data_7HWZ
# 
_entry.id   7HWZ 
# 
_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   7HWZ         pdb_00007hwz 10.2210/pdb7hwz/pdb 
WWPDB D_1001408035 ?            ?                   
# 
_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                        7HWZ 
_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 '(4S)-1-[(2-methoxyphenyl)acetyl]azepane-4-carboxamide' 290.357   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                              65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                    78.133    2   ?         ? ? ? 
5 water       nat water                                                   18.015    290 ?         ? ? ? 
# 
_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 '(4S)-1-[(2-methoxyphenyl)acetyl]azepane-4-carboxamide' A1BSJ 
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 
A1BSJ non-polymer         . '(4S)-1-[(2-methoxyphenyl)acetyl]azepane-4-carboxamide' ? 'C16 H22 N2 O3'  290.357 
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 ?   ?   ?   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 ?   ?   ?   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        A1BSJ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BSJ 
_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 A1BSJ 1   201 201 A1BSJ LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 2 A1BSJ 1   201 201 A1BSJ LIG C . 
G 3 ZN    1   202 1   ZN    ZN  C . 
H 4 DMS   1   203 6   DMS   DMS C . 
I 5 HOH   1   301 168 HOH   HOH A . 
I 5 HOH   2   302 408 HOH   HOH A . 
I 5 HOH   3   303 336 HOH   HOH A . 
I 5 HOH   4   304 463 HOH   HOH A . 
I 5 HOH   5   305 437 HOH   HOH A . 
I 5 HOH   6   306 452 HOH   HOH A . 
I 5 HOH   7   307 189 HOH   HOH A . 
I 5 HOH   8   308 87  HOH   HOH A . 
I 5 HOH   9   309 128 HOH   HOH A . 
I 5 HOH   10  310 195 HOH   HOH A . 
I 5 HOH   11  311 22  HOH   HOH A . 
I 5 HOH   12  312 2   HOH   HOH A . 
I 5 HOH   13  313 52  HOH   HOH A . 
I 5 HOH   14  314 55  HOH   HOH A . 
I 5 HOH   15  315 10  HOH   HOH A . 
I 5 HOH   16  316 29  HOH   HOH A . 
I 5 HOH   17  317 40  HOH   HOH A . 
I 5 HOH   18  318 436 HOH   HOH A . 
I 5 HOH   19  319 47  HOH   HOH A . 
I 5 HOH   20  320 59  HOH   HOH A . 
I 5 HOH   21  321 474 HOH   HOH A . 
I 5 HOH   22  322 94  HOH   HOH A . 
I 5 HOH   23  323 426 HOH   HOH A . 
I 5 HOH   24  324 134 HOH   HOH A . 
I 5 HOH   25  325 229 HOH   HOH A . 
I 5 HOH   26  326 76  HOH   HOH A . 
I 5 HOH   27  327 465 HOH   HOH A . 
I 5 HOH   28  328 454 HOH   HOH A . 
I 5 HOH   29  329 424 HOH   HOH A . 
I 5 HOH   30  330 54  HOH   HOH A . 
I 5 HOH   31  331 12  HOH   HOH A . 
I 5 HOH   32  332 53  HOH   HOH A . 
I 5 HOH   33  333 262 HOH   HOH A . 
I 5 HOH   34  334 89  HOH   HOH A . 
I 5 HOH   35  335 185 HOH   HOH A . 
I 5 HOH   36  336 107 HOH   HOH A . 
I 5 HOH   37  337 63  HOH   HOH A . 
I 5 HOH   38  338 139 HOH   HOH A . 
I 5 HOH   39  339 462 HOH   HOH A . 
I 5 HOH   40  340 13  HOH   HOH A . 
I 5 HOH   41  341 96  HOH   HOH A . 
I 5 HOH   42  342 108 HOH   HOH A . 
I 5 HOH   43  343 14  HOH   HOH A . 
I 5 HOH   44  344 456 HOH   HOH A . 
I 5 HOH   45  345 31  HOH   HOH A . 
I 5 HOH   46  346 57  HOH   HOH A . 
I 5 HOH   47  347 239 HOH   HOH A . 
I 5 HOH   48  348 453 HOH   HOH A . 
I 5 HOH   49  349 17  HOH   HOH A . 
I 5 HOH   50  350 27  HOH   HOH A . 
I 5 HOH   51  351 444 HOH   HOH A . 
I 5 HOH   52  352 62  HOH   HOH A . 
I 5 HOH   53  353 78  HOH   HOH A . 
I 5 HOH   54  354 81  HOH   HOH A . 
I 5 HOH   55  355 120 HOH   HOH A . 
I 5 HOH   56  356 272 HOH   HOH A . 
I 5 HOH   57  357 9   HOH   HOH A . 
I 5 HOH   58  358 60  HOH   HOH A . 
I 5 HOH   59  359 170 HOH   HOH A . 
I 5 HOH   60  360 5   HOH   HOH A . 
I 5 HOH   61  361 423 HOH   HOH A . 
I 5 HOH   62  362 177 HOH   HOH A . 
I 5 HOH   63  363 1   HOH   HOH A . 
I 5 HOH   64  364 184 HOH   HOH A . 
I 5 HOH   65  365 116 HOH   HOH A . 
I 5 HOH   66  366 26  HOH   HOH A . 
I 5 HOH   67  367 84  HOH   HOH A . 
I 5 HOH   68  368 48  HOH   HOH A . 
I 5 HOH   69  369 261 HOH   HOH A . 
I 5 HOH   70  370 234 HOH   HOH A . 
I 5 HOH   71  371 171 HOH   HOH A . 
I 5 HOH   72  372 449 HOH   HOH A . 
I 5 HOH   73  373 91  HOH   HOH A . 
I 5 HOH   74  374 486 HOH   HOH A . 
I 5 HOH   75  375 476 HOH   HOH A . 
I 5 HOH   76  376 395 HOH   HOH A . 
I 5 HOH   77  377 472 HOH   HOH A . 
I 5 HOH   78  378 421 HOH   HOH A . 
I 5 HOH   79  379 148 HOH   HOH A . 
I 5 HOH   80  380 118 HOH   HOH A . 
I 5 HOH   81  381 41  HOH   HOH A . 
I 5 HOH   82  382 209 HOH   HOH A . 
I 5 HOH   83  383 65  HOH   HOH A . 
I 5 HOH   84  384 18  HOH   HOH A . 
I 5 HOH   85  385 162 HOH   HOH A . 
I 5 HOH   86  386 140 HOH   HOH A . 
I 5 HOH   87  387 455 HOH   HOH A . 
I 5 HOH   88  388 429 HOH   HOH A . 
I 5 HOH   89  389 44  HOH   HOH A . 
I 5 HOH   90  390 447 HOH   HOH A . 
I 5 HOH   91  391 183 HOH   HOH A . 
I 5 HOH   92  392 188 HOH   HOH A . 
I 5 HOH   93  393 466 HOH   HOH A . 
I 5 HOH   94  394 86  HOH   HOH A . 
I 5 HOH   95  395 38  HOH   HOH A . 
I 5 HOH   96  396 478 HOH   HOH A . 
I 5 HOH   97  397 136 HOH   HOH A . 
I 5 HOH   98  398 428 HOH   HOH A . 
I 5 HOH   99  399 99  HOH   HOH A . 
I 5 HOH   100 400 6   HOH   HOH A . 
I 5 HOH   101 401 439 HOH   HOH A . 
I 5 HOH   102 402 122 HOH   HOH A . 
I 5 HOH   103 403 173 HOH   HOH A . 
I 5 HOH   104 404 459 HOH   HOH A . 
I 5 HOH   105 405 125 HOH   HOH A . 
I 5 HOH   106 406 166 HOH   HOH A . 
I 5 HOH   107 407 51  HOH   HOH A . 
I 5 HOH   108 408 430 HOH   HOH A . 
I 5 HOH   109 409 277 HOH   HOH A . 
I 5 HOH   110 410 488 HOH   HOH A . 
I 5 HOH   111 411 212 HOH   HOH A . 
I 5 HOH   112 412 433 HOH   HOH A . 
I 5 HOH   113 413 24  HOH   HOH A . 
I 5 HOH   114 414 469 HOH   HOH A . 
I 5 HOH   115 415 196 HOH   HOH A . 
I 5 HOH   116 416 479 HOH   HOH A . 
I 5 HOH   117 417 152 HOH   HOH A . 
I 5 HOH   118 418 238 HOH   HOH A . 
I 5 HOH   119 419 391 HOH   HOH A . 
I 5 HOH   120 420 377 HOH   HOH A . 
I 5 HOH   121 421 256 HOH   HOH A . 
I 5 HOH   122 422 104 HOH   HOH A . 
I 5 HOH   123 423 481 HOH   HOH A . 
I 5 HOH   124 424 271 HOH   HOH A . 
I 5 HOH   125 425 200 HOH   HOH A . 
I 5 HOH   126 426 146 HOH   HOH A . 
I 5 HOH   127 427 487 HOH   HOH A . 
I 5 HOH   128 428 202 HOH   HOH A . 
I 5 HOH   129 429 369 HOH   HOH A . 
I 5 HOH   130 430 420 HOH   HOH A . 
I 5 HOH   131 431 218 HOH   HOH A . 
I 5 HOH   132 432 397 HOH   HOH A . 
I 5 HOH   133 433 204 HOH   HOH A . 
I 5 HOH   134 434 390 HOH   HOH A . 
I 5 HOH   135 435 418 HOH   HOH A . 
I 5 HOH   136 436 366 HOH   HOH A . 
I 5 HOH   137 437 368 HOH   HOH A . 
J 5 HOH   1   301 489 HOH   HOH C . 
J 5 HOH   2   302 458 HOH   HOH C . 
J 5 HOH   3   303 50  HOH   HOH C . 
J 5 HOH   4   304 117 HOH   HOH C . 
J 5 HOH   5   305 147 HOH   HOH C . 
J 5 HOH   6   306 374 HOH   HOH C . 
J 5 HOH   7   307 45  HOH   HOH C . 
J 5 HOH   8   308 443 HOH   HOH C . 
J 5 HOH   9   309 325 HOH   HOH C . 
J 5 HOH   10  310 16  HOH   HOH C . 
J 5 HOH   11  311 150 HOH   HOH C . 
J 5 HOH   12  312 398 HOH   HOH C . 
J 5 HOH   13  313 73  HOH   HOH C . 
J 5 HOH   14  314 174 HOH   HOH C . 
J 5 HOH   15  315 165 HOH   HOH C . 
J 5 HOH   16  316 130 HOH   HOH C . 
J 5 HOH   17  317 163 HOH   HOH C . 
J 5 HOH   18  318 457 HOH   HOH C . 
J 5 HOH   19  319 43  HOH   HOH C . 
J 5 HOH   20  320 467 HOH   HOH C . 
J 5 HOH   21  321 280 HOH   HOH C . 
J 5 HOH   22  322 111 HOH   HOH C . 
J 5 HOH   23  323 39  HOH   HOH C . 
J 5 HOH   24  324 61  HOH   HOH C . 
J 5 HOH   25  325 131 HOH   HOH C . 
J 5 HOH   26  326 144 HOH   HOH C . 
J 5 HOH   27  327 448 HOH   HOH C . 
J 5 HOH   28  328 473 HOH   HOH C . 
J 5 HOH   29  329 105 HOH   HOH C . 
J 5 HOH   30  330 4   HOH   HOH C . 
J 5 HOH   31  331 101 HOH   HOH C . 
J 5 HOH   32  332 72  HOH   HOH C . 
J 5 HOH   33  333 71  HOH   HOH C . 
J 5 HOH   34  334 425 HOH   HOH C . 
J 5 HOH   35  335 109 HOH   HOH C . 
J 5 HOH   36  336 442 HOH   HOH C . 
J 5 HOH   37  337 37  HOH   HOH C . 
J 5 HOH   38  338 25  HOH   HOH C . 
J 5 HOH   39  339 19  HOH   HOH C . 
J 5 HOH   40  340 32  HOH   HOH C . 
J 5 HOH   41  341 233 HOH   HOH C . 
J 5 HOH   42  342 20  HOH   HOH C . 
J 5 HOH   43  343 33  HOH   HOH C . 
J 5 HOH   44  344 438 HOH   HOH C . 
J 5 HOH   45  345 74  HOH   HOH C . 
J 5 HOH   46  346 372 HOH   HOH C . 
J 5 HOH   47  347 441 HOH   HOH C . 
J 5 HOH   48  348 386 HOH   HOH C . 
J 5 HOH   49  349 446 HOH   HOH C . 
J 5 HOH   50  350 266 HOH   HOH C . 
J 5 HOH   51  351 75  HOH   HOH C . 
J 5 HOH   52  352 178 HOH   HOH C . 
J 5 HOH   53  353 98  HOH   HOH C . 
J 5 HOH   54  354 237 HOH   HOH C . 
J 5 HOH   55  355 114 HOH   HOH C . 
J 5 HOH   56  356 440 HOH   HOH C . 
J 5 HOH   57  357 198 HOH   HOH C . 
J 5 HOH   58  358 267 HOH   HOH C . 
J 5 HOH   59  359 34  HOH   HOH C . 
J 5 HOH   60  360 46  HOH   HOH C . 
J 5 HOH   61  361 381 HOH   HOH C . 
J 5 HOH   62  362 422 HOH   HOH C . 
J 5 HOH   63  363 491 HOH   HOH C . 
J 5 HOH   64  364 265 HOH   HOH C . 
J 5 HOH   65  365 85  HOH   HOH C . 
J 5 HOH   66  366 464 HOH   HOH C . 
J 5 HOH   67  367 95  HOH   HOH C . 
J 5 HOH   68  368 8   HOH   HOH C . 
J 5 HOH   69  369 126 HOH   HOH C . 
J 5 HOH   70  370 435 HOH   HOH C . 
J 5 HOH   71  371 434 HOH   HOH C . 
J 5 HOH   72  372 23  HOH   HOH C . 
J 5 HOH   73  373 315 HOH   HOH C . 
J 5 HOH   74  374 112 HOH   HOH C . 
J 5 HOH   75  375 3   HOH   HOH C . 
J 5 HOH   76  376 88  HOH   HOH C . 
J 5 HOH   77  377 471 HOH   HOH C . 
J 5 HOH   78  378 69  HOH   HOH C . 
J 5 HOH   79  379 450 HOH   HOH C . 
J 5 HOH   80  380 250 HOH   HOH C . 
J 5 HOH   81  381 42  HOH   HOH C . 
J 5 HOH   82  382 115 HOH   HOH C . 
J 5 HOH   83  383 80  HOH   HOH C . 
J 5 HOH   84  384 460 HOH   HOH C . 
J 5 HOH   85  385 113 HOH   HOH C . 
J 5 HOH   86  386 217 HOH   HOH C . 
J 5 HOH   87  387 36  HOH   HOH C . 
J 5 HOH   88  388 28  HOH   HOH C . 
J 5 HOH   89  389 445 HOH   HOH C . 
J 5 HOH   90  390 82  HOH   HOH C . 
J 5 HOH   91  391 480 HOH   HOH C . 
J 5 HOH   92  392 153 HOH   HOH C . 
J 5 HOH   93  393 143 HOH   HOH C . 
J 5 HOH   94  394 451 HOH   HOH C . 
J 5 HOH   95  395 7   HOH   HOH C . 
J 5 HOH   96  396 15  HOH   HOH C . 
J 5 HOH   97  397 35  HOH   HOH C . 
J 5 HOH   98  398 470 HOH   HOH C . 
J 5 HOH   99  399 110 HOH   HOH C . 
J 5 HOH   100 400 49  HOH   HOH C . 
J 5 HOH   101 401 432 HOH   HOH C . 
J 5 HOH   102 402 68  HOH   HOH C . 
J 5 HOH   103 403 58  HOH   HOH C . 
J 5 HOH   104 404 106 HOH   HOH C . 
J 5 HOH   105 405 461 HOH   HOH C . 
J 5 HOH   106 406 172 HOH   HOH C . 
J 5 HOH   107 407 137 HOH   HOH C . 
J 5 HOH   108 408 477 HOH   HOH C . 
J 5 HOH   109 409 167 HOH   HOH C . 
J 5 HOH   110 410 30  HOH   HOH C . 
J 5 HOH   111 411 21  HOH   HOH C . 
J 5 HOH   112 412 431 HOH   HOH C . 
J 5 HOH   113 413 11  HOH   HOH C . 
J 5 HOH   114 414 468 HOH   HOH C . 
J 5 HOH   115 415 127 HOH   HOH C . 
J 5 HOH   116 416 475 HOH   HOH C . 
J 5 HOH   117 417 66  HOH   HOH C . 
J 5 HOH   118 418 119 HOH   HOH C . 
J 5 HOH   119 419 483 HOH   HOH C . 
J 5 HOH   120 420 77  HOH   HOH C . 
J 5 HOH   121 421 485 HOH   HOH C . 
J 5 HOH   122 422 97  HOH   HOH C . 
J 5 HOH   123 423 145 HOH   HOH C . 
J 5 HOH   124 424 482 HOH   HOH C . 
J 5 HOH   125 425 210 HOH   HOH C . 
J 5 HOH   126 426 192 HOH   HOH C . 
J 5 HOH   127 427 224 HOH   HOH C . 
J 5 HOH   128 428 393 HOH   HOH C . 
J 5 HOH   129 429 367 HOH   HOH C . 
J 5 HOH   130 430 380 HOH   HOH C . 
J 5 HOH   131 431 382 HOH   HOH C . 
J 5 HOH   132 432 230 HOH   HOH C . 
J 5 HOH   133 433 373 HOH   HOH C . 
J 5 HOH   134 434 201 HOH   HOH C . 
J 5 HOH   135 435 400 HOH   HOH C . 
J 5 HOH   136 436 305 HOH   HOH C . 
J 5 HOH   137 437 396 HOH   HOH C . 
J 5 HOH   138 438 102 HOH   HOH C . 
J 5 HOH   139 439 211 HOH   HOH C . 
J 5 HOH   140 440 370 HOH   HOH C . 
J 5 HOH   141 441 154 HOH   HOH C . 
J 5 HOH   142 442 394 HOH   HOH C . 
J 5 HOH   143 443 181 HOH   HOH C . 
J 5 HOH   144 444 67  HOH   HOH C . 
J 5 HOH   145 445 384 HOH   HOH C . 
J 5 HOH   146 446 484 HOH   HOH C . 
J 5 HOH   147 447 286 HOH   HOH C . 
J 5 HOH   148 448 203 HOH   HOH C . 
J 5 HOH   149 449 376 HOH   HOH C . 
J 5 HOH   150 450 417 HOH   HOH C . 
J 5 HOH   151 451 406 HOH   HOH C . 
J 5 HOH   152 452 379 HOH   HOH C . 
J 5 HOH   153 453 490 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           7HWZ 
_cell.length_a           72.581 
_cell.length_b           61.407 
_cell.length_c           65.196 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.85 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWZ 
_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          7HWZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.28 
_exptl_crystal.density_percent_sol   46.11 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-21 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HWZ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             32.53 
_reflns.d_resolution_high            1.39 
_reflns.number_obs                   57533 
_reflns.percent_possible_obs         99.7 
_reflns.pdbx_Rmerge_I_obs            0.069 
_reflns.pdbx_netI_over_sigmaI        14.0 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.075 
_reflns.pdbx_Rpim_I_all              0.029 
_reflns.pdbx_CC_half                 0.994 
_reflns.pdbx_number_measured_all     359239 
_reflns.pdbx_chi_squared             0.66 
_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                  1.39 
_reflns_shell.d_res_low                   1.41 
_reflns_shell.number_measured_all         11978 
_reflns_shell.number_unique_obs           2836 
_reflns_shell.Rmerge_I_obs                1.558 
_reflns_shell.pdbx_chi_squared            0.28 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        96.2 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             1.781 
_reflns_shell.pdbx_Rpim_I_all             0.849 
_reflns_shell.pdbx_CC_half                0.341 
_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                                 7HWZ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     57504 
_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                             19.94 
_refine.ls_d_res_high                            1.389 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_obs                          0.1972 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1966 
_refine.ls_R_factor_R_free                       0.2142 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.290 
_refine.ls_number_reflns_R_free                  1893 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.B_iso_mean                               26.09 
_refine.aniso_B[1][1]                            -0.35890 
_refine.aniso_B[2][2]                            -0.11790 
_refine.aniso_B[3][3]                            0.47670 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.03980 
_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             0.062 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.062 
_refine.pdbx_overall_SU_R_Blow_DPI               0.065 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.064 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWZ 
_refine_analyze.Luzzati_coordinate_error_obs    0.19 
_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        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             290 
_refine_hist.number_atoms_total               2482 
_refine_hist.d_res_high                       1.389 
_refine_hist.d_res_low                        19.94 
# 
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                  0.011 ? 2.00  2262 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  3077 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  759  '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  408  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2256 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.50  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.72 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  277  '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  2019 '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                       1.39 
_refine_ls_shell.d_res_low                        1.40 
_refine_ls_shell.number_reflns_R_work             1122 
_refine_ls_shell.R_factor_R_work                  0.3388 
_refine_ls_shell.percent_reflns_obs               93.12 
_refine_ls_shell.R_factor_R_free                  0.4166 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            2.52 
_refine_ls_shell.number_reflns_R_free             29 
_refine_ls_shell.number_reflns_all                1151 
_refine_ls_shell.R_factor_all                     0.3407 
# 
_struct.entry_id                  7HWZ 
_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-0032634-001 (A71EV2A-x4018)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWZ 
_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 2 ? 
G N N 3 ? 
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 7HWZ A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7HWZ 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 ? ? ? ? ? ? ? 2.372 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.346 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.335 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.097 ? ? 
# 
_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_555 109.3 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.7 ? 
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_555 115.0 ? 
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_555 108.1 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.8 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 115.6 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.0 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.1 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.1 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.9 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.8 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 113.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
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                   7HWZ 
_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 333 ? ? O A HOH 360 ? ? 2.09 
2 1 O A HOH 328 ? ? O A HOH 330 ? ? 2.11 
3 1 O A HOH 375 ? ? O A HOH 389 ? ? 2.17 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    C 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -131.58 
_pdbx_validate_torsion.psi             -31.33 
# 
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 14.9893 7.6029   14.2251 -0.0436 -0.0132 -0.0040 -0.0003 -0.0007 -0.0004 1.5461 1.9049 0.8899 
1.0233  -0.4406 -0.5788 -0.0441 0.0245  0.1552 0.0064  0.0823 -0.0255 0.0320 -0.0457 -0.0382 
'X-RAY DIFFRACTION' 2 ? refined 19.3691 -22.9308 18.4250 -0.0376 -0.0034 -0.0059 -0.0018 -0.0020 0.0094  1.3347 1.6793 0.5780 
-0.7472 0.2569  0.0325  -0.0405 -0.0338 0.1338 -0.0502 0.0707 0.0031  0.0377 0.0015  -0.0302 
# 
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 GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 1 Y 1 C GLN 150 ? B GLN 144 
11 1 N 0 A DMS 203 ? E DMS ?   
12 1 N 0 C DMS 203 ? H DMS ?   
# 
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 
A1BSJ N1   N  N N 1   
A1BSJ C4   C  Y N 2   
A1BSJ C5   C  Y N 3   
A1BSJ C6   C  Y N 4   
A1BSJ C7   C  N N 5   
A1BSJ C8   C  N N 6   
A1BSJ C10  C  N N 7   
A1BSJ C13  C  N N 8   
A1BSJ C15  C  N N 9   
A1BSJ O2   O  N N 10  
A1BSJ C12  C  N S 11  
A1BSJ C11  C  N N 12  
A1BSJ C9   C  N N 13  
A1BSJ C14  C  N N 14  
A1BSJ N    N  N N 15  
A1BSJ O1   O  N N 16  
A1BSJ C1   C  Y N 17  
A1BSJ O    O  N N 18  
A1BSJ C    C  N N 19  
A1BSJ C3   C  Y N 20  
A1BSJ C2   C  Y N 21  
A1BSJ H17  H  N N 22  
A1BSJ H16  H  N N 23  
A1BSJ H6   H  N N 24  
A1BSJ H7   H  N N 25  
A1BSJ H9   H  N N 26  
A1BSJ H8   H  N N 27  
A1BSJ H12  H  N N 28  
A1BSJ H13  H  N N 29  
A1BSJ H20  H  N N 30  
A1BSJ H21  H  N N 31  
A1BSJ H    H  N N 32  
A1BSJ H14  H  N N 33  
A1BSJ H15  H  N N 34  
A1BSJ H10  H  N N 35  
A1BSJ H11  H  N N 36  
A1BSJ H18  H  N N 37  
A1BSJ H19  H  N N 38  
A1BSJ H2   H  N N 39  
A1BSJ H1   H  N N 40  
A1BSJ H3   H  N N 41  
A1BSJ H5   H  N N 42  
A1BSJ H4   H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
DMS   S    S  N N 131 
DMS   O    O  N N 132 
DMS   C1   C  N N 133 
DMS   C2   C  N N 134 
DMS   H11  H  N N 135 
DMS   H12  H  N N 136 
DMS   H13  H  N N 137 
DMS   H21  H  N N 138 
DMS   H22  H  N N 139 
DMS   H23  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
HIS   N    N  N N 190 
HIS   CA   C  N S 191 
HIS   C    C  N N 192 
HIS   O    O  N N 193 
HIS   CB   C  N N 194 
HIS   CG   C  Y N 195 
HIS   ND1  N  Y N 196 
HIS   CD2  C  Y N 197 
HIS   CE1  C  Y N 198 
HIS   NE2  N  Y N 199 
HIS   OXT  O  N N 200 
HIS   H    H  N N 201 
HIS   H2   H  N N 202 
HIS   HA   H  N N 203 
HIS   HB2  H  N N 204 
HIS   HB3  H  N N 205 
HIS   HD1  H  N N 206 
HIS   HD2  H  N N 207 
HIS   HE1  H  N N 208 
HIS   HE2  H  N N 209 
HIS   HXT  H  N N 210 
HOH   O    O  N N 211 
HOH   H1   H  N N 212 
HOH   H2   H  N N 213 
ILE   N    N  N N 214 
ILE   CA   C  N S 215 
ILE   C    C  N N 216 
ILE   O    O  N N 217 
ILE   CB   C  N S 218 
ILE   CG1  C  N N 219 
ILE   CG2  C  N N 220 
ILE   CD1  C  N N 221 
ILE   OXT  O  N N 222 
ILE   H    H  N N 223 
ILE   H2   H  N N 224 
ILE   HA   H  N N 225 
ILE   HB   H  N N 226 
ILE   HG12 H  N N 227 
ILE   HG13 H  N N 228 
ILE   HG21 H  N N 229 
ILE   HG22 H  N N 230 
ILE   HG23 H  N N 231 
ILE   HD11 H  N N 232 
ILE   HD12 H  N N 233 
ILE   HD13 H  N N 234 
ILE   HXT  H  N N 235 
LEU   N    N  N N 236 
LEU   CA   C  N S 237 
LEU   C    C  N N 238 
LEU   O    O  N N 239 
LEU   CB   C  N N 240 
LEU   CG   C  N N 241 
LEU   CD1  C  N N 242 
LEU   CD2  C  N N 243 
LEU   OXT  O  N N 244 
LEU   H    H  N N 245 
LEU   H2   H  N N 246 
LEU   HA   H  N N 247 
LEU   HB2  H  N N 248 
LEU   HB3  H  N N 249 
LEU   HG   H  N N 250 
LEU   HD11 H  N N 251 
LEU   HD12 H  N N 252 
LEU   HD13 H  N N 253 
LEU   HD21 H  N N 254 
LEU   HD22 H  N N 255 
LEU   HD23 H  N N 256 
LEU   HXT  H  N N 257 
LYS   N    N  N N 258 
LYS   CA   C  N S 259 
LYS   C    C  N N 260 
LYS   O    O  N N 261 
LYS   CB   C  N N 262 
LYS   CG   C  N N 263 
LYS   CD   C  N N 264 
LYS   CE   C  N N 265 
LYS   NZ   N  N N 266 
LYS   OXT  O  N N 267 
LYS   H    H  N N 268 
LYS   H2   H  N N 269 
LYS   HA   H  N N 270 
LYS   HB2  H  N N 271 
LYS   HB3  H  N N 272 
LYS   HG2  H  N N 273 
LYS   HG3  H  N N 274 
LYS   HD2  H  N N 275 
LYS   HD3  H  N N 276 
LYS   HE2  H  N N 277 
LYS   HE3  H  N N 278 
LYS   HZ1  H  N N 279 
LYS   HZ2  H  N N 280 
LYS   HZ3  H  N N 281 
LYS   HXT  H  N N 282 
MET   N    N  N N 283 
MET   CA   C  N S 284 
MET   C    C  N N 285 
MET   O    O  N N 286 
MET   CB   C  N N 287 
MET   CG   C  N N 288 
MET   SD   S  N N 289 
MET   CE   C  N N 290 
MET   OXT  O  N N 291 
MET   H    H  N N 292 
MET   H2   H  N N 293 
MET   HA   H  N N 294 
MET   HB2  H  N N 295 
MET   HB3  H  N N 296 
MET   HG2  H  N N 297 
MET   HG3  H  N N 298 
MET   HE1  H  N N 299 
MET   HE2  H  N N 300 
MET   HE3  H  N N 301 
MET   HXT  H  N N 302 
PHE   N    N  N N 303 
PHE   CA   C  N S 304 
PHE   C    C  N N 305 
PHE   O    O  N N 306 
PHE   CB   C  N N 307 
PHE   CG   C  Y N 308 
PHE   CD1  C  Y N 309 
PHE   CD2  C  Y N 310 
PHE   CE1  C  Y N 311 
PHE   CE2  C  Y N 312 
PHE   CZ   C  Y N 313 
PHE   OXT  O  N N 314 
PHE   H    H  N N 315 
PHE   H2   H  N N 316 
PHE   HA   H  N N 317 
PHE   HB2  H  N N 318 
PHE   HB3  H  N N 319 
PHE   HD1  H  N N 320 
PHE   HD2  H  N N 321 
PHE   HE1  H  N N 322 
PHE   HE2  H  N N 323 
PHE   HZ   H  N N 324 
PHE   HXT  H  N N 325 
PRO   N    N  N N 326 
PRO   CA   C  N S 327 
PRO   C    C  N N 328 
PRO   O    O  N N 329 
PRO   CB   C  N N 330 
PRO   CG   C  N N 331 
PRO   CD   C  N N 332 
PRO   OXT  O  N N 333 
PRO   H    H  N N 334 
PRO   HA   H  N N 335 
PRO   HB2  H  N N 336 
PRO   HB3  H  N N 337 
PRO   HG2  H  N N 338 
PRO   HG3  H  N N 339 
PRO   HD2  H  N N 340 
PRO   HD3  H  N N 341 
PRO   HXT  H  N N 342 
SER   N    N  N N 343 
SER   CA   C  N S 344 
SER   C    C  N N 345 
SER   O    O  N N 346 
SER   CB   C  N N 347 
SER   OG   O  N N 348 
SER   OXT  O  N N 349 
SER   H    H  N N 350 
SER   H2   H  N N 351 
SER   HA   H  N N 352 
SER   HB2  H  N N 353 
SER   HB3  H  N N 354 
SER   HG   H  N N 355 
SER   HXT  H  N N 356 
THR   N    N  N N 357 
THR   CA   C  N S 358 
THR   C    C  N N 359 
THR   O    O  N N 360 
THR   CB   C  N R 361 
THR   OG1  O  N N 362 
THR   CG2  C  N N 363 
THR   OXT  O  N N 364 
THR   H    H  N N 365 
THR   H2   H  N N 366 
THR   HA   H  N N 367 
THR   HB   H  N N 368 
THR   HG1  H  N N 369 
THR   HG21 H  N N 370 
THR   HG22 H  N N 371 
THR   HG23 H  N N 372 
THR   HXT  H  N N 373 
TRP   N    N  N N 374 
TRP   CA   C  N S 375 
TRP   C    C  N N 376 
TRP   O    O  N N 377 
TRP   CB   C  N N 378 
TRP   CG   C  Y N 379 
TRP   CD1  C  Y N 380 
TRP   CD2  C  Y N 381 
TRP   NE1  N  Y N 382 
TRP   CE2  C  Y N 383 
TRP   CE3  C  Y N 384 
TRP   CZ2  C  Y N 385 
TRP   CZ3  C  Y N 386 
TRP   CH2  C  Y N 387 
TRP   OXT  O  N N 388 
TRP   H    H  N N 389 
TRP   H2   H  N N 390 
TRP   HA   H  N N 391 
TRP   HB2  H  N N 392 
TRP   HB3  H  N N 393 
TRP   HD1  H  N N 394 
TRP   HE1  H  N N 395 
TRP   HE3  H  N N 396 
TRP   HZ2  H  N N 397 
TRP   HZ3  H  N N 398 
TRP   HH2  H  N N 399 
TRP   HXT  H  N N 400 
TYR   N    N  N N 401 
TYR   CA   C  N S 402 
TYR   C    C  N N 403 
TYR   O    O  N N 404 
TYR   CB   C  N N 405 
TYR   CG   C  Y N 406 
TYR   CD1  C  Y N 407 
TYR   CD2  C  Y N 408 
TYR   CE1  C  Y N 409 
TYR   CE2  C  Y N 410 
TYR   CZ   C  Y N 411 
TYR   OH   O  N N 412 
TYR   OXT  O  N N 413 
TYR   H    H  N N 414 
TYR   H2   H  N N 415 
TYR   HA   H  N N 416 
TYR   HB2  H  N N 417 
TYR   HB3  H  N N 418 
TYR   HD1  H  N N 419 
TYR   HD2  H  N N 420 
TYR   HE1  H  N N 421 
TYR   HE2  H  N N 422 
TYR   HH   H  N N 423 
TYR   HXT  H  N N 424 
VAL   N    N  N N 425 
VAL   CA   C  N S 426 
VAL   C    C  N N 427 
VAL   O    O  N N 428 
VAL   CB   C  N N 429 
VAL   CG1  C  N N 430 
VAL   CG2  C  N N 431 
VAL   OXT  O  N N 432 
VAL   H    H  N N 433 
VAL   H2   H  N N 434 
VAL   HA   H  N N 435 
VAL   HB   H  N N 436 
VAL   HG11 H  N N 437 
VAL   HG12 H  N N 438 
VAL   HG13 H  N N 439 
VAL   HG21 H  N N 440 
VAL   HG22 H  N N 441 
VAL   HG23 H  N N 442 
VAL   HXT  H  N N 443 
ZN    ZN   ZN N N 444 
# 
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 
A1BSJ C   O    sing N N 1   
A1BSJ O   C1   sing N N 2   
A1BSJ C1  C2   doub Y N 3   
A1BSJ C2  C3   sing Y N 4   
A1BSJ C3  C4   doub Y N 5   
A1BSJ C4  C5   sing Y N 6   
A1BSJ C5  C6   doub Y N 7   
A1BSJ C1  C6   sing Y N 8   
A1BSJ C6  C7   sing N N 9   
A1BSJ C7  C8   sing N N 10  
A1BSJ O1  C8   doub N N 11  
A1BSJ C8  N    sing N N 12  
A1BSJ N   C9   sing N N 13  
A1BSJ C9  C10  sing N N 14  
A1BSJ C10 C11  sing N N 15  
A1BSJ C11 C12  sing N N 16  
A1BSJ C12 C13  sing N N 17  
A1BSJ N1  C13  sing N N 18  
A1BSJ C13 O2   doub N N 19  
A1BSJ C14 C12  sing N N 20  
A1BSJ C15 C14  sing N N 21  
A1BSJ N   C15  sing N N 22  
A1BSJ N1  H17  sing N N 23  
A1BSJ N1  H16  sing N N 24  
A1BSJ C4  H6   sing N N 25  
A1BSJ C5  H7   sing N N 26  
A1BSJ C7  H9   sing N N 27  
A1BSJ C7  H8   sing N N 28  
A1BSJ C10 H12  sing N N 29  
A1BSJ C10 H13  sing N N 30  
A1BSJ C15 H20  sing N N 31  
A1BSJ C15 H21  sing N N 32  
A1BSJ C12 H    sing N N 33  
A1BSJ C11 H14  sing N N 34  
A1BSJ C11 H15  sing N N 35  
A1BSJ C9  H10  sing N N 36  
A1BSJ C9  H11  sing N N 37  
A1BSJ C14 H18  sing N N 38  
A1BSJ C14 H19  sing N N 39  
A1BSJ C   H2   sing N N 40  
A1BSJ C   H1   sing N N 41  
A1BSJ C   H3   sing N N 42  
A1BSJ C3  H5   sing N N 43  
A1BSJ C2  H4   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
DMS   S   O    doub N N 127 
DMS   S   C1   sing N N 128 
DMS   S   C2   sing N N 129 
DMS   C1  H11  sing N N 130 
DMS   C1  H12  sing N N 131 
DMS   C1  H13  sing N N 132 
DMS   C2  H21  sing N N 133 
