE   B 117 ? 0.1604 0.1678 0.2081 0.0050  0.0100  0.0247  123 ILE   C CD1 
2008 N N   . VAL   B 118 ? 0.1294 0.1305 0.1525 0.0077  0.0054  0.0194  124 VAL   C N   
2009 C CA  . VAL   B 118 ? 0.1302 0.1328 0.1558 0.0084  0.0067  0.0200  124 VAL   C CA  
2010 C C   . VAL   B 118 ? 0.1265 0.1324 0.1614 0.0079  0.0083  0.0218  124 VAL   C C   
2011 O O   . VAL   B 118 ? 0.1304 0.1371 0.1684 0.0065  0.0078  0.0246  124 VAL   C O   
2012 C CB  . VAL   B 118 ? 0.1320 0.1319 0.1503 0.0079  0.0056  0.0221  124 VAL   C CB  
2013 C CG1 . VAL   B 118 ? 0.1440 0.1452 0.1644 0.0087  0.0077  0.0234  124 VAL   C CG1 
2014 C CG2 . VAL   B 118 ? 0.1488 0.1444 0.1580 0.0087  0.0046  0.0200  124 VAL   C CG2 
2015 N N   . SER   B 119 ? 0.1259 0.1339 0.1666 0.0089  0.0103  0.0203  125 SER   C N   
2016 C CA  . SER   B 119 ? 0.1334 0.1441 0.1839 0.0085  0.0122  0.0219  125 SER   C CA  
2017 C C   . SER   B 119 ? 0.1391 0.1512 0.1933 0.0091  0.0141  0.0231  125 SER   C C   
2018 O O   . SER   B 119 ? 0.1427 0.1564 0.2036 0.0086  0.0156  0.0260  125 SER   C O   
2019 C CB  . SER   B 119 ? 0.1375 0.1490 0.1935 0.0088  0.0132  0.0184  125 SER   C CB  
2020 O OG  . SER   B 119 ? 0.1450 0.1582 0.2108 0.0084  0.0155  0.0193  125 SER   C OG  
2021 N N   . THR   B 120 ? 0.1277 0.1394 0.1787 0.0103  0.0145  0.0212  126 THR   C N   
2022 C CA  . THR   B 120 ? 0.1307 0.1440 0.1865 0.0110  0.0170  0.0225  126 THR   C CA  
2023 C C   . THR   B 120 ? 0.1296 0.1408 0.1770 0.0122  0.0175  0.0232  126 THR   C C   
2024 O O   . THR   B 120 ? 0.1347 0.1433 0.1738 0.0126  0.0156  0.0215  126 THR   C O   
2025 C CB  . THR   B 120 ? 0.1270 0.1430 0.1921 0.0115  0.0182  0.0193  126 THR   C CB  
2026 O OG1 . THR   B 120 ? 0.1552 0.1709 0.2164 0.0127  0.0167  0.0159  126 THR   C OG1 
2027 C CG2 . THR   B 120 ? 0.1465 0.1632 0.2182 0.0105  0.0179  0.0175  126 THR   C CG2 
2028 N N   . GLY   B 121 ? 0.1432 0.1551 0.1928 0.0128  0.0203  0.0255  127 GLY   C N   
2029 C CA  . GLY   B 121 ? 0.1765 0.1861 0.2184 0.0143  0.0219  0.0260  127 GLY   C CA  
2030 C C   . GLY   B 121 ? 0.2011 0.2126 0.2492 0.0153  0.0261  0.0280  127 GLY   C C   
2031 O O   . GLY   B 121 ? 0.2372 0.2511 0.2937 0.0145  0.0276  0.0302  127 GLY   C O   
2032 N N   . GLY   B 122 ? 0.2505 0.2603 0.2936 0.0171  0.0286  0.0281  128 GLY   C N   
2033 C CA  . GLY   B 122 ? 0.2860 0.2973 0.3343 0.0183  0.0335  0.0305  128 GLY   C CA  
2034 C C   . GLY   B 122 ? 0.2914 0.3050 0.3460 0.0203  0.0355  0.0281  128 GLY   C C   