DMS   C2  H22  sing N N 134 
DMS   C2  H23  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
HIS   N   CA   sing N N 182 
HIS   N   H    sing N N 183 
HIS   N   H2   sing N N 184 
HIS   CA  C    sing N N 185 
HIS   CA  CB   sing N N 186 
HIS   CA  HA   sing N N 187 
HIS   C   O    doub N N 188 
HIS   C   OXT  sing N N 189 
HIS   CB  CG   sing N N 190 
HIS   CB  HB2  sing N N 191 
HIS   CB  HB3  sing N N 192 
HIS   CG  ND1  sing Y N 193 
HIS   CG  CD2  doub Y N 194 
HIS   ND1 CE1  doub Y N 195 
HIS   ND1 HD1  sing N N 196 
HIS   CD2 NE2  sing Y N 197 
HIS   CD2 HD2  sing N N 198 
HIS   CE1 NE2  sing Y N 199 
HIS   CE1 HE1  sing N N 200 
HIS   NE2 HE2  sing N N 201 
HIS   OXT HXT  sing N N 202 
HOH   O   H1   sing N N 203 
HOH   O   H2   sing N N 204 
ILE   N   CA   sing N N 205 
ILE   N   H    sing N N 206 
ILE   N   H2   sing N N 207 
ILE   CA  C    sing N N 208 
ILE   CA  CB   sing N N 209 
ILE   CA  HA   sing N N 210 
ILE   C   O    doub N N 211 
ILE   C   OXT  sing N N 212 
ILE   CB  CG1  sing N N 213 
ILE   CB  CG2  sing N N 214 
ILE   CB  HB   sing N N 215 
ILE   CG1 CD1  sing N N 216 
ILE   CG1 HG12 sing N N 217 
ILE   CG1 HG13 sing N N 218 
ILE   CG2 HG21 sing N N 219 
ILE   CG2 HG22 sing N N 220 
ILE   CG2 HG23 sing N N 221 
ILE   CD1 HD11 sing N N 222 
ILE   CD1 HD12 sing N N 223 
ILE   CD1 HD13 sing N N 224 
ILE   OXT HXT  sing N N 225 
LEU   N   CA   sing N N 226 
LEU   N   H    sing N N 227 
LEU   N   H2   sing N N 228 
LEU   CA  C    sing N N 229 
LEU   CA  CB   sing N N 230 
LEU   CA  HA   sing N N 231 
LEU   C   O    doub N N 232 
LEU   C   OXT  sing N N 233 
LEU   CB  CG   sing N N 234 
LEU   CB  HB2  sing N N 235 
LEU   CB  HB3  sing N N 236 
LEU   CG  CD1  sing N N 237 
LEU   CG  CD2  sing N N 238 
LEU   CG  HG   sing N N 239 
LEU   CD1 HD11 sing N N 240 
LEU   CD1 HD12 sing N N 241 
LEU   CD1 HD13 sing N N 242 
LEU   CD2 HD21 sing N N 243 
LEU   CD2 HD22 sing N N 244 
LEU   CD2 HD23 sing N N 245 
LEU   OXT HXT  sing N N 246 
LYS   N   CA   sing N N 247 
LYS   N   H    sing N N 248 
LYS   N   H2   sing N N 249 
LYS   CA  C    sing N N 250 
LYS   CA  CB   sing N N 251 
LYS   CA  HA   sing N N 252 
LYS   C   O    doub N N 253 
LYS   C   OXT  sing N N 254 
LYS   CB  CG   sing N N 255 
LYS   CB  HB2  sing N N 256 
LYS   CB  HB3  sing N N 257 
LYS   CG  CD   sing N N 258 
LYS   CG  HG2  sing N N 259 
LYS   CG  HG3  sing N N 260 
LYS   CD  CE   sing N N 261 
LYS   CD  HD2  sing N N 262 
LYS   CD  HD3  sing N N 263 
LYS   CE  NZ   sing N N 264 
LYS   CE  HE2  sing N N 265 
LYS   CE  HE3  sing N N 266 
LYS   NZ  HZ1  sing N N 267 
LYS   NZ  HZ2  sing N N 268 
LYS   NZ  HZ3  sing N N 269 
LYS   OXT HXT  sing N N 270 
MET   N   CA   sing N N 271 
MET   N   H    sing N N 272 
MET   N   H2   sing N N 273 
MET   CA  C    sing N N 274 
MET   CA  CB   sing N N 275 
MET   CA  HA   sing N N 276 
MET   C   O    doub N N 277 
MET   C   OXT  sing N N 278 
MET   CB  CG   sing N N 279 
MET   CB  HB2  sing N N 280 
MET   CB  HB3  sing N N 281 
MET   CG  SD   sing N N 282 
MET   CG  HG2  sing N N 283 
MET   CG  HG3  sing N N 284 
MET   SD  CE   sing N N 285 
MET   CE  HE1  sing N N 286 
MET   CE  HE2  sing N N 287 
MET   CE  HE3  sing N N 288 
MET   OXT HXT  sing N N 289 
PHE   N   CA   sing N N 290 
PHE   N   H    sing N N 291 
PHE   N   H2   sing N N 292 
PHE   CA  C    sing N N 293 
PHE   CA  CB   sing N N 294 
PHE   CA  HA   sing N N 295 
PHE   C   O    doub N N 296 
PHE   C   OXT  sing N N 297 
PHE   CB  CG   sing N N 298 
PHE   CB  HB2  sing N N 299 
PHE   CB  HB3  sing N N 300 
PHE   CG  CD1  doub Y N 301 
PHE   CG  CD2  sing Y N 302 
PHE   CD1 CE1  sing Y N 303 
PHE   CD1 HD1  sing N N 304 
PHE   CD2 CE2  doub Y N 305 
PHE   CD2 HD2  sing N N 306 
PHE   CE1 CZ   doub Y N 307 
PHE   CE1 HE1  sing N N 308 
PHE   CE2 CZ   sing Y N 309 
PHE   CE2 HE2  sing N N 310 
PHE   CZ  HZ   sing N N 311 
PHE   OXT HXT  sing N N 312 
PRO   N   CA   sing N N 313 
PRO   N   CD   sing N N 314 
PRO   N   H    sing N N 315 
PRO   CA  C    sing N N 316 
PRO   CA  CB   sing N N 317 
PRO   CA  HA   sing N N 318 
PRO   C   O    doub N N 319 
PRO   C   OXT  sing N N 320 
PRO   CB  CG   sing N N 321 
PRO   CB  HB2  sing N N 322 
PRO   CB  HB3  sing N N 323 
PRO   CG  CD   sing N N 324 
PRO   CG  HG2  sing N N 325 
PRO   CG  HG3  sing N N 326 
PRO   CD  HD2  sing N N 327 
PRO   CD  HD3  sing N N 328 
PRO   OXT HXT  sing N N 329 
SER   N   CA   sing N N 330 
SER   N   H    sing N N 331 
SER   N   H2   sing N N 332 
SER   CA  C    sing N N 333 
SER   CA  CB   sing N N 334 
SER   CA  HA   sing N N 335 
SER   C   O    doub N N 336 
SER   C   OXT  sing N N 337 
SER   CB  OG   sing N N 338 
SER   CB  HB2  sing N N 339 
SER   CB  HB3  sing N N 340 
SER   OG  HG   sing N N 341 
SER   OXT HXT  sing N N 342 
THR   N   CA   sing N N 343 
THR   N   H    sing N N 344 
THR   N   H2   sing N N 345 
THR   CA  C    sing N N 346 
THR   CA  CB   sing N N 347 
THR   CA  HA   sing N N 348 
THR   C   O    doub N N 349 
THR   C   OXT  sing N N 350 
THR   CB  OG1  sing N N 351 
THR   CB  CG2  sing N N 352 
THR   CB  HB   sing N N 353 
THR   OG1 HG1  sing N N 354 
THR   CG2 HG21 sing N N 355 
THR   CG2 HG22 sing N N 356 
THR   CG2 HG23 sing N N 357 
THR   OXT HXT  sing N N 358 
TRP   N   CA   sing N N 359 
TRP   N   H    sing N N 360 
TRP   N   H2   sing N N 361 
TRP   CA  C    sing N N 362 
TRP   CA  CB   sing N N 363 
TRP   CA  HA   sing N N 364 
TRP   C   O    doub N N 365 
TRP   C   OXT  sing N N 366 
TRP   CB  CG   sing N N 367 
TRP   CB  HB2  sing N N 368 
TRP   CB  HB3  sing N N 369 
TRP   CG  CD1  doub Y N 370 
TRP   CG  CD2  sing Y N 371 
TRP   CD1 NE1  sing Y N 372 
TRP   CD1 HD1  sing N N 373 
TRP   CD2 CE2  doub Y N 374 
TRP   CD2 CE3  sing Y N 375 
TRP   NE1 CE2  sing Y N 376 
TRP   NE1 HE1  sing N N 377 
TRP   CE2 CZ2  sing Y N 378 
TRP   CE3 CZ3  doub Y N 379 
TRP   CE3 HE3  sing N N 380 
TRP   CZ2 CH2  doub Y N 381 
TRP   CZ2 HZ2  sing N N 382 
TRP   CZ3 CH2  sing Y N 383 
TRP   CZ3 HZ3  sing N N 384 
TRP   CH2 HH2  sing N N 385 
TRP   OXT HXT  sing N N 386 
TYR   N   CA   sing N N 387 
TYR   N   H    sing N N 388 
TYR   N   H2   sing N N 389 
TYR   CA  C    sing N N 390 
TYR   CA  CB   sing N N 391 
TYR   CA  HA   sing N N 392 
TYR   C   O    doub N N 393 
TYR   C   OXT  sing N N 394 
TYR   CB  CG   sing N N 395 
TYR   CB  HB2  sing N N 396 
TYR   CB  HB3  sing N N 397 
TYR   CG  CD1  doub Y N 398 
TYR   CG  CD2  sing Y N 399 
TYR   CD1 CE1  sing Y N 400 
TYR   CD1 HD1  sing N N 401 
TYR   CD2 CE2  doub Y N 402 
TYR   CD2 HD2  sing N N 403 
TYR   CE1 CZ   doub Y N 404 
TYR   CE1 HE1  sing N N 405 
TYR   CE2 CZ   sing Y N 406 
TYR   CE2 HE2  sing N N 407 
TYR   CZ  OH   sing N N 408 
TYR   OH  HH   sing N N 409 
TYR   OXT HXT  sing N N 410 
VAL   N   CA   sing N N 411 
VAL   N   H    sing N N 412 
VAL   N   H2   sing N N 413 
VAL   CA  C    sing N N 414 
VAL   CA  CB   sing N N 415 
VAL   CA  HA   sing N N 416 
VAL   C   O    doub N N 417 
VAL   C   OXT  sing N N 418 
VAL   CB  CG1  sing N N 419 
VAL   CB  CG2  sing N N 420 
VAL   CB  HB   sing N N 421 
VAL   CG1 HG11 sing N N 422 
VAL   CG1 HG12 sing N N 423 
VAL   CG1 HG13 sing N N 424 
VAL   CG2 HG21 sing N N 425 
VAL   CG2 HG22 sing N N 426 
VAL   CG2 HG23 sing N N 427 
VAL   OXT HXT  sing N N 428 
# 
_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                    7HWZ 
_atom_sites.fract_transf_matrix[1][1]   0.013778 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000686 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016285 
_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]   0.015357 
_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   ? 18.363 7.282   24.412 1.00 22.76 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.548 7.414   23.574 1.00 22.62 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.708 6.244   22.611 1.00 23.11 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.056 5.210   22.765 1.00 23.52 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.781 7.547   24.472 1.00 25.43 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.943 6.340   25.201 1.00 29.51 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.569 6.417   21.592 1.00 21.66 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.871 5.380   20.618 1.00 20.32 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.284 5.911   19.260 1.00 19.10 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.920 7.034   18.897 1.00 19.53 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.977 5.087   18.477 1.00 17.46 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.430 5.504   17.170 1.00 19.23 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.494 4.316   16.211 1.00 19.33 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.610 3.163   16.660 1.00 20.37 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.838 6.108   17.303 1.00 20.32 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.468 4.607   14.888 1.00 17.27 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.674 3.617   13.839 1.00 17.60 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.093 3.840   13.329 1.00 18.53 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.456 4.970   13.025 1.00 18.67 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.685 3.812   12.670 1.00 17.13 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.231 3.757   13.190 1.00 16.93 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.908 2.762   11.591 1.00 18.90 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.258 4.322   12.080 1.00 17.80 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.898 2.778   13.247 1.00 19.52 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.253 2.902   12.709 1.00 20.37 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.317 2.130   11.427 1.00 21.33 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.246 0.902   11.474 1.00 23.39 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.279 2.351   13.720 1.00 20.90 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.358 3.171   14.980 1.00 22.32 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 26.543 2.892   16.061 1.00 23.88 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 28.198 4.272   15.063 1.00 23.60 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 26.577 3.665   17.207 1.00 25.63 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 28.256 5.043   16.213 1.00 25.41 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.440 4.729   17.281 1.00 26.50 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.445 5.492   18.414 1.00 30.04 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.374 2.817   10.268 1.00 21.58 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.396 2.164   8.956  1.00 22.48 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.533 2.735   8.152  1.00 24.01 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.645 3.953   8.031  1.00 24.57 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.025 2.348   8.220  1.00 23.96 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.550 3.805   8.241  1.00 24.24 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.101 1.828   6.782  1.00 25.70 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.447 1.891   7.659  1.00 25.44 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.590 2.382   6.890  1.00 25.84 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.419 3.344   7.728  1.00 26.52 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.661 3.073   8.906  1.00 27.14 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.716 4.524   7.191  1.00 26.03 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.428 5.531   7.971  1.00 26.53 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.480 6.637   8.424  1.00 24.61 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.876 7.809   8.523  1.00 25.40 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.618 6.076   7.203  1.00 29.48 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.709 5.059   7.062  1.00 36.23 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.391 4.717   8.035  1.00 39.34 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.869 4.548   5.858  1.00 37.56 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.231 6.250   8.775  1.00 22.21 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.218 7.225   9.212  1.00 20.73 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.616 6.787   10.550 1.00 19.60 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.506 5.586   10.822 1.00 19.74 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.053 7.268   8.202  1.00 20.94 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.428 7.841   6.854  1.00 21.68 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.072 9.072   6.751  1.00 23.21 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.185 7.133   5.688  1.00 23.94 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.396 9.616   5.513  1.00 24.58 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.543 7.650   4.441  1.00 25.58 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.157 8.892   4.362  1.00 26.30 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.516 9.433   3.151  1.00 29.24 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.203 7.776   11.362 1.00 18.91 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.494 7.577   12.610 1.00 19.52 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.180 8.395   12.449 1.00 18.88 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.226 9.586   12.123 1.00 18.95 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.348 8.085   13.791 1.00 20.34 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.607 8.350   15.085 1.00 23.83 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.543 8.723   16.222 1.00 23.49 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.967 9.705   17.133 1.00 25.69 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.531 9.451   18.360 1.00 28.90 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.550 8.209   18.839 1.00 30.26 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.054 10.433  19.117 1.00 28.02 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.013 7.743   12.610 1.00 18.42 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.713 8.412   12.499 1.00 17.23 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.130 8.528   13.879 1.00 17.04 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.993 7.509   14.580 1.00 16.81 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.731 7.581   11.621 1.00 16.73 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.440 8.396   11.381 1.00 16.50 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.394 7.138   10.308 1.00 17.41 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.825 9.746   14.311 1.00 15.90 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.273 9.984   15.639 1.00 16.37 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.054 10.892  15.552 1.00 15.56 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.818 11.571  14.525 1.00 15.99 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.325 10.638  16.579 1.00 18.33 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.461 9.665   16.869 1.00 20.74 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.857 11.948  15.967 1.00 18.78 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.273 10.988  16.649 1.00 14.91 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.220 12.003  16.716 1.00 15.30 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.928 13.378  16.730 1.00 15.85 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.884 13.583  17.512 1.00 16.25 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.436 11.907  18.033 1.00 16.05 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.609 10.651  18.109 1.00 17.04 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.077 9.624   18.637 1.00 17.75 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.388 10.701  17.577 1.00 16.64 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.484 14.298  15.868 1.00 14.79 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.132 15.620  15.809 1.00 15.46 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.126 16.312  17.205 1.00 16.67 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.140 16.931  17.580 1.00 19.11 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.429 16.470  14.766 1.00 14.79 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.175 17.766  14.459 1.00 17.04 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.229 18.599  13.602 1.00 17.53 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 18.837 19.841  13.091 1.00 19.53 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 18.870 20.987  13.763 1.00 18.82 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.385 21.057  14.996 1.00 20.80 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.381 22.087  13.197 1.00 20.35 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.039 16.121  17.986 1.00 16.65 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.957 16.801  19.303 1.00 17.74 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.889 16.197  20.352 1.00 19.25 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.086 16.836  21.401 1.00 22.81 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.496 16.899  19.812 1.00 18.68 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.903 15.612  20.306 1.00 19.68 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.318 14.688  19.433 1.00 20.03 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.818 15.135  21.573 1.00 20.17 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.895 13.682  20.210 1.00 20.56 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.188 13.901  21.502 1.00 20.73 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.478 15.020  20.077 1.00 18.24 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.418 14.363  20.981 1.00 18.48 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.862 14.388  20.439 1.00 18.97 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.760 13.826  21.077 1.00 21.17 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 19.963 12.921  21.269 1.00 18.04 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.589 12.794  21.937 1.00 19.86 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.245 11.301  22.150 1.00 20.54 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.533 13.605  23.279 1.00 20.80 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.105 15.016  19.264 1.00 18.98 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.456 15.025  18.684 1.00 18.59 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.443 15.728  19.637 1.00 20.15 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.079 16.683  20.280 1.00 20.55 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.435 15.779  17.354 1.00 18.85 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.638 15.223  19.698 1.00 21.24 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.672 15.765  20.600 1.00 22.59 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.484 16.857  19.913 1.00 24.29 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.378 17.047  18.702 1.00 24.34 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.590 14.602  21.044 1.00 24.66 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.350 14.132  19.922 1.00 24.93 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.827 13.451  21.681 1.00 26.16 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.420 17.519  20.665 1.00 24.48 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.323 18.482  20.032 1.00 25.72 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.148 17.771  18.944 1.00 23.33 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.353 18.332  17.872 1.00 24.11 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.306 19.074  21.082 1.00 29.48 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 29.640 19.807  22.210 1.00 38.48 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 28.946 20.991  21.998 1.00 42.65 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.664 19.548  23.540 1.00 41.92 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 28.536 21.389  23.196 1.00 44.02 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 28.948 20.551  24.158 1.00 44.08 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.568 16.508  19.201 1.00 24.21 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.335 15.767  18.209 1.00 24.20 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.541 15.446  16.952 1.00 22.54 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.074 15.466  15.840 1.00 22.99 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.919 14.495  18.787 1.00 27.41 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.384 14.524  18.585 1.00 35.66 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.043 15.526  18.933 1.00 35.38 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.916 13.476  17.955 1.00 40.55 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.241 15.124  17.106 1.00 20.37 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.399 14.909  15.922 1.00 20.14 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.378 16.168  15.048 1.00 19.78 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.535 16.070  13.822 1.00 20.55 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 26.964 14.575  16.355 1.00 19.30 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.824 13.159  16.855 1.00 22.56 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.419 12.270  16.243 1.00 23.19 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.095 12.949  17.882 1.00 22.07 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.188 17.357  15.685 1.00 19.73 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.105 18.604  14.923 1.00 21.13 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.443 18.981  14.274 1.00 23.35 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.476 19.549  13.168 1.00 24.03 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.578 19.721  15.821 1.00 20.43 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.064 19.718  15.913 1.00 20.65 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.308 19.286  16.963 1.00 22.52 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.141 20.227  14.936 1.00 20.38 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 23.960 19.478  16.689 1.00 22.14 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 23.838 20.052  15.451 1.00 21.64 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.288 20.813  13.673 1.00 21.73 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.687 20.447  14.742 1.00 21.65 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.140 21.190  12.976 1.00 21.97 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.870 21.007  13.513 1.00 22.34 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.552 18.634  14.938 1.00 23.28 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 31.893 18.923  14.376 1.00 25.07 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.218 18.021  13.165 1.00 25.88 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.167 18.296  12.423 1.00 26.53 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 32.950 18.720  15.447 1.00 25.31 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.546 16.883  13.041 1.00 23.49 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.761 15.958  11.935 1.00 23.74 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.439 15.810  11.139 1.00 22.59 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.135 14.747  10.599 1.00 21.54 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.181 14.606  12.510 1.00 24.82 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.532 14.655  13.150 1.00 28.14 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.547 14.641  12.439 1.00 28.87 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.555 14.736  14.484 1.00 27.87 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.692 16.904  11.006 1.00 20.90 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.395 16.883  10.336 1.00 20.92 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.452 16.506  8.846  1.00 22.86 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.261 17.056  8.086  1.00 24.74 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.771 18.247  10.515 1.00 21.05 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.429 18.456  9.812  1.00 21.60 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.353 17.587  10.452 1.00 21.85 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.006 19.930  9.881  1.00 22.24 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.570 15.575  8.422  1.00 22.26 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.406 15.204  7.014  1.00 22.36 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.070 15.796  6.496  1.00 22.73 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.993 16.416  5.423  1.00 24.08 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.413 13.655  6.881  1.00 23.36 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.010 13.211  5.482  1.00 23.67 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.784 13.091  7.257  1.00 24.27 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.004 15.634  7.304  1.00 21.28 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.675 16.093  6.898  1.00 21.09 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.773 16.175  8.121  1.00 19.41 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.918 15.358  9.033  1.00 19.50 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.078 15.090  5.873  1.00 21.88 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.613 15.259  5.542  1.00 22.90 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.057 16.096  4.614  1.00 24.52 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.531 14.528  6.119  1.00 22.40 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.679 15.958  4.611  1.00 24.89 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.335 14.985  5.517  1.00 22.98 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.455 13.532  7.089  1.00 22.02 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.083 14.444  5.836  1.00 22.89 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.215 13.012  7.413  1.00 22.83 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.045 13.485  6.798  1.00 22.59 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.892 17.152  8.142  1.00 19.00 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.894 17.228  9.222  1.00 19.36 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.596 17.785  8.693  1.00 18.56 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.619 18.596  7.758  1.00 19.37 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.396 18.031  10.437 1.00 21.71 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 21.953 19.426  10.141 1.00 21.54 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 20.927 20.542  9.952  1.00 21.77 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.216 21.485  9.180  1.00 27.10 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.830 20.472  10.535 1.00 21.37 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.482 17.414  9.316  1.00 18.08 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.183 17.931  8.886  1.00 18.30 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.309 18.095  10.120 1.00 18.75 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.866 17.090  10.693 1.00 18.13 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.537 16.982  7.846  1.00 19.80 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.277 17.550  7.214  1.00 28.28 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.596 18.372  7.876  1.00 29.99 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.949 17.143  6.076  1.00 27.36 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.112 19.359  10.564 1.00 18.90 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.324 19.646  11.752 0.50 20.59 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.314 