2035 O O   . GLY   B 122 ? 0.2781 0.2934 0.3359 0.0204  0.0326  0.0245  128 GLY   C O   
2036 N N   . ASN   B 123 ? 0.2858 0.2998 0.3426 0.0219  0.0406  0.0303  129 ASN   C N   
2037 C CA  . ASN   B 123 ? 0.2982 0.3149 0.3623 0.0241  0.0431  0.0288  129 ASN   C CA  
2038 C C   . ASN   B 123 ? 0.2564 0.2705 0.3128 0.0257  0.0409  0.0256  129 ASN   C C   
2039 O O   . ASN   B 123 ? 0.2692 0.2865 0.3335 0.0270  0.0405  0.0236  129 ASN   C O   
2040 C CB  . ASN   B 123 ? 0.3584 0.3816 0.4399 0.0231  0.0424  0.0276  129 ASN   C CB  
2041 C CG  . ASN   B 123 ? 0.4520 0.4781 0.5441 0.0235  0.0481  0.0311  129 ASN   C CG  
2042 O OD1 . ASN   B 123 ? 0.4800 0.5033 0.5661 0.0243  0.0527  0.0349  129 ASN   C OD1 
2043 N ND2 . ASN   B 123 ? 0.4735 0.5050 0.5815 0.0228  0.0479  0.0300  129 ASN   C ND2 
2044 N N   . GLY   B 124 ? 0.2266 0.2348 0.2682 0.0255  0.0393  0.0253  130 GLY   C N   
2045 C CA  . GLY   B 124 ? 0.2145 0.2193 0.2484 0.0270  0.0374  0.0225  130 GLY   C CA  
2046 C C   . GLY   B 124 ? 0.1947 0.2013 0.2312 0.0259  0.0319  0.0194  130 GLY   C C   
2047 O O   . GLY   B 124 ? 0.1926 0.1972 0.2252 0.0274  0.0304  0.0173  130 GLY   C O   
2048 N N   . LEU   B 125 ? 0.1769 0.1866 0.2194 0.0235  0.0290  0.0193  131 LEU   C N   
2049 C CA  . LEU   B 125 ? 0.1620 0.1730 0.2060 0.0225  0.0243  0.0165  131 LEU   C CA  
2050 C C   . LEU   B 125 ? 0.1713 0.1797 0.2089 0.0201  0.0217  0.0171  131 LEU   C C   
2051 O O   . LEU   B 125 ? 0.1951 0.2029 0.2317 0.0189  0.0230  0.0199  131 LEU   C O   
2052 C CB  . LEU   B 125 ? 0.1884 0.2052 0.2460 0.0218  0.0233  0.0152  131 LEU   C CB  
2053 C CG  . LEU   B 125 ? 0.2167 0.2373 0.2837 0.0238  0.0254  0.0149  131 LEU   C CG  
2054 C CD1 . LEU   B 125 ? 0.2739 0.3002 0.3553 0.0224  0.0246  0.0140  131 LEU   C CD1 
2055 C CD2 . LEU   B 125 ? 0.2338 0.2535 0.2971 0.0259  0.0233  0.0129  131 LEU   C CD2 
2056 N N   . VAL   B 126 ? 0.1413 0.1482 0.1746 0.0197  0.0182  0.0151  132 VAL   C N   
2057 C CA  . VAL   B 126 ? 0.1365 0.1418 0.1659 0.0174  0.0157  0.0156  132 VAL   C CA  
2058 C C   . VAL   B 126 ? 0.1227 0.1309 0.1583 0.0168  0.0134  0.0131  132 VAL   C C   
2059 O O   . VAL   B 126 ? 0.1275 0.1363 0.1637 0.0180  0.0120  0.0107  132 VAL   C O   
2060 C CB  . VAL   B 126 ? 0.1375 0.1374 0.1549 0.0172  0.0139  0.0156  132 VAL   C CB  
2061 C CG1 . VAL   B 126 ? 0.1697 0.1678 0.1837 0.0191  0.0129  0.0131  132 VAL   C CG1 
2062 C CG2 . VAL   B 126 ? 0.1489 0.1480 0.1643 0.0149  0.0113  0.0163  132 VAL   C CG2 
2063 N N   . GLY   B 127 ? 0.1276 0.1372 0.1675 0.0150  0.0132  0.0138  133 GLY   C N   
2064 C CA  . GLY   B 127 ? 0.1177 0.1289 0.1622 0.0144  0.0116  0.0112  133 GLY   C CA  
2065 C C   . GLY   B 127 ? 0.1241 0.1330 0.1635 0.0131  0.0102  0.0117  133 GLY   C C   
2066 O O   . GLY   B 127 ? 0.1278 0.1357 0.1656 0.0120  0.0105  0.0146  133 GLY   C O   
2067 N N   . PHE   B 128 ? 0.1137 0.1219 0.1509 0.0134  0.0085  0.0090  134 PHE   C N   
2068 C CA  . PHE   B 128 ? 0.1169 0.1229 0.1498 0.0124  0.0077  0.0094  134 PHE   C CA  
2069 C C   . PHE   B 128 ? 0.1176 0.1247 0.1551 0.0119  0.0082  0.0072  134 PHE   C C   
2070 O O   . PHE   B 128 ? 0.1270 0.1350 0.1661 0.0126  0.0074  0.0041  134 PHE   C O   
2071 C CB  . PHE   B 128 ? 0.1243 0.1274 0.1486 0.0134  0.0058  0.0083  134 PHE   C CB  
2072 C CG  . PHE   B 128 ? 0.1284 0.1295 0.1476 0.0143  0.0056  0.0095  134 PHE   C CG  
2073 C CD1 . PHE   B 128 ? 0.1327 0.1311 0.1469 0.0131  0.0053  0.0119  134 PHE   C CD1 
2074 C CD2 . PHE   B 128 ? 0.1361 0.1379 0.1556 0.0162  0.0055  0.0081  134 PHE   C CD2 
2075 C CE1 . PHE   B 128 ? 0.1483 0.1435 0.1563 0.0139  0.0053  0.0124  134 PHE   C CE1 
2076 C CE2 . PHE   B 128 ? 0.1473 0.1465 0.1617 0.0174  0.0060  0.0090  134 PHE   C CE2 
2077 C CZ  . PHE   B 128 ? 0.1508 0.1462 0.1588 0.0162  0.0060  0.0109  134 PHE   C CZ  
2078 N N   . ALA   B 129 ? 0.1185 0.1253 0.1582 0.0107  0.0094  0.0089  135 ALA   C N   
2079 C CA  . ALA   B 129 ? 0.1182 0.1248 0.1609 0.0105  0.0107  0.0068  135 ALA   C CA  
2080 C C   . ALA   B 129 ? 0.1291 0.1330 0.1639 0.0110  0.0098  0.0053  135 ALA   C C   
2081 O O   . ALA   B 129 ? 0.1323 0.1347 0.1629 0.0106  0.0096  0.0077  135 ALA   C O   
2082 C CB  . ALA   B 129 ? 0.1335 0.1408 0.1824 0.0094  0.0129  0.0098  135 ALA   C CB  
2083 N N   . ASP   B 130 ? 0.1311 0.1344 0.1635 0.0118  0.0090  0.0015  136 ASP   C N   
2084 C CA  . ASP   B 130 ? 0.1363 0.1368 0.1602 0.0125  0.0082  0.0002  136 ASP   C CA  
2085 C C   . ASP   B 130 ? 0.1423 0.1411 0.1662 0.0120  0.0111  0.0009  136 ASP   C C   
2086 O O   . ASP   B 130 ? 0.1527 0.1520 0.1829 0.0114  0.0136  0.0002  136 ASP   C O   
2087 C CB  . ASP   B 130 ? 0.1523 0.1527 0.1738 0.0134  0.0062  -0.0040 136 ASP   C CB  
2088 C CG  . ASP   B 130 ? 0.1941 0.1914 0.2056 0.0144  0.0049  -0.0051 136 ASP   C CG  
2089 O OD1 . ASP   B 130 ? 0.1952 0.1913 0.2016 0.0150  0.0042  -0.0028 136 ASP   C OD1 