19.651  11.752 0.50 20.23 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.878 19.153  11.598 1.00 21.42 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.275 18.677  12.572 1.00 22.93 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.376 21.140  12.067 0.50 23.33 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.330 21.147  12.063 0.50 21.95 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.508 21.490  13.131 0.50 27.02 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.730 21.907  11.027 0.50 23.79 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.324 19.218  10.375 1.00 20.95 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.946 18.733  10.165 1.00 21.73 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.825 17.221  10.310 1.00 21.64 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.719 16.743  10.461 1.00 23.22 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.394 19.169  8.806  1.00 26.35 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.860 18.342  7.754  1.00 31.47 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.942 16.483  10.247 1.00 18.92 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.885 15.012  10.419 1.00 17.40 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.464 14.562  11.775 1.00 17.39 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.416 13.368  12.076 1.00 17.06 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.728 14.308  9.310  1.00 17.19 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.106 14.502  7.913  1.00 17.58 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.934 13.861  6.804  1.00 19.57 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.970 12.382  6.921  1.00 18.70 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.184 11.554  5.895  1.00 20.00 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.363 12.038  4.660  1.00 20.88 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.155 10.234  6.077  1.00 18.73 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.037 15.478  12.571 1.00 16.24 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.737 15.123  13.813 1.00 15.94 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.896 14.167  13.530 1.00 14.87 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.194 13.314  14.379 1.00 15.84 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.809 14.545  14.901 1.00 16.60 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.502 14.303  16.235 1.00 18.17 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.321 15.161  16.656 1.00 17.63 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.183 13.266  16.905 1.00 17.74 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.585 14.317  12.385 1.00 14.25 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.743 13.464  12.094 1.00 14.35 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.024 14.235  11.912 1.00 15.09 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.016 15.321  11.330 1.00 15.60 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.544 12.636  10.808 1.00 14.58 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.498 11.516  10.866 1.00 15.35 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.473 10.814  9.490  1.00 16.29 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.850 10.502  11.979 1.00 14.73 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.135 13.617  12.288 1.00 14.32 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.460 14.155  12.041 1.00 15.47 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.367 12.992  11.728 1.00 16.47 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.287 11.957  12.404 1.00 16.53 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 21.994 14.969  13.235 1.00 15.34 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.375 15.651  13.007 1.00 16.60 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.452 16.947  13.807 1.00 18.04 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.513 14.746  13.499 1.00 17.84 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.235 13.128  10.707 1.00 15.91 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.214 12.098  10.343 1.00 16.73 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.606 12.726  10.440 1.00 18.26 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.827 13.825  9.923  1.00 19.05 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.966 11.574  8.908  1.00 17.76 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.040 10.546  8.505  1.00 19.10 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.576 10.954  8.810  1.00 17.58 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.492 12.045  11.143 1.00 18.65 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.874 12.481  11.284 1.00 19.73 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.817 11.423  10.712 1.00 21.83 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.445 10.254  10.545 1.00 21.40 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.205 12.808  12.743 1.00 21.64 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.053 11.703  13.625 1.00 22.10 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.076 11.835  10.430 1.00 22.93 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.053 10.871  9.911  1.00 24.72 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.825 10.159  11.033 1.00 25.64 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.046 10.726  12.098 1.00 25.67 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.003 11.570  8.946  1.00 27.53 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.649 12.612  9.645  1.00 30.40 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.240 8.920   10.800 1.00 26.90 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.004 8.141   11.784 1.00 29.52 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.313 7.644   11.128 1.00 33.91 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.411 7.580   9.899  1.00 34.59 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.200 6.923   12.297 1.00 30.72 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.126 5.947   11.257 1.00 32.14 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.808 7.280   12.745 1.00 29.91 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.276 7.248   11.940 1.00 37.29 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.530 6.691   11.436 1.00 40.17 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.440 5.153   11.367 1.00 42.38 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.048 4.525   10.487 1.00 43.79 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.685 7.151   12.335 1.00 43.24 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.375 6.791   13.689 1.00 45.25 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.905 8.645   12.261 1.00 44.03 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.700 4.541   12.305 1.00 41.82 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.554 3.094   12.356 1.00 41.50 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.337 2.651   11.536 1.00 41.40 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.345 3.378   11.464 1.00 40.67 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.402 2.651   13.803 1.00 41.50 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.407 1.466   10.927 1.00 41.30 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.298 0.951   10.118 1.00 42.17 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.160 0.489   11.023 1.00 41.89 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.395 -0.195  12.018 1.00 42.73 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.778 -0.207  9.231  1.00 45.58 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.709 -0.738  8.279  1.00 51.98 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.660 -0.008  6.954  1.00 59.23 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.453 0.899   6.669  1.00 61.78 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.727 -0.410  6.097  1.00 60.35 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.949 0.916   10.695 1.00 40.37 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.755 0.626   11.481 1.00 39.68 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.341 -0.822  11.543 1.00 38.64 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.793 -1.630  10.738 1.00 40.21 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.422 -1.126  12.480 1.00 35.53 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.897 -2.432  12.791 1.00 33.17 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.529 -2.773  12.121 1.00 31.52 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.163 -3.938  12.074 1.00 30.76 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.827 -2.598  14.314 1.00 33.57 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 26.675 -1.469  15.168 1.00 34.47 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.803 -1.789  11.582 1.00 30.11 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.420 -1.952  11.053 1.00 28.80 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 24.251 -2.008  9.494  1.00 27.71 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 25.112 -1.481  8.775  1.00 29.38 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.544 -0.796  11.618 1.00 28.03 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.324 -0.821  13.132 1.00 30.75 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.822 -1.841  13.632 1.00 31.92 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.642 0.208   13.821 1.00 26.09 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 23.082 -2.538  9.000  1.00 26.18 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.572 -2.671  7.606  1.00 27.42 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 21.180 -1.922  7.520  1.00 24.85 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.380 -2.113  8.415  1.00 25.52 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 22.391 -4.198  7.261  1.00 33.56 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.647 -4.664  6.768  1.00 38.58 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 21.251 -4.493  6.218  1.00 35.32 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.906 -1.089  6.477  1.00 21.85 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.638 -0.349  6.346  1.00 19.74 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.643 -1.101  5.482  1.00 20.01 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.995 -1.575  4.383  1.00 21.59 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.865 1.073   5.736  1.00 19.39 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.985 1.841   6.460  1.00 20.98 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.566 1.900   5.712  1.00 20.05 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.687 2.080   7.975  1.00 21.09 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.400 -1.229  5.953  1.00 18.25 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.339 -1.881  5.173  1.00 18.19 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.981 -0.994  3.961  1.00 19.47 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.943 0.230   4.058  1.00 20.03 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 15.078 -2.041  6.055  1.00 18.03 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.708 -1.638  2.798  1.00 20.53 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.278 -0.887  1.595  1.00 21.38 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.005 -1.617  1.190  1.00 23.35 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.054 -2.617  0.463  1.00 24.95 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.359 -0.932  0.477  1.00 21.96 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.696 -0.372  0.947  1.00 22.33 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.673 1.119   1.303  1.00 23.72 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.016 1.580   1.674  1.00 22.73 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.263 2.717   2.311  1.00 24.09 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.271 3.548   2.612  1.00 22.32 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.508 3.050   2.625  1.00 24.28 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.877 -1.198  1.771  1.00 22.57 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.631 -1.972  1.671  1.00 23.19 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.424 -1.093  2.026  1.00 23.27 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.577 0.051   2.464  1.00 24.34 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.723 -3.154  2.629  1.00 22.92 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.719 -2.644  4.391  1.00 21.46 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.207  -1.716  1.987  1.00 24.32 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.993  -1.018  2.405  1.00 24.83 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.329  -1.737  3.573  1.00 25.06 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.096  -1.677  3.717  1.00 26.16 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.983  -0.879  1.240  1.00 29.46 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.515  -2.186  0.640  1.00 37.15 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 7.006  -3.260  1.072  1.00 36.24 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.655  -2.144  -0.275 1.00 44.38 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 8.118  -2.416  4.445  1.00 22.65 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.515  -3.089  5.607  1.00 21.41 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.763  -2.081  6.478  1.00 21.08 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.210  -0.915  6.643  1.00 21.00 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.581  -3.804  6.441  1.00 21.09 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.276  -5.339  5.727  1.00 22.14 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.635  -2.524  7.063  1.00 20.36 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.868  -1.739  8.034  1.00 19.80 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.724  -2.498  9.352  1.00 17.84 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.853  -2.169  10.161 1.00 18.03 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.495  -1.327  7.511  1.00 22.54 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.542  -0.196  6.533  1.00 27.82 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 2.123  0.180   6.133  1.00 33.70 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.694  -0.035  4.987  1.00 36.10 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.343  0.737   7.077  1.00 31.17 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.526  -3.596  9.556  1.00 17.45 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.625  -4.301  10.827 1.00 17.28 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.122  -4.499  11.096 1.00 16.46 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.973  -4.555  10.172 1.00 17.52 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.898  -5.653  10.818 1.00 19.34 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.555  -6.534  9.900  1.00 22.75 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.435  -5.508  10.474 1.00 20.26 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.433  -4.525  12.381 1.00 15.71 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.816  -4.676  12.810 1.00 14.62 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.895  -4.758  14.323 1.00 14.28 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.876  -4.977  14.981 1.00 15.02 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.107 -4.629  14.848 1.00 13.64 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.341 -4.746  16.290 1.00 14.28 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.209 -3.557  16.665 1.00 13.67 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.209 -3.288  15.995 1.00 14.66 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.049 -6.098  16.594 1.00 16.38 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.462 -6.189  18.082 1.00 17.98 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.111 -7.272  16.266 1.00 17.17 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.876 -2.893  17.793 1.00 12.90 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.738 -1.803  18.273 1.00 13.29 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.245 -2.054  19.680 1.00 14.32 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.628 -2.791  20.440 1.00 14.60 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.037 -0.407  18.193 1.00 13.14 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.031 -0.128  19.298 1.00 12.96 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.764  -0.713  19.283 1.00 14.28 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.323 0.755   20.331 1.00 14.11 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.808  -0.394  20.247 1.00 14.61 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.371  1.060   21.318 1.00 15.13 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.126  0.462   21.279 1.00 15.58 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.156  0.708   22.247 1.00 18.74 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.383 -1.432  20.013 1.00 14.18 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.925 -1.543  21.355 1.00 14.76 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.407 -0.372  22.215 1.00 14.96 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.517 0.786   21.806 1.00 14.85 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.467 -1.530  21.334 1.00 14.94 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.008 -1.661  22.734 1.00 15.78 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.794 -2.812  23.469 1.00 17.07 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.681 -0.605  23.342 1.00 17.60 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.258 -2.927  24.777 1.00 18.95 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.127 -0.692  24.646 1.00 18.00 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 16.905 -1.850  25.362 1.00 19.81 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.358 -1.951  26.656 1.00 24.09 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.821 -0.687  23.383 1.00 14.84 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.269 0.309   24.316 1.00 14.34 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.146 0.319   25.590 1.00 16.03 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.025 -0.555  26.463 1.00 16.61 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.828 -0.070  24.633 1.00 15.41 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.054 0.993   25.898 1.00 17.62 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.028 1.325   25.692 1.00 15.64 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 14.961 1.392   26.799 1.00 16.89 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.288 1.550   28.162 1.00 17.00 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.746 0.955   29.156 1.00 18.30 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.000 2.487   26.570 1.00 21.50 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.400 3.759   26.653 1.00 27.98 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.102 2.214   28.191 1.00 15.95 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.353 2.393   29.448 1.00 17.41 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.668 1.130   29.963 1.00 17.29 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.130 1.148   31.084 1.00 18.52 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.349 3.532   29.360 1.00 19.22 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.309 3.214   28.441 1.00 18.67 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.732 0.038   29.190 1.00 17.00 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.258 -1.259  29.640 1.00 17.92 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.357 -2.350  29.497 1.00 19.15 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.079 -3.519  29.801 1.00 20.59 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.028 -1.670  28.834 1.00 17.73 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.820  -0.768  29.071 1.00 18.60 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.194  -1.070  30.427 1.00 19.62 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.009  -0.233  30.669 1.00 21.31 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.038  0.952   31.256 1.00 21.70 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.190  1.472   31.662 1.00 21.69 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 5.908  1.636   31.449 1.00 22.50 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.570 -1.983  28.983 1.00 19.72 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.638 -2.950  28.681 1.00 21.44 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.111 -4.130  27.862 1.00 21.85 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.364 -5.312  28.182 1.00 23.79 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.320 -3.459  29.954 1.00 25.50 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.260 -2.477  30.496 1.00 30.09 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.196 -3.208  31.471 1.00 30.51 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.853 -2.255  32.326 1.00 31.50 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.584 -2.102  33.622 1.00 33.15 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.687 -2.891  34.226 1.00 33.70 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.197 -1.164  34.322 1.00 33.04 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.261 -3.811  26.878 1.00 19.66 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.607 -4.886  26.106 1.00 19.60 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.392 -4.476  24.678 1.00 17.91 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.274 -3.296  24.386 1.00 18.22 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.185 -5.113  26.678 1.00 23.50 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.061 -6.113  27.824 1.00 31.55 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.585  -6.199  28.242 1.00 39.04 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.293  -7.392  29.131 1.00 45.32 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.106  -7.010  30.563 1.00 48.83 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.244 -5.462  23.805 1.00 16.95 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.853 -5.202  22.429 1.00 16.34 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.362 -5.524  22.283 1.00 16.78 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.825  -6.488  22.884 1.00 17.96 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.618 -6.124  21.471 1.00 15.41 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.101 -5.946  21.510 1.00 16.72 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.793 -5.194  20.550 1.00 19.65 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 14.994 -6.498  22.347 1.00 16.79 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.083 -5.309  20.862 1.00 18.71 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.257 -6.059  21.931 1.00 21.59 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.674  -4.723  21.470 1.00 14.94 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.238  -4.926  21.251 1.00 15.47 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.927  -4.995  19.744 1.00 15.75 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.453  -4.192  18.968 1.00 14.88 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.431  -3.719  21.801 1.00 15.83 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.391  -3.623  23.307 1.00 17.54 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.632  -4.510  24.065 1.00 19.98 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.063  -2.611  23.973 1.00 16.99 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.591  -4.425  25.461 1.00 20.78 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.003  -2.493  25.362 1.00 17.88 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.267  -3.404  26.102 1.00 21.23 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.199  -3.279  27.484 1.00 24.43 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.027  -5.882  19.332 1.00 15.42 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.600  -5.895  17.922 1.00 16.24 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.568  -4.762  17.684 1.00 17.93 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.736  -4.464  18.581 1.00 20.16 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.932  -7.271  17.768 1.00 17.16 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.435  -7.595  19.189 1.00 17.49 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.350  -6.915  20.154 1.00 15.12 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.593  -4.152  16.519 1.00 15.52 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.705  -3.027  16.209 1.00 17.22 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.222  -3.073  14.787 1.00 16.81 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.910  -3.548  13.876 1.00 16.77 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.433  -1.652  16.374 1.00 19.80 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.438  -1.200  17.836 1.00 21.88 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.840  -1.675  15.782 1.00 19.36 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.007  -2.543  14.578 1.00 16.73 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.485  -2.221  13.250 1.00 17.79 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.574  -0.687  13.146 1.00 17.17 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.174  -0.014  14.098 1.00 18.82 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.015  -2.618  13.122 1.00 21.65 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.907  -4.030  13.066 1.00 29.71 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.210  -0.150  12.090 1.00 15.91 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.427  1.299   12.023 1.00 16.21 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.956  1.883   10.695 1.00 17.41 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.854  1.179   9.672  1.00 18.57 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.935  1.618   12.315 1.00 15.68 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.951  0.839   11.480 1.00 15.18 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.489  -0.352  11.947 1.00 15.84 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.470  1.371   10.309 1.00 15.60 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.432  -1.060  11.192 1.00 16.62 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.423  0.658   9.546  1.00 17.00 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.910  -0.541  10.013 1.00 16.13 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.563  3.179   10.740 1.00 17.89 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.112  3.851   9.533  1.00 18.87 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.258  4.179   8.561  1.00 19.79 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.431  4.138   8.922  1.00 18.85 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.336  5.121   9.882  1.00 20.16 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.170  6.019   10.605 1.00 23.49 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.910  4.467   7.292  1.00 19.66 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.908  4.846   6.286  1.00 20.49 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.501  6.198   6.675  1.00 21.97 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.832  7.002   7.328  1.00 22.24 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.242  4.932   4.887  1.00 24.75 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.859  3.552   4.381  1.00 29.70 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.386  3.638   2.936  1.00 36.11 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.444  2.255   2.347  1.00 42.29 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.341  2.010   1.400  1.00 46.41 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.748  6.494   6.267  1.00 20.88 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.350  7.795   6.634  1.00 21.59 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.469  8.948   6.146  1.00 22.62 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.062  8.969   4.982  1.00 23.67 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.697  7.804   5.907  1.00 22.91 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.991  6.343   5.596  1.00 24.16 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.658  5.648   5.472  1.00 21.38 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.161  9.877   7.048  1.00 21.47 ? 80  SER   A N   1 