2090 O OD2 . ASP   B 130 ? 0.2390 0.2346 0.2473 0.0146  0.0051  -0.0083 136 ASP   C OD2 
2091 N N   . VAL   B 131 ? 0.1426 0.1390 0.1599 0.0122  0.0114  0.0022  137 VAL   C N   
2092 C CA  . VAL   B 131 ? 0.1491 0.1436 0.1658 0.0120  0.0148  0.0029  137 VAL   C CA  
2093 C C   . VAL   B 131 ? 0.1687 0.1598 0.1756 0.0132  0.0149  0.0009  137 VAL   C C   
2094 O O   . VAL   B 131 ? 0.1788 0.1676 0.1837 0.0133  0.0183  0.0014  137 VAL   C O   
2095 C CB  . VAL   B 131 ? 0.1580 0.1531 0.1781 0.0109  0.0161  0.0076  137 VAL   C CB  
2096 C CG1 . VAL   B 131 ? 0.1562 0.1546 0.1857 0.0098  0.0160  0.0098  137 VAL   C CG1 
2097 C CG2 . VAL   B 131 ? 0.1626 0.1562 0.1764 0.0107  0.0136  0.0096  137 VAL   C CG2 
2098 N N   . ARG   B 132 ? 0.1569 0.1472 0.1573 0.0142  0.0114  -0.0008 138 ARG   C N   
2099 C CA  . ARG   B 132 ? 0.1611 0.1481 0.1511 0.0155  0.0109  -0.0018 138 ARG   C CA  
2100 C C   . ARG   B 132 ? 0.1705 0.1551 0.1564 0.0159  0.0127  -0.0055 138 ARG   C C   
2101 O O   . ARG   B 132 ? 0.2013 0.1824 0.1778 0.0169  0.0137  -0.0057 138 ARG   C O   
2102 C CB  . ARG   B 132 ? 0.1634 0.1506 0.1487 0.0166  0.0064  -0.0025 138 ARG   C CB  
2103 C CG  . ARG   B 132 ? 0.1604 0.1483 0.1474 0.0164  0.0053  0.0009  138 ARG   C CG  
2104 C CD  . ARG   B 132 ? 0.1612 0.1493 0.1447 0.0180  0.0015  0.0002  138 ARG   C CD  
2105 N NE  . ARG   B 132 ? 0.1561 0.1479 0.1459 0.0180  -0.0003 -0.0022 138 ARG   C NE  
2106 C CZ  . ARG   B 132 ? 0.1656 0.1591 0.1562 0.0193  -0.0034 -0.0028 138 ARG   C CZ  
2107 N NH1 . ARG   B 132 ? 0.1642 0.1557 0.1487 0.0210  -0.0052 -0.0015 138 ARG   C NH1 
2108 N NH2 . ARG   B 132 ? 0.1645 0.1616 0.1626 0.0191  -0.0044 -0.0045 138 ARG   C NH2 
2109 N N   . ASP   B 133 ? 0.1764 0.1623 0.1682 0.0153  0.0131  -0.0086 139 ASP   C N   
2110 C CA  . ASP   B 133 ? 0.1857 0.1684 0.1730 0.0156  0.0149  -0.0128 139 ASP   C CA  
2111 C C   . ASP   B 133 ? 0.1991 0.1796 0.1886 0.0155  0.0211  -0.0117 139 ASP   C C   
2112 O O   . ASP   B 133 ? 0.2138 0.1903 0.1978 0.0160  0.0237  -0.0152 139 ASP   C O   
2113 C CB  . ASP   B 133 ? 0.2010 0.1854 0.1943 0.0148  0.0127  -0.0169 139 ASP   C CB  
2114 C CG  . ASP   B 133 ? 0.2247 0.2119 0.2308 0.0137  0.0151  -0.0153 139 ASP   C CG  
2115 O OD1 . ASP   B 133 ? 0.2159 0.2060 0.2269 0.0134  0.0151  -0.0110 139 ASP   C OD1 
2116 O OD2 . ASP   B 133 ? 0.2561 0.2422 0.2669 0.0130  0.0172  -0.0182 139 ASP   C OD2 
2117 N N   . LEU   B 134 ? 0.1862 0.1690 0.1836 0.0149  0.0235  -0.0071 140 LEU   C N   
2118 C CA  . LEU   B 134 ? 0.1833 0.1651 0.1858 0.0148  0.0294  -0.0054 140 LEU   C CA  
2119 C C   . LEU   B 134 ? 0.1942 0.1732 0.1894 0.0156  0.0323  -0.0030 140 LEU   C C   
2120 O O   . LEU   B 134 ? 0.1849 0.1656 0.1840 0.0150  0.0332  0.0018  140 LEU   C O   
2121 C CB  . LEU   B 134 ? 0.1694 0.1557 0.1845 0.0136  0.0296  -0.0011 140 LEU   C CB  
2122 C CG  . LEU   B 134 ? 0.1842 0.1734 0.2071 0.0129  0.0272  -0.0026 140 LEU   C CG  
2123 C CD1 . LEU   B 134 ? 0.1858 0.1790 0.2193 0.0118  0.0271  0.0023  140 LEU   C CD1 
2124 C CD2 . LEU   B 134 ? 0.2110 0.1979 0.2365 0.0132  0.0301  -0.0070 140 LEU   C CD2 
2125 N N   . LEU   B 135 ? 0.2006 0.1749 0.1844 0.0168  0.0336  -0.0063 141 LEU   C N   
2126 C CA  . LEU   B 135 ? 0.2171 0.1882 0.1920 0.0178  0.0362  -0.0039 141 LEU   C CA  
2127 C C   . LEU   B 135 ? 0.2238 0.1946 0.2046 0.0179  0.0430  -0.0002 141 LEU   C C   
2128 O O   . LEU   B 135 ? 0.2381 0.2082 0.2166 0.0180  0.0447  0.0037  141 LEU   C O   
2129 C CB  . LEU   B 135 ? 0.2238 0.1896 0.1835 0.0193  0.0359  -0.0080 141 LEU   C CB  
2130 C CG  . LEU   B 135 ? 0.2329 0.1994 0.1875 0.0192  0.0288  -0.0119 141 LEU   C CG  
2131 C CD1 . LEU   B 135 ? 0.2548 0.2157 0.1935 0.0205  0.0281  -0.0158 141 LEU   C CD1 
2132 C CD2 . LEU   B 135 ? 0.2441 0.2141 0.2003 0.0189  0.0233  -0.0087 141 LEU   C CD2 
2133 N N   . TRP   B 136 ? 0.2275 0.1990 0.2172 0.0178  0.0468  -0.0013 142 TRP   C N   
2134 C CA  . TRP   B 136 ? 0.2300 0.2018 0.2280 0.0181  0.0536  0.0023  142 TRP   C CA  
2135 C C   . TRP   B 136 ? 0.2231 0.2001 0.2320 0.0165  0.0522  0.0086  142 TRP   C C   
2136 O O   . TRP   B 136 ? 0.2379 0.2157 0.2535 0.0166  0.0572  0.0126  142 TRP   C O   
2137 C CB  . TRP   B 136 ? 0.2307 0.2019 0.2365 0.0185  0.0578  -0.0003 142 TRP   C CB  
2138 C CG  . TRP   B 136 ? 0.2085 0.1837 0.2235 0.0173  0.0533  -0.0012 142 TRP   C CG  
2139 C CD1 . TRP   B 136 ? 0.2294 0.2033 0.2412 0.0171  0.0499  -0.0065 142 TRP   C CD1 
2140 C CD2 . TRP   B 136 ? 0.2096 0.1905 0.2392 0.0161  0.0522  0.0034  142 TRP   C CD2 
2141 N NE1 . TRP   B 136 ? 0.2294 0.2079 0.2529 0.0159  0.0470  -0.0051 142 TRP   C NE1 
2142 C CE2 . TRP   B 136 ? 0.2170 0.1996 0.2508 0.0154  0.0485  0.0009  142 TRP   C CE2 
2143 C CE3 . TRP   B 136 ? 0.2122 0.1969 0.2517 0.0154  0.0538  0.0096  142 TRP   C CE3 
2144 C CZ2 . TRP   B 136 ? 0.2177 0.2053 0.2641 0.0142  0.0467  0.0046  142 TRP   C CZ2 