ATOM   582  C  CA  A SER   A 1 74  ? 4.256  10.966  6.684  0.50 23.02 ? 80  SER   A CA  1 
ATOM   583  C  CA  B SER   A 1 74  ? 4.201  10.939  6.738  0.50 22.58 ? 80  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 4.551  12.236  7.481  1.00 23.04 ? 80  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 5.450  12.252  8.335  1.00 22.58 ? 80  SER   A O   1 
ATOM   586  C  CB  A SER   A 1 74  ? 2.807  10.514  6.874  0.50 26.06 ? 80  SER   A CB  1 
ATOM   587  C  CB  B SER   A 1 74  ? 2.792  10.501  7.167  0.50 24.30 ? 80  SER   A CB  1 
ATOM   588  O  OG  A SER   A 1 74  ? 2.548  10.276  8.244  0.50 29.06 ? 80  SER   A OG  1 
ATOM   589  O  OG  B SER   A 1 74  ? 2.484  9.143   6.892  0.50 25.98 ? 80  SER   A OG  1 
ATOM   590  N  N   . LEU   A 1 75  ? 3.826  13.349  7.140  1.00 22.32 ? 81  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 75  ? 3.994  14.630  7.798  1.00 24.16 ? 81  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 75  ? 2.958  14.646  8.912  1.00 25.15 ? 81  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 75  ? 1.729  14.595  8.635  1.00 26.70 ? 81  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 75  ? 3.666  15.729  6.779  1.00 25.79 ? 81  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 75  ? 4.080  17.118  7.121  1.00 29.36 ? 81  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 75  ? 5.588  17.262  7.262  1.00 30.31 ? 81  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 75  ? 3.593  18.092  6.048  1.00 31.73 ? 81  LEU   A CD2 1 
ATOM   598  N  N   . ILE   A 1 76  ? 3.426  14.704  10.164 1.00 25.58 ? 82  ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 76  ? 2.594  14.578  11.359 1.00 27.24 ? 82  ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 76  ? 2.843  15.728  12.296 1.00 27.75 ? 82  ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 76  ? 4.002  16.065  12.554 1.00 26.78 ? 82  ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 76  ? 2.927  13.223  12.049 1.00 28.96 ? 82  ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 76  ? 2.494  12.058  11.161 1.00 30.34 ? 82  ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 76  ? 2.323  13.126  13.453 1.00 30.03 ? 82  ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 76  ? 2.857  10.762  11.637 1.00 31.96 ? 82  ILE   A CD1 1 
ATOM   606  N  N   . PHE   A 1 77  ? 1.765  16.317  12.843 1.00 27.90 ? 83  PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 77  ? 1.917  17.407  13.783 1.00 29.63 ? 83  PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 77  ? 2.519  16.909  15.082 1.00 30.95 ? 83  PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 77  ? 2.065  15.923  15.644 1.00 31.43 ? 83  PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 77  ? 0.557  18.081  14.054 1.00 30.88 ? 83  PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 77  ? 0.683  19.251  14.990 1.00 33.68 ? 83  PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 77  ? 1.265  20.431  14.570 1.00 36.02 ? 83  PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 77  ? 0.314  19.139  16.318 1.00 35.37 ? 83  PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 77  ? 1.394  21.507  15.439 1.00 37.73 ? 83  PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 77  ? 0.424  20.227  17.176 1.00 36.70 ? 83  PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 77  ? 0.954  21.399  16.732 1.00 37.30 ? 83  PHE   A CZ  1 
ATOM   617  N  N   . VAL   A 1 78  ? 3.569  17.604  15.555 1.00 31.64 ? 84  VAL   A N   1 
ATOM   618  C  CA  . VAL   A 1 78  ? 4.234  17.252  16.804 1.00 32.57 ? 84  VAL   A CA  1 
ATOM   619  C  C   . VAL   A 1 78  ? 4.214  18.505  17.667 1.00 35.24 ? 84  VAL   A C   1 
ATOM   620  O  O   . VAL   A 1 78  ? 4.655  19.585  17.228 1.00 36.51 ? 84  VAL   A O   1 
ATOM   621  C  CB  . VAL   A 1 78  ? 5.691  16.769  16.546 1.00 32.33 ? 84  VAL   A CB  1 
ATOM   622  C  CG1 . VAL   A 1 78  ? 6.424  16.554  17.859 1.00 33.75 ? 84  VAL   A CG1 1 
ATOM   623  C  CG2 . VAL   A 1 78  ? 5.692  15.478  15.738 1.00 31.81 ? 84  VAL   A CG2 1 
ATOM   624  N  N   . GLU   A 1 79  ? 3.678  18.366  18.875 1.00 36.49 ? 85  GLU   A N   1 
ATOM   625  C  CA  . GLU   A 1 79  ? 3.520  19.479  19.811 1.00 38.42 ? 85  GLU   A CA  1 
ATOM   626  C  C   . GLU   A 1 79  ? 4.874  20.035  20.243 1.00 39.25 ? 85  GLU   A C   1 
ATOM   627  O  O   . GLU   A 1 79  ? 5.878  19.321  20.152 1.00 39.13 ? 85  GLU   A O   1 
ATOM   628  C  CB  . GLU   A 1 79  ? 2.685  19.045  21.043 1.00 42.49 ? 85  GLU   A CB  1 
ATOM   629  C  CG  . GLU   A 1 79  ? 2.861  17.595  21.477 1.00 50.75 ? 85  GLU   A CG  1 
ATOM   630  C  CD  . GLU   A 1 79  ? 1.969  16.574  20.793 1.00 60.19 ? 85  GLU   A CD  1 
ATOM   631  O  OE1 . GLU   A 1 79  ? 0.752  16.543  21.093 1.00 62.69 ? 85  GLU   A OE1 1 
ATOM   632  O  OE2 . GLU   A 1 79  ? 2.490  15.820  19.935 1.00 60.71 ? 85  GLU   A OE2 1 
ATOM   633  N  N   . ALA   A 1 80  ? 4.907  21.287  20.721 1.00 40.05 ? 86  ALA   A N   1 
ATOM   634  C  CA  . ALA   A 1 80  ? 6.145  21.903  21.177 1.00 40.51 ? 86  ALA   A CA  1 
ATOM   635  C  C   . ALA   A 1 80  ? 6.776  21.102  22.310 1.00 40.64 ? 86  ALA   A C   1 
ATOM   636  O  O   . ALA   A 1 80  ? 6.082  20.443  23.098 1.00 41.34 ? 86  ALA   A O   1 
ATOM   637  C  CB  . ALA   A 1 80  ? 5.881  23.324  21.642 1.00 40.80 ? 86  ALA   A CB  1 
ATOM   638  N  N   . SER   A 1 81  ? 8.100  21.103  22.347 1.00 39.51 ? 87  SER   A N   1 
ATOM   639  C  CA  . SER   A 1 81  ? 8.849  20.438  23.401 1.00 38.88 ? 87  SER   A CA  1 
ATOM   640  C  C   . SER   A 1 81  ? 9.998  21.387  23.777 1.00 38.85 ? 87  SER   A C   1 
ATOM   641  O  O   . SER   A 1 81  ? 10.113 22.486  23.219 1.00 38.71 ? 87  SER   A O   1 
ATOM   642  C  CB  . SER   A 1 81  ? 9.401  19.096  22.899 1.00 40.39 ? 87  SER   A CB  1 
ATOM   643  O  OG  . SER   A 1 81  ? 10.420 19.274  21.925 1.00 41.37 ? 87  SER   A OG  1 
ATOM   644  N  N   . GLU   A 1 82  ? 10.821 20.976  24.740 1.00 39.21 ? 88  GLU   A N   1 
ATOM   645  C  CA  . GLU   A 1 82  ? 12.024 21.716  25.113 1.00 40.05 ? 88  GLU   A CA  1 
ATOM   646  C  C   . GLU   A 1 82  ? 13.002 21.784  23.911 1.00 38.94 ? 88  GLU   A C   1 
ATOM   647  O  O   . GLU   A 1 82  ? 13.900 22.617  23.905 1.00 39.90 ? 88  GLU   A O   1 
ATOM   648  C  CB  . GLU   A 1 82  ? 12.758 20.982  26.256 1.00 44.29 ? 88  GLU   A CB  1 
ATOM   649  C  CG  . GLU   A 1 82  ? 11.868 20.404  27.340 1.00 52.47 ? 88  GLU   A CG  1 
ATOM   650  C  CD  . GLU   A 1 82  ? 11.531 18.938  27.139 1.00 60.52 ? 88  GLU   A CD  1 
ATOM   651  O  OE1 . GLU   A 1 82  ? 12.179 18.090  27.795 1.00 63.31 ? 88  GLU   A OE1 1 
ATOM   652  O  OE2 . GLU   A 1 82  ? 10.623 18.636  26.330 1.00 61.53 ? 88  GLU   A OE2 1 
ATOM   653  N  N   . TYR   A 1 83  ? 12.870 20.865  22.926 1.00 37.10 ? 89  TYR   A N   1 
ATOM   654  C  CA  . TYR   A 1 83  ? 13.778 20.760  21.804 1.00 35.25 ? 89  TYR   A CA  1 
ATOM   655  C  C   . TYR   A 1 83  ? 13.301 21.415  20.531 1.00 33.45 ? 89  TYR   A C   1 
ATOM   656  O  O   . TYR   A 1 83  ? 14.131 21.796  19.724 1.00 32.99 ? 89  TYR   A O   1 
ATOM   657  C  CB  . TYR   A 1 83  ? 14.063 19.284  21.528 1.00 34.69 ? 89  TYR   A CB  1 
ATOM   658  C  CG  . TYR   A 1 83  ? 14.657 18.558  22.715 1.00 35.37 ? 89  TYR   A CG  1 
ATOM   659  C  CD1 . TYR   A 1 83  ? 13.867 17.778  23.541 1.00 36.61 ? 89  TYR   A CD1 1 
ATOM   660  C  CD2 . TYR   A 1 83  ? 16.018 18.621  22.988 1.00 36.03 ? 89  TYR   A CD2 1 
ATOM   661  C  CE1 . TYR   A 1 83  ? 14.417 17.051  24.588 1.00 37.80 ? 89  TYR   A CE1 1 
ATOM   662  C  CE2 . TYR   A 1 83  ? 16.574 17.924  24.055 1.00 36.98 ? 89  TYR   A CE2 1 
ATOM   663  C  CZ  . TYR   A 1 83  ? 15.765 17.157  24.866 1.00 38.71 ? 89  TYR   A CZ  1 
ATOM   664  O  OH  . TYR   A 1 83  ? 16.315 16.454  25.917 1.00 41.23 ? 89  TYR   A OH  1 
ATOM   665  N  N   . TYR   A 1 84  ? 11.975 21.508  20.321 1.00 32.78 ? 90  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 11.471 22.086  19.077 1.00 32.81 ? 90  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 10.228 22.914  19.285 1.00 35.85 ? 90  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 9.408  22.582  20.137 1.00 36.68 ? 90  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 11.079 20.961  18.081 1.00 30.61 ? 90  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 12.214 20.108  17.547 1.00 27.28 ? 90  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 13.051 20.578  16.549 1.00 27.32 ? 90  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 12.382 18.799  17.970 1.00 26.00 ? 90  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 14.099 19.801  16.059 1.00 25.75 ? 90  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 13.391 17.991  17.445 1.00 24.28 ? 90  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 14.247 18.495  16.488 1.00 24.40 ? 90  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 15.279 17.716  16.013 1.00 22.01 ? 90  TYR   A OH  1 
ATOM   677  N  N   . PRO   A 1 85  ? 9.995  23.913  18.414 1.00 37.59 ? 91  PRO   A N   1 
ATOM   678  C  CA  . PRO   A 1 85  ? 8.687  24.589  18.448 1.00 38.80 ? 91  PRO   A CA  1 
ATOM   679  C  C   . PRO   A 1 85  ? 7.631  23.608  17.924 1.00 39.68 ? 91  PRO   A C   1 
ATOM   680  O  O   . PRO   A 1 85  ? 7.958  22.581  17.292 1.00 40.52 ? 91  PRO   A O   1 
ATOM   681  C  CB  . PRO   A 1 85  ? 8.865  25.732  17.443 1.00 39.54 ? 91  PRO   A CB  1 
ATOM   682  C  CG  . PRO   A 1 85  ? 9.886  25.183  16.448 1.00 40.29 ? 91  PRO   A CG  1 
ATOM   683  C  CD  . PRO   A 1 85  ? 10.842 24.394  17.302 1.00 38.24 ? 91  PRO   A CD  1 
ATOM   684  N  N   . ALA   A 1 86  ? 6.344  23.944  18.099 1.00 39.14 ? 92  ALA   A N   1 
ATOM   685  C  CA  . ALA   A 1 86  ? 5.241  23.157  17.540 1.00 39.21 ? 92  ALA   A CA  1 
ATOM   686  C  C   . ALA   A 1 86  ? 5.416  23.166  15.996 1.00 38.12 ? 92  ALA   A C   1 
ATOM   687  O  O   . ALA   A 1 86  ? 5.747  24.220  15.435 1.00 38.28 ? 92  ALA   A O   1 
ATOM   688  C  CB  . ALA   A 1 86  ? 3.918  23.818  17.915 1.00 40.22 ? 92  ALA   A CB  1 
ATOM   689  N  N   . ARG   A 1 87  ? 5.403  21.976  15.357 1.00 36.40 ? 93  ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 87  ? 5.678  21.923  13.914 1.00 34.29 ? 93  ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 87  ? 5.218  20.583  13.299 1.00 32.75 ? 93  ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 87  ? 4.845  19.672  14.026 1.00 33.55 ? 93  ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 87  ? 7.206  22.103  13.703 1.00 33.64 ? 93  ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 87  ? 7.986  20.813  14.061 1.00 33.90 ? 93  ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 87  ? 9.413  21.003  14.527 1.00 32.80 ? 93  ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 87  ? 10.302 19.879  14.145 1.00 31.01 ? 93  ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 87  ? 10.303 18.685  14.742 1.00 29.35 ? 93  ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 87  ? 11.171 17.748  14.369 1.00 27.30 ? 93  ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 87  ? 9.403  18.405  15.684 1.00 29.23 ? 93  ARG   A NH2 1 
ATOM   700  N  N   . TYR   A 1 88  ? 5.290  20.465  11.975 1.00 31.23 ? 94  TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 88  ? 5.036  19.197  11.322 1.00 30.97 ? 94  TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 88  ? 6.375  18.506  11.162 1.00 28.74 ? 94  TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 88  ? 7.323  19.095  10.625 1.00 29.75 ? 94  TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 88  ? 4.373  19.389  9.959  1.00 32.13 ? 94  TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 88  ? 2.934  19.813  10.113 1.00 33.84 ? 94  TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 88  ? 2.595  21.153  10.217 1.00 35.60 ? 94  TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 88  ? 1.919  18.875  10.218 1.00 34.97 ? 94  TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 88  ? 1.278  21.549  10.409 1.00 37.54 ? 94  TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 88  ? 0.590  19.261  10.382 1.00 37.20 ? 94  TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 88  ? 0.277  20.598  10.488 1.00 38.96 ? 94  TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 88  ? -1.037 20.981  10.658 1.00 42.86 ? 94  TYR   A OH  1 
ATOM   712  N  N   . GLN   A 1 89  ? 6.485  17.304  11.692 1.00 25.43 ? 95  GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 89  ? 7.704  16.508  11.520 1.00 22.33 ? 95  GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 89  ? 7.427  15.611  10.305 1.00 21.07 ? 95  GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 89  ? 6.357  14.981  10.199 1.00 23.17 ? 95  GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 89  ? 8.037  15.687  12.769 1.00 22.35 ? 95  GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 89  ? 9.254  14.741  12.552 1.00 22.27 ? 95  GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 89  ? 9.896  14.291  13.849 1.00 23.92 ? 95  GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 89  ? 9.962  15.041  14.838 1.00 24.51 ? 95  GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 89  ? 10.391 13.062  13.875 1.00 19.10 ? 95  GLN   A NE2 1 
ATOM   721  N  N   . SER   A 1 90  ? 8.346  15.590  9.364  1.00 19.74 ? 96  SER   A N   1 
ATOM   722  C  CA  . SER   A 1 90  ? 8.207  14.801  8.155  1.00 19.70 ? 96  SER   A CA  1 
ATOM   723  C  C   . SER   A 1 90  ? 8.890  13.421  8.310  1.00 20.32 ? 96  SER   A C   1 
ATOM   724  O  O   . SER   A 1 90  ? 9.727  13.221  9.226  1.00 19.75 ? 96  SER   A O   1 
ATOM   725  C  CB  . SER   A 1 90  ? 8.795  15.567  6.969  1.00 21.53 ? 96  SER   A CB  1 
ATOM   726  O  OG  . SER   A 1 90  ? 10.191 15.757  7.146  1.00 23.29 ? 96  SER   A OG  1 
ATOM   727  N  N   . HIS   A 1 91  ? 8.513  12.472  7.412  1.00 19.40 ? 97  HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 91  ? 9.103  11.123  7.359  1.00 18.45 ? 97  HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 91  ? 8.927  10.406  8.705  1.00 17.90 ? 97  HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 91  ? 9.779  9.613   9.094  1.00 17.84 ? 97  HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 91  ? 10.589 11.197  6.935  1.00 19.57 ? 97  HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 91  ? 10.786 11.818  5.568  1.00 22.60 ? 97  HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 91  ? 10.883 11.035  4.422  1.00 25.06 ? 97  HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 91  ? 10.828 13.123  5.213  1.00 23.67 ? 97  HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 91  ? 11.010 11.900  3.401  1.00 25.40 ? 97  HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 91  ? 11.001 13.165  3.839  1.00 25.20 ? 97  HIS   A NE2 1 
ATOM   737  N  N   . LEU   A 1 92  ? 7.799  10.653  9.378  1.00 17.26 ? 98  LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 92  ? 7.544  10.044  10.687 1.00 16.95 ? 98  LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 92  ? 6.511  8.926   10.566 1.00 17.08 ? 98  LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 92  ? 5.520  9.047   9.824  1.00 18.15 ? 98  LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 92  ? 6.989  11.135  11.652 1.00 18.17 ? 98  LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 92  ? 6.747  10.748  13.133 1.00 20.09 ? 98  LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 92  ? 8.058  10.335  13.849 1.00 19.58 ? 98  LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 92  ? 6.141  11.969  13.908 1.00 22.61 ? 98  LEU   A CD2 1 
ATOM   745  N  N   . MET   A 1 93  ? 6.756  7.826   11.321 1.00 17.20 ? 99  MET   A N   1 
ATOM   746  C  CA  . MET   A 1 93  ? 5.838  6.671   11.313 1.00 16.99 ? 99  MET   A CA  1 
ATOM   747  C  C   . MET   A 1 93  ? 5.318  6.461   12.718 1.00 17.34 ? 99  MET   A C   1 
ATOM   748  O  O   . MET   A 1 93  ? 6.130  6.399   13.661 1.00 17.38 ? 99  MET   A O   1 
ATOM   749  C  CB  . MET   A 1 93  ? 6.623  5.441   10.874 1.00 18.24 ? 99  MET   A CB  1 
ATOM   750  C  CG  . MET   A 1 93  ? 7.200  5.612   9.451  1.00 19.05 ? 99  MET   A CG  1 
ATOM   751  S  SD  . MET   A 1 93  ? 8.299  4.308   8.914  1.00 22.47 ? 99  MET   A SD  1 
ATOM   752  C  CE  . MET   A 1 93  ? 9.682  4.528   10.126 1.00 23.82 ? 99  MET   A CE  1 
ATOM   753  N  N   . LEU   A 1 94  ? 3.988  6.315   12.888 1.00 16.26 ? 100 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 94  ? 3.461  6.121   14.241 1.00 17.51 ? 100 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 94  ? 3.015  4.688   14.476 1.00 16.69 ? 100 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 94  ? 2.552  4.014   13.530 1.00 17.32 ? 100 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 94  ? 2.208  7.006   14.531 1.00 19.93 ? 100 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 94  ? 2.421  8.492   14.492 1.00 24.59 ? 100 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 94  ? 1.125  9.249   14.916 1.00 26.03 ? 100 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 94  ? 3.548  8.920   15.394 1.00 26.11 ? 100 LEU   A CD2 1 
ATOM   761  N  N   . ALA   A 1 95  ? 3.112  4.249   15.731 1.00 17.24 ? 101 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 95  ? 2.631  2.936   16.136 1.00 16.29 ? 101 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 95  ? 2.093  3.004   17.545 1.00 16.90 ? 101 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 95  ? 2.403  3.955   18.278 1.00 17.49 ? 101 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 95  ? 3.801  1.920   16.127 1.00 17.11 ? 101 ALA   A CB  1 
ATOM   766  N  N   . VAL   A 1 96  ? 1.261  2.037   17.940 1.00 16.43 ? 102 VAL   A N   1 
ATOM   767  C  CA  . VAL   A 1 96  ? 0.835  1.937   19.322 1.00 17.00 ? 102 VAL   A CA  1 
ATOM   768  C  C   . VAL   A 1 96  ? 1.929  1.120   20.055 1.00 18.78 ? 102 VAL   A C   1 
ATOM   769  O  O   . VAL   A 1 96  ? 2.269  0.000   19.672 1.00 20.55 ? 102 VAL   A O   1 
ATOM   770  C  CB  . VAL   A 1 96  ? -0.539 1.256   19.392 1.00 18.08 ? 102 VAL   A CB  1 
ATOM   771  C  CG1 . VAL   A 1 96  ? -0.954 1.029   20.845 1.00 18.83 ? 102 VAL   A CG1 1 
ATOM   772  C  CG2 . VAL   A 1 96  ? -1.539 2.121   18.650 1.00 18.84 ? 102 VAL   A CG2 1 
ATOM   773  N  N   . GLY   A 1 97  ? 2.467  1.732   21.078 1.00 18.04 ? 103 GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 97  ? 3.551  1.125   21.851 1.00 19.18 ? 103 GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 97  ? 4.017  2.108   22.905 1.00 19.42 ? 103 GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 97  ? 3.731  3.313   22.845 1.00 21.21 ? 103 GLY   A O   1 
ATOM   777  N  N   . HIS   A 1 98  ? 4.686  1.593   23.937 1.00 18.96 ? 104 HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 98  ? 5.189  2.420   24.996 1.00 18.78 ? 104 HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 98  ? 6.415  3.188   24.584 1.00 19.11 ? 104 HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 98  ? 7.332  2.628   23.988 1.00 19.22 ? 104 HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 98  ? 5.553  1.567   26.237 1.00 18.42 ? 104 HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 98  ? 6.026  2.407   27.377 1.00 19.34 ? 104 HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 98  ? 5.176  3.278   28.017 1.00 21.46 ? 104 HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 98  ? 7.280  2.551   27.900 1.00 19.33 ? 104 HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 98  ? 5.924  3.931   28.903 1.00 21.99 ? 104 HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 98  ? 7.197  3.501   28.875 1.00 20.40 ? 104 HIS   A NE2 1 
ATOM   787  N  N   . SER   A 1 99  ? 6.496  4.431   24.977 1.00 19.52 ? 105 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 99  ? 7.662  5.267   24.818 1.00 19.45 ? 105 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 99  ? 7.596  6.419   25.834 1.00 22.38 ? 105 SER   A C   1 
ATOM   790  O  O   . SER   A 1 99  ? 6.488  6.829   26.236 1.00 24.12 ? 105 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 99  ? 7.817  5.774   23.392 1.00 20.58 ? 105 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 99  ? 6.776  6.674   23.055 1.00 23.20 ? 105 SER   A OG  1 
ATOM   793  N  N   . GLU   A 1 100 ? 8.773  6.799   26.319 1.00 21.09 ? 106 GLU   A N   1 
ATOM   794  C  CA  . GLU   A 1 100 ? 9.136  7.903   27.223 1.00 22.04 ? 106 GLU   A CA  1 
ATOM   795  C  C   . GLU   A 1 100 ? 10.249 8.708   26.554 1.00 24.23 ? 106 GLU   A C   1 
ATOM   796  O  O   . GLU   A 1 100 ? 10.909 8.212   25.638 1.00 25.00 ? 106 GLU   A O   1 
ATOM   797  C  CB  . GLU   A 1 100 ? 9.640  7.333   28.569 1.00 23.48 ? 106 GLU   A CB  1 
ATOM   798  C  CG  . GLU   A 1 100 ? 8.499  6.676   29.275 1.00 25.35 ? 106 GLU   A CG  1 
ATOM   799  C  CD  . GLU   A 1 100 ? 8.889  6.074   30.606 1.00 26.58 ? 106 GLU   A CD  1 
ATOM   800  O  OE1 . GLU   A 1 100 ? 9.682  6.699   31.354 1.00 28.68 ? 106 GLU   A OE1 1 
ATOM   801  O  OE2 . GLU   A 1 100 ? 8.403  4.961   30.889 1.00 24.32 ? 106 GLU   A OE2 1 
ATOM   802  N  N   . PRO   A 1 101 ? 10.467 9.982   26.944 1.00 25.80 ? 107 PRO   A N   1 
ATOM   803  C  CA  . PRO   A 1 101 ? 11.464 10.820  26.214 1.00 25.71 ? 107 PRO   A CA  1 
ATOM   804  C  C   . PRO   A 1 101 ? 12.866 10.206  25.978 1.00 25.90 ? 107 PRO   A C   1 
ATOM   805  O  O   . PRO   A 1 101 ? 13.394 10.243  24.836 1.00 26.84 ? 107 PRO   A O   1 
ATOM   806  C  CB  . PRO   A 1 101 ? 11.531 12.102  27.062 1.00 27.10 ? 107 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A 1 101 ? 10.168 12.181  27.726 1.00 28.15 ? 107 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A 1 101 ? 9.705  10.751  27.952 1.00 26.20 ? 107 PRO   A CD  1 
ATOM   809  N  N   . GLY   A 1 102 ? 13.430 9.578   27.006 1.00 23.68 ? 108 GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 102 ? 14.720 8.896   26.949 1.00 21.64 ? 108 GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 102 ? 14.753 7.680   26.016 1.00 19.48 ? 108 GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 102 ? 15.812 7.082   25.787 1.00 19.96 ? 108 GLY   A O   1 
ATOM   813  N  N   . ASP   A 1 103 ? 13.571 7.244   25.522 1.00 17.91 ? 109 ASP   A N   1 
ATOM   814  C  CA  . ASP   A 1 103 ? 13.524 6.146   24.565 1.00 16.29 ? 109 ASP   A CA  1 
ATOM   815  C  C   . ASP   A 1 103 ? 13.965 6.559   23.159 1.00 16.24 ? 109 ASP   A C   1 
ATOM   816  O  O   . ASP   A 1 103 ? 14.205 5.684   22.323 1.00 16.08 ? 109 ASP   A O   1 
ATOM   817  C  CB  . ASP   A 1 103 ? 12.114 5.527   24.478 1.00 16.15 ? 109 ASP   A CB  1 
ATOM   818  C  CG  . ASP   A 1 103 ? 11.827 4.684   25.713 1.00 18.11 ? 109 ASP   A CG  1 
ATOM   819  O  OD1 . ASP   A 1 103 ? 12.785 4.058   26.231 1.00 18.41 ? 109 ASP   A OD1 1 
ATOM   820  O  OD2 . ASP   A 1 103 ? 10.633 4.676   26.187 1.00 17.52 ? 109 ASP   A OD2 1 
ATOM   821  N  N   . CYS   A 1 104 ? 14.128 7.863   22.897 1.00 16.65 ? 110 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 104 ? 14.584 8.311   21.567 1.00 16.00 ? 110 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 104 ? 15.930 7.697   21.234 1.00 15.96 ? 110 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 104 ? 16.789 7.588   22.098 1.00 17.91 ? 110 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 104 ? 14.633 9.840   21.484 1.00 16.58 ? 110 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 104 ? 12.999 10.607  21.368 1.00 19.96 ? 110 CYS   A SG  1 
ATOM   827  N  N   . GLY   A 1 105 ? 16.048 7.199   20.019 1.00 14.59 ? 111 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 105 ? 17.290 6.563   19.596 1.00 14.76 ? 111 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 105 ? 17.175 5.044   19.535 1.00 15.61 ? 111 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 105 ? 18.023 4.372   18.928 1.00 16.03 ? 111 GLY   A O   1 
ATOM   831  N  N   . GLY   A 1 106 ? 16.136 4.478   20.154 1.00 14.72 ? 112 GLY   A N   1 
ATOM   832  C  CA  . GLY   A 1 106 ? 15.900 3.039   20.030 1.00 14.13 ? 112 GLY   A CA  1 
ATOM   833  C  C   . GLY   A 1 106 ? 15.654 2.639   18.574 1.00 14.50 ? 112 GLY   A C   1 
ATOM   834  O  O   . GLY   A 1 106 ? 14.951 3.353   17.851 1.00 14.45 ? 112 GLY   A O   1 
ATOM   835  N  N   . ILE   A 1 107 ? 16.268 1.544   18.123 1.00 13.56 ? 113 ILE   A N   1 
ATOM   836  C  CA  . ILE   A 1 107 ? 16.120 1.143   16.721 1.00 12.85 ? 113 ILE   A CA  1 
ATOM   837  C  C   . ILE   A 1 107 ? 14.872 0.328   16.433 1.00 13.53 ? 113 ILE   A C   1 
ATOM   838  O  O   . ILE   A 1 107 ? 14.546 -0.580  17.216 1.00 14.24 ? 113 ILE   A O   1 
ATOM   839  C  CB  . ILE   A 1 107 ? 17.409 0.401   16.270 1.00 15.73 ? 113 ILE   A CB  1 
ATOM   840  C  CG1 . ILE   A 1 107 ? 18.567 1.421   16.181 1.00 16.78 ? 113 ILE   A CG1 1 
ATOM   841  C  CG2 . ILE   A 1 107 ? 17.244 -0.381  14.961 1.00 18.50 ? 113 ILE   A CG2 1 
ATOM   842  C  CD1 . ILE   A 1 107 ? 19.968 0.694   15.871 1.00 19.16 ? 113 ILE   A CD1 1 
ATOM   843  N  N   . LEU   A 1 108 ? 14.228 0.617   15.307 1.00 12.58 ? 114 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 108 ? 13.120 -0.187  14.757 1.00 12.78 ? 114 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 108 ? 13.732 -0.980  13.570 1.00 15.25 ? 114 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 108 ? 14.398 -0.394  12.713 1.00 15.10 ? 114 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 108 ? 12.064 0.781   14.205 1.00 12.74 ? 114 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 108 ? 10.886 0.112   13.426 1.00 14.23 ? 114 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 108 ? 10.038 -0.812  14.344 1.00 15.56 ? 114 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 108 ? 9.973  1.196   12.793 1.00 15.67 ? 114 LEU   A CD2 1 
ATOM   851  N  N   . ARG   A 1 109 ? 13.517 -2.305  13.573 1.00 14.65 ? 115 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 109 ? 14.024 -3.184  12.535 1.00 14.80 ? 115 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 109 ? 12.915 -4.036  11.993 1.00 15.46 ? 115 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 109 ? 12.026 -4.511  12.722 1.00 16.88 ? 115 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 109 ? 15.021 -4.196  13.168 1.00 17.58 ? 115 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 109 ? 16.241 -3.567  13.771 1.00 23.31 ? 115 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 109 ? 17.126 -4.636  14.439 1.00 25.42 ? 115 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 109 ? 17.969 -5.201  13.406 1.00 30.80 ? 115 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 109 ? 19.123 -4.676  13.010 1.00 31.33 ? 115 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 109 ? 19.659 -3.674  13.677 1.00 28.82 ? 115 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 109 ? 19.726 -5.137  11.931 1.00 30.95 ? 115 ARG   A NH2 1 
ATOM   862  N  N   . CYS   A 1 110 ? 13.093 -4.418  10.741 1.00 15.89 ? 116 CYS   A N   1 
ATOM   863  C  CA  . CYS   A 1 110 ? 12.251 -5.463  10.129 1.00 17.16 ? 116 CYS   A CA  1 
ATOM   864  C  C   . CYS   A 1 110 ? 13.206 -6.585  9.672  1.00 18.37 ? 116 CYS   A C   1 
ATOM   865  O  O   . CYS   A 1 110 ? 14.427 -6.525  9.935  1.00 19.04 ? 116 CYS   A O   1 
ATOM   866  C  CB  . CYS   A 1 110 ? 11.494 -4.866  8.955  1.00 17.83 ? 116 CYS   A CB  1 
ATOM   867  S  SG  . CYS   A 1 110 ? 12.602 -4.369  7.585  1.00 17.85 ? 116 CYS   A SG  1 