2145 C CZ3 . TRP   B 136 ? 0.2208 0.2106 0.2729 0.0142  0.0515  0.0130  142 TRP   C CZ3 
2146 C CH2 . TRP   B 136 ? 0.2141 0.2051 0.2686 0.0137  0.0480  0.0106  142 TRP   C CH2 
2147 N N   . LEU   B 137 ? 0.2126 0.1931 0.2238 0.0151  0.0457  0.0095  143 LEU   C N   
2148 C CA  . LEU   B 137 ? 0.2126 0.1970 0.2320 0.0133  0.0437  0.0150  143 LEU   C CA  
2149 C C   . LEU   B 137 ? 0.2434 0.2257 0.2573 0.0133  0.0452  0.0182  143 LEU   C C   
2150 O O   . LEU   B 137 ? 0.2625 0.2473 0.2841 0.0117  0.0452  0.0229  143 LEU   C O   
2151 C CB  . LEU   B 137 ? 0.2087 0.1957 0.2286 0.0121  0.0368  0.0148  143 LEU   C CB  
2152 C CG  . LEU   B 137 ? 0.1957 0.1858 0.2237 0.0117  0.0353  0.0136  143 LEU   C CG  
2153 C CD1 . LEU   B 137 ? 0.2066 0.1982 0.2322 0.0109  0.0292  0.0127  143 LEU   C CD1 
2154 C CD2 . LEU   B 137 ? 0.2017 0.1956 0.2432 0.0106  0.0371  0.0181  143 LEU   C CD2 
2155 N N   . ASP   B 138 ? 0.2326 0.2102 0.2333 0.0148  0.0461  0.0157  144 ASP   C N   
2156 C CA  . ASP   B 138 ? 0.2626 0.2376 0.2572 0.0149  0.0476  0.0189  144 ASP   C CA  
2157 C C   . ASP   B 138 ? 0.3006 0.2737 0.2971 0.0158  0.0556  0.0213  144 ASP   C C   
2158 O O   . ASP   B 138 ? 0.3232 0.2942 0.3155 0.0158  0.0576  0.0245  144 ASP   C O   
2159 C CB  . ASP   B 138 ? 0.2649 0.2356 0.2441 0.0163  0.0448  0.0161  144 ASP   C CB  
2160 C CG  . ASP   B 138 ? 0.2864 0.2587 0.2636 0.0158  0.0373  0.0145  144 ASP   C CG  
2161 O OD1 . ASP   B 138 ? 0.2782 0.2542 0.2645 0.0141  0.0343  0.0162  144 ASP   C OD1 
2162 O OD2 . ASP   B 138 ? 0.3145 0.2841 0.2808 0.0171  0.0345  0.0118  144 ASP   C OD2 
2163 N N   . GLU   B 139 ? 0.3233 0.2969 0.3259 0.0166  0.0606  0.0200  145 GLU   C N   
2164 C CA  . GLU   B 139 ? 0.3739 0.3454 0.3780 0.0180  0.0693  0.0220  145 GLU   C CA  
2165 C C   . GLU   B 139 ? 0.4153 0.3909 0.4363 0.0176  0.0734  0.0245  145 GLU   C C   
2166 O O   . GLU   B 139 ? 0.4142 0.3939 0.4442 0.0165  0.0693  0.0241  145 GLU   C O   
2167 C CB  . GLU   B 139 ? 0.4412 0.4061 0.4303 0.0204  0.0727  0.0165  145 GLU   C CB  
2168 C CG  . GLU   B 139 ? 0.5424 0.5072 0.5325 0.0208  0.0710  0.0109  145 GLU   C CG  
2169 C CD  . GLU   B 139 ? 0.6715 0.6301 0.6452 0.0224  0.0708  0.0045  145 GLU   C CD  
2170 O OE1 . GLU   B 139 ? 0.6874 0.6447 0.6622 0.0227  0.0711  -0.0003 145 GLU   C OE1 
2171 O OE2 . GLU   B 139 ? 0.7027 0.6573 0.6624 0.0233  0.0703  0.0043  145 GLU   C OE2 
2172 N N   . GLU   B 140 ? 0.4567 0.4311 0.4820 0.0189  0.0819  0.0271  146 GLU   C N   
2173 C CA  . GLU   B 140 ? 0.5005 0.4783 0.5421 0.0194  0.0877  0.0298  146 GLU   C CA  
2174 C C   . GLU   B 140 ? 0.5417 0.5262 0.5996 0.0171  0.0863  0.0370  146 GLU   C C   
2175 O O   . GLU   B 140 ? 0.5631 0.5489 0.6306 0.0177  0.0933  0.0413  146 GLU   C O   
2176 C CB  . GLU   B 140 ? 0.5246 0.5033 0.5711 0.0199  0.0864  0.0259  146 GLU   C CB  
2177 C CG  . GLU   B 140 ? 0.5908 0.5741 0.6563 0.0202  0.0905  0.0295  146 GLU   C CG  
2178 C CD  . GLU   B 140 ? 0.6772 0.6562 0.7436 0.0231  0.1009  0.0279  146 GLU   C CD  
2179 O OE1 . GLU   B 140 ? 0.7055 0.6820 0.7721 0.0244  0.1024  0.0234  146 GLU   C OE1 
2180 O OE2 . GLU   B 140 ? 0.7020 0.6796 0.7690 0.0242  0.1079  0.0311  146 GLU   C OE2 
2181 N N1  . A1BO5 C .   ? 0.3164 0.2566 0.3698 0.0310  0.0697  -0.0180 201 A1BO5 A N1  
2182 C C4  . A1BO5 C .   ? 0.3062 0.2576 0.3288 0.0221  0.0733  -0.0285 201 A1BO5 A C4  
2183 C C5  . A1BO5 C .   ? 0.3106 0.2619 0.3352 0.0231  0.0663  -0.0247 201 A1BO5 A C5  
2184 C C6  . A1BO5 C .   ? 0.3586 0.2907 0.3818 0.0197  0.0761  -0.0359 201 A1BO5 A C6  
2185 C C7  . A1BO5 C .   ? 0.3661 0.2888 0.4013 0.0224  0.0826  -0.0370 201 A1BO5 A C7  
2186 C C8  . A1BO5 C .   ? 0.3471 0.2747 0.3927 0.0266  0.0751  -0.0277 201 A1BO5 A C8  
2187 C C10 . A1BO5 C .   ? 0.2517 0.1987 0.3097 0.0318  0.0564  -0.0073 201 A1BO5 A C10 
2188 C C13 . A1BO5 C .   ? 0.2930 0.2514 0.3116 0.0217  0.0558  -0.0201 201 A1BO5 A C13 
2189 O O1  . A1BO5 C .   ? 0.2859 0.2434 0.3422 0.0337  0.0647  -0.0092 201 A1BO5 A O1  
2190 C C12 . A1BO5 C .   ? 0.3129 0.2607 0.3608 0.0303  0.0677  -0.0172 201 A1BO5 A C12 
2191 C C9  . A1BO5 C .   ? 0.2780 0.2234 0.3452 0.0351  0.0656  -0.0081 201 A1BO5 A C9  
2192 C C11 . A1BO5 C .   ? 0.2449 0.1991 0.3144 0.0345  0.0514  0.0028  201 A1BO5 A C11 
2193 O O   . A1BO5 C .   ? 0.2492 0.2014 0.3339 0.0381  0.0556  0.0077  201 A1BO5 A O   
2194 N N2  . A1BO5 C .   ? 0.2271 0.1898 0.2896 0.0322  0.0430  0.0062  201 A1BO5 A N2  
2195 N N   . A1BO5 C .   ? 0.3329 0.2765 0.3663 0.0251  0.0705  -0.0257 201 A1BO5 A N   
2196 C C3  . A1BO5 C .   ? 0.2941 0.2530 0.3081 0.0197  0.0687  -0.0269 201 A1BO5 A C3  
2197 C C2  . A1BO5 C .   ? 0.2805 0.2460 0.2896 0.0188  0.0579  -0.0217 201 A1BO5 A C2  
2198 C C1  . A1BO5 C .   ? 0.2787 0.2438 0.2902 0.0198  0.0519  -0.0187 201 A1BO5 A C1  
2199 C C   . A1BO5 C .   ? 0.2833 0.2540 0.2895 0.0182  0.0420  -0.0146 201 A1BO5 A C   
# 