ATOM   868  N  N   . GLN   A 1 111 ? 12.683 -7.608  8.955  1.00 19.88 ? 117 GLN   A N   1 
ATOM   869  C  CA  . GLN   A 1 111 ? 13.539 -8.705  8.488  1.00 21.52 ? 117 GLN   A CA  1 
ATOM   870  C  C   . GLN   A 1 111 ? 14.660 -8.240  7.534  1.00 22.00 ? 117 GLN   A C   1 
ATOM   871  O  O   . GLN   A 1 111 ? 15.617 -9.000  7.297  1.00 22.98 ? 117 GLN   A O   1 
ATOM   872  C  CB  . GLN   A 1 111 ? 12.691 -9.826  7.819  1.00 24.54 ? 117 GLN   A CB  1 
ATOM   873  C  CG  . GLN   A 1 111 ? 12.079 -9.354  6.487  1.00 30.19 ? 117 GLN   A CG  1 
ATOM   874  C  CD  . GLN   A 1 111 ? 11.066 -10.333 5.931  1.00 40.49 ? 117 GLN   A CD  1 
ATOM   875  O  OE1 . GLN   A 1 111 ? 9.844  -10.191 6.120  1.00 44.81 ? 117 GLN   A OE1 1 
ATOM   876  N  NE2 . GLN   A 1 111 ? 11.557 -11.330 5.235  1.00 39.68 ? 117 GLN   A NE2 1 
ATOM   877  N  N   . HIS   A 1 112 ? 14.545 -7.038  6.946  1.00 20.82 ? 118 HIS   A N   1 
ATOM   878  C  CA  . HIS   A 1 112 ? 15.521 -6.515  5.968  1.00 20.73 ? 118 HIS   A CA  1 
ATOM   879  C  C   . HIS   A 1 112 ? 16.629 -5.670  6.556  1.00 20.65 ? 118 HIS   A C   1 
ATOM   880  O  O   . HIS   A 1 112 ? 17.621 -5.385  5.853  1.00 21.35 ? 118 HIS   A O   1 
ATOM   881  C  CB  . HIS   A 1 112 ? 14.808 -5.729  4.842  1.00 20.61 ? 118 HIS   A CB  1 
ATOM   882  C  CG  . HIS   A 1 112 ? 13.693 -6.508  4.193  1.00 22.51 ? 118 HIS   A CG  1 
ATOM   883  N  ND1 . HIS   A 1 112 ? 12.345 -6.183  4.395  1.00 23.87 ? 118 HIS   A ND1 1 
ATOM   884  C  CD2 . HIS   A 1 112 ? 13.763 -7.564  3.325  1.00 25.01 ? 118 HIS   A CD2 1 
ATOM   885  C  CE1 . HIS   A 1 112 ? 11.651 -7.061  3.676  1.00 26.61 ? 118 HIS   A CE1 1 
ATOM   886  N  NE2 . HIS   A 1 112 ? 12.459 -7.923  3.035  1.00 26.37 ? 118 HIS   A NE2 1 
ATOM   887  N  N   . GLY   A 1 113 ? 16.442 -5.227  7.805  1.00 18.51 ? 119 GLY   A N   1 
ATOM   888  C  CA  . GLY   A 1 113 ? 17.439 -4.383  8.420  1.00 18.38 ? 119 GLY   A CA  1 
ATOM   889  C  C   . GLY   A 1 113 ? 16.835 -3.232  9.203  1.00 16.76 ? 119 GLY   A C   1 
ATOM   890  O  O   . GLY   A 1 113 ? 15.675 -3.273  9.628  1.00 17.69 ? 119 GLY   A O   1 
ATOM   891  N  N   . VAL   A 1 114 ? 17.637 -2.197  9.410  1.00 15.88 ? 120 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 114 ? 17.187 -1.023  10.184 1.00 15.78 ? 120 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 114 ? 16.179 -0.184  9.394  1.00 15.08 ? 120 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 114 ? 16.446 0.219   8.241  1.00 16.21 ? 120 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 114 ? 18.392 -0.164  10.607 1.00 16.07 ? 120 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 114 ? 17.912 1.131   11.275 1.00 17.19 ? 120 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 114 ? 19.296 -0.973  11.553 1.00 17.41 ? 120 VAL   A CG2 1 
ATOM   898  N  N   . VAL   A 1 115 ? 15.046 0.110   10.021 1.00 14.86 ? 121 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 115 ? 13.995 0.938   9.406  1.00 14.91 ? 121 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 115 ? 14.064 2.412   9.885  1.00 15.72 ? 121 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 115 ? 13.807 3.348   9.112  1.00 15.32 ? 121 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 115 ? 12.618 0.345   9.800  1.00 16.05 ? 121 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 115 ? 11.447 1.257   9.372  1.00 17.05 ? 121 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 115 ? 12.454 -1.048  9.210  1.00 15.95 ? 121 VAL   A CG2 1 
ATOM   905  N  N   . GLY   A 1 116 ? 14.319 2.611   11.179 1.00 14.34 ? 122 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 116 ? 14.342 3.972   11.710 1.00 15.16 ? 122 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 116 ? 14.626 3.995   13.185 1.00 13.79 ? 122 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 116 ? 15.064 2.978   13.744 1.00 13.36 ? 122 GLY   A O   1 
ATOM   909  N  N   . ILE   A 1 117 ? 14.477 5.175   13.802 1.00 13.53 ? 123 ILE   A N   1 
ATOM   910  C  CA  . ILE   A 1 117 ? 14.813 5.315   15.223 1.00 13.15 ? 123 ILE   A CA  1 
ATOM   911  C  C   . ILE   A 1 117 ? 13.680 6.014   15.960 1.00 13.57 ? 123 ILE   A C   1 
ATOM   912  O  O   . ILE   A 1 117 ? 13.014 6.881   15.382 1.00 13.09 ? 123 ILE   A O   1 
ATOM   913  C  CB  . ILE   A 1 117 ? 16.122 6.110   15.470 1.00 15.58 ? 123 ILE   A CB  1 
ATOM   914  C  CG1 . ILE   A 1 117 ? 16.119 7.465   14.716 1.00 16.94 ? 123 ILE   A CG1 1 
ATOM   915  C  CG2 . ILE   A 1 117 ? 17.351 5.234   15.163 1.00 17.90 ? 123 ILE   A CG2 1 
ATOM   916  C  CD1 . ILE   A 1 117 ? 17.426 8.305   15.205 1.00 19.51 ? 123 ILE   A CD1 1 
ATOM   917  N  N   . VAL   A 1 118 ? 13.434 5.646   17.241 1.00 12.91 ? 124 VAL   A N   1 
ATOM   918  C  CA  . VAL   A 1 118 ? 12.386 6.352   18.019 1.00 12.71 ? 124 VAL   A CA  1 
ATOM   919  C  C   . VAL   A 1 118 ? 12.679 7.861   18.066 1.00 13.44 ? 124 VAL   A C   1 
ATOM   920  O  O   . VAL   A 1 118 ? 13.839 8.239   18.301 1.00 13.72 ? 124 VAL   A O   1 
ATOM   921  C  CB  . VAL   A 1 118 ? 12.355 5.799   19.448 1.00 13.80 ? 124 VAL   A CB  1 
ATOM   922  C  CG1 . VAL   A 1 118 ? 11.365 6.607   20.329 1.00 14.13 ? 124 VAL   A CG1 1 
ATOM   923  C  CG2 . VAL   A 1 118 ? 11.980 4.304   19.449 1.00 15.03 ? 124 VAL   A CG2 1 
ATOM   924  N  N   . SER   A 1 119 ? 11.641 8.674   17.807 1.00 13.56 ? 125 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 119 ? 11.796 10.126  17.777 1.00 14.74 ? 125 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 119 ? 10.694 10.868  18.557 1.00 17.04 ? 125 SER   A C   1 
ATOM   927  O  O   . SER   A 1 119 ? 10.925 11.981  19.035 1.00 19.86 ? 125 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 119 ? 11.813 10.594  16.318 1.00 16.99 ? 125 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 119 ? 11.857 12.011  16.182 1.00 18.44 ? 125 SER   A OG  1 
ATOM   930  N  N   . THR   A 1 120 ? 9.487  10.268  18.658 1.00 17.42 ? 126 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 120 ? 8.365  10.948  19.365 1.00 18.74 ? 126 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 120 ? 7.566  9.879   20.162 1.00 19.83 ? 126 THR   A C   1 
ATOM   933  O  O   . THR   A 1 120 ? 7.817  8.673   20.033 1.00 18.25 ? 126 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 120 ? 7.400  11.660  18.339 1.00 22.60 ? 126 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 120 ? 6.593  10.701  17.661 1.00 25.16 ? 126 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 120 ? 8.097  12.590  17.354 1.00 24.90 ? 126 THR   A CG2 1 
ATOM   937  N  N   . GLY   A 1 121 ? 6.549  10.301  20.915 1.00 21.49 ? 127 GLY   A N   1 
ATOM   938  C  CA  . GLY   A 1 121 ? 5.685  9.347   21.583 1.00 22.14 ? 127 GLY   A CA  1 
ATOM   939  C  C   . GLY   A 1 121 ? 4.767  10.026  22.570 1.00 23.15 ? 127 GLY   A C   1 
ATOM   940  O  O   . GLY   A 1 121 ? 4.691  11.244  22.589 1.00 24.14 ? 127 GLY   A O   1 
ATOM   941  N  N   . GLY   A 1 122 ? 4.152  9.217   23.399 1.00 24.85 ? 128 GLY   A N   1 
ATOM   942  C  CA  . GLY   A 1 122 ? 3.272  9.662   24.465 1.00 26.24 ? 128 GLY   A CA  1 
ATOM   943  C  C   . GLY   A 1 122 ? 1.935  8.988   24.363 1.00 26.74 ? 128 GLY   A C   1 
ATOM   944  O  O   . GLY   A 1 122 ? 1.502  8.619   23.271 1.00 27.23 ? 128 GLY   A O   1 
ATOM   945  N  N   . ASN   A 1 123 ? 1.255  8.832   25.503 1.00 26.46 ? 129 ASN   A N   1 
ATOM   946  C  CA  . ASN   A 1 123 ? -0.097 8.278   25.581 1.00 27.31 ? 129 ASN   A CA  1 
ATOM   947  C  C   . ASN   A 1 123 ? -0.294 6.985   24.852 1.00 25.68 ? 129 ASN   A C   1 
ATOM   948  O  O   . ASN   A 1 123 ? -1.389 6.728   24.328 1.00 26.45 ? 129 ASN   A O   1 
ATOM   949  C  CB  . ASN   A 1 123 ? -1.095 9.335   25.102 1.00 31.67 ? 129 ASN   A CB  1 
ATOM   950  C  CG  . ASN   A 1 123 ? -1.145 10.483  26.073 1.00 38.54 ? 129 ASN   A CG  1 
ATOM   951  O  OD1 . ASN   A 1 123 ? -1.203 10.258  27.281 1.00 41.48 ? 129 ASN   A OD1 1 
ATOM   952  N  ND2 . ASN   A 1 123 ? -1.088 11.724  25.573 1.00 39.35 ? 129 ASN   A ND2 1 
ATOM   953  N  N   . GLY   A 1 124 ? 0.688  6.113   24.933 1.00 22.51 ? 130 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 124 ? 0.599  4.800   24.316 1.00 20.71 ? 130 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 124 ? 0.916  4.813   22.840 1.00 18.85 ? 130 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 124 ? 0.752  3.775   22.189 1.00 20.85 ? 130 GLY   A O   1 
ATOM   957  N  N   . LEU   A 1 125 ? 1.542  5.894   22.343 1.00 17.73 ? 131 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 125 ? 2.028  5.950   20.963 1.00 17.05 ? 131 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 125 ? 3.557  6.002   20.957 1.00 16.72 ? 131 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 125 ? 4.181  6.473   21.918 1.00 18.15 ? 131 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 125 ? 1.514  7.194   20.216 1.00 18.07 ? 131 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 125 ? -0.000 7.193   19.951 1.00 21.16 ? 131 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 125 ? -0.494 8.608   19.633 1.00 24.02 ? 131 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 125 ? -0.363 6.199   18.828 1.00 20.83 ? 131 LEU   A CD2 1 
ATOM   965  N  N   . VAL   A 1 126 ? 4.137  5.587   19.826 1.00 15.11 ? 132 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 126 ? 5.568  5.723   19.634 1.00 14.87 ? 132 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 126 ? 5.777  6.141   18.160 1.00 15.55 ? 132 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 126 ? 5.132  5.573   17.268 1.00 16.79 ? 132 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 126 ? 6.373  4.482   20.050 1.00 15.05 ? 132 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 126 ? 5.897  3.230   19.318 1.00 17.71 ? 132 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 126 ? 7.872  4.714   19.791 1.00 15.24 ? 132 VAL   A CG2 1 
ATOM   972  N  N   . GLY   A 1 127 ? 6.625  7.138   17.936 1.00 15.69 ? 133 GLY   A N   1 
ATOM   973  C  CA  . GLY   A 1 127 ? 6.875  7.635   16.589 1.00 15.81 ? 133 GLY   A CA  1 
ATOM   974  C  C   . GLY   A 1 127 ? 8.313  7.397   16.178 1.00 15.30 ? 133 GLY   A C   1 
ATOM   975  O  O   . GLY   A 1 127 ? 9.217  7.611   16.981 1.00 15.72 ? 133 GLY   A O   1 
ATOM   976  N  N   . PHE   A 1 128 ? 8.539  6.908   14.965 1.00 15.07 ? 134 PHE   A N   1 
ATOM   977  C  CA  . PHE   A 1 128 ? 9.888  6.589   14.481 1.00 14.30 ? 134 PHE   A CA  1 
ATOM   978  C  C   . PHE   A 1 128 ? 10.240 7.468   13.262 1.00 14.91 ? 134 PHE   A C   1 
ATOM   979  O  O   . PHE   A 1 128 ? 9.452  7.581   12.321 1.00 15.54 ? 134 PHE   A O   1 
ATOM   980  C  CB  . PHE   A 1 128 ? 9.922  5.126   14.007 1.00 13.39 ? 134 PHE   A CB  1 
ATOM   981  C  CG  . PHE   A 1 128 ? 9.417  4.120   15.027 1.00 14.28 ? 134 PHE   A CG  1 
ATOM   982  C  CD1 . PHE   A 1 128 ? 10.267 3.599   15.985 1.00 13.65 ? 134 PHE   A CD1 1 
ATOM   983  C  CD2 . PHE   A 1 128 ? 8.087  3.674   14.993 1.00 15.55 ? 134 PHE   A CD2 1 
ATOM   984  C  CE1 . PHE   A 1 128 ? 9.809  2.691   16.922 1.00 14.59 ? 134 PHE   A CE1 1 
ATOM   985  C  CE2 . PHE   A 1 128 ? 7.637  2.710   15.901 1.00 16.03 ? 134 PHE   A CE2 1 
ATOM   986  C  CZ  . PHE   A 1 128 ? 8.503  2.245   16.882 1.00 15.53 ? 134 PHE   A CZ  1 
ATOM   987  N  N   . ALA   A 1 129 ? 11.451 8.019   13.289 1.00 13.78 ? 135 ALA   A N   1 
ATOM   988  C  CA  . ALA   A 1 129 ? 11.986 8.748   12.152 1.00 14.24 ? 135 ALA   A CA  1 
ATOM   989  C  C   . ALA   A 1 129 ? 12.478 7.685   11.137 1.00 14.27 ? 135 ALA   A C   1 
ATOM   990  O  O   . ALA   A 1 129 ? 13.415 6.923   11.445 1.00 14.05 ? 135 ALA   A O   1 
ATOM   991  C  CB  . ALA   A 1 129 ? 13.145 9.630   12.621 1.00 14.73 ? 135 ALA   A CB  1 
ATOM   992  N  N   . ASP   A 1 130 ? 11.911 7.657   9.916  1.00 14.10 ? 136 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 130 ? 12.328 6.690   8.903  1.00 14.91 ? 136 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 130 ? 13.709 7.056   8.372  1.00 15.98 ? 136 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 130 ? 14.030 8.264   8.224  1.00 16.45 ? 136 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 130 ? 11.342 6.761   7.726  1.00 18.09 ? 136 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 130 ? 11.601 5.722   6.649  1.00 23.56 ? 136 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 130 ? 11.765 4.562   6.985  1.00 22.93 ? 136 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 130 ? 11.728 6.108   5.465  1.00 27.18 ? 136 ASP   A OD2 1 
ATOM   1000 N  N   . VAL   A 1 131 ? 14.524 6.019   8.021  1.00 15.20 ? 137 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 131 ? 15.810 6.275   7.343  1.00 14.71 ? 137 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 131 ? 15.916 5.497   6.019  1.00 15.72 ? 137 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 131 ? 16.954 5.561   5.358  1.00 16.23 ? 137 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 131 ? 17.041 5.941   8.234  1.00 15.76 ? 137 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 131 ? 17.055 6.810   9.511  1.00 16.15 ? 137 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 131 ? 17.074 4.441   8.584  1.00 16.02 ? 137 VAL   A CG2 1 
ATOM   1007 N  N   . ARG   A 1 132 ? 14.864 4.743   5.622  1.00 15.89 ? 138 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 132 ? 14.953 3.882   4.442  1.00 15.09 ? 138 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 132 ? 15.112 4.605   3.138  1.00 18.84 ? 138 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 132 ? 15.574 3.991   2.172  1.00 21.22 ? 138 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 132 ? 13.740 2.937   4.376  1.00 16.68 ? 138 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 132 ? 13.689 1.962   5.562  1.00 17.42 ? 138 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 132 ? 12.410 1.154   5.470  1.00 17.88 ? 138 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 132 ? 11.252 1.989   5.781  1.00 18.04 ? 138 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 132 ? 10.009 1.522   5.906  1.00 19.33 ? 138 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 132 ? 9.738  0.237   5.635  1.00 19.85 ? 138 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 132 ? 9.027  2.330   6.296  1.00 20.00 ? 138 ARG   A NH2 1 
ATOM   1018 N  N   . ASP   A 1 133 ? 14.700 5.876   3.092  1.00 19.23 ? 139 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 133 ? 14.852 6.664   1.863  1.00 20.89 ? 139 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 133 ? 16.255 7.242   1.681  1.00 20.67 ? 139 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 133 ? 16.543 7.766   0.612  1.00 21.34 ? 139 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 133 ? 13.831 7.803   1.828  1.00 22.37 ? 139 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 133 ? 14.032 8.822   2.926  1.00 25.18 ? 139 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 133 ? 14.246 8.404   4.106  1.00 23.58 ? 139 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 133 ? 13.963 10.033  2.628  1.00 29.02 ? 139 ASP   A OD2 1 
ATOM   1026 N  N   . LEU   A 1 134 ? 17.108 7.192   2.703  1.00 19.46 ? 140 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 134 ? 18.463 7.785   2.649  1.00 19.04 ? 140 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 134 ? 19.422 6.806   1.983  1.00 19.76 ? 140 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 134 ? 20.213 6.104   2.641  1.00 19.03 ? 140 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 134 ? 18.895 8.145   4.082  1.00 18.71 ? 140 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 134 ? 17.939 9.108   4.821  1.00 20.04 ? 140 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 134 ? 18.399 9.343   6.269  1.00 19.77 ? 140 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 134 ? 17.771 10.439  4.086  1.00 20.78 ? 140 LEU   A CD2 1 
ATOM   1034 N  N   . LEU   A 1 135 ? 19.328 6.716   0.645  1.00 20.72 ? 141 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 135 ? 20.098 5.693   -0.067 1.00 22.60 ? 141 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 135 ? 21.603 5.871   0.028  1.00 23.75 ? 141 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 135 ? 22.350 4.876   -0.035 1.00 24.34 ? 141 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 135 ? 19.660 5.575   -1.529 1.00 23.45 ? 141 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 135 ? 18.156 5.528   -1.779 1.00 25.45 ? 141 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 135 ? 17.894 5.276   -3.282 1.00 27.12 ? 141 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 135 ? 17.450 4.446   -0.916 1.00 25.60 ? 141 LEU   A CD2 1 
ATOM   1042 N  N   . TRP   A 1 136 ? 22.050 7.128   0.180  1.00 23.23 ? 142 TRP   A N   1 
ATOM   1043 C  CA  . TRP   A 1 136 ? 23.476 7.448   0.250  1.00 24.45 ? 142 TRP   A CA  1 
ATOM   1044 C  C   . TRP   A 1 136 ? 24.147 6.878   1.507  1.00 25.34 ? 142 TRP   A C   1 
ATOM   1045 O  O   . TRP   A 1 136 ? 25.388 6.851   1.568  1.00 26.63 ? 142 TRP   A O   1 
ATOM   1046 C  CB  . TRP   A 1 136 ? 23.677 8.971   0.156  1.00 24.37 ? 142 TRP   A CB  1 
ATOM   1047 C  CG  . TRP   A 1 136 ? 22.838 9.759   1.136  1.00 23.58 ? 142 TRP   A CG  1 
ATOM   1048 C  CD1 . TRP   A 1 136 ? 21.597 10.289  0.928  1.00 23.15 ? 142 TRP   A CD1 1 
ATOM   1049 C  CD2 . TRP   A 1 136 ? 23.211 10.116  2.463  1.00 23.06 ? 142 TRP   A CD2 1 
ATOM   1050 N  NE1 . TRP   A 1 136 ? 21.185 10.980  2.046  1.00 23.43 ? 142 TRP   A NE1 1 
ATOM   1051 C  CE2 . TRP   A 1 136 ? 22.164 10.900  3.000  1.00 23.59 ? 142 TRP   A CE2 1 
ATOM   1052 C  CE3 . TRP   A 1 136 ? 24.343 9.871   3.243  1.00 24.04 ? 142 TRP   A CE3 1 
ATOM   1053 C  CZ2 . TRP   A 1 136 ? 22.217 11.435  4.288  1.00 24.17 ? 142 TRP   A CZ2 1 
ATOM   1054 C  CZ3 . TRP   A 1 136 ? 24.419 10.434  4.502  1.00 24.57 ? 142 TRP   A CZ3 1 
ATOM   1055 C  CH2 . TRP   A 1 136 ? 23.366 11.218  5.005  1.00 24.23 ? 142 TRP   A CH2 1 
ATOM   1056 N  N   . LEU   A 1 137 ? 23.372 6.436   2.526  1.00 24.08 ? 143 LEU   A N   1 
ATOM   1057 C  CA  . LEU   A 1 137 ? 23.995 5.858   3.727  1.00 25.16 ? 143 LEU   A CA  1 
ATOM   1058 C  C   . LEU   A 1 137 ? 24.788 4.579   3.383  1.00 29.92 ? 143 LEU   A C   1 
ATOM   1059 O  O   . LEU   A 1 137 ? 25.684 4.207   4.145  1.00 30.54 ? 143 LEU   A O   1 
ATOM   1060 C  CB  . LEU   A 1 137 ? 22.934 5.493   4.776  1.00 23.34 ? 143 LEU   A CB  1 
ATOM   1061 C  CG  . LEU   A 1 137 ? 22.286 6.636   5.522  1.00 21.66 ? 143 LEU   A CG  1 
ATOM   1062 C  CD1 . LEU   A 1 137 ? 21.163 6.096   6.426  1.00 22.28 ? 143 LEU   A CD1 1 
ATOM   1063 C  CD2 . LEU   A 1 137 ? 23.314 7.422   6.407  1.00 22.01 ? 143 LEU   A CD2 1 
ATOM   1064 N  N   . ASP   A 1 138 ? 24.391 3.882   2.284  1.00 33.11 ? 144 ASP   A N   1 
ATOM   1065 C  CA  . ASP   A 1 138 ? 24.917 2.603   1.795  1.00 37.99 ? 144 ASP   A CA  1 
ATOM   1066 C  C   . ASP   A 1 138 ? 26.213 2.690   1.039  1.00 42.44 ? 144 ASP   A C   1 
ATOM   1067 O  O   . ASP   A 1 138 ? 26.680 1.637   0.600  1.00 43.70 ? 144 ASP   A O   1 
ATOM   1068 C  CB  . ASP   A 1 138 ? 23.915 1.963   0.819  1.00 40.74 ? 144 ASP   A CB  1 
ATOM   1069 C  CG  . ASP   A 1 138 ? 22.710 1.315   1.424  1.00 47.75 ? 144 ASP   A CG  1 
ATOM   1070 O  OD1 . ASP   A 1 138 ? 22.696 1.138   2.652  1.00 49.26 ? 144 ASP   A OD1 1 
ATOM   1071 O  OD2 . ASP   A 1 138 ? 21.763 0.983   0.658  1.00 52.16 ? 144 ASP   A OD2 1 
ATOM   1072 N  N   . GLU   A 1 139 ? 26.758 3.888   0.798  1.00 44.79 ? 145 GLU   A N   1 
ATOM   1073 C  CA  . GLU   A 1 139 ? 28.029 4.030   0.070  1.00 47.91 ? 145 GLU   A CA  1 
ATOM   1074 C  C   . GLU   A 1 139 ? 28.835 5.237   0.553  1.00 49.52 ? 145 GLU   A C   1 
ATOM   1075 O  O   . GLU   A 1 139 ? 28.264 6.221   1.032  1.00 50.72 ? 145 GLU   A O   1 
ATOM   1076 C  CB  . GLU   A 1 139 ? 27.814 4.104   -1.454 1.00 51.49 ? 145 GLU   A CB  1 
ATOM   1077 C  CG  . GLU   A 1 139 ? 27.081 5.352   -1.915 1.00 57.80 ? 145 GLU   A CG  1 
ATOM   1078 C  CD  . GLU   A 1 139 ? 25.617 5.129   -2.234 1.00 66.25 ? 145 GLU   A CD  1 
ATOM   1079 O  OE1 . GLU   A 1 139 ? 25.045 5.936   -3.003 1.00 68.07 ? 145 GLU   A OE1 1 
ATOM   1080 O  OE2 . GLU   A 1 139 ? 25.042 4.141   -1.723 1.00 68.90 ? 145 GLU   A OE2 1 
ATOM   1081 N  N   . SER   B 1 1   ? 15.108 -23.777 8.585  1.00 27.27 ? 7   SER   C N   1 
ATOM   1082 C  CA  . SER   B 1 1   ? 14.010 -23.600 9.541  1.00 27.55 ? 7   SER   C CA  1 
ATOM   1083 C  C   . SER   B 1 1   ? 13.993 -24.760 10.574 1.00 26.41 ? 7   SER   C C   1 
ATOM   1084 O  O   . SER   B 1 1   ? 14.649 -25.789 10.365 1.00 27.04 ? 7   SER   C O   1 
ATOM   1085 C  CB  . SER   B 1 1   ? 12.673 -23.538 8.799  1.00 31.12 ? 7   SER   C CB  1 
ATOM   1086 O  OG  . SER   B 1 1   ? 12.442 -24.782 8.153  1.00 35.87 ? 7   SER   C OG  1 
ATOM   1087 N  N   . GLY   B 1 2   ? 13.237 -24.587 11.661 1.00 24.35 ? 8   GLY   C N   1 
ATOM   1088 C  CA  . GLY   B 1 2   ? 13.082 -25.602 12.695 1.00 23.06 ? 8   GLY   C CA  1 
ATOM   1089 C  C   . GLY   B 1 2   ? 12.765 -25.053 14.066 1.00 21.59 ? 8   GLY   C C   1 
ATOM   1090 O  O   . GLY   B 1 2   ? 13.095 -23.909 14.364 1.00 23.30 ? 8   GLY   C O   1 
ATOM   1091 N  N   . ALA   B 1 3   ? 12.143 -25.852 14.921 1.00 20.28 ? 9   ALA   C N   1 
ATOM   1092 C  CA  . ALA   B 1 3   ? 11.771 -25.420 16.266 1.00 20.74 ? 9   ALA   C CA  1 
ATOM   1093 C  C   . ALA   B 1 3   ? 11.842 -26.575 17.262 1.00 19.91 ? 9   ALA   C C   1 
ATOM   1094 O  O   . ALA   B 1 3   ? 11.702 -27.749 16.874 1.00 21.05 ? 9   ALA   C O   1 
ATOM   1095 C  CB  . ALA   B 1 3   ? 10.342 -24.866 16.251 1.00 21.11 ? 9   ALA   C CB  1 
ATOM   1096 N  N   . ILE   B 1 4   ? 11.940 -26.234 18.559 1.00 18.25 ? 10  ILE   C N   1 
ATOM   1097 C  CA  . ILE   B 1 4   ? 11.847 -27.176 19.656 1.00 17.72 ? 10  ILE   C CA  1 
ATOM   1098 C  C   . ILE   B 1 4   ? 10.512 -26.965 20.341 1.00 19.33 ? 10  ILE   C C   1 
ATOM   1099 O  O   . ILE   B 1 4   ? 10.132 -25.848 20.631 1.00 18.99 ? 10  ILE   C O   1 
ATOM   1100 C  CB  . ILE   B 1 4   ? 12.988 -26.928 20.675 1.00 17.33 ? 10  ILE   C CB  1 
ATOM   1101 C  CG1 . ILE   B 1 4   ? 14.369 -26.959 19.984 1.00 18.16 ? 10  ILE   C CG1 1 
ATOM   1102 C  CG2 . ILE   B 1 4   ? 12.896 -27.932 21.817 1.00 19.16 ? 10  ILE   C CG2 1 
ATOM   1103 C  CD1 . ILE   B 1 4   ? 15.468 -26.321 20.943 1.00 19.82 ? 10  ILE   C CD1 1 
ATOM   1104 N  N   . TYR   B 1 5   ? 9.749  -28.058 20.589 1.00 20.06 ? 11  TYR   C N   1 
ATOM   1105 C  CA  . TYR   B 1 5   ? 8.449  -27.960 21.240 1.00 20.99 ? 11  TYR   C CA  1 
ATOM   1106 C  C   . TYR   B 1 5   ? 8.536  -28.685 22.564 1.00 22.66 ? 11  TYR   C C   1 
ATOM   1107 O  O   . TYR   B 1 5   ? 8.688  -29.910 22.588 1.00 24.10 ? 11  TYR   C O   1 
ATOM   1108 C  CB  . TYR   B 1 5   ? 7.374  -28.605 20.345 1.00 21.50 ? 11  TYR   C CB  1 
ATOM   1109 C  CG  . TYR   B 1 5   ? 7.160  -27.822 19.063 1.00 20.91 ? 11  TYR   C CG  1 
ATOM   1110 C  CD1 . TYR   B 1 5   ? 6.290  -26.743 19.022 1.00 22.17 ? 11  TYR   C CD1 1 
ATOM   1111 C  CD2 . TYR   B 1 5   ? 7.889  -28.110 17.919 1.00 22.70 ? 11  TYR   C CD2 1 
ATOM   1112 C  CE1 . TYR   B 1 5   ? 6.115  -25.996 17.860 1.00 24.68 ? 11  TYR   C CE1 1 
ATOM   1113 C  CE2 . TYR   B 1 5   ? 7.719  -27.377 16.749 1.00 24.16 ? 11  TYR   C CE2 1 
ATOM   1114 C  CZ  . TYR   B 1 5   ? 6.829  -26.319 16.720 1.00 25.94 ? 11  TYR   C CZ  1 
ATOM   1115 O  OH  . TYR   B 1 5   ? 6.711  -25.569 15.569 1.00 29.27 ? 11  TYR   C OH  1 
ATOM   1116 N  N   . VAL   B 1 6   ? 8.498  -27.946 23.679 1.00 23.31 ? 12  VAL   C N   1 
ATOM   1117 C  CA  . VAL   B 1 6   ? 8.637  -28.538 25.013 1.00 24.52 ? 12  VAL   C CA  1 
ATOM   1118 C  C   . VAL   B 1 6   ? 7.553  -27.951 25.903 1.00 25.57 ? 12  VAL   C C   1 
ATOM   1119 O  O   . VAL   B 1 6   ? 7.419  -26.734 25.985 1.00 24.76 ? 12  VAL   C O   1 
ATOM   1120 C  CB  . VAL   B 1 6   ? 10.084 -28.305 25.577 1.00 26.10 ? 12  VAL   C CB  1 
ATOM   1121 C  CG1 . VAL   B 1 6   ? 10.515 -26.845 25.439 1.00 26.91 ? 12  VAL   C CG1 1 
ATOM   1122 C  CG2 . VAL   B 1 6   ? 10.172 -28.777 27.020 1.00 26.95 ? 12  VAL   C CG2 1 
ATOM   1123 N  N   . GLY   B 1 7   ? 6.685  -28.799 26.489 1.00 26.95 ? 13  GLY   C N   1 
ATOM   1124 C  CA  . GLY   B 1 7   ? 5.592  -28.296 27.317 1.00 28.42 ? 13  GLY   C CA  1 
ATOM   1125 C  C   . GLY   B 1 7   ? 4.698  -27.349 26.531 1.00 29.01 ? 13  GLY   C C   1 
ATOM   1126 O  O   . GLY   B 1 7   ? 4.369  -27.648 25.382 1.00 29.95 ? 13  GLY   C O   1 
ATOM   1127 N  N   . ASN   B 1 8   ? 4.410  -26.154 27.073 1.00 28.72 ? 14  ASN   C N   1 
ATOM   1128 C  CA  . ASN   B 1 8   ? 3.619  -25.181 26.316 1.00 28.37 ? 14  ASN   C CA  1 
ATOM   1129 C  C   . ASN   B 1 8   ? 4.504  -24.090 25.701 1.00 25.46 ? 14  ASN   C C   1 
ATOM   1130 O  O   . ASN   B 1 8   ? 4.069  -22.934 25.565 1.00 24.58 ? 14  ASN   C O   1 
ATOM   1131 C  CB  . ASN   B 1 8   ? 2.494  -24.597 27.149 1.00 32.41 ? 14  ASN   C CB  1 
ATOM   1132 C  CG  . ASN   B 1 8   ? 1.417  -25.608 27.432 1.00 39.98 ? 14  ASN   C CG  1 
ATOM   1133 O  OD1 . ASN   B 1 8   ? 0.690  -26.045 26.530 1.00 42.53 ? 14  ASN   C OD1 1 
ATOM   1134 N  ND2 . ASN   B 1 8   ? 1.301  -26.011 28.688 1.00 41.91 ? 14  ASN   C ND2 1 
ATOM   1135 N  N   . TYR   B 1 9   ? 5.719  -24.474 25.284 1.00 23.89 ? 15  TYR   C N   1 
ATOM   1136 C  CA  . TYR   B 1 9   ? 6.671  -23.529 24.688 1.00 22.05 ? 15  TYR   C CA  1 
ATOM   1137 C  C   . TYR   B 1 9   ? 7.162  -24.002 23.322 1.00 20.45 ? 15  TYR   C C   1 
ATOM   1138 O  O   . TYR   B 1 9   ? 7.299  -25.212 23.080 1.00 21.22 ? 15  TYR   C O   1 
ATOM   1139 C  CB  . TYR   B 1 9   ? 7.922  -23.416 25.579 1.00 22.34 ? 15  TYR   C CB  1 
ATOM   1140 C  CG  . TYR   B 1 9   ? 7.663  -22.824 26.945 1.00 24.40 ? 15  TYR   C CG  1 
ATOM   1141 C  CD1 . TYR   B 1 9   ? 6.999  -21.608 27.083 1.00 26.54 ? 15  TYR   C CD1 1 
ATOM   1142 C  CD2 . TYR   B 1 9   ? 8.052  -23.494 28.105 1.00 26.00 ? 15  TYR   C CD2 1 
ATOM   1143 C  CE1 . TYR   B 1 9   ? 6.754  -21.060 28.338 1.00 28.12 ? 15  TYR   C CE1 1 
ATOM   1144 C  CE2 . TYR   B 1 9   ? 7.811  -22.954 29.368 1.00 27.36 ? 15  TYR   C CE2 1 
ATOM   1145 C  CZ  . TYR   B 1 9   ? 7.165  -21.733 29.479 1.00 29.56 ? 15  TYR   C CZ  1 
ATOM   1146 O  OH  . TYR   B 1 9   ? 6.946  -21.181 30.731 1.00 32.35 ? 15  TYR   C OH  1 
ATOM   1147 N  N   . ARG   B 1 10  ? 7.449  -23.032 22.437 1.00 18.94 ? 16  ARG   C N   1 
ATOM   1148 C  CA  . ARG   B 1 10  ? 8.058  -23.261 21.117 1.00 18.81 ? 16  ARG   C CA  1 
ATOM   1149 C  C   . ARG   B 1 10  ? 9.334  -22.403 21.088 1.00 18.42 ? 16  ARG   C C   1 
ATOM   1150 O  O   . ARG   B 1 10  ? 9.269  -21.211 21.375 1.00 18.97 ? 16  ARG   C O   1 
ATOM   1151 C  CB  . ARG   B 1 10  ? 7.086  -22.820 20.007 1.00 18.74 ? 16  ARG   C CB  1 
ATOM   1152 C  CG  . ARG   B 1 10  ? 7.693  -22.551 18.639 1.00 20.80 ? 16  ARG   C CG  1 
ATOM   1153 C  CD  . ARG   B 1 10  ? 6.628  -22.239 17.584 1.00 21.25 ? 16  ARG   C CD  1 
ATOM   1154 N  NE  . ARG   B 1 10  ? 7.066  -21.262 16.584 1.00 23.03 ? 16  ARG   C NE  1 
ATOM   1155 C  CZ  . ARG   B 1 10  ? 7.434  -21.543 15.336 1.00 27.90 ? 16  ARG   C CZ  1 
ATOM   1156 N  NH1 . ARG   B 1 10  ? 7.460  -22.806 14.909 1.00 28.67 ? 16  ARG   C NH1 1 
ATOM   1157 N  NH2 . ARG   B 1 10  ? 7.794  -20.566 14.509 1.00 26.29 ? 16  ARG   C NH2 1 
ATOM   1158 N  N   . VAL   B 1 11  ? 10.495 -23.038 20.851 1.00 17.30 ? 17  VAL   C N   1 
ATOM   1159 C  CA  . VAL   B 1 11  ? 11.791 -22.335 20.823 1.00 17.36 ? 17  VAL   C CA  1 
ATOM   1160 C  C   . VAL   B 1 11  ? 12.249 -22.252 19.382 1.00 17.09 ? 17  VAL   C C   1 
ATOM   1161 O  O   . VAL   B 1 11  ? 12.354 -23.293 18.710 1.00 17.97 ? 17  VAL   C O   1 
ATOM   1162 C  CB  . VAL   B 1 11  ? 12.867 -23.119 21.622 1.00 18.64 ? 17  VAL   C CB  1 
ATOM   1163 C  CG1 . VAL   B 1 11  ? 14.153 -22.293 21.725 1.00 19.00 ? 17  VAL   C CG1 1 
ATOM   1164 C  CG2 . VAL   B 1 11  ? 12.355 -23.534 23.007 1.00 20.10 ? 17  VAL   C CG2 1 
ATOM   1165 N  N   . VAL   B 1 12  ? 12.477 -21.038 18.884 1.00 16.05 ? 18  VAL   C N   1 
ATOM   1166 C  CA  . VAL   B 1 12  ? 12.905 -20.856 17.508 1.00 15.89 ? 18  VAL   C CA  1 
ATOM   1167 C  C   . VAL   B 1 12  ? 14.109 -19.903 17.445 1.00 15.45 ? 18  VAL   C C   1 
ATOM   1168 O  O   . VAL   B 1 12  ? 14.413 -19.172 18.412 1.00 16.00 ? 18  VAL   C O   1 
ATOM   1169 C  CB  . VAL   B 1 12  ? 11.750 -20.243 16.646 1.00 17.33 ? 18  VAL   C CB  1 
ATOM   1170 C  CG1 . VAL   B 1 12  ? 10.613 -21.241 16.500 1.00 20.22 ? 18  VAL   C CG1 1 
ATOM   1171 C  CG2 . VAL   B 1 12  ? 11.244 -18.921 17.267 1.00 16.84 ? 18  VAL   C CG2 1 
ATOM   1172 N  N   . ASN   B 1 13  ? 14.791 -19.839 16.277 1.00 15.02 ? 19  ASN   C N   1 
ATOM   1173 C  CA  . ASN   B 1 13  ? 15.807 -18.796 16.079 1.00 15.63 ? 19  ASN   C CA  1 
ATOM   1174 C  C   . ASN   B 1 13  ? 15.047 -17.443 16.120 1.00 16.44 ? 19  ASN   C C   1 
ATOM   1175 O  O   . ASN   B 1 13  ? 14.020 -17.274 15.419 1.00 17.24 ? 19  ASN   C O   1 
ATOM   1176 C  CB  . ASN   B 1 13  ? 16.455 -18.900 14.703 1.00 16.35 ? 19  ASN   C CB  1 
ATOM   1177 C  CG  . ASN   B 1 13  ? 17.336 -20.131 14.560 1.00 17.94 ? 19  ASN   C CG  1 
ATOM   1178 O  OD1 . ASN   B 1 13  ? 16.866 -21.190 14.111 1.00 16.77 ? 19  ASN   C OD1 1 
ATOM   1179 N  ND2 . ASN   B 1 13  ? 18.601 -20.019 14.971 1.00 17.14 ? 19  ASN   C ND2 1 
ATOM   1180 N  N   . ARG   B 1 14  ? 15.557 -16.483 16.912 1.00 15.58 ? 20  ARG   C N   1 
ATOM   1181 C  CA  . ARG   B 1 14  ? 14.869 -15.177 17.008 1.00 15.92 ? 20  ARG   C CA  1 
ATOM   1182 C  C   . ARG   B 1 14  ? 14.712 -14.514 15.622 1.00 16.59 ? 20  ARG   C C   1 
ATOM   1183 O  O   . ARG   B 1 14  ? 13.649 -13.940 15.325 1.00 17.74 ? 20  ARG   C O   1 
ATOM   1184 C  CB  . ARG   B 1 14  ? 15.650 -14.269 17.960 1.00 16.67 ? 20  ARG   C CB  1 
ATOM   1185 C  CG  . ARG   B 1 14  ? 14.918 -12.964 18.316 1.00 18.14 ? 20  ARG   C CG  1 
ATOM   1186 C  CD  . ARG   B 1 14  ? 15.904 -12.091 19.086 1.00 18.36 ? 20  ARG   C CD  1 
ATOM   1187 N  NE  . ARG   B 1 14  ? 15.332 -10.839 19.622 1.00 18.56 ? 20  ARG   C NE  1 
ATOM   1188 C  CZ  . ARG   B 1 14  ? 15.250 -9.704  18.936 1.00 20.55 ? 20  ARG   C CZ  1 
ATOM   1189 N  NH1 . ARG   B 1 14  ? 15.609 -9.664  17.664 1.00 21.90 ? 20  ARG   C NH1 1 
ATOM   1190 N  NH2 . ARG   B 1 14  ? 14.765 -8.599  19.515 1.00 20.31 ? 20  ARG   C NH2 1 
ATOM   1191 N  N   . HIS   B 1 15  ? 15.720 -14.690 14.739 1.00 16.47 ? 21  HIS   C N   1 
ATOM   1192 C  CA  . HIS   B 1 15  ? 15.635 -14.043 13.412 1.00 17.46 ? 21  HIS   C CA  1 
ATOM   1193 C  C   . HIS   B 1 15  ? 14.614 -14.697 12.468 1.00 18.00 ? 21  HIS   C C   1 
ATOM   1194 O  O   . HIS   B 1 15  ? 14.284 -14.113 11.433 1.00 19.92 ? 21  HIS   C O   1 
ATOM   1195 C  CB  . HIS   B 1 15  ? 17.029 -13.922 12.759 1.00 17.33 ? 21  HIS   C CB  1 
ATOM   1196 C  CG  . HIS   B 1 15  ? 17.609 -15.199 12.218 1.00 18.91 ? 21  HIS   C CG  1 
ATOM   1197 N  ND1 . HIS   B 1 15  ? 18.298 -16.088 13.044 1.00 18.57 ? 21  HIS   C ND1 1 
ATOM   1198 C  CD2 . HIS   B 1 15  ? 17.580 -15.703 10.956 1.00 20.76 ? 21  HIS   C CD2 1 
ATOM   1199 C  CE1 . HIS   B 1 15  ? 18.691 -17.096 12.255 1.00 20.23 ? 21  HIS   C CE1 1 
ATOM   1200 N  NE2 . HIS   B 1 15  ? 18.258 -16.933 10.998 1.00 22.16 ? 21  HIS   C NE2 1 
ATOM   1201 N  N   . LEU   B 1 16  ? 14.097 -15.897 12.830 1.00 17.57 ? 22  LEU   C N   1 
ATOM   1202 C  CA  . LEU   B 1 16  ? 13.093 -16.576 12.014 1.00 17.98 ? 22  LEU   C CA  1 
ATOM   1203 C  C   . LEU   B 1 16  ? 11.701 -16.572 12.697 1.00 19.13 ? 22  LEU   C C   1 
ATOM   1204 O  O   . LEU   B 1 16  ? 10.757 -17.181 12.167 1.00 20.30 ? 22  LEU   C O   1 
ATOM   1205 C  CB  . LEU   B 1 16  ? 13.545 -18.030 11.738 1.00 19.24 ? 22  LEU   C CB  1 
ATOM   1206 C  CG  . LEU   B 1 16  ? 14.866 -18.149 10.939 1.00 20.76 ? 22  LEU   C CG  1 
ATOM   1207 C  CD1 . LEU   B 1 16  ? 15.243 -19.657 10.724 1.00 22.25 ? 22  LEU   C CD1 1 
ATOM   1208 C  CD2 . LEU   B 1 16  ? 14.778 -17.387 9.575  1.00 22.00 ? 22  LEU   C CD2 1 
ATOM   1209 N  N   . ALA   B 1 17  ? 11.563 -15.909 13.871 1.00 17.99 ? 23  ALA   C N   1 
ATOM   1210 C  CA  . ALA   B 1 17  ? 10.274 -15.894 14.578 1.00 19.02 ? 23  ALA   C CA  1 
ATOM   1211 C  C   . ALA   B 1 17  ? 9.199  -15.228 13.712 1.00 19.94 ? 23  ALA   C C   1 
ATOM   1212 O  O   . ALA   B 1 17  ? 9.487  -14.276 12.996 1.00 20.81 ? 23  ALA   C O   1 
ATOM   1213 C  CB  . ALA   B 1 17  ? 10.418 -15.105 15.886 1.00 19.25 ? 23  ALA   C CB  1 
ATOM   1214 N  N   . THR   B 1 18  ? 7.990  -15.759 13.757 1.00 20.66 ? 24  THR   C N   1 
ATOM   1215 C  CA  . THR   B 1 18  ? 6.872  -15.225 12.964 1.00 21.21 ? 24  THR   C CA  1 
ATOM   1216 C  C   . THR   B 1 18  ? 6.110  -14.109 13.723 1.00 22.14 ? 24  THR   C C   1 
ATOM   1217 O  O   . THR   B 1 18  ? 6.343  -13.886 14.909 1.00 21.56 ? 24  THR   C O   1 
ATOM   1218 C  CB  . THR   B 1 18  ? 5.928  -16.389 12.645 1.00 22.53 ? 24  THR   C CB  1 
ATOM   1219 O  OG1 . THR   B 1 18  ? 5.279  -16.821 13.857 1.00 24.05 ? 24  THR   C OG1 1 
ATOM   1220 C  CG2 . THR   B 1 18  ? 6.628  -17.541 11.966 1.00 22.63 ? 24  THR   C CG2 1 
ATOM   1221 N  N   . HIS   B 1 19  ? 5.102  -13.447 13.070 1.00 22.12 ? 25  HIS   C N   1 
ATOM   1222 C  CA  . HIS   B 1 19  ? 4.261  -12.490 13.786 1.00 22.59 ? 25  HIS   C CA  1 
ATOM   1223 C  C   . HIS   B 1 19  ? 3.553  -13.202 14.957 1.00 22.46 ? 25  HIS   C C   1 
ATOM   1224 O  O   . HIS   B 1 19  ? 3.407  -12.615 16.025 1.00 23.48 ? 25  HIS   C O   1 
ATOM   1225 C  CB  . HIS   B 1 19  ? 3.188  -11.921 12.838 1.00 26.36 ? 25  HIS   C CB  1 
ATOM   1226 C  CG  . HIS   B 1 19  ? 3.735  -11.111 11.700 1.00 34.16 ? 25  HIS   C CG  1 
ATOM   1227 N  ND1 . HIS   B 1 19  ? 4.359  -9.884  11.913 1.00 37.99 ? 25  HIS   C ND1 1 
ATOM   1228 C  CD2 . HIS   B 1 19  ? 3.663  -11.334 10.364 1.00 37.26 ? 25  HIS   C CD2 1 
ATOM   1229 C  CE1 . HIS   B 1 19  ? 4.659  -9.413  10.712 1.00 38.86 ? 25  HIS   C CE1 1 
ATOM   1230 N  NE2 . HIS   B 1 19  ? 4.274  -10.255 9.748  1.00 39.14 ? 25  HIS   C NE2 1 
ATOM   1231 N  N   . ASN   B 1 20  ? 3.148  -14.472 14.755 1.00 22.65 ? 26  ASN   C N   1 
ATOM   1232 C  CA  . ASN   B 1 20  ? 2.478  -15.205 15.834 1.00 22.92 ? 26  ASN   C CA  1 
ATOM   1233 C  C   . ASN   B 1 20  ? 3.401  -15.482 16.998 1.00 21.82 ? 26  ASN   C C   1 
ATOM   1234 O  O   . ASN   B 1 20  ? 2.983  -15.412 18.153 1.00 21.84 ? 26  ASN   C O   1 
ATOM   1235 C  CB  . ASN   B 1 20  ? 1.861  -16.500 15.342 1.00 26.61 ? 26  ASN   C CB  1 
ATOM   1236 C  CG  . ASN   B 1 20  ? 0.415  -16.457 15.694 1.00 36.69 ? 26  ASN   C CG  1 
ATOM   1237 O  OD1 . ASN   B 1 20  ? -0.269 -15.466 15.395 1.00 37.37 ? 26  ASN   C OD1 1 
ATOM   1238 N  ND2 . ASN   B 1 20  ? -0.057 -17.465 16.407 1.00 40.31 ? 26  ASN   C ND2 1 
ATOM   1239 N  N   . ASP   B 1 21  ? 4.678  -15.803 16.717 1.00 21.51 ? 27  ASP   C N   1 
ATOM   1240 C  CA  . ASP   B 1 21  ? 5.636  -15.993 17.813 1.00 21.31 ? 27  ASP   C CA  1 
ATOM   1241 C  C   . ASP   B 1 21  ? 5.765  -14.700 18.646 1.00 21.00 ? 27  ASP   C C   1 
ATOM   1242 O  O   . ASP   B 1 21  ? 5.710  -14.757 19.864 1.00 21.62 ? 27  ASP   C O   1 
ATOM   1243 C  CB  . ASP   B 1 21  ? 7.038  -16.334 17.252 1.00 19.49 ? 27  ASP   C CB  1 
ATOM   1244 C  CG  . ASP   B 1 21  ? 7.127  -17.765 16.737 1.00 21.06 ? 27  ASP   C CG  1 
ATOM   1245 O  OD1 . ASP   B 1 21  ? 6.587  -18.666 17.408 1.00 23.60 ? 27  ASP   C OD1 1 
ATOM   1246 O  OD2 . ASP   B 1 21  ? 7.749  -17.976 15.664 1.00 21.13 ? 27  ASP   C OD2 1 
ATOM   1247 N  N   . TRP   B 1 22  ? 5.866  -13.539 17.974 1.00 21.35 ? 28  TRP   C N   1 
ATOM   1248 C  CA  . TRP   B 1 22  ? 6.005  -12.269 18.690 1.00 21.74 ? 28  TRP   C CA  1 
ATOM   1249 C  C   . TRP   B 1 22  ? 4.724  -11.871 19.457 1.00 23.31 ? 28  TRP   C C   1 
ATOM   1250 O  O   . TRP   B 1 22  ? 4.810  -11.249 20.520 1.00 24.46 ? 28  TRP   C O   1 
ATOM   1251 C  CB  . TRP   B 1 22  ? 6.438  -11.156 17.710 1.00 20.77 ? 28  TRP   C CB  1 
ATOM   1252 C  CG  . TRP   B 1 22  ? 7.920  -11.124 17.473 1.00 20.06 ? 28  TRP   C CG  1 
ATOM   1253 C  CD1 . TRP   B 1 22  ? 8.586  -11.587 16.383 1.00 20.28 ? 28  TRP   C CD1 1 
ATOM   1254 C  CD2 . TRP   B 1 22  ? 8.906  -10.560 18.347 1.00 19.34 ? 28  TRP   C CD2 1 
ATOM   1255 N  NE1 . TRP   B 1 22  ? 9.942  -11.378 16.535 1.00 21.14 ? 28  TRP   C NE1 1 
ATOM   1256 C  CE2 . TRP   B 1 22  ? 10.160 -10.707 17.716 1.00 20.35 ? 28  TRP   C CE2 1 
ATOM   1257 C  CE3 . TRP   B 1 22  ? 8.849  -9.927  19.594 1.00 20.50 ? 28  TRP   C CE3 1 
ATOM   1258 C  CZ2 . TRP   B 1 22  ? 11.353 -10.297 18.321 1.00 20.39 ? 28  TRP   C CZ2 1 
ATOM   1259 C  CZ3 . TRP   B 1 22  ? 10.032 -9.514  20.186 1.00 20.58 ? 28  TRP   C CZ3 1 
ATOM   1260 C  CH2 . TRP   B 1 22  ? 11.258 -9.697  19.547 1.00 20.52 ? 28  TRP   C CH2 1 
ATOM   1261 N  N   . ALA   B 1 23  ? 3.559  -12.238 18.929 1.00 22.99 ? 29  ALA   C N   1 
ATOM   1262 C  CA  . ALA   B 1 23  ? 2.293  -11.933 19.609 1.00 24.04 ? 29  ALA   C CA  1 
ATOM   1263 C  C   . ALA   B 1 23  ? 2.079  -12.802 20.854 1.00 25.72 ? 29  ALA   C C   1 
ATOM   1264 O  O   . ALA   B 1 23  ? 1.215  -12.497 21.692 1.00 28.54 ? 29  ALA   C O   1 
ATOM   1265 C  CB  . ALA   B 1 23  ? 1.125  -12.132 18.646 1.00 23.49 ? 29  ALA   C CB  1 
ATOM   1266 N  N   . ASN   B 1 24  ? 2.758  -13.953 20.928 1.00 23.13 ? 30  ASN   C N   1 
ATOM   1267 C  CA  . ASN   B 1 24  ? 2.636  -14.876 22.049 1.00 22.19 ? 30  ASN   C CA  1 
ATOM   1268 C  C   . ASN   B 1 24  ? 4.029  -15.027 22.705 1.00 22.65 ? 30  ASN   C C   1 
ATOM   1269 O  O   . ASN   B 1 24  ? 4.395  -16.096 23.159 1.00 22.60 ? 30  ASN   C O   1 
ATOM   1270 C  CB  . ASN   B 1 24  ? 2.147  -16.228 21.544 1.00 22.65 ? 30  ASN   C CB  1 
ATOM   1271 C  CG  . ASN   B 1 24  ? 0.723  -16.139 21.060 1.00 27.05 ? 30  ASN   C CG  1 
ATOM   1272 O  OD1 . ASN   B 1 24  ? -0.228 -16.100 21.852 1.00 26.59 ? 30  ASN   C OD1 1 
ATOM   1273 N  ND2 . ASN   B 1 24  ? 0.565  -16.034 19.739 1.00 27.41 ? 30  ASN   C ND2 1 
ATOM   1274 N  N   . LEU   B 1 25  ? 4.758  -13.929 22.791 1.00 22.43 ? 31  LEU   C N   1 
ATOM   1275 C  CA  . LEU   B 1 25  ? 6.107  -13.926 23.322 1.00 22.62 ? 31  LEU   C CA  1 
ATOM   1276 C  C   . LEU   B 1 25  ? 6.196  -14.283 24.800 1.00 23.37 ? 31  LEU   C C   1 
ATOM   1277 O  O   . LEU   B 1 25  ? 5.470  -13.718 25.623 1.00 24.97 ? 31  LEU   C O   1 
ATOM   1278 C  CB  . LEU   B 1 25  ? 6.687  -12.541 23.064 1.00 22.59 ? 31  LEU   C CB  1 
ATOM   1279 C  CG  . LEU   B 1 25  ? 8.098  -12.314 23.592 1.00 22.16 ? 31  LEU   C CG  1 
ATOM   1280 C  CD1 . LEU   B 1 25  ? 9.110  -13.204 22.841 1.00 23.20 ? 31  LEU   C CD1 1 
ATOM   1281 C  CD2 . LEU   B 1 25  ? 8.481  -10.869 23.414 1.00 22.46 ? 31  LEU   C CD2 1 
ATOM   1282 N  N   . VAL   B 1 26  ? 7.132  -15.200 25.150 1.00 21.78 ? 32  VAL   C N   1 
ATOM   1283 C  CA  . VAL   B 1 26  ? 7.443  -15.555 26.530 1.00 22.34 ? 32  VAL   C CA  1 
ATOM   1284 C  C   . VAL   B 1 26  ? 8.795  -14.907 26.906 1.00 22.90 ? 32  VAL   C C   1 
ATOM   1285 O  O   . VAL   B 1 26  ? 8.948  -14.284 27.963 1.00 24.63 ? 32  VAL   C O   1 
ATOM   1286 C  CB  . VAL   B 1 26  ? 7.494  -17.091 26.700 1.00 23.60 ? 32  VAL   C CB  1 
ATOM   1287 C  CG1 . VAL   B 1 26  ? 8.031  -17.480 28.083 1.00 24.45 ? 32  VAL   C CG1 1 
ATOM   1288 C  CG2 . VAL   B 1 26  ? 6.111  -17.701 26.431 1.00 24.61 ? 32  VAL   C CG2 1 
ATOM   1289 N  N   . TRP   B 1 27  ? 9.787  -15.054 26.019 1.00 20.35 ? 33  TRP   C N   1 
ATOM   1290 C  CA  . TRP   B 1 27  ? 11.135 -14.570 26.281 1.00 20.18 ? 33  TRP   C CA  1 
ATOM   1291 C  C   . TRP   B 1 27  ? 11.905 -14.493 24.989 1.00 19.97 ? 33  TRP   C C   1 
ATOM   1292 O  O   . TRP   B 1 27  ? 11.712 -15.341 24.109 1.00 20.08 ? 33  TRP   C O   1 
ATOM   1293 C  CB  . TRP   B 1 27  ? 11.832 -15.537 27.277 1.00 21.03 ? 33  TRP   C CB  1 
ATOM   1294 C  CG  . TRP   B 1 27  ? 13.314 -15.328 27.481 1.00 21.35 ? 33  TRP   C CG  1 
ATOM   1295 C  CD1 . TRP   B 1 27  ? 13.924 -14.464 28.346 1.00 23.62 ? 33  TRP   C CD1 1 
ATOM   1296 C  CD2 . TRP   B 1 27  ? 14.371 -16.033 26.802 1.00 20.12 ? 33  TRP   C CD2 1 
ATOM   1297 N  NE1 . TRP   B 1 27  ? 15.306 -14.596 28.246 1.00 23.72 ? 33  TRP   C NE1 1 
ATOM   1298 C  CE2 . TRP   B 1 27  ? 15.598 -15.548 27.301 1.00 21.96 ? 33  TRP   C CE2 1 
ATOM   1299 C  CE3 . TRP   B 1 27  ? 14.393 -17.048 25.836 1.00 20.31 ? 33  TRP   C CE3 1 
ATOM   1300 C  CZ2 . TRP   B 1 27  ? 16.839 -16.071 26.882 1.00 21.35 ? 33  TRP   C CZ2 1 
ATOM   1301 C  CZ3 . TRP   B 1 27  ? 15.620 -17.550 25.419 1.00 21.23 ? 33  TRP   C CZ3 1 
ATOM   1302 C  CH2 . TRP   B 1 27  ? 16.822 -17.048 25.923 1.00 21.00 ? 33  TRP   C CH2 1 
ATOM   1303 N  N   . GLU   B 1 28  ? 12.771 -13.494 24.862 1.00 19.37 ? 34  GLU   C N   1 
ATOM   1304 C  CA  . GLU   B 1 28  ? 13.668 -13.432 23.703 1.00 19.24 ? 34  GLU   C CA  1 
ATOM   1305 C  C   . GLU   B 1 28  ? 14.992 -12.829 24.120 1.00 19.12 ? 34  GLU   C C   1 
ATOM   1306 O  O   . GLU   B 1 28  ? 15.030 -11.996 25.041 1.00 19.82 ? 34  GLU   C O   1 
ATOM   1307 C  CB  . GLU   B 1 28  ? 13.060 -12.667 22.513 1.00 20.05 ? 34  GLU   C CB  1 
ATOM   1308 C  CG  . GLU   B 1 28  ? 12.493 -11.278 22.830 1.00 20.99 ? 34  GLU   C CG  1 
ATOM   1309 C  CD  . GLU   B 1 28  ? 13.514 -10.143 22.900 1.00 23.26 ? 34  GLU   C CD  1 
ATOM   1310 O  OE1 . GLU   B 1 28  ? 13.271 -9.141  23.612 1.00 27.28 ? 34  GLU   C OE1 1 
ATOM   1311 O  OE2 . GLU   B 1 28  ? 14.562 -10.239 22.233 1.00 21.61 ? 34  GLU   C OE2 1 
ATOM   1312 N  N   . ASP   B 1 29  ? 16.071 -13.211 23.426 1.00 18.05 ? 35  ASP   C N   1 
ATOM   1313 C  CA  . ASP   B 1 29  ? 17.377 -12.636 23.739 1.00 17.96 ? 35  ASP   C CA  1 
ATOM   1314 C  C   . ASP   B 1 29  ? 18.126 -12.482 22.418 1.00 18.57 ? 35  ASP   C C   1 
ATOM   1315 O  O   . ASP   B 1 29  ? 18.542 -13.474 21.816 1.00 18.43 ? 35  ASP   C O   1 
ATOM   1316 C  CB  . ASP   B 1 29  ? 18.136 -13.552 24.726 1.00 18.54 ? 35  ASP   C CB  1 
ATOM   1317 C  CG  . ASP   B 1 29  ? 19.437 -12.964 25.217 1.00 25.25 ? 35  ASP   C CG  1 
ATOM   1318 O  OD1 . ASP   B 1 29  ? 20.040 -12.177 24.478 1.00 27.68 ? 35  ASP   C OD1 1 
ATOM   1319 O  OD2 . ASP   B 1 29  ? 19.891 -13.357 26.324 1.00 26.25 ? 35  ASP   C OD2 1 
ATOM   1320 N  N   . SER   B 1 30  ? 18.245 -11.209 21.949 1.00 18.12 ? 36  SER   C N   1 
ATOM   1321 C  CA  A SER   B 1 30  ? 18.913 -10.916 20.696 0.50 19.37 ? 36  SER   C CA  1 
ATOM   1322 C  CA  B SER   B 1 30  ? 18.923 -10.909 20.695 0.50 18.98 ? 36  SER   C CA  1 
ATOM   1323 C  C   . SER   B 1 30  ? 20.370 -11.383 20.711 1.00 20.18 ? 36  SER   C C   1 
ATOM   1324 O  O   . SER   B 1 30  ? 20.851 -11.879 19.690 1.00 21.87 ? 36  SER   C O   1 
ATOM   1325 C  CB  A SER   B 1 30  ? 18.804 -9.426  20.385 0.50 22.32 ? 36  SER   C CB  1 
ATOM   1326 C  CB  B SER   B 1 30  ? 18.858 -9.415  20.387 0.50 20.87 ? 36  SER   C CB  1 
ATOM   1327 O  OG  A SER   B 1 30  ? 19.543 -9.065  19.235 0.50 25.55 ? 36  SER   C OG  1 
ATOM   1328 O  OG  B SER   B 1 30  ? 19.520 -8.651  21.388 0.50 22.00 ? 36  SER   C OG  1 
ATOM   1329 N  N   . SER   B 1 31  ? 21.044 -11.281 21.877 1.00 18.26 ? 37  SER   C N   1 
ATOM   1330 C  CA  . SER   B 1 31  ? 22.440 -11.724 21.948 1.00 18.57 ? 37  SER   C CA  1 
ATOM   1331 C  C   . SER   B 1 31  ? 22.580 -13.229 21.789 1.00 20.02 ? 37  SER   C C   1 
ATOM   1332 O  O   . SER   B 1 31  ? 23.695 -13.675 21.515 1.00 21.83 ? 37  SER   C O   1 
ATOM   1333 C  CB  . SER   B 1 31  ? 23.103 -11.262 23.245 1.00 23.42 ? 37  SER   C CB  1 
ATOM   1334 O  OG  . SER   B 1 31  ? 22.778 -12.111 24.338 1.00 28.02 ? 37  SER   C OG  1 
ATOM   1335 N  N   . ARG   B 1 32  ? 21.508 -13.998 21.973 1.00 16.88 ? 38  ARG   C N   1 
ATOM   1336 C  CA  . ARG   B 1 32  ? 21.583 -15.473 21.804 1.00 16.84 ? 38  ARG   C CA  1 
ATOM   1337 C  C   . ARG   B 1 32  ? 20.905 -15.957 20.521 1.00 16.30 ? 38  ARG   C C   1 
ATOM   1338 O  O   . ARG   B 1 32  ? 20.968 -17.148 20.223 1.00 16.66 ? 38  ARG   C O   1 
ATOM   1339 C  CB  . ARG   B 1 32  ? 20.885 -16.196 22.990 1.00 16.46 ? 38  ARG   C CB  1 
ATOM   1340 C  CG  . ARG   B 1 32  ? 21.636 -15.953 24.304 1.00 17.32 ? 38  ARG   C CG  1 
ATOM   1341 C  CD  . ARG   B 1 32  ? 20.922 -16.577 25.509 1.00 18.29 ? 38  ARG   C CD  1 
ATOM   1342 N  NE  . ARG   B 1 32  ? 20.915 -18.038 25.424 1.00 16.70 ? 38  ARG   C NE  1 
ATOM   1343 C  CZ  . ARG   B 1 32  ? 20.851 -18.836 26.488 1.00 18.48 ? 38  ARG   C CZ  1 
ATOM   1344 N  NH1 . ARG   B 1 32  ? 20.769 -18.319 27.717 1.00 19.90 ? 38  ARG   C NH1 1 
ATOM   1345 N  NH2 . ARG   B 1 32  ? 20.912 -20.157 26.339 1.00 18.73 ? 38  ARG   C NH2 1 
ATOM   1346 N  N   . ASP   B 1 33  ? 20.233 -15.088 19.779 1.00 16.03 ? 39  ASP   C N   1 
ATOM   1347 C  CA  . ASP   B 1 33  ? 19.432 -15.490 18.618 1.00 15.46 ? 39  ASP   C CA  1 
ATOM   1348 C  C   . ASP   B 1 33  ? 18.350 -16.479 19.015 1.00 14.69 ? 39  ASP   C C   1 
ATOM   1349 O  O   . ASP   B 1 33  ? 17.997 -17.349 18.203 1.00 15.03 ? 39  ASP   C O   1 
ATOM   1350 C  CB  . ASP   B 1 33  ? 20.269 -16.057 17.437 1.00 15.68 ? 39  ASP   C CB  1 
ATOM   1351 C  CG  . ASP   B 1 33  ? 19.465 -16.338 16.165 1.00 16.48 ? 39  ASP   C CG  1 
ATOM   1352 O  OD1 . ASP   B 1 33  ? 18.542 -15.506 15.814 1.00 17.48 ? 39  ASP   C OD1 1 
ATOM   1353 O  OD2 . ASP   B 1 33  ? 19.726 -17.399 15.490 1.00 16.87 ? 39  ASP   C OD2 1 
ATOM   1354 N  N   . LEU   B 1 34  ? 17.745 -16.310 20.213 1.00 14.36 ? 40  LEU   C N   1 
ATOM   1355 C  CA  . LEU   B 1 34  ? 16.647 -17.194 20.612 1.00 14.72 ? 40  LEU   C CA  1 
ATOM   1356 C  C   . LEU   B 1 34  ? 15.372 -16.437 20.901 1.00 15.90 ? 40  LEU   C C   1 
ATOM   1357 O  O   . LEU   B 1 34  ? 15.410 -15.356 21.479 1.00 16.19 ? 40  LEU   C O   1 
ATOM   1358 C  CB  . LEU   B 1 34  ? 16.993 -17.979 21.893 1.00 15.28 ? 40  LEU   C CB  1 
ATOM   1359 C  CG  . LEU   B 1 34  ? 18.071 -19.057 21.763 1.00 15.90 ? 40  LEU   C CG  1 
ATOM   1360 C  CD1 . LEU   B 1 34  ? 18.239 -19.748 23.145 1.00 16.83 ? 40  LEU   C CD1 1 
ATOM   1361 C  CD2 . LEU   B 1 34  ? 17.648 -20.114 20.705 1.00 15.98 ? 40  LEU   C CD2 1 
ATOM   1362 N  N   . LEU   B 1 35  ? 14.244 -17.086 20.618 1.00 14.80 ? 41  LEU   C N   1 
ATOM   1363 C  CA  . LEU   B 1 35  ? 12.945 -16.565 20.996 1.00 15.95 ? 41  LEU   C CA  1 
ATOM   1364 C  C   . LEU   B 1 35  ? 12.068 -17.745 21.415 1.00 15.80 ? 41  LEU   C C   1 
ATOM   1365 O  O   . LEU   B 1 35  ? 12.122 -18.807 20.782 1.00 17.08 ? 41  LEU   C O   1 
ATOM   1366 C  CB  . LEU   B 1 35  ? 12.302 -15.785 19.843 1.00 16.95 ? 41  LEU   C CB  1 
ATOM   1367 C  CG  . LEU   B 1 35  ? 10.927 -15.129 20.177 1.00 17.97 ? 41  LEU   C CG  1 
ATOM   1368 C  CD1 . LEU   B 1 35  ? 10.747 -13.813 19.368 1.00 18.28 ? 41  LEU   C CD1 1 
ATOM   1369 C  CD2 . LEU   B 1 35  ? 9.754  -16.067 19.807 1.00 19.82 ? 41  LEU   C CD2 1 
ATOM   1370 N  N   . VAL   B 1 36  ? 11.295 -17.589 22.494 1.00 15.70 ? 42  VAL   C N   1 
ATOM   1371 C  CA  . VAL   B 1 36  ? 10.380 -18.619 22.987 1.00 16.94 ? 42  VAL   C CA  1 
ATOM   1372 C  C   . VAL   B 1 36  ? 8.976  -18.033 22.990 1.00 18.07 ? 42  VAL   C C   1 
ATOM   1373 O  O   . VAL   B 1 36  ? 8.763  -16.925 23.506 1.00 18.20 ? 42  VAL   C O   1 
ATOM   1374 C  CB  . VAL   B 1 36  ? 10.779 -19.105 24.409 1.00 17.46 ? 42  VAL   C CB  1 
ATOM   1375 C  CG1 . VAL   B 1 36  ? 9.749  -20.116 24.936 1.00 18.70 ? 42  VAL   C CG1 1 
ATOM   1376 C  CG2 . VAL   B 1 36  ? 12.191 -19.723 24.391 1.00 17.96 ? 42  VAL   C CG2 1 
ATOM   1377 N  N   . SER   B 1 37  ? 8.049  -18.755 22.392 1.00 17.98 ? 43  SER   C N   1 
ATOM   1378 C  CA  . SER   B 1 37  ? 6.645  -18.337 22.366 1.00 19.73 ? 43  SER   C CA  1 
ATOM   1379 C  C   . SER   B 1 37  ? 5.766  -19.406 23.037 1.00 21.43 ? 43  SER   C C   1 
ATOM   1380 O  O   . SER   B 1 37  ? 6.184  -20.560 23.226 1.00 21.42 ? 43  SER   C O   1 
ATOM   1381 C  CB  . SER   B 1 37  ? 6.191  -18.040 20.945 1.00 19.72 ? 43  SER   C CB  1 
ATOM   1382 O  OG  . SER   B 1 37  ? 6.266  -19.173 20.087 1.00 22.08 ? 43  SER   C OG  1 
ATOM   1383 N  N   . SER   B 1 38  ? 4.540  -19.008 23.410 1.00 22.78 ? 44  SER   C N   1 
ATOM   1384 C  CA  . SER   B 1 38  ? 3.645  -19.969 24.062 1.00 25.68 ? 44  SER   C CA  1 
ATOM   1385 C  C   . SER   B 1 38  ? 2.789  -20.725 23.024 1.00 27.82 ? 44  SER   C C   1 
ATOM   1386 O  O   . SER   B 1 38  ? 2.434  -20.179 21.973 1.00 28.40 ? 44  SER   C O   1 
ATOM   1387 C  CB  . SER   B 1 38  ? 2.758  -19.253 25.066 1.00 27.60 ? 44  SER   C CB  1 
ATOM   1388 O  OG  . SER   B 1 38  ? 2.012  -18.266 24.382 1.00 31.53 ? 44  SER   C OG  1 
ATOM   1389 N  N   . THR   B 1 39  ? 2.465  -21.981 23.336 1.00 29.32 ? 45  THR   C N   1 
ATOM   1390 C  CA  . THR   B 1 39  ? 1.636  -22.836 22.477 1.00 32.09 ? 45  THR   C CA  1 
ATOM   1391 C  C   . THR   B 1 39  ? 0.419  -23.337 23.264 1.00 35.26 ? 45  THR   C C   1 
ATOM   1392 O  O   . THR   B 1 39  ? 0.416  -23.325 24.498 1.00 35.54 ? 45  THR   C O   1 
ATOM   1393 C  CB  . THR   B 1 39  ? 2.451  -24.065 21.978 1.00 33.09 ? 45  THR   C CB  1 
ATOM   1394 O  OG1 . THR   B 1 39  ? 2.654  -24.969 23.067 1.00 34.75 ? 45  THR   C OG1 1 
ATOM   1395 C  CG2 . THR   B 1 39  ? 3.784  -23.684 21.383 1.00 32.79 ? 45  THR   C CG2 1 
ATOM   1396 N  N   . THR   B 1 40  ? -0.588 -23.831 22.552 1.00 37.80 ? 46  THR   C N   1 
ATOM   1397 C  CA  . THR   B 1 40  ? -1.770 -24.412 23.185 1.00 40.47 ? 46  THR   C CA  1 
ATOM   1398 C  C   . THR   B 1 40  ? -1.606 -25.930 23.342 1.00 42.56 ? 46  THR   C C   1 
ATOM   1399 O  O   . THR   B 1 40  ? -2.109 -26.509 24.305 1.00 44.14 ? 46  THR   C O   1 
ATOM   1400 C  CB  . THR   B 1 40  ? -3.011 -24.061 22.356 1.00 42.69 ? 46  THR   C CB  1 
ATOM   1401 O  OG1 . THR   B 1 40  ? -2.775 -24.446 20.998 1.00 45.05 ? 46  THR   C OG1 1 
ATOM   1402 C  CG2 . THR   B 1 40  ? -3.326 -22.574 22.402 1.00 42.83 ? 46  THR   C CG2 1 
ATOM   1403 N  N   . ALA   B 1 41  ? -0.918 -26.580 22.391 1.00 42.64 ? 47  ALA   C N   1 
ATOM   1404 C  CA  . ALA   B 1 41  ? -0.701 -28.022 22.421 1.00 43.21 ? 47  ALA   C CA  1 
ATOM   1405 C  C   . ALA   B 1 41  ? 0.581  -28.358 23.198 1.00 43.22 ? 47  ALA   C C   1 
ATOM   1406 O  O   . ALA   B 1 41  ? 1.545  -27.601 23.146 1.00 43.46 ? 47  ALA   C O   1 
ATOM   1407 C  CB  . ALA   B 1 41  ? -0.593 -28.554 20.996 1.00 43.61 ? 47  ALA   C CB  1 
ATOM   1408 N  N   . GLN   B 1 42  ? 0.594  -29.493 23.896 1.00 42.89 ? 48  GLN   C N   1 
ATOM   1409 C  CA  . GLN   B 1 42  ? 1.740  -29.926 24.685 1.00 42.81 ? 48  GLN   C CA  1 
ATOM   1410 C  C   . GLN   B 1 42  ? 2.831  -30.457 23.764 1.00 40.90 ? 48  GLN   C C   1 
ATOM   1411 O  O   . GLN   B 1 42  ? 2.553  -31.278 22.892 1.00 42.15 ? 48  GLN   C O   1 
ATOM   1412 C  CB  . GLN   B 1 42  ? 1.314  -31.006 25.699 1.00 46.44 ? 48  GLN   C CB  1 
ATOM   1413 C  CG  . GLN   B 1 42  ? 2.437  -31.469 26.631 1.00 52.48 ? 48  GLN   C CG  1 
ATOM   1414 C  CD  . GLN   B 1 42  ? 2.573  -30.627 27.882 1.00 60.11 ? 48  GLN   C CD  1 
ATOM   1415 O  OE1 . GLN   B 1 42  ? 1.785  -29.706 28.141 1.00 62.52 ? 48  GLN   C OE1 1 
ATOM   1416 N  NE2 . GLN   B 1 42  ? 3.584  -30.928 28.696 1.00 61.48 ? 48  GLN   C NE2 1 
ATOM   1417 N  N   . GLY   B 1 43  ? 4.049  -29.959 23.945 1.00 37.30 ? 49  GLY   C N   1 
ATOM   1418 C  CA  . GLY   B 1 43  ? 5.219  -30.385 23.183 1.00 35.70 ? 49  GLY   C CA  1 
ATOM   1419 C  C   . GLY   B 1 43  ? 5.907  -31.512 23.912 1.00 34.09 ? 49  GLY   C C   1 
ATOM   1420 O  O   . GLY   B 1 43  ? 5.902  -31.531 25.152 1.00 34.44 ? 49  GLY   C O   1 
ATOM   1421 N  N   . CYS   B 1 44  ? 6.495  -32.455 23.170 1.00 32.52 ? 50  CYS   C N   1 
ATOM   1422 C  CA  . CYS   B 1 44  ? 7.078  -33.616 23.810 1.00 32.64 ? 50  CYS   C CA  1 
ATOM   1423 C  C   . CYS   B 1 44  ? 8.592  -33.719 23.703 1.00 30.26 ? 50  CYS   C C   1 
ATOM   1424 O  O   . CYS   B 1 44  ? 9.116  -34.773 24.062 1.00 31.16 ? 50  CYS   C O   1 
ATOM   1425 C  CB  . CYS   B 1 44  ? 6.404  -34.893 23.321 1.00 36.29 ? 50  CYS   C CB  1 
ATOM   1426 S  SG  . CYS   B 1 44  ? 4.631  -34.964 23.682 1.00 47.24 ? 50  CYS   C SG  1 
ATOM   1427 N  N   . ASP   B 1 45  ? 9.295  -32.676 23.220 1.00 26.08 ? 51  ASP   C N   1 
ATOM   1428 C  CA  . ASP   B 1 45  ? 10.774 -32.771 23.155 1.00 24.44 ? 51  ASP   C CA  1 
ATOM   1429 C  C   . ASP   B 1 45  ? 11.357 -32.705 24.575 1.00 24.66 ? 51  ASP   C C   1 
ATOM   1430 O  O   . ASP   B 1 45  ? 10.820 -32.002 25.437 1.00 26.18 ? 51  ASP   C O   1 
ATOM   1431 C  CB  . ASP   B 1 45  ? 11.390 -31.605 22.339 1.00 26.18 ? 51  ASP   C CB  1 
ATOM   1432 C  CG  . ASP   B 1 45  ? 11.066 -31.645 20.854 1.00 32.08 ? 51  ASP   C CG  1 
ATOM   1433 O  OD1 . ASP   B 1 45  ? 10.656 -32.716 20.367 1.00 34.82 ? 51  ASP   C OD1 1 
ATOM   1434 O  OD2 . ASP   B 1 45  ? 11.180 -30.584 20.183 1.00 31.27 ? 51  ASP   C OD2 1 
ATOM   1435 N  N   . THR   B 1 46  ? 12.401 -33.463 24.825 1.00 22.80 ? 52  THR   C N   1 
ATOM   1436 C  CA  . THR   B 1 46  ? 13.092 -33.429 26.117 1.00 23.41 ? 52  THR   C CA  1 
ATOM   1437 C  C   . THR   B 1 46  ? 14.351 -32.609 25.927 1.00 22.06 ? 52  THR   C C   1 
ATOM   1438 O  O   . THR   B 1 46  ? 15.104 -32.903 25.005 1.00 22.39 ? 52  THR   C O   1 
ATOM   1439 C  CB  . THR   B 1 46  ? 13.500 -34.842 26.541 1.00 27.28 ? 52  THR   C CB  1 
ATOM   1440 O  OG1 . THR   B 1 46  ? 12.301 -35.593 26.805 1.00 31.01 ? 52  THR   C OG1 1 
ATOM   1441 C  CG2 . THR   B 1 46  ? 14.387 -34.847 27.781 1.00 27.79 ? 52  THR   C CG2 1 
ATOM   1442 N  N   . ILE   B 1 47  ? 14.572 -31.622 26.805 1.00 21.02 ? 53  ILE   C N   1 
ATOM   1443 C  CA  . ILE   B 1 47  ? 15.771 -30.807 26.771 1.00 19.66 ? 53  ILE   C CA  1 
ATOM   1444 C  C   . ILE   B 1 47  ? 16.875 -31.494 27.569 1.00 18.71 ? 53  ILE   C C   1 
ATOM   1445 O  O   . ILE   B 1 47  ? 16.652 -31.971 28.705 1.00 19.75 ? 53  ILE   C O   1 
ATOM   1446 C  CB  . ILE   B 1 47  ? 15.528 -29.411 27.372 1.00 20.37 ? 53  ILE   C CB  1 
ATOM   1447 C  CG1 . ILE   B 1 47  ? 14.298 -28.711 26.764 1.00 22.35 ? 53  ILE   C CG1 1 
ATOM   1448 C  CG2 . ILE   B 1 47  ? 16.765 -28.540 27.254 1.00 20.66 ? 53  ILE   C CG2 1 
ATOM   1449 C  CD1 . ILE   B 1 47  ? 14.435 -28.505 25.229 1.00 24.35 ? 53  ILE   C CD1 1 
ATOM   1450 N  N   . ALA   B 1 48  ? 18.063 -31.598 26.967 1.00 17.69 ? 54  ALA   C N   1 
ATOM   1451 C  CA  . ALA   B 1 48  ? 19.203 -32.182 27.684 1.00 16.17 ? 54  ALA   C CA  1 
ATOM   1452 C  C   . ALA   B 1 48  ? 19.641 -31.264 28.837 1.00 16.72 ? 54  ALA   C C   1 
ATOM   1453 O  O   . ALA   B 1 48  ? 19.619 -30.047 28.692 1.00 16.63 ? 54  ALA   C O   1 
ATOM   1454 C  CB  . ALA   B 1 48  ? 20.370 -32.295 26.701 1.00 16.22 ? 54  ALA   C CB  1 
ATOM   1455 N  N   . ARG   B 1 49  ? 20.053 -31.872 29.981 1.00 16.10 ? 55  ARG   C N   1 
ATOM   1456 C  CA  . ARG   B 1 49  ? 20.543 -31.099 31.140 1.00 16.32 ? 55  ARG   C CA  1 
ATOM   1457 C  C   . ARG   B 1 49  ? 21.891 -31.753 31.423 1.00 17.07 ? 55  ARG   C C   1 
ATOM   1458 O  O   . ARG   B 1 49  ? 21.972 -32.722 32.178 1.00 19.39 ? 55  ARG   C O   1 
ATOM   1459 C  CB  . ARG   B 1 49  ? 19.568 -31.203 32.332 1.00 17.05 ? 55  ARG   C CB  1 
ATOM   1460 C  CG  . ARG   B 1 49  ? 18.185 -30.664 31.978 1.00 18.03 ? 55  ARG   C CG  1 
ATOM   1461 C  CD  . ARG   B 1 49  ? 18.141 -29.179 31.600 1.00 20.41 ? 55  ARG   C CD  1 
ATOM   1462 N  NE  . ARG   B 1 49  ? 16.752 -28.762 31.342 1.00 21.63 ? 55  ARG   C NE  1 
ATOM   1463 C  CZ  . ARG   B 1 49  ? 16.414 -27.653 30.691 1.00 22.56 ? 55  ARG   C CZ  1 
ATOM   1464 N  NH1 . ARG   B 1 49  ? 17.345 -26.815 30.270 1.00 20.40 ? 55  ARG   C NH1 1 
ATOM   1465 N  NH2 . ARG   B 1 49  ? 15.132 -27.356 30.492 1.00 24.62 ? 55  ARG   C NH2 1 
ATOM   1466 N  N   . CYS   B 1 50  ? 22.963 -31.213 30.804 1.00 16.59 ? 56  CYS   C N   1 
ATOM   1467 C  CA  . CYS   B 1 50  ? 24.250 -31.884 30.808 1.00 16.66 ? 56  CYS   C CA  1 
ATOM   1468 C  C   . CYS   B 1 50  ? 25.368 -30.949 30.313 1.00 18.00 ? 56  CYS   C C   1 
ATOM   1469 O  O   . CYS   B 1 50  ? 25.097 -29.861 29.841 1.00 17.02 ? 56  CYS   C O   1 
ATOM   1470 C  CB  . CYS   B 1 50  ? 24.145 -33.098 29.882 1.00 18.10 ? 56  CYS   C CB  1 
ATOM   1471 S  SG  . CYS   B 1 50  ? 23.978 -32.631 28.113 1.00 17.07 ? 56  CYS   C SG  1 
ATOM   1472 N  N   . ASP   B 1 51  ? 26.625 -31.502 30.264 1.00 17.95 ? 57  ASP   C N   1 
ATOM   1473 C  CA  . ASP   B 1 51  ? 27.778 -30.813 29.705 1.00 18.63 ? 57  ASP   C CA  1 
ATOM   1474 C  C   . ASP   B 1 51  ? 28.368 -31.583 28.531 1.00 19.17 ? 57  ASP   C C   1 
ATOM   1475 O  O   . ASP   B 1 51  ? 29.562 -31.454 28.263 1.00 19.60 ? 57  ASP   C O   1 
ATOM   1476 C  CB  . ASP   B 1 51  ? 28.865 -30.548 30.771 1.00 20.39 ? 57  ASP   C CB  1 
ATOM   1477 C  CG  . ASP   B 1 51  ? 29.472 -31.784 31.373 1.00 25.77 ? 57  ASP   C CG  1 
ATOM   1478 O  OD1 . ASP   B 1 51  ? 29.057 -32.912 31.002 1.00 26.91 ? 57  ASP   C OD1 1 
ATOM   1479 O  OD2 . ASP   B 1 51  ? 30.420 -31.641 32.189 1.00 31.82 ? 57  ASP   C OD2 1 
ATOM   1480 N  N   . CYS   B 1 52  ? 27.547 -32.352 27.782 1.00 16.93 ? 58  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 52  ? 28.038 -33.084 26.610 1.00 15.43 ? 58  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 52  ? 28.701 -32.141 25.640 1.00 15.34 ? 58  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 52  ? 28.251 -30.975 25.449 1.00 15.89 ? 58  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 52  ? 26.891 -33.808 25.896 1.00 16.19 ? 58  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 52  ? 26.330 -35.308 26.732 1.00 18.68 ? 58  CYS   C SG  1 
ATOM   1486 N  N   . GLN   B 1 53  ? 29.721 -32.670 24.957 1.00 14.98 ? 59  GLN   C N   1 
ATOM   1487 C  CA  . GLN   B 1 53  ? 30.373 -31.973 23.854 1.00 15.39 ? 59  GLN   C CA  1 
ATOM   1488 C  C   . GLN   B 1 53  ? 30.385 -32.832 22.608 1.00 14.98 ? 59  GLN   C C   1 
ATOM   1489 O  O   . GLN   B 1 53  ? 31.168 -32.561 21.686 1.00 16.00 ? 59  GLN   C O   1 
ATOM   1490 C  CB  . GLN   B 1 53  ? 31.807 -31.532 24.194 1.00 16.35 ? 59  GLN   C CB  1 
ATOM   1491 C  CG  . GLN   B 1 53  ? 31.829 -30.274 25.104 1.00 17.70 ? 59  GLN   C CG  1 
ATOM   1492 C  CD  . GLN   B 1 53  ? 33.254 -29.867 25.386 1.00 21.23 ? 59  GLN   C CD  1 
ATOM   1493 O  OE1 . GLN   B 1 53  ? 33.766 -30.038 26.515 1.00 25.03 ? 59  GLN   C OE1 1 
ATOM   1494 N  NE2 . GLN   B 1 53  ? 33.929 -29.382 24.337 1.00 20.06 ? 59  GLN   C NE2 1 
ATOM   1495 N  N   . THR   B 1 54  ? 29.538 -33.896 22.548 1.00 15.49 ? 60  THR   C N   1 
ATOM   1496 C  CA  . THR   B 1 54  ? 29.373 -34.689 21.330 1.00 15.79 ? 60  THR   C CA  1 
ATOM   1497 C  C   . THR   B 1 54  ? 27.879 -34.922 21.157 1.00 15.27 ? 60  THR   C C   1 
ATOM   1498 O  O   . THR   B 1 54  ? 27.108 -34.989 22.142 1.00 16.88 ? 60  THR   C O   1 
ATOM   1499 C  CB  . THR   B 1 54  ? 30.099 -36.027 21.355 1.00 20.36 ? 60  THR   C CB  1 
ATOM   1500 O  OG1 . THR   B 1 54  ? 29.558 -36.853 22.395 1.00 23.65 ? 60  THR   C OG1 1 
ATOM   1501 C  CG2 . THR   B 1 54  ? 31.597 -35.878 21.550 1.00 20.76 ? 60  THR   C CG2 1 
ATOM   1502 N  N   . GLY   B 1 55  ? 27.462 -34.945 19.885 1.00 14.53 ? 61  GLY   C N   1 
ATOM   1503 C  CA  . GLY   B 1 55  ? 26.043 -35.134 19.590 1.00 14.07 ? 61  GLY   C CA  1 
ATOM   1504 C  C   . GLY   B 1 55  ? 25.813 -35.260 18.096 1.00 13.59 ? 61  GLY   C C   1 
ATOM   1505 O  O   . GLY   B 1 55  ? 26.768 -35.496 17.364 1.00 15.23 ? 61  GLY   C O   1 
ATOM   1506 N  N   . VAL   B 1 56  ? 24.558 -35.132 17.666 1.00 13.52 ? 62  VAL   C N   1 
ATOM   1507 C  CA  . VAL   B 1 56  ? 24.207 -35.298 16.239 1.00 13.82 ? 62  VAL   C CA  1 
ATOM   1508 C  C   . VAL   B 1 56  ? 23.312 -34.131 15.880 1.00 13.60 ? 62  VAL   C C   1 
ATOM   1509 O  O   . VAL   B 1 56  ? 22.356 -33.857 16.603 1.00 13.95 ? 62  VAL   C O   1 
ATOM   1510 C  CB  . VAL   B 1 56  ? 23.460 -36.644 16.023 1.00 15.05 ? 62  VAL   C CB  1 
ATOM   1511 C  CG1 . VAL   B 1 56  ? 22.962 -36.799 14.563 1.00 17.14 ? 62  VAL   C CG1 1 
ATOM   1512 C  CG2 . VAL   B 1 56  ? 24.362 -37.813 16.386 1.00 15.76 ? 62  VAL   C CG2 1 
ATOM   1513 N  N   . TYR   B 1 57  ? 23.562 -33.492 14.705 1.00 13.94 ? 63  TYR   C N   1 
ATOM   1514 C  CA  . TYR   B 1 57  ? 22.651 -32.418 14.259 1.00 13.68 ? 63  TYR   C CA  1 
ATOM   1515 C  C   . TYR   B 1 57  ? 22.039 -32.695 12.897 1.00 14.87 ? 63  TYR   C C   1 
ATOM   1516 O  O   . TYR   B 1 57  ? 22.617 -33.443 12.114 1.00 15.28 ? 63  TYR   C O   1 
ATOM   1517 C  CB  . TYR   B 1 57  ? 23.325 -30.997 14.273 1.00 13.43 ? 63  TYR   C CB  1 
ATOM   1518 C  CG  . TYR   B 1 57  ? 24.246 -30.714 13.101 1.00 14.39 ? 63  TYR   C CG  1 
ATOM   1519 C  CD1 . TYR   B 1 57  ? 25.515 -31.284 13.032 1.00 16.67 ? 63  TYR   C CD1 1 
ATOM   1520 C  CD2 . TYR   B 1 57  ? 23.856 -29.861 12.074 1.00 14.98 ? 63  TYR   C CD2 1 
ATOM   1521 C  CE1 . TYR   B 1 57  ? 26.404 -30.959 12.002 1.00 18.08 ? 63  TYR   C CE1 1 
ATOM   1522 C  CE2 . TYR   B 1 57  ? 24.728 -29.559 11.013 1.00 16.93 ? 63  TYR   C CE2 1 
ATOM   1523 C  CZ  . TYR   B 1 57  ? 25.994 -30.124 10.978 1.00 18.39 ? 63  TYR   C CZ  1 
ATOM   1524 O  OH  . TYR   B 1 57  ? 26.876 -29.835 9.933  1.00 20.87 ? 63  TYR   C OH  1 
ATOM   1525 N  N   . TYR   B 1 58  ? 20.876 -32.111 12.641 1.00 15.35 ? 64  TYR   C N   1 
ATOM   1526 C  CA  . TYR   B 1 58  ? 20.221 -32.251 11.345 1.00 14.97 ? 64  TYR   C CA  1 
ATOM   1527 C  C   . TYR   B 1 58  ? 20.648 -31.119 10.432 1.00 16.21 ? 64  TYR   C C   1 
ATOM   1528 O  O   . TYR   B 1 58  ? 20.531 -29.967 10.813 1.00 16.00 ? 64  TYR   C O   1 
ATOM   1529 C  CB  . TYR   B 1 58  ? 18.686 -32.277 11.475 1.00 15.85 ? 64  TYR   C CB  1 
ATOM   1530 C  CG  . TYR   B 1 58  ? 18.054 -32.463 10.114 1.00 18.06 ? 64  TYR   C CG  1 
ATOM   1531 C  CD1 . TYR   B 1 58  ? 18.215 -33.652 9.408  1.00 19.51 ? 64  TYR   C CD1 1 
ATOM   1532 C  CD2 . TYR   B 1 58  ? 17.309 -31.452 9.530  1.00 20.59 ? 64  TYR   C CD2 1 
ATOM   1533 C  CE1 . TYR   B 1 58  ? 17.675 -33.819 8.125  1.00 22.07 ? 64  TYR   C CE1 1 
ATOM   1534 C  CE2 . TYR   B 1 58  ? 16.772 -31.603 8.250  1.00 21.31 ? 64  TYR   C CE2 1 
ATOM   1535 C  CZ  . TYR   B 1 58  ? 16.957 -32.786 7.555  1.00 22.56 ? 64  TYR   C CZ  1 
ATOM   1536 O  OH  . TYR   B 1 58  ? 16.420 -32.954 6.279  1.00 24.91 ? 64  TYR   C OH  1 
ATOM   1537 N  N   . CYS   B 1 59  ? 21.162 -31.467 9.233  1.00 16.27 ? 65  CYS   C N   1 
ATOM   1538 C  CA  . CYS   B 1 59  ? 21.617 -30.479 8.244  1.00 16.47 ? 65  CYS   C CA  1 
ATOM   1539 C  C   . CYS   B 1 59  ? 20.656 -30.543 7.024  1.00 17.87 ? 65  CYS   C C   1 
ATOM   1540 O  O   . CYS   B 1 59  ? 20.759 -31.446 6.175  1.00 18.89 ? 65  CYS   C O   1 
ATOM   1541 C  CB  . CYS   B 1 59  ? 23.051 -30.803 7.849  1.00 16.92 ? 65  CYS   C CB  1 
ATOM   1542 S  SG  . CYS   B 1 59  ? 23.682 -29.754 6.510  1.00 20.21 ? 65  CYS   C SG  1 
ATOM   1543 N  N   . SER   B 1 60  ? 19.714 -29.578 6.955  1.00 18.02 ? 66  SER   C N   1 
ATOM   1544 C  CA  . SER   B 1 60  ? 18.718 -29.591 5.887  1.00 20.68 ? 66  SER   C CA  1 
ATOM   1545 C  C   . SER   B 1 60  ? 19.318 -29.463 4.502  1.00 21.09 ? 66  SER   C C   1 
ATOM   1546 O  O   . SER   B 1 60  ? 18.826 -30.118 3.566  1.00 21.60 ? 66  SER   C O   1 
ATOM   1547 C  CB  . SER   B 1 60  ? 17.643 -28.536 6.128  1.00 25.83 ? 66  SER   C CB  1 
ATOM   1548 O  OG  . SER   B 1 60  ? 18.180 -27.241 5.989  1.00 31.27 ? 66  SER   C OG  1 
ATOM   1549 N  N   . SER   B 1 61  ? 20.438 -28.727 4.373  1.00 20.07 ? 67  SER   C N   1 
ATOM   1550 C  CA  . SER   B 1 61  ? 21.097 -28.575 3.053  1.00 21.49 ? 67  SER   C CA  1 
ATOM   1551 C  C   . SER   B 1 61  ? 21.803 -29.824 2.546  1.00 22.07 ? 67  SER   C C   1 
ATOM   1552 O  O   . SER   B 1 61  ? 22.257 -29.847 1.382  1.00 23.45 ? 67  SER   C O   1 
ATOM   1553 C  CB  . SER   B 1 61  ? 22.047 -27.387 3.055  1.00 22.43 ? 67  SER   C CB  1 
ATOM   1554 O  OG  . SER   B 1 61  ? 23.161 -27.608 3.897  1.00 22.90 ? 67  SER   C OG  1 
ATOM   1555 N  N   . ARG   B 1 62  ? 21.845 -30.892 3.363  1.00 20.42 ? 68  ARG   C N   1 
ATOM   1556 C  CA  . ARG   B 1 62  ? 22.345 -32.171 2.930  1.00 20.14 ? 68  ARG   C CA  1 
ATOM   1557 C  C   . ARG   B 1 62  ? 21.292 -33.297 3.151  1.00 21.90 ? 68  ARG   C C   1 
ATOM   1558 O  O   . ARG   B 1 62  ? 21.576 -34.460 2.841  1.00 23.77 ? 68  ARG   C O   1 
ATOM   1559 C  CB  . ARG   B 1 62  ? 23.647 -32.510 3.672  1.00 20.85 ? 68  ARG   C CB  1 
ATOM   1560 C  CG  . ARG   B 1 62  ? 24.791 -31.556 3.364  1.00 22.81 ? 68  ARG   C CG  1 
ATOM   1561 C  CD  . ARG   B 1 62  ? 25.370 -31.884 1.979  1.00 23.70 ? 68  ARG   C CD  1 
ATOM   1562 N  NE  . ARG   B 1 62  ? 26.495 -31.014 1.653  1.00 27.27 ? 68  ARG   C NE  1 
ATOM   1563 C  CZ  . ARG   B 1 62  ? 26.389 -29.839 1.048  1.00 31.07 ? 68  ARG   C CZ  1 
ATOM   1564 N  NH1 . ARG   B 1 62  ? 25.195 -29.377 0.672  1.00 30.78 ? 68  ARG   C NH1 1 
ATOM   1565 N  NH2 . ARG   B 1 62  ? 27.474 -29.126 0.785  1.00 31.10 ? 68  ARG   C NH2 1 
ATOM   1566 N  N   . ARG   B 1 63  ? 20.088 -32.965 3.708  1.00 21.89 ? 69  ARG   C N   1 
ATOM   1567 C  CA  . ARG   B 1 63  ? 19.047 -33.945 4.085  1.00 23.51 ? 69  ARG   C CA  1 
ATOM   1568 C  C   . ARG   B 1 63  ? 19.654 -35.080 4.895  1.00 24.74 ? 69  ARG   C C   1 
ATOM   1569 O  O   . ARG   B 1 63  ? 19.401 -36.263 4.642  1.00 26.57 ? 69  ARG   C O   1 
ATOM   1570 C  CB  . ARG   B 1 63  ? 18.302 -34.492 2.846  1.00 25.36 ? 69  ARG   C CB  1 
ATOM   1571 C  CG  . ARG   B 1 63  ? 17.347 -33.471 2.256  1.00 30.12 ? 69  ARG   C CG  1 
ATOM   1572 C  CD  . ARG   B 1 63  ? 16.509 -34.141 1.202  1.00 37.30 ? 69  ARG   C CD  1 
ATOM   1573 N  NE  . ARG   B 1 63  ? 15.978 -33.184 0.232  1.00 43.45 ? 69  ARG   C NE  1 
ATOM   1574 C  CZ  . ARG   B 1 63  ? 16.156 -33.273 -1.083 1.00 48.08 ? 69  ARG   C CZ  1 
ATOM   1575 N  NH1 . ARG   B 1 63  ? 16.880 -34.263 -1.597 1.00 48.43 ? 69  ARG   C NH1 1 
ATOM   1576 N  NH2 . ARG   B 1 63  ? 15.631 -32.358 -1.897 1.00 48.16 ? 69  ARG   C NH2 1 
ATOM   1577 N  N   . LYS   B 1 64  ? 20.553 -34.709 5.849  1.00 23.11 ? 70  LYS   C N   1 
ATOM   1578 C  CA  . LYS   B 1 64  ? 21.280 -35.729 6.593  1.00 22.31 ? 70  LYS   C CA  1 
ATOM   1579 C  C   . LYS   B 1 64  ? 21.566 -35.268 7.995  1.00 19.73 ? 70  LYS   C C   1 
ATOM   1580 O  O   . LYS   B 1 64  ? 21.708 -34.069 8.238  1.00 19.34 ? 70  LYS   C O   1 
ATOM   1581 C  CB  . LYS   B 1 64  ? 22.697 -35.924 5.947  1.00 26.77 ? 70  LYS   C CB  1 
ATOM   1582 C  CG  . LYS   B 1 64  ? 22.803 -36.949 4.839  1.00 37.94 ? 70  LYS   C CG  1 
ATOM   1583 C  CD  . LYS   B 1 64  ? 24.258 -36.991 4.352  1.00 46.96 ? 70  LYS   C CD  1 
ATOM   1584 C  CE  . LYS   B 1 64  ? 24.571 -38.209 3.501  1.00 53.40 ? 70  LYS   C CE  1 
ATOM   1585 N  NZ  . LYS   B 1 64  ? 24.684 -37.867 2.056  1.00 56.49 ? 70  LYS   C NZ  1 
ATOM   1586 N  N   . HIS   B 1 65  ? 21.806 -36.225 8.867  1.00 18.67 ? 71  HIS   C N   1 
ATOM   1587 C  CA  . HIS   B 1 65  ? 22.280 -35.921 10.218 1.00 17.65 ? 71  HIS   C CA  1 
ATOM   1588 C  C   . HIS   B 1 65  ? 23.782 -36.206 10.270 1.00 18.68 ? 71  HIS   C C   1 
ATOM   1589 O  O   . HIS   B 1 65  ? 24.276 -37.192 9.670  1.00 21.77 ? 71  HIS   C O   1 
ATOM   1590 C  CB  . HIS   B 1 65  ? 21.593 -36.836 11.226 1.00 16.67 ? 71  HIS   C CB  1 
ATOM   1591 C  CG  . HIS   B 1 65  ? 20.110 -36.666 11.301 1.00 18.62 ? 71  HIS   C CG  1 
ATOM   1592 N  ND1 . HIS   B 1 65  ? 19.495 -35.898 12.294 1.00 20.13 ? 71  HIS   C ND1 1 
ATOM   1593 C  CD2 . HIS   B 1 65  ? 19.148 -37.241 10.538 1.00 19.77 ? 71  HIS   C CD2 1 
ATOM   1594 C  CE1 . HIS   B 1 65  ? 18.185 -36.031 12.084 1.00 19.11 ? 71  HIS   C CE1 1 
ATOM   1595 N  NE2 . HIS   B 1 65  ? 17.935 -36.811 11.045 1.00 22.49 ? 71  HIS   C NE2 1 
ATOM   1596 N  N   . TYR   B 1 66  ? 24.514 -35.391 11.033 1.00 16.30 ? 72  TYR   C N   1 
ATOM   1597 C  CA  . TYR   B 1 66  ? 25.952 -35.590 11.174 1.00 16.20 ? 72  TYR   C CA  1 
ATOM   1598 C  C   . TYR   B 1 66  ? 26.355 -35.633 12.660 1.00 15.87 ? 72  TYR   C C   1 
ATOM   1599 O  O   . TYR   B 1 66  ? 25.924 -34.787 13.449 1.00 15.25 ? 72  TYR   C O   1 
ATOM   1600 C  CB  . TYR   B 1 66  ? 26.701 -34.374 10.580 1.00 17.98 ? 72  TYR   C CB  1 
ATOM   1601 C  CG  . TYR   B 1 66  ? 26.662 -34.273 9.074  1.00 19.85 ? 72  TYR   C CG  1 
ATOM   1602 C  CD1 . TYR   B 1 66  ? 27.394 -35.151 8.277  1.00 20.86 ? 72  TYR   C CD1 1 
ATOM   1603 C  CD2 . TYR   B 1 66  ? 25.939 -33.265 8.439  1.00 20.74 ? 72  TYR   C CD2 1 
ATOM   1604 C  CE1 . TYR   B 1 66  ? 27.366 -35.053 6.887  1.00 22.84 ? 72  TYR   C CE1 1 
ATOM   1605 C  CE2 . TYR   B 1 66  ? 25.899 -33.169 7.053  1.00 22.54 ? 72  TYR   C CE2 1 
ATOM   1606 C  CZ  . TYR   B 1 66  ? 26.625 -34.055 6.286  1.00 24.71 ? 72  TYR   C CZ  1 
ATOM   1607 O  OH  . TYR   B 1 66  ? 26.599 -33.946 4.905  1.00 28.18 ? 72  TYR   C OH  1 
ATOM   1608 N  N   . PRO   B 1 67  ? 27.213 -36.607 13.034 1.00 15.52 ? 73  PRO   C N   1 
ATOM   1609 C  CA  . PRO   B 1 67  ? 27.734 -36.655 14.399 1.00 16.05 ? 73  PRO   C CA  1 
ATOM   1610 C  C   . PRO   B 1 67  ? 28.872 -35.613 14.498 1.00 17.73 ? 73  PRO   C C   1 
ATOM   1611 O  O   . PRO   B 1 67  ? 29.699 -35.520 13.553 1.00 19.39 ? 73  PRO   C O   1 
ATOM   1612 C  CB  . PRO   B 1 67  ? 28.259 -38.097 14.525 1.00 17.01 ? 73  PRO   C CB  1 
ATOM   1613 C  CG  . PRO   B 1 67  ? 28.626 -38.478 13.132 1.00 16.98 ? 73  PRO   C CG  1 
ATOM   1614 C  CD  . PRO   B 1 67  ? 27.739 -37.704 12.183 1.00 15.27 ? 73  PRO   C CD  1 
ATOM   1615 N  N   . VAL   B 1 68  ? 28.877 -34.799 15.576 1.00 16.03 ? 74  VAL   C N   1 
ATOM   1616 C  CA  . VAL   B 1 68  ? 29.942 -33.784 15.738 1.00 17.04 ? 74  VAL   C CA  1 
ATOM   1617 C  C   . VAL   B 1 68  ? 30.390 -33.690 17.173 1.00 16.27 ? 74  VAL   C C   1 
ATOM   1618 O  O   . VAL   B 1 68  ? 29.626 -33.977 18.103 1.00 17.33 ? 74  VAL   C O   1 
ATOM   1619 C  CB  . VAL   B 1 68  ? 29.446 -32.386 15.311 1.00 19.68 ? 74  VAL   C CB  1 
ATOM   1620 C  CG1 . VAL   B 1 68  ? 29.325 -32.275 13.783 1.00 22.51 ? 74  VAL   C CG1 1 
ATOM   1621 C  CG2 . VAL   B 1 68  ? 28.136 -32.018 16.024 1.00 19.27 ? 74  VAL   C CG2 1 
ATOM   1622 N  N   . SER   B 1 69  ? 31.641 -33.208 17.363 1.00 15.35 ? 75  SER   C N   1 
ATOM   1623 C  CA  . SER   B 1 69  ? 32.101 -32.715 18.640 1.00 15.79 ? 75  SER   C CA  1 
ATOM   1624 C  C   . SER   B 1 69  ? 31.848 -31.172 18.566 1.00 15.33 ? 75  SER   C C   1 
ATOM   1625 O  O   . SER   B 1 69  ? 31.939 -30.529 17.481 1.00 17.41 ? 75  SER   C O   1 
ATOM   1626 C  CB  . SER   B 1 69  ? 33.613 -32.956 18.802 1.00 19.12 ? 75  SER   C CB  1 
ATOM   1627 O  OG  . SER   B 1 69  ? 33.920 -34.343 18.825 1.00 25.52 ? 75  SER   C OG  1 
ATOM   1628 N  N   . PHE   B 1 70  ? 31.494 -30.542 19.699 1.00 15.19 ? 76  PHE   C N   1 
ATOM   1629 C  CA  . PHE   B 1 70  ? 31.204 -29.089 19.693 1.00 15.04 ? 76  PHE   C CA  1 
ATOM   1630 C  C   . PHE   B 1 70  ? 31.768 -28.428 20.966 1.00 15.91 ? 76  PHE   C C   1 
ATOM   1631 O  O   . PHE   B 1 70  ? 32.024 -29.109 21.973 1.00 16.89 ? 76  PHE   C O   1 
ATOM   1632 C  CB  . PHE   B 1 70  ? 29.682 -28.806 19.527 1.00 14.50 ? 76  PHE   C CB  1 
ATOM   1633 C  CG  . PHE   B 1 70  ? 28.796 -29.568 20.490 1.00 13.99 ? 76  PHE   C CG  1 
ATOM   1634 C  CD1 . PHE   B 1 70  ? 28.260 -30.793 20.142 1.00 14.14 ? 76  PHE   C CD1 1 
ATOM   1635 C  CD2 . PHE   B 1 70  ? 28.357 -28.975 21.668 1.00 14.81 ? 76  PHE   C CD2 1 
ATOM   1636 C  CE1 . PHE   B 1 70  ? 27.418 -31.497 21.025 1.00 14.18 ? 76  PHE   C CE1 1 
ATOM   1637 C  CE2 . PHE   B 1 70  ? 27.520 -29.666 22.549 1.00 14.93 ? 76  PHE   C CE2 1 
ATOM   1638 C  CZ  . PHE   B 1 70  ? 27.027 -30.917 22.212 1.00 14.73 ? 76  PHE   C CZ  1 
ATOM   1639 N  N   . SER   B 1 71  ? 32.007 -27.123 20.901 1.00 14.97 ? 77  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 71  ? 32.637 -26.440 22.014 1.00 16.95 ? 77  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 71  ? 31.685 -26.151 23.177 1.00 17.17 ? 77  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 71  ? 30.486 -26.446 23.116 1.00 17.85 ? 77  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 71  ? 33.284 -25.157 21.505 1.00 17.09 ? 77  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 71  ? 32.329 -24.233 21.019 1.00 19.06 ? 77  SER   C OG  1 
ATOM   1645 N  N   . LYS   B 1 72  ? 32.215 -25.578 24.249 1.00 17.72 ? 78  LYS   C N   1 
ATOM   1646 C  CA  . LYS   B 1 72  ? 31.380 -25.156 25.363 1.00 18.72 ? 78  LYS   C CA  1 
ATOM   1647 C  C   . LYS   B 1 72  ? 30.691 -23.840 24.983 1.00 18.20 ? 78  LYS   C C   1 
ATOM   1648 O  O   . LYS   B 1 72  ? 31.263 -23.029 24.243 1.00 20.92 ? 78  LYS   C O   1 
ATOM   1649 C  CB  . LYS   B 1 72  ? 32.303 -24.951 26.582 1.00 21.46 ? 78  LYS   C CB  1 
ATOM   1650 C  CG  . LYS   B 1 72  ? 32.926 -26.293 26.996 1.00 24.66 ? 78  LYS   C CG  1 
ATOM   1651 C  CD  . LYS   B 1 72  ? 33.538 -26.230 28.383 1.00 35.32 ? 78  LYS   C CD  1 
ATOM   1652 C  CE  . LYS   B 1 72  ? 33.435 -27.581 29.084 1.00 43.40 ? 78  LYS   C CE  1 
ATOM   1653 N  NZ  . LYS   B 1 72  ? 32.049 -27.823 29.614 1.00 47.75 ? 78  LYS   C NZ  1 
ATOM   1654 N  N   . PRO   B 1 73  ? 29.497 -23.559 25.511 1.00 17.62 ? 79  PRO   C N   1 
ATOM   1655 C  CA  . PRO   B 1 73  ? 28.797 -22.311 25.145 1.00 17.89 ? 79  PRO   C CA  1 
ATOM   1656 C  C   . PRO   B 1 73  ? 29.630 -21.086 25.509 1.00 19.79 ? 79  PRO   C C   1 
ATOM   1657 O  O   . PRO   B 1 73  ? 30.169 -20.991 26.636 1.00 21.07 ? 79  PRO   C O   1 
ATOM   1658 C  CB  . PRO   B 1 73  ? 27.513 -22.330 25.996 1.00 19.54 ? 79  PRO   C CB  1 
ATOM   1659 C  CG  . PRO   B 1 73  ? 27.295 -23.747 26.370 1.00 20.55 ? 79  PRO   C CG  1 
ATOM   1660 C  CD  . PRO   B 1 73  ? 28.687 -24.415 26.408 1.00 17.17 ? 79  PRO   C CD  1 
ATOM   1661 N  N   . SER   B 1 74  ? 29.777 -20.164 24.541 1.00 19.84 ? 80  SER   C N   1 
ATOM   1662 C  CA  . SER   B 1 74  ? 30.634 -19.010 24.784 1.00 21.94 ? 80  SER   C CA  1 
ATOM   1663 C  C   . SER   B 1 74  ? 30.261 -17.813 23.922 1.00 21.69 ? 80  SER   C C   1 
ATOM   1664 O  O   . SER   B 1 74  ? 29.298 -17.877 23.149 1.00 20.64 ? 80  SER   C O   1 
ATOM   1665 C  CB  . SER   B 1 74  ? 32.089 -19.414 24.572 1.00 26.64 ? 80  SER   C CB  1 
ATOM   1666 O  OG  . SER   B 1 74  ? 32.339 -19.623 23.190 1.00 31.92 ? 80  SER   C OG  1 
ATOM   1667 N  N   . LEU   B 1 75  ? 30.962 -16.665 24.151 1.00 21.80 ? 81  LEU   C N   1 
ATOM   1668 C  CA  . LEU   B 1 75  ? 30.714 -15.428 23.426 1.00 22.96 ? 81  LEU   C CA  1 
ATOM   1669 C  C   . LEU   B 1 75  ? 31.628 -15.448 22.201 1.00 24.62 ? 81  LEU   C C   1 
ATOM   1670 O  O   . LEU   B 1 75  ? 32.880 -15.431 22.351 1.00 26.47 ? 81  LEU   C O   1 
ATOM   1671 C  CB  . LEU   B 1 75  ? 31.165 -14.257 24.318 1.00 25.31 ? 81  LEU   C CB  1 
ATOM   1672 C  CG  . LEU   B 1 75  ? 30.186 -13.509 25.110 1.00 30.73 ? 81  LEU   C CG  1 
ATOM   1673 C  CD1 . LEU   B 1 75  ? 30.914 -12.526 26.007 1.00 33.70 ? 81  LEU   C CD1 1 
ATOM   1674 C  CD2 . LEU   B 1 75  ? 29.147 -12.805 24.242 1.00 31.48 ? 81  LEU   C CD2 1 
ATOM   1675 N  N   . ILE   B 1 76  ? 31.032 -15.437 21.000 1.00 23.08 ? 82  ILE   C N   1 
ATOM   1676 C  CA  . ILE   B 1 76  ? 31.720 -15.543 19.720 1.00 23.86 ? 82  ILE   C CA  1 
ATOM   1677 C  C   . ILE   B 1 76  ? 31.322 -14.419 18.784 1.00 24.56 ? 82  ILE   C C   1 
ATOM   1678 O  O   . ILE   B 1 76  ? 30.132 -14.113 18.676 1.00 22.75 ? 82  ILE   C O   1 
ATOM   1679 C  CB  . ILE   B 1 76  ? 31.378 -16.926 19.113 1.00 26.19 ? 82  ILE   C CB  1 
ATOM   1680 C  CG1 . ILE   B 1 76  ? 31.929 -18.040 20.031 1.00 29.20 ? 82  ILE   C CG1 1 
ATOM   1681 C  CG2 . ILE   B 1 76  ? 31.824 -17.047 17.653 1.00 27.38 ? 82  ILE   C CG2 1 
ATOM   1682 C  CD1 . ILE   B 1 76  ? 31.579 -19.389 19.670 1.00 32.19 ? 82  ILE   C CD1 1 
ATOM   1683 N  N   . PHE   B 1 77  ? 32.295 -13.799 18.110 1.00 24.93 ? 83  PHE   C N   1 
ATOM   1684 C  CA  . PHE   B 1 77  ? 31.982 -12.700 17.199 1.00 26.73 ? 83  PHE   C CA  1 
ATOM   1685 C  C   . PHE   B 1 77  ? 31.255 -13.218 15.980 1.00 28.36 ? 83  PHE   C C   1 
ATOM   1686 O  O   . PHE   B 1 77  ? 31.699 -14.178 15.349 1.00 29.54 ? 83  PHE   C O   1 
ATOM   1687 C  CB  . PHE   B 1 77  ? 33.280 -11.971 16.769 1.00 27.05 ? 83  PHE   C CB  1 
ATOM   1688 C  CG  . PHE   B 1 77  ? 33.003 -10.790 15.878 1.00 28.34 ? 83  PHE   C CG  1 
ATOM   1689 C  CD1 . PHE   B 1 77  ? 32.416 -9.642  16.386 1.00 30.48 ? 83  PHE   C CD1 1 
ATOM   1690 C  CD2 . PHE   B 1 77  ? 33.228 -10.863 14.516 1.00 29.96 ? 83  PHE   C CD2 1 
ATOM   1691 C  CE1 . PHE   B 1 77  ? 32.140 -8.556  15.554 1.00 32.53 ? 83  PHE   C CE1 1 
ATOM   1692 C  CE2 . PHE   B 1 77  ? 32.961 -9.766  13.686 1.00 31.85 ? 83  PHE   C CE2 1 
ATOM   1693 C  CZ  . PHE   B 1 77  ? 32.423 -8.625  14.212 1.00 32.71 ? 83  PHE   C CZ  1 
ATOM   1694 N  N   . VAL   B 1 78  ? 30.147 -12.551 15.631 1.00 29.44 ? 84  VAL   C N   1 
ATOM   1695 C  CA  . VAL   B 1 78  ? 29.353 -12.899 14.463 1.00 30.31 ? 84  VAL   C CA  1 
ATOM   1696 C  C   . VAL   B 1 78  ? 29.200 -11.618 13.628 1.00 31.19 ? 84  VAL   C C   1 
ATOM   1697 O  O   . VAL   B 1 78  ? 28.791 -10.569 14.135 1.00 32.02 ? 84  VAL   C O   1 
ATOM   1698 C  CB  . VAL   B 1 78  ? 27.968 -13.475 14.879 1.00 29.56 ? 84  VAL   C CB  1 
ATOM   1699 C  CG1 . VAL   B 1 78  ? 27.104 -13.734 13.644 1.00 30.44 ? 84  VAL   C CG1 1 
ATOM   1700 C  CG2 . VAL   B 1 78  ? 28.131 -14.764 15.691 1.00 28.60 ? 84  VAL   C CG2 1 
ATOM   1701 N  N   . GLU   B 1 79  ? 29.564 -11.701 12.362 1.00 31.84 ? 85  GLU   C N   1 
ATOM   1702 C  CA  . GLU   B 1 79  ? 29.532 -10.566 11.438 1.00 33.48 ? 85  GLU   C CA  1 
ATOM   1703 C  C   . GLU   B 1 79  ? 28.104 -10.076 11.192 1.00 33.19 ? 85  GLU   C C   1 
ATOM   1704 O  O   . GLU   B 1 79  ? 27.144 -10.834 11.405 1.00 32.71 ? 85  GLU   C O   1 
ATOM   1705 C  CB  . GLU   B 1 79  ? 30.188 -10.941 10.098 1.00 38.15 ? 85  GLU   C CB  1 
ATOM   1706 C  CG  . GLU   B 1 79  ? 31.409 -11.837 10.222 1.00 46.04 ? 85  GLU   C CG  1 
ATOM   1707 C  CD  . GLU   B 1 79  ? 31.122 -13.326 10.137 1.00 54.64 ? 85  GLU   C CD  1 
ATOM   1708 O  OE1 . GLU   B 1 79  ? 30.544 -13.904 11.089 1.00 55.66 ? 85  GLU   C OE1 1 
ATOM   1709 O  OE2 . GLU   B 1 79  ? 31.489 -13.922 9.099  1.00 57.03 ? 85  GLU   C OE2 1 
ATOM   1710 N  N   . ALA   B 1 80  ? 27.959 -8.812  10.756 1.00 33.23 ? 86  ALA   C N   1 
ATOM   1711 C  CA  . ALA   B 1 80  ? 26.641 -8.234  10.487 1.00 33.20 ? 86  ALA   C CA  1 
ATOM   1712 C  C   . ALA   B 1 80  ? 25.887 -9.041  9.434  1.00 33.84 ? 86  ALA   C C   1 
ATOM   1713 O  O   . ALA   B 1 80  ? 26.486 -9.652  8.543  1.00 34.70 ? 86  ALA   C O   1 
ATOM   1714 C  CB  . ALA   B 1 80  ? 26.780 -6.781  10.021 1.00 33.68 ? 86  ALA   C CB  1 
ATOM   1715 N  N   . SER   B 1 81  ? 24.568 -9.062  9.560  1.00 32.00 ? 87  SER   C N   1 
ATOM   1716 C  CA  . SER   B 1 81  ? 23.699 -9.713  8.600  1.00 30.69 ? 87  SER   C CA  1 
ATOM   1717 C  C   . SER   B 1 81  ? 22.468 -8.761  8.433  1.00 31.42 ? 87  SER   C C   1 
ATOM   1718 O  O   . SER   B 1 81  ? 22.421 -7.683  9.060  1.00 31.91 ? 87  SER   C O   1 
ATOM   1719 C  CB  . SER   B 1 81  ? 23.272 -11.092 9.111  1.00 30.41 ? 87  SER   C CB  1 
ATOM   1720 O  OG  . SER   B 1 81  ? 22.400 -10.959 10.222 1.00 29.42 ? 87  SER   C OG  1 
ATOM   1721 N  N   . GLU   B 1 82  ? 21.507 -9.117  7.576  1.00 30.46 ? 88  GLU   C N   1 
ATOM   1722 C  CA  . GLU   B 1 82  ? 20.270 -8.327  7.468  1.00 30.40 ? 88  GLU   C CA  1 
ATOM   1723 C  C   . GLU   B 1 82  ? 19.495 -8.376  8.815  1.00 29.97 ? 88  GLU   C C   1 
ATOM   1724 O  O   . GLU   B 1 82  ? 18.669 -7.503  9.104  1.00 29.96 ? 88  GLU   C O   1 
ATOM   1725 C  CB  . GLU   B 1 82  ? 19.332 -8.976  6.430  1.00 35.14 ? 88  GLU   C CB  1 
ATOM   1726 C  CG  . GLU   B 1 82  ? 19.714 -8.784  4.974  1.00 43.24 ? 88  GLU   C CG  1 
ATOM   1727 C  CD  . GLU   B 1 82  ? 18.723 -9.491  4.064  1.00 54.03 ? 88  GLU   C CD  1 
ATOM   1728 O  OE1 . GLU   B 1 82  ? 18.353 -10.645 4.379  1.00 56.37 ? 88  GLU   C OE1 1 
ATOM   1729 O  OE2 . GLU   B 1 82  ? 18.286 -8.883  3.061  1.00 57.47 ? 88  GLU   C OE2 1 
ATOM   1730 N  N   . TYR   B 1 83  ? 19.733 -9.421  9.615  1.00 29.20 ? 89  TYR   C N   1 
ATOM   1731 C  CA  . TYR   B 1 83  ? 19.014 -9.659  10.844 1.00 30.29 ? 89  TYR   C CA  1 
ATOM   1732 C  C   . TYR   B 1 83  ? 19.639 -9.004  12.080 1.00 29.98 ? 89  TYR   C C   1 
ATOM   1733 O  O   . TYR   B 1 83  ? 18.917 -8.702  13.039 1.00 30.66 ? 89  TYR   C O   1 
ATOM   1734 C  CB  . TYR   B 1 83  ? 18.898 -11.170 11.079 1.00 30.83 ? 89  TYR   C CB  1 
ATOM   1735 C  CG  . TYR   B 1 83  ? 18.340 -11.964 9.916  1.00 32.64 ? 89  TYR   C CG  1 
ATOM   1736 C  CD1 . TYR   B 1 83  ? 16.975 -11.978 9.644  1.00 33.95 ? 89  TYR   C CD1 1 
ATOM   1737 C  CD2 . TYR   B 1 83  ? 19.173 -12.698 9.091  1.00 33.82 ? 89  TYR   C CD2 1 
ATOM   1738 C  CE1 . TYR   B 1 83  ? 16.454 -12.740 8.601  1.00 35.35 ? 89  TYR   C CE1 1 
ATOM   1739 C  CE2 . TYR   B 1 83  ? 18.663 -13.485 8.066  1.00 35.32 ? 89  TYR   C CE2 1 
ATOM   1740 C  CZ  . TYR   B 1 83  ? 17.302 -13.492 7.812  1.00 36.99 ? 89  TYR   C CZ  1 
ATOM   1741 O  OH  . TYR   B 1 83  ? 16.786 -14.268 6.792  1.00 40.69 ? 89  TYR   C OH  1 
ATOM   1742 N  N   . TYR   B 1 84  ? 20.971 -8.862  12.104 1.00 28.14 ? 90  TYR   C N   1 
ATOM   1743 C  CA  . TYR   B 1 84  ? 21.636 -8.318  13.285 1.00 28.32 ? 90  TYR   C CA  1 
ATOM   1744 C  C   . TYR   B 1 84  ? 22.800 -7.421  12.933 1.00 30.18 ? 90  TYR   C C   1 
ATOM   1745 O  O   . TYR   B 1 84  ? 23.523 -7.677  11.965 1.00 30.41 ? 90  TYR   C O   1 
ATOM   1746 C  CB  . TYR   B 1 84  ? 22.255 -9.483  14.118 1.00 26.76 ? 90  TYR   C CB  1 
ATOM   1747 C  CG  . TYR   B 1 84  ? 21.265 -10.418 14.743 1.00 25.49 ? 90  TYR   C CG  1 
ATOM   1748 C  CD1 . TYR   B 1 84  ? 21.064 -11.685 14.230 1.00 25.49 ? 90  TYR   C CD1 1 
ATOM   1749 C  CD2 . TYR   B 1 84  ? 20.537 -10.043 15.866 1.00 25.04 ? 90  TYR   C CD2 1 
ATOM   1750 C  CE1 . TYR   B 1 84  ? 20.175 -12.567 14.809 1.00 24.84 ? 90  TYR   C CE1 1 
ATOM   1751 C  CE2 . TYR   B 1 84  ? 19.639 -10.906 16.448 1.00 24.17 ? 90  TYR   C CE2 1 
ATOM   1752 C  CZ  . TYR   B 1 84  ? 19.491 -12.183 15.935 1.00 24.58 ? 90  TYR   C CZ  1 
ATOM   1753 O  OH  . TYR   B 1 84  ? 18.542 -12.979 16.468 1.00 23.06 ? 90  TYR   C OH  1 
ATOM   1754 N  N   . PRO   B 1 85  ? 23.115 -6.459  13.818 1.00 30.06 ? 91  PRO   C N   1 
ATOM   1755 C  CA  . PRO   B 1 85  ? 24.365 -5.731  13.651 1.00 30.33 ? 91  PRO   C CA  1 
ATOM   1756 C  C   . PRO   B 1 85  ? 25.534 -6.687  13.948 1.00 30.96 ? 91  PRO   C C   1 
ATOM   1757 O  O   . PRO   B 1 85  ? 25.350 -7.725  14.576 1.00 31.10 ? 91  PRO   C O   1 
ATOM   1758 C  CB  . PRO   B 1 85  ? 24.295 -4.657  14.753 1.00 30.61 ? 91  PRO   C CB  1 
ATOM   1759 C  CG  . PRO   B 1 85  ? 23.442 -5.282  15.811 1.00 30.95 ? 91  PRO   C CG  1 
ATOM   1760 C  CD  . PRO   B 1 85  ? 22.404 -6.062  15.056 1.00 29.32 ? 91  PRO   C CD  1 
ATOM   1761 N  N   . ALA   B 1 86  ? 26.767 -6.293  13.607 1.00 30.99 ? 92  ALA   C N   1 
ATOM   1762 C  CA  . ALA   B 1 86  ? 27.980 -7.039  13.985 1.00 31.17 ? 92  ALA   C CA  1 
ATOM   1763 C  C   . ALA   B 1 86  ? 28.019 -7.061  15.535 1.00 30.74 ? 92  ALA   C C   1 
ATOM   1764 O  O   . ALA   B 1 86  ? 27.716 -6.027  16.152 1.00 30.73 ? 92  ALA   C O   1 
ATOM   1765 C  CB  . ALA   B 1 86  ? 29.206 -6.300  13.455 1.00 31.70 ? 92  ALA   C CB  1 
ATOM   1766 N  N   . ARG   B 1 87  ? 28.193 -8.249  16.150 1.00 30.17 ? 93  ARG   C N   1 
ATOM   1767 C  CA  . ARG   B 1 87  ? 28.090 -8.333  17.604 1.00 29.67 ? 93  ARG   C CA  1 
ATOM   1768 C  C   . ARG   B 1 87  ? 28.675 -9.646  18.128 1.00 29.88 ? 93  ARG   C C   1 
ATOM   1769 O  O   . ARG   B 1 87  ? 28.984 -10.553 17.353 1.00 30.12 ? 93  ARG   C O   1 
ATOM   1770 C  CB  . ARG   B 1 87  ? 26.588 -8.239  18.013 1.00 29.28 ? 93  ARG   C CB  1 
ATOM   1771 C  CG  . ARG   B 1 87  ? 25.845 -9.573  17.697 1.00 26.74 ? 93  ARG   C CG  1 
ATOM   1772 C  CD  . ARG   B 1 87  ? 24.378 -9.437  17.422 1.00 25.73 ? 93  ARG   C CD  1 
ATOM   1773 N  NE  . ARG   B 1 87  ? 23.592 -10.591 17.852 1.00 25.45 ? 93  ARG   C NE  1 
ATOM   1774 C  CZ  . ARG   B 1 87  ? 23.571 -11.775 17.248 1.00 28.33 ? 93  ARG   C CZ  1 
ATOM   1775 N  NH1 . ARG   B 1 87  ? 22.782 -12.738 17.699 1.00 25.89 ? 93  ARG   C NH1 1 
ATOM   1776 N  NH2 . ARG   B 1 87  ? 24.358 -12.011 16.202 1.00 28.48 ? 93  ARG   C NH2 1 
ATOM   1777 N  N   . TYR   B 1 88  ? 28.761 -9.766  19.459 1.00 29.51 ? 94  TYR   C N   1 
ATOM   1778 C  CA  . TYR   B 1 88  ? 29.156 -11.015 20.059 1.00 29.36 ? 94  TYR   C CA  1 
ATOM   1779 C  C   . TYR   B 1 88  ? 27.874 -11.764 20.378 1.00 26.27 ? 94  TYR   C C   1 
ATOM   1780 O  O   . TYR   B 1 88  ? 26.981 -11.213 21.046 1.00 27.03 ? 94  TYR   C O   1 
ATOM   1781 C  CB  . TYR   B 1 88  ? 29.950 -10.773 21.331 1.00 31.35 ? 94  TYR   C CB  1 
ATOM   1782 C  CG  . TYR   B 1 88  ? 31.356 -10.352 21.011 1.00 34.73 ? 94  TYR   C CG  1 
ATOM   1783 C  CD1 . TYR   B 1 88  ? 32.313 -11.286 20.649 1.00 36.95 ? 94  TYR   C CD1 1 
ATOM   1784 C  CD2 . TYR   B 1 88  ? 31.715 -9.015  21.005 1.00 37.12 ? 94  TYR   C CD2 1 
ATOM   1785 C  CE1 . TYR   B 1 88  ? 33.606 -10.903 20.322 1.00 38.61 ? 94  TYR   C CE1 1 
ATOM   1786 C  CE2 . TYR   B 1 88  ? 33.017 -8.620  20.702 1.00 38.93 ? 94  TYR   C CE2 1 
ATOM   1787 C  CZ  . TYR   B 1 88  ? 33.946 -9.569  20.328 1.00 40.18 ? 94  TYR   C CZ  1 
ATOM   1788 O  OH  . TYR   B 1 88  ? 35.235 -9.218  20.000 1.00 43.21 ? 94  TYR   C OH  1 
ATOM   1789 N  N   . GLN   B 1 89  ? 27.727 -12.976 19.818 1.00 22.31 ? 95  GLN   C N   1 
ATOM   1790 C  CA  . GLN   B 1 89  ? 26.577 -13.822 20.150 1.00 20.12 ? 95  GLN   C CA  1 
ATOM   1791 C  C   . GLN   B 1 89  ? 27.012 -14.656 21.352 1.00 18.98 ? 95  GLN   C C   1 
ATOM   1792 O  O   . GLN   B 1 89  ? 28.093 -15.256 21.355 1.00 20.73 ? 95  GLN   C O   1 
ATOM   1793 C  CB  . GLN   B 1 89  ? 26.149 -14.679 18.951 1.00 19.59 ? 95  GLN   C CB  1 
ATOM   1794 C  CG  . GLN   B 1 89  ? 25.004 -15.651 19.312 1.00 20.02 ? 95  GLN   C CG  1 
ATOM   1795 C  CD  . GLN   B 1 89  ? 24.245 -16.139 18.095 1.00 20.61 ? 95  GLN   C CD  1 
ATOM   1796 O  OE1 . GLN   B 1 89  ? 24.056 -15.410 17.103 1.00 22.10 ? 95  GLN   C OE1 1 
ATOM   1797 N  NE2 . GLN   B 1 89  ? 23.788 -17.393 18.162 1.00 19.58 ? 95  GLN   C NE2 1 
ATOM   1798 N  N   . SER   B 1 90  ? 26.171 -14.705 22.375 1.00 18.03 ? 96  SER   C N   1 
ATOM   1799 C  CA  . SER   B 1 90  ? 26.473 -15.452 23.586 1.00 18.10 ? 96  SER   C CA  1 
ATOM   1800 C  C   . SER   B 1 90  ? 25.830 -16.863 23.525 1.00 17.85 ? 96  SER   C C   1 
ATOM   1801 O  O   . SER   B 1 90  ? 24.915 -17.128 22.714 1.00 18.02 ? 96  SER   C O   1 
ATOM   1802 C  CB  . SER   B 1 90  ? 25.984 -14.690 24.825 1.00 20.17 ? 96  SER   C CB  1 
ATOM   1803 O  OG  . SER   B 1 90  ? 24.573 -14.542 24.795 1.00 22.07 ? 96  SER   C OG  1 
ATOM   1804 N  N   . HIS   B 1 91  ? 26.312 -17.751 24.436 1.00 17.29 ? 97  HIS   C N   1 
ATOM   1805 C  CA  . HIS   B 1 91  ? 25.801 -19.121 24.597 1.00 17.07 ? 97  HIS   C CA  1 
ATOM   1806 C  C   . HIS   B 1 91  ? 25.878 -19.879 23.269 1.00 17.98 ? 97  HIS   C C   1 
ATOM   1807 O  O   . HIS   B 1 91  ? 25.009 -20.712 22.985 1.00 18.70 ? 97  HIS   C O   1 
ATOM   1808 C  CB  . HIS   B 1 91  ? 24.358 -19.104 25.173 1.00 16.60 ? 97  HIS   C CB  1 
ATOM   1809 C  CG  . HIS   B 1 91  ? 24.243 -18.431 26.509 1.00 18.40 ? 97  HIS   C CG  1 
ATOM   1810 N  ND1 . HIS   B 1 91  ? 24.304 -19.157 27.678 1.00 21.59 ? 97  HIS   C ND1 1 
ATOM   1811 C  CD2 . HIS   B 1 91  ? 24.171 -17.112 26.815 1.00 20.75 ? 97  HIS   C CD2 1 
ATOM   1812 C  CE1 . HIS   B 1 91  ? 24.207 -18.270 28.671 1.00 21.97 ? 97  HIS   C CE1 1 
ATOM   1813 N  NE2 . HIS   B 1 91  ? 24.141 -17.027 28.200 1.00 22.75 ? 97  HIS   C NE2 1 
ATOM   1814 N  N   . LEU   B 1 92  ? 26.920 -19.602 22.463 1.00 17.72 ? 98  LEU   C N   1 
ATOM   1815 C  CA  . LEU   B 1 92  ? 27.070 -20.230 21.151 1.00 16.50 ? 98  LEU   C CA  1 
ATOM   1816 C  C   . LEU   B 1 92  ? 28.159 -21.326 21.202 1.00 16.83 ? 98  LEU   C C   1 
ATOM   1817 O  O   . LEU   B 1 92  ? 29.215 -21.159 21.831 1.00 17.26 ? 98  LEU   C O   1 
ATOM   1818 C  CB  . LEU   B 1 92  ? 27.463 -19.162 20.099 1.00 18.25 ? 98  LEU   C CB  1 
ATOM   1819 C  CG  . LEU   B 1 92  ? 27.576 -19.590 18.628 1.00 20.63 ? 98  LEU   C CG  1 
ATOM   1820 C  CD1 . LEU   B 1 92  ? 26.208 -20.019 18.076 1.00 20.26 ? 98  LEU   C CD1 1 
ATOM   1821 C  CD2 . LEU   B 1 92  ? 28.060 -18.377 17.745 1.00 21.99 ? 98  LEU   C CD2 1 
ATOM   1822 N  N   . MET   B 1 93  ? 27.881 -22.456 20.529 1.00 15.68 ? 99  MET   C N   1 
ATOM   1823 C  CA  . MET   B 1 93  ? 28.852 -23.582 20.501 1.00 15.72 ? 99  MET   C CA  1 
ATOM   1824 C  C   . MET   B 1 93  ? 29.248 -23.845 19.057 1.00 16.65 ? 99  MET   C C   1 
ATOM   1825 O  O   . MET   B 1 93  ? 28.349 -23.880 18.203 1.00 16.95 ? 99  MET   C O   1 
ATOM   1826 C  CB  . MET   B 1 93  ? 28.165 -24.859 21.064 1.00 15.25 ? 99  MET   C CB  1 
ATOM   1827 C  CG  . MET   B 1 93  ? 27.738 -24.610 22.491 1.00 19.02 ? 99  MET   C CG  1 
ATOM   1828 S  SD  . MET   B 1 93  ? 26.747 -25.934 23.153 1.00 19.93 ? 99  MET   C SD  1 
ATOM   1829 C  CE  . MET   B 1 93  ? 25.197 -25.790 22.052 1.00 18.83 ? 99  MET   C CE  1 
ATOM   1830 N  N   . LEU   B 1 94  ? 30.549 -24.052 18.769 1.00 15.49 ? 100 LEU   C N   1 
ATOM   1831 C  CA  . LEU   B 1 94  ? 30.953 -24.297 17.392 1.00 16.32 ? 100 LEU   C CA  1 
ATOM   1832 C  C   . LEU   B 1 94  ? 31.360 -25.733 17.178 1.00 16.11 ? 100 LEU   C C   1 
ATOM   1833 O  O   . LEU   B 1 94  ? 31.891 -26.388 18.073 1.00 16.05 ? 100 LEU   C O   1 
ATOM   1834 C  CB  . LEU   B 1 94  ? 32.188 -23.415 16.993 1.00 17.32 ? 100 LEU   C CB  1 
ATOM   1835 C  CG  . LEU   B 1 94  ? 31.961 -21.902 17.049 1.00 19.15 ? 100 LEU   C CG  1 
ATOM   1836 C  CD1 . LEU   B 1 94  ? 33.213 -21.143 16.554 1.00 20.87 ? 100 LEU   C CD1 1 
ATOM   1837 C  CD2 . LEU   B 1 94  ? 30.724 -21.457 16.233 1.00 20.55 ? 100 LEU   C CD2 1 
ATOM   1838 N  N   . ALA   B 1 95  ? 31.175 -26.207 15.950 1.00 16.52 ? 101 ALA   C N   1 
ATOM   1839 C  CA  . ALA   B 1 95  ? 31.648 -27.526 15.530 1.00 16.64 ? 101 ALA   C CA  1 
ATOM   1840 C  C   . ALA   B 1 95  ? 32.191 -27.391 14.088 1.00 16.94 ? 101 ALA   C C   1 
ATOM   1841 O  O   . ALA   B 1 95  ? 31.817 -26.453 13.357 1.00 17.78 ? 101 ALA   C O   1 
ATOM   1842 C  CB  . ALA   B 1 95  ? 30.487 -28.551 15.548 1.00 17.06 ? 101 ALA   C CB  1 
ATOM   1843 N  N   . VAL   B 1 96  ? 33.039 -28.348 13.662 1.00 16.89 ? 102 VAL   C N   1 
ATOM   1844 C  CA  . VAL   B 1 96  ? 33.464 -28.406 12.290 1.00 17.92 ? 102 VAL   C CA  1 
ATOM   1845 C  C   . VAL   B 1 96  ? 32.365 -29.183 11.543 1.00 20.43 ? 102 VAL   C C   1 
ATOM   1846 O  O   . VAL   B 1 96  ? 32.096 -30.344 11.844 1.00 22.11 ? 102 VAL   C O   1 
ATOM   1847 C  CB  . VAL   B 1 96  ? 34.833 -29.135 12.223 1.00 19.71 ? 102 VAL   C CB  1 
ATOM   1848 C  CG1 . VAL   B 1 96  ? 35.258 -29.312 10.767 1.00 20.06 ? 102 VAL   C CG1 1 
ATOM   1849 C  CG2 . VAL   B 1 96  ? 35.867 -28.318 13.015 1.00 20.23 ? 102 VAL   C CG2 1 
ATOM   1850 N  N   . GLY   B 1 97  ? 31.759 -28.531 10.589 1.00 22.28 ? 103 GLY   C N   1 
ATOM   1851 C  CA  . GLY   B 1 97  ? 30.672 -29.161 9.843  1.00 23.74 ? 103 GLY   C CA  1 
ATOM   1852 C  C   . GLY   B 1 97  ? 30.050 -28.215 8.864  1.00 25.18 ? 103 GLY   C C   1 
ATOM   1853 O  O   . GLY   B 1 97  ? 30.298 -26.995 8.885  1.00 25.47 ? 103 GLY   C O   1 
ATOM   1854 N  N   . HIS   B 1 98  ? 29.201 -28.783 8.008  1.00 24.52 ? 104 HIS   C N   1 
ATOM   1855 C  CA  . HIS   B 1 98  ? 28.544 -28.013 6.986  1.00 25.49 ? 104 HIS   C CA  1 
ATOM   1856 C  C   . HIS   B 1 98  ? 27.312 -27.304 7.495  1.00 25.67 ? 104 HIS   C C   1 
ATOM   1857 O  O   . HIS   B 1 98  ? 26.493 -27.907 8.186  1.00 24.84 ? 104 HIS   C O   1 
ATOM   1858 C  CB  . HIS   B 1 98  ? 28.151 -28.939 5.831  1.00 25.07 ? 104 HIS   C CB  1 
ATOM   1859 C  CG  . HIS   B 1 98  ? 27.545 -28.173 4.711  1.00 26.32 ? 104 HIS   C CG  1 
ATOM   1860 N  ND1 . HIS   B 1 98  ? 28.296 -27.246 3.983  1.00 27.61 ? 104 HIS   C ND1 1 
ATOM   1861 C  CD2 . HIS   B 1 98  ? 26.250 -28.116 4.300  1.00 27.02 ? 104 HIS   C CD2 1 
ATOM   1862 C  CE1 . HIS   B 1 98  ? 27.447 -26.681 3.141  1.00 28.80 ? 104 HIS   C CE1 1 
ATOM   1863 N  NE2 . HIS   B 1 98  ? 26.198 -27.183 3.287  1.00 29.16 ? 104 HIS   C NE2 1 
ATOM   1864 N  N   . SER   B 1 99  ? 27.151 -26.028 7.108  1.00 26.30 ? 105 SER   C N   1 
ATOM   1865 C  CA  . SER   B 1 99  ? 26.009 -25.179 7.427  1.00 27.49 ? 105 SER   C CA  1 
ATOM   1866 C  C   . SER   B 1 99  ? 25.850 -24.145 6.279  1.00 29.47 ? 105 SER   C C   1 
ATOM   1867 O  O   . SER   B 1 99  ? 26.853 -23.671 5.739  1.00 31.80 ? 105 SER   C O   1 
ATOM   1868 C  CB  . SER   B 1 99  ? 26.256 -24.448 8.744  1.00 30.25 ? 105 SER   C CB  1 
ATOM   1869 O  OG  . SER   B 1 99  ? 25.040 -23.990 9.311  1.00 38.13 ? 105 SER   C OG  1 
ATOM   1870 N  N   . GLU   B 1 100 ? 24.592 -23.885 5.871  1.00 27.35 ? 106 GLU   C N   1 
ATOM   1871 C  CA  . GLU   B 1 100 ? 24.104 -22.859 4.914  1.00 27.91 ? 106 GLU   C CA  1 
ATOM   1872 C  C   . GLU   B 1 100 ? 22.971 -22.083 5.604  1.00 28.33 ? 106 GLU   C C   1 
ATOM   1873 O  O   . GLU   B 1 100 ? 22.420 -22.586 6.572  1.00 27.21 ? 106 GLU   C O   1 
ATOM   1874 C  CB  . GLU   B 1 100 ? 23.592 -23.503 3.646  1.00 29.88 ? 106 GLU   C CB  1 
ATOM   1875 C  CG  . GLU   B 1 100 ? 24.744 -24.100 2.896  1.00 37.76 ? 106 GLU   C CG  1 
ATOM   1876 C  CD  . GLU   B 1 100 ? 24.326 -24.759 1.602  1.00 42.95 ? 106 GLU   C CD  1 
ATOM   1877 O  OE1 . GLU   B 1 100 ? 23.472 -24.185 0.893  1.00 47.04 ? 106 GLU   C OE1 1 
ATOM   1878 O  OE2 . GLU   B 1 100 ? 24.846 -25.856 1.305  1.00 42.52 ? 106 GLU   C OE2 1 
ATOM   1879 N  N   . PRO   B 1 101 ? 22.602 -20.861 5.162  1.00 29.31 ? 107 PRO   C N   1 
ATOM   1880 C  CA  . PRO   B 1 101 ? 21.593 -20.075 5.920  1.00 29.16 ? 107 PRO   C CA  1 
ATOM   1881 C  C   . PRO   B 1 101 ? 20.280 -20.793 6.278  1.00 26.67 ? 107 PRO   C C   1 
ATOM   1882 O  O   . PRO   B 1 101 ? 19.804 -20.707 7.443  1.00 27.67 ? 107 PRO   C O   1 
ATOM   1883 C  CB  . PRO   B 1 101 ? 21.358 -18.856 5.027  1.00 30.82 ? 107 PRO   C CB  1 
ATOM   1884 C  CG  . PRO   B 1 101 ? 22.682 -18.673 4.299  1.00 31.79 ? 107 PRO   C CG  1 
ATOM   1885 C  CD  . PRO   B 1 101 ? 23.200 -20.073 4.059  1.00 30.08 ? 107 PRO   C CD  1 
ATOM   1886 N  N   . GLY   B 1 102 ? 19.747 -21.539 5.304  1.00 23.85 ? 108 GLY   C N   1 
ATOM   1887 C  CA  . GLY   B 1 102 ? 18.542 -22.342 5.441  1.00 23.06 ? 108 GLY   C CA  1 
ATOM   1888 C  C   . GLY   B 1 102 ? 18.644 -23.462 6.461  1.00 21.35 ? 108 GLY   C C   1 
ATOM   1889 O  O   . GLY   B 1 102 ? 17.634 -24.075 6.814  1.00 21.37 ? 108 GLY   C O   1 
ATOM   1890 N  N   . ASP   B 1 103 ? 19.865 -23.721 6.959  1.00 19.54 ? 109 ASP   C N   1 
ATOM   1891 C  CA  . ASP   B 1 103 ? 20.046 -24.762 7.966  1.00 18.59 ? 109 ASP   C CA  1 
ATOM   1892 C  C   . ASP   B 1 103 ? 19.692 -24.299 9.374  1.00 17.92 ? 109 ASP   C C   1 
ATOM   1893 O  O   . ASP   B 1 103 ? 19.596 -25.152 10.263 1.00 17.63 ? 109 ASP   C O   1 
ATOM   1894 C  CB  . ASP   B 1 103 ? 21.491 -25.295 7.950  1.00 18.05 ? 109 ASP   C CB  1 
ATOM   1895 C  CG  . ASP   B 1 103 ? 21.760 -26.157 6.719  1.00 21.05 ? 109 ASP   C CG  1 
ATOM   1896 O  OD1 . ASP   B 1 103 ? 20.820 -26.835 6.259  1.00 21.55 ? 109 ASP   C OD1 1 
ATOM   1897 O  OD2 . ASP   B 1 103 ? 22.919 -26.118 6.194  1.00 21.81 ? 109 ASP   C OD2 1 
ATOM   1898 N  N   . CYS   B 1 104 ? 19.519 -22.984 9.611  1.00 16.89 ? 110 CYS   C N   1 
ATOM   1899 C  CA  . CYS   B 1 104 ? 19.147 -22.497 10.954 1.00 17.08 ? 110 CYS   C CA  1 
ATOM   1900 C  C   . CYS   B 1 104 ? 17.867 -23.144 11.422 1.00 17.39 ? 110 CYS   C C   1 
ATOM   1901 O  O   . CYS   B 1 104 ? 16.957 -23.350 10.613 1.00 17.45 ? 110 CYS   C O   1 
ATOM   1902 C  CB  . CYS   B 1 104 ? 19.033 -20.974 10.998 1.00 18.54 ? 110 CYS   C CB  1 
ATOM   1903 S  SG  . CYS   B 1 104 ? 20.636 -20.140 10.919 1.00 22.05 ? 110 CYS   C SG  1 
ATOM   1904 N  N   . GLY   B 1 105 ? 17.873 -23.597 12.669 1.00 15.72 ? 111 GLY   C N   1 
ATOM   1905 C  CA  . GLY   B 1 105 ? 16.717 -24.268 13.229 1.00 16.31 ? 111 GLY   C CA  1 
ATOM   1906 C  C   . GLY   B 1 105 ? 16.885 -25.776 13.306 1.00 16.77 ? 111 GLY   C C   1 
ATOM   1907 O  O   . GLY   B 1 105 ? 16.127 -26.448 14.008 1.00 17.89 ? 111 GLY   C O   1 
ATOM   1908 N  N   . GLY   B 1 106 ? 17.911 -26.316 12.615 1.00 15.46 ? 112 GLY   C N   1 
ATOM   1909 C  CA  . GLY   B 1 106 ? 18.224 -27.738 12.731 1.00 14.62 ? 112 GLY   C CA  1 
ATOM   1910 C  C   . GLY   B 1 106 ? 18.600 -28.089 14.169 1.00 14.25 ? 112 GLY   C C   1 
ATOM   1911 O  O   . GLY   B 1 106 ? 19.351 -27.337 14.809 1.00 14.76 ? 112 GLY   C O   1 
ATOM   1912 N  N   . ILE   B 1 107 ? 18.065 -29.191 14.691 1.00 14.39 ? 113 ILE   C N   1 
ATOM   1913 C  CA  . ILE   B 1 107 ? 18.327 -29.541 16.092 1.00 14.77 ? 113 ILE   C CA  1 
ATOM   1914 C  C   . ILE   B 1 107 ? 19.602 -30.316 16.293 1.00 14.52 ? 113 ILE   C C   1 
ATOM   1915 O  O   . ILE   B 1 107 ? 19.890 -31.253 15.510 1.00 15.12 ? 113 ILE   C O   1 
ATOM   1916 C  CB  . ILE   B 1 107 ? 17.081 -30.293 16.679 1.00 17.26 ? 113 ILE   C CB  1 
ATOM   1917 C  CG1 . ILE   B 1 107 ? 15.897 -29.295 16.826 1.00 20.16 ? 113 ILE   C CG1 1 
ATOM   1918 C  CG2 . ILE   B 1 107 ? 17.382 -30.974 18.040 1.00 19.33 ? 113 ILE   C CG2 1 
ATOM   1919 C  CD1 . ILE   B 1 107 ? 14.563 -30.032 17.295 1.00 23.42 ? 113 ILE   C CD1 1 
ATOM   1920 N  N   . LEU   B 1 108 ? 20.332 -29.970 17.366 1.00 12.79 ? 114 LEU   C N   1 
ATOM   1921 C  CA  . LEU   B 1 108 ? 21.504 -30.736 17.837 1.00 12.70 ? 114 LEU   C CA  1 
ATOM   1922 C  C   . LEU   B 1 108 ? 21.014 -31.507 19.083 1.00 14.00 ? 114 LEU   C C   1 
ATOM   1923 O  O   . LEU   B 1 108 ? 20.412 -30.912 19.986 1.00 14.34 ? 114 LEU   C O   1 
ATOM   1924 C  CB  . LEU   B 1 108 ? 22.599 -29.730 18.249 1.00 13.23 ? 114 LEU   C CB  1 
ATOM   1925 C  CG  . LEU   B 1 108 ? 23.836 -30.338 18.938 1.00 14.47 ? 114 LEU   C CG  1 
ATOM   1926 C  CD1 . LEU   B 1 108 ? 24.632 -31.296 17.992 1.00 15.82 ? 114 LEU   C CD1 1 
ATOM   1927 C  CD2 . LEU   B 1 108 ? 24.762 -29.203 19.484 1.00 15.17 ? 114 LEU   C CD2 1 
ATOM   1928 N  N   . ARG   B 1 109 ? 21.262 -32.823 19.099 1.00 13.56 ? 115 ARG   C N   1 
ATOM   1929 C  CA  . ARG   B 1 109 ? 20.840 -33.700 20.200 1.00 13.94 ? 115 ARG   C CA  1 
ATOM   1930 C  C   . ARG   B 1 109 ? 22.030 -34.481 20.692 1.00 15.42 ? 115 ARG   C C   1 
ATOM   1931 O  O   . ARG   B 1 109 ? 22.877 -34.950 19.913 1.00 16.95 ? 115 ARG   C O   1 
ATOM   1932 C  CB  . ARG   B 1 109 ? 19.817 -34.758 19.683 1.00 16.69 ? 115 ARG   C CB  1 
ATOM   1933 C  CG  . ARG   B 1 109 ? 18.584 -34.174 19.145 1.00 23.38 ? 115 ARG   C CG  1 
ATOM   1934 C  CD  . ARG   B 1 109 ? 17.712 -35.281 18.547 1.00 28.70 ? 115 ARG   C CD  1 
ATOM   1935 N  NE  . ARG   B 1 109 ? 16.532 -35.377 19.376 1.00 39.28 ? 115 ARG   C NE  1 
ATOM   1936 C  CZ  . ARG   B 1 109 ? 15.433 -34.649 19.178 1.00 43.83 ? 115 ARG   C CZ  1 
ATOM   1937 N  NH1 . ARG   B 1 109 ? 15.350 -33.820 18.139 1.00 44.09 ? 115 ARG   C NH1 1 
ATOM   1938 N  NH2 . ARG   B 1 109 ? 14.398 -34.770 19.993 1.00 46.50 ? 115 ARG   C NH2 1 
ATOM   1939 N  N   . CYS   B 1 110 ? 22.003 -34.782 21.956 1.00 14.68 ? 116 CYS   C N   1 
ATOM   1940 C  CA  . CYS   B 1 110 ? 22.962 -35.732 22.565 1.00 16.38 ? 116 CYS   C CA  1 
ATOM   1941 C  C   . CYS   B 1 110 ? 22.136 -36.909 23.133 1.00 18.80 ? 116 CYS   C C   1 
ATOM   1942 O  O   . CYS   B 1 110 ? 20.921 -36.967 22.978 1.00 18.74 ? 116 CYS   C O   1 
ATOM   1943 C  CB  . CYS   B 1 110 ? 23.796 -35.047 23.642 1.00 16.65 ? 116 CYS   C CB  1 
ATOM   1944 S  SG  . CYS   B 1 110 ? 22.806 -34.522 25.076 1.00 15.79 ? 116 CYS   C SG  1 
ATOM   1945 N  N   . GLN   B 1 111 ? 22.816 -37.847 23.851 1.00 21.69 ? 117 GLN   C N   1 
ATOM   1946 C  CA  . GLN   B 1 111 ? 22.107 -38.965 24.451 1.00 23.74 ? 117 GLN   C CA  1 
ATOM   1947 C  C   . GLN   B 1 111 ? 21.047 -38.510 25.490 1.00 24.13 ? 117 GLN   C C   1 
ATOM   1948 O  O   . GLN   B 1 111 ? 20.157 -39.287 25.837 1.00 26.66 ? 117 GLN   C O   1 
ATOM   1949 C  CB  . GLN   B 1 111 ? 23.125 -39.946 25.085 1.00 26.85 ? 117 GLN   C CB  1 
ATOM   1950 C  CG  . GLN   B 1 111 ? 23.809 -39.368 26.316 1.00 30.66 ? 117 GLN   C CG  1 
ATOM   1951 C  CD  . GLN   B 1 111 ? 24.876 -40.294 26.864 1.00 39.46 ? 117 GLN   C CD  1 
ATOM   1952 O  OE1 . GLN   B 1 111 ? 26.075 -40.099 26.617 1.00 43.02 ? 117 GLN   C OE1 1 
ATOM   1953 N  NE2 . GLN   B 1 111 ? 24.460 -41.301 27.631 1.00 39.58 ? 117 GLN   C NE2 1 
ATOM   1954 N  N   . HIS   B 1 112 ? 21.121 -37.248 25.989 1.00 21.42 ? 118 HIS   C N   1 
ATOM   1955 C  CA  . HIS   B 1 112 ? 20.198 -36.762 27.018 1.00 20.82 ? 118 HIS   C CA  1 
ATOM   1956 C  C   . HIS   B 1 112 ? 19.003 -35.979 26.471 1.00 21.43 ? 118 HIS   C C   1 
ATOM   1957 O  O   . HIS   B 1 112 ? 18.065 -35.696 27.232 1.00 23.96 ? 118 HIS   C O   1 
ATOM   1958 C  CB  . HIS   B 1 112 ? 20.946 -35.892 28.036 1.00 20.30 ? 118 HIS   C CB  1 
ATOM   1959 C  CG  . HIS   B 1 112 ? 22.155 -36.586 28.629 1.00 19.84 ? 118 HIS   C CG  1 
ATOM   1960 N  ND1 . HIS   B 1 112 ? 23.451 -36.181 28.331 1.00 19.79 ? 118 HIS   C ND1 1 
ATOM   1961 C  CD2 . HIS   B 1 112 ? 22.227 -37.571 29.563 1.00 21.22 ? 118 HIS   C CD2 1 
ATOM   1962 C  CE1 . HIS   B 1 112 ? 24.261 -36.974 29.012 1.00 22.43 ? 118 HIS   C CE1 1 
ATOM   1963 N  NE2 . HIS   B 1 112 ? 23.577 -37.832 29.772 1.00 23.15 ? 118 HIS   C NE2 1 
ATOM   1964 N  N   . GLY   B 1 113 ? 19.019 -35.640 25.180 1.00 19.08 ? 119 GLY   C N   1 
ATOM   1965 C  CA  . GLY   B 1 113 ? 17.914 -34.884 24.607 1.00 18.66 ? 119 GLY   C CA  1 
ATOM   1966 C  C   . GLY   B 1 113 ? 18.381 -33.724 23.736 1.00 16.82 ? 119 GLY   C C   1 
ATOM   1967 O  O   . GLY   B 1 113 ? 19.495 -33.726 23.210 1.00 17.16 ? 119 GLY   C O   1 
ATOM   1968 N  N   . VAL   B 1 114 ? 17.527 -32.708 23.582 1.00 16.24 ? 120 VAL   C N   1 
ATOM   1969 C  CA  . VAL   B 1 114 ? 17.864 -31.537 22.760 1.00 15.20 ? 120 VAL   C CA  1 
ATOM   1970 C  C   . VAL   B 1 114 ? 18.902 -30.638 23.415 1.00 14.30 ? 120 VAL   C C   1 
ATOM   1971 O  O   . VAL   B 1 114 ? 18.724 -30.205 24.577 1.00 15.61 ? 120 VAL   C O   1 
ATOM   1972 C  CB  . VAL   B 1 114 ? 16.595 -30.732 22.429 1.00 16.52 ? 120 VAL   C CB  1 
ATOM   1973 C  CG1 . VAL   B 1 114 ? 16.951 -29.457 21.682 1.00 16.31 ? 120 VAL   C CG1 1 
ATOM   1974 C  CG2 . VAL   B 1 114 ? 15.635 -31.599 21.588 1.00 17.26 ? 120 VAL   C CG2 1 
ATOM   1975 N  N   . VAL   B 1 115 ? 19.989 -30.331 22.692 1.00 13.95 ? 121 VAL   C N   1 
ATOM   1976 C  CA  . VAL   B 1 115 ? 21.049 -29.461 23.204 1.00 14.00 ? 121 VAL   C CA  1 
ATOM   1977 C  C   . VAL   B 1 115 ? 20.869 -28.018 22.705 1.00 14.95 ? 121 VAL   C C   1 
ATOM   1978 O  O   . VAL   B 1 115 ? 21.134 -27.056 23.452 1.00 14.38 ? 121 VAL   C O   1 
ATOM   1979 C  CB  . VAL   B 1 115 ? 22.415 -30.010 22.715 1.00 13.75 ? 121 VAL   C CB  1 
ATOM   1980 C  CG1 . VAL   B 1 115 ? 23.559 -29.047 23.048 1.00 14.96 ? 121 VAL   C CG1 1 
ATOM   1981 C  CG2 . VAL   B 1 115 ? 22.656 -31.369 23.322 1.00 14.20 ? 121 VAL   C CG2 1 
ATOM   1982 N  N   . GLY   B 1 116 ? 20.495 -27.870 21.433 1.00 14.12 ? 122 GLY   C N   1 
ATOM   1983 C  CA  . GLY   B 1 116 ? 20.398 -26.523 20.878 1.00 15.24 ? 122 GLY   C CA  1 
ATOM   1984 C  C   . GLY   B 1 116 ? 19.987 -26.553 19.431 1.00 13.73 ? 122 GLY   C C   1 
ATOM   1985 O  O   . GLY   B 1 116 ? 19.554 -27.600 18.935 1.00 14.24 ? 122 GLY   C O   1 
ATOM   1986 N  N   . ILE   B 1 117 ? 20.078 -25.380 18.760 1.00 13.52 ? 123 ILE   C N   1 
ATOM   1987 C  CA  . ILE   B 1 117 ? 19.611 -25.286 17.377 1.00 14.39 ? 123 ILE   C CA  1 
ATOM   1988 C  C   . ILE   B 1 117 ? 20.647 -24.570 16.539 1.00 13.99 ? 123 ILE   C C   1 
ATOM   1989 O  O   . ILE   B 1 117 ? 21.314 -23.645 17.035 1.00 14.21 ? 123 ILE   C O   1 
ATOM   1990 C  CB  . ILE   B 1 117 ? 18.261 -24.556 17.238 1.00 16.22 ? 123 ILE   C CB  1 
ATOM   1991 C  CG1 . ILE   B 1 117 ? 18.283 -23.188 17.947 1.00 16.68 ? 123 ILE   C CG1 1 
ATOM   1992 C  CG2 . ILE   B 1 117 ? 17.073 -25.456 17.673 1.00 18.34 ? 123 ILE   C CG2 1 
ATOM   1993 C  CD1 . ILE   B 1 117 ? 16.881 -22.385 17.602 1.00 19.14 ? 123 ILE   C CD1 1 
ATOM   1994 N  N   . VAL   B 1 118 ? 20.799 -24.965 15.257 1.00 12.78 ? 124 VAL   C N   1 
ATOM   1995 C  CA  . VAL   B 1 118 ? 21.755 -24.258 14.379 1.00 13.44 ? 124 VAL   C CA  1 
ATOM   1996 C  C   . VAL   B 1 118 ? 21.388 -22.757 14.303 1.00 13.79 ? 124 VAL   C C   1 
ATOM   1997 O  O   . VAL   B 1 118 ? 20.196 -22.422 14.128 1.00 14.57 ? 124 VAL   C O   1 
ATOM   1998 C  CB  . VAL   B 1 118 ? 21.700 -24.848 12.952 1.00 14.45 ? 124 VAL   C CB  1 
ATOM   1999 C  CG1 . VAL   B 1 118 ? 22.553 -24.018 11.979 1.00 15.20 ? 124 VAL   C CG1 1 
ATOM   2000 C  CG2 . VAL   B 1 118 ? 22.139 -26.314 12.953 1.00 15.81 ? 124 VAL   C CG2 1 
ATOM   2001 N  N   . SER   B 1 119 ? 22.403 -21.895 14.461 1.00 14.80 ? 125 SER   C N   1 
ATOM   2002 C  CA  . SER   B 1 119 ? 22.203 -20.448 14.467 1.00 15.41 ? 125 SER   C CA  1 
ATOM   2003 C  C   . SER   B 1 119 ? 23.169 -19.685 13.561 1.00 17.89 ? 125 SER   C C   1 
ATOM   2004 O  O   . SER   B 1 119 ? 22.821 -18.592 13.058 1.00 17.97 ? 125 SER   C O   1 
ATOM   2005 C  CB  . SER   B 1 119 ? 22.310 -19.943 15.909 1.00 17.52 ? 125 SER   C CB  1 
ATOM   2006 O  OG  . SER   B 1 119 ? 22.172 -18.529 15.987 1.00 18.00 ? 125 SER   C OG  1 
ATOM   2007 N  N   . THR   B 1 120 ? 24.394 -20.205 13.397 1.00 18.03 ? 126 THR   C N   1 
ATOM   2008 C  CA  . THR   B 1 120 ? 25.433 -19.526 12.573 1.00 19.69 ? 126 THR   C CA  1 
ATOM   2009 C  C   . THR   B 1 120 ? 26.164 -20.571 11.706 1.00 20.21 ? 126 THR   C C   1 
ATOM   2010 O  O   . THR   B 1 120 ? 26.068 -21.777 11.953 1.00 18.69 ? 126 THR   C O   1 
ATOM   2011 C  CB  . THR   B 1 120 ? 26.460 -18.769 13.477 1.00 21.94 ? 126 THR   C CB  1 
ATOM   2012 O  OG1 . THR   B 1 120 ? 27.348 -19.693 14.129 1.00 23.89 ? 126 THR   C OG1 1 
ATOM   2013 C  CG2 . THR   B 1 120 ? 25.829 -17.848 14.488 1.00 23.56 ? 126 THR   C CG2 1 
ATOM   2014 N  N   . GLY   B 1 121 ? 26.877 -20.110 10.687 1.00 22.24 ? 127 GLY   C N   1 
ATOM   2015 C  CA  . GLY   B 1 121 ? 27.662 -21.018 9.844  1.00 24.87 ? 127 GLY   C CA  1 
ATOM   2016 C  C   . GLY   B 1 121 ? 28.655 -20.268 8.984  1.00 27.21 ? 127 GLY   C C   1 
ATOM   2017 O  O   . GLY   B 1 121 ? 28.575 -19.054 8.856  1.00 27.16 ? 127 GLY   C O   1 
ATOM   2018 N  N   . GLY   B 1 122 ? 29.584 -20.993 8.386  1.00 29.79 ? 128 GLY   C N   1 
ATOM   2019 C  CA  . GLY   B 1 122 ? 30.582 -20.377 7.505  1.00 30.88 ? 128 GLY   C CA  1 
ATOM   2020 C  C   . GLY   B 1 122 ? 31.971 -20.891 7.763  1.00 31.82 ? 128 GLY   C C   1 
ATOM   2021 O  O   . GLY   B 1 122 ? 32.233 -21.396 8.842  1.00 31.22 ? 128 GLY   C O   1 
ATOM   2022 N  N   . ASN   B 1 123 ? 32.887 -20.769 6.772  1.00 32.34 ? 129 ASN   C N   1 
ATOM   2023 C  CA  . ASN   B 1 123 ? 34.262 -21.270 6.923  1.00 33.17 ? 129 ASN   C CA  1 
ATOM   2024 C  C   . ASN   B 1 123 ? 34.353 -22.714 7.372  1.00 31.46 ? 129 ASN   C C   1 
ATOM   2025 O  O   . ASN   B 1 123 ? 35.304 -23.087 8.076  1.00 33.11 ? 129 ASN   C O   1 
ATOM   2026 C  CB  . ASN   B 1 123 ? 35.066 -20.371 7.848  1.00 35.75 ? 129 ASN   C CB  1 
ATOM   2027 C  CG  . ASN   B 1 123 ? 35.387 -19.079 7.182  1.00 41.13 ? 129 ASN   C CG  1 
ATOM   2028 O  OD1 . ASN   B 1 123 ? 35.682 -19.043 5.989  1.00 42.54 ? 129 ASN   C OD1 1 
ATOM   2029 N  ND2 . ASN   B 1 123 ? 35.317 -17.995 7.928  1.00 44.05 ? 129 ASN   C ND2 1 
ATOM   2030 N  N   . GLY   B 1 124 ? 33.356 -23.524 7.010  1.00 28.20 ? 130 GLY   C N   1 
ATOM   2031 C  CA  . GLY   B 1 124 ? 33.370 -24.924 7.407  1.00 25.41 ? 130 GLY   C CA  1 
ATOM   2032 C  C   . GLY   B 1 124 ? 33.066 -25.169 8.877  1.00 22.73 ? 130 GLY   C C   1 
ATOM   2033 O  O   . GLY   B 1 124 ? 33.368 -26.240 9.392  1.00 23.51 ? 130 GLY   C O   1 
ATOM   2034 N  N   . LEU   B 1 125 ? 32.450 -24.190 9.544  1.00 21.54 ? 131 LEU   C N   1 
ATOM   2035 C  CA  . LEU   B 1 125 ? 32.051 -24.319 10.925 1.00 20.47 ? 131 LEU   C CA  1 
ATOM   2036 C  C   . LEU   B 1 125 ? 30.514 -24.184 10.987 1.00 20.01 ? 131 LEU   C C   1 
ATOM   2037 O  O   . LEU   B 1 125 ? 29.899 -23.471 10.184 1.00 22.35 ? 131 LEU   C O   1 
ATOM   2038 C  CB  . LEU   B 1 125 ? 32.665 -23.176 11.746 1.00 22.55 ? 131 LEU   C CB  1 
ATOM   2039 C  CG  . LEU   B 1 125 ? 34.196 -23.091 11.723 1.00 25.71 ? 131 LEU   C CG  1 
ATOM   2040 C  CD1 . LEU   B 1 125 ? 34.673 -21.729 12.252 1.00 27.67 ? 131 LEU   C CD1 1 
ATOM   2041 C  CD2 . LEU   B 1 125 ? 34.819 -24.249 12.502 1.00 26.57 ? 131 LEU   C CD2 1 
ATOM   2042 N  N   . VAL   B 1 126 ? 29.927 -24.817 11.990 1.00 16.56 ? 132 VAL   C N   1 
ATOM   2043 C  CA  . VAL   B 1 126 ? 28.500 -24.645 12.267 1.00 16.76 ? 132 VAL   C CA  1 
ATOM   2044 C  C   . VAL   B 1 126 ? 28.384 -24.196 13.724 1.00 16.51 ? 132 VAL   C C   1 
ATOM   2045 O  O   . VAL   B 1 126 ? 29.076 -24.747 14.606 1.00 16.67 ? 132 VAL   C O   1 
ATOM   2046 C  CB  . VAL   B 1 126 ? 27.706 -25.938 11.957 1.00 17.76 ? 132 VAL   C CB  1 
ATOM   2047 C  CG1 . VAL   B 1 126 ? 28.273 -27.167 12.652 1.00 20.07 ? 132 VAL   C CG1 1 
ATOM   2048 C  CG2 . VAL   B 1 126 ? 26.199 -25.753 12.281 1.00 18.15 ? 132 VAL   C CG2 1 
ATOM   2049 N  N   . GLY   B 1 127 ? 27.513 -23.213 13.977 1.00 15.59 ? 133 GLY   C N   1 
ATOM   2050 C  CA  . GLY   B 1 127 ? 27.308 -22.701 15.327 1.00 15.88 ? 133 GLY   C CA  1 
ATOM   2051 C  C   . GLY   B 1 127 ? 25.909 -23.014 15.843 1.00 15.61 ? 133 GLY   C C   1 
ATOM   2052 O  O   . GLY   B 1 127 ? 24.940 -22.849 15.110 1.00 16.12 ? 133 GLY   C O   1 
ATOM   2053 N  N   . PHE   B 1 128 ? 25.815 -23.465 17.094 1.00 14.53 ? 134 PHE   C N   1 
ATOM   2054 C  CA  . PHE   B 1 128 ? 24.529 -23.844 17.704 1.00 14.56 ? 134 PHE   C CA  1 
ATOM   2055 C  C   . PHE   B 1 128 ? 24.244 -22.971 18.910 1.00 15.34 ? 134 PHE   C C   1 
ATOM   2056 O  O   . PHE   B 1 128 ? 25.101 -22.817 19.783 1.00 15.85 ? 134 PHE   C O   1 
ATOM   2057 C  CB  . PHE   B 1 128 ? 24.595 -25.309 18.211 1.00 14.02 ? 134 PHE   C CB  1 
ATOM   2058 C  CG  . PHE   B 1 128 ? 25.046 -26.309 17.165 1.00 14.05 ? 134 PHE   C CG  1 
ATOM   2059 C  CD1 . PHE   B 1 128 ? 24.138 -26.901 16.321 1.00 13.45 ? 134 PHE   C CD1 1 
ATOM   2060 C  CD2 . PHE   B 1 128 ? 26.373 -26.706 17.092 1.00 15.95 ? 134 PHE   C CD2 1 
ATOM   2061 C  CE1 . PHE   B 1 128 ? 24.554 -27.788 15.350 1.00 14.19 ? 134 PHE   C CE1 1 
ATOM   2062 C  CE2 . PHE   B 1 128 ? 26.781 -27.660 16.163 1.00 16.45 ? 134 PHE   C CE2 1 
ATOM   2063 C  CZ  . PHE   B 1 128 ? 25.857 -28.188 15.290 1.00 16.07 ? 134 PHE   C CZ  1 
ATOM   2064 N  N   . ALA   B 1 129 ? 23.012 -22.464 18.984 1.00 14.15 ? 135 ALA   C N   1 
ATOM   2065 C  CA  . ALA   B 1 129 ? 22.560 -21.720 20.149 1.00 13.54 ? 135 ALA   C CA  1 
ATOM   2066 C  C   . ALA   B 1 129 ? 22.183 -22.756 21.220 1.00 14.05 ? 135 ALA   C C   1 
ATOM   2067 O  O   . ALA   B 1 129 ? 21.249 -23.560 21.025 1.00 13.17 ? 135 ALA   C O   1 
ATOM   2068 C  CB  . ALA   B 1 129 ? 21.346 -20.866 19.758 1.00 13.67 ? 135 ALA   C CB  1 
ATOM   2069 N  N   . ASP   B 1 130 ? 22.867 -22.730 22.381 1.00 14.12 ? 136 ASP   C N   1 
ATOM   2070 C  CA  . ASP   B 1 130 ? 22.569 -23.692 23.446 1.00 13.66 ? 136 ASP   C CA  1 
ATOM   2071 C  C   . ASP   B 1 130 ? 21.227 -23.370 24.090 1.00 15.33 ? 136 ASP   C C   1 
ATOM   2072 O  O   . ASP   B 1 130 ? 20.886 -22.195 24.277 1.00 15.71 ? 136 ASP   C O   1 
ATOM   2073 C  CB  . ASP   B 1 130 ? 23.657 -23.515 24.533 1.00 15.31 ? 136 ASP   C CB  1 
ATOM   2074 C  CG  . ASP   B 1 130 ? 23.561 -24.534 25.651 1.00 22.10 ? 136 ASP   C CG  1 
ATOM   2075 O  OD1 . ASP   B 1 130 ? 23.403 -25.713 25.356 1.00 21.31 ? 136 ASP   C OD1 1 
ATOM   2076 O  OD2 . ASP   B 1 130 ? 23.536 -24.123 26.827 1.00 25.36 ? 136 ASP   C OD2 1 
ATOM   2077 N  N   . VAL   B 1 131 ? 20.486 -24.412 24.543 1.00 14.29 ? 137 VAL   C N   1 
ATOM   2078 C  CA  . VAL   B 1 131 ? 19.243 -24.159 25.330 1.00 14.39 ? 137 VAL   C CA  1 
ATOM   2079 C  C   . VAL   B 1 131 ? 19.289 -24.932 26.663 1.00 15.93 ? 137 VAL   C C   1 
ATOM   2080 O  O   . VAL   B 1 131 ? 18.317 -24.876 27.425 1.00 17.03 ? 137 VAL   C O   1 
ATOM   2081 C  CB  . VAL   B 1 131 ? 17.940 -24.561 24.559 1.00 15.55 ? 137 VAL   C CB  1 
ATOM   2082 C  CG1 . VAL   B 1 131 ? 17.773 -23.722 23.272 1.00 16.10 ? 137 VAL   C CG1 1 
ATOM   2083 C  CG2 . VAL   B 1 131 ? 17.937 -26.062 24.233 1.00 16.88 ? 137 VAL   C CG2 1 
ATOM   2084 N  N   . ARG   B 1 132 ? 20.414 -25.629 26.976 1.00 14.80 ? 138 ARG   C N   1 
ATOM   2085 C  CA  . ARG   B 1 132 ? 20.487 -26.461 28.163 1.00 14.85 ? 138 ARG   C CA  1 
ATOM   2086 C  C   . ARG   B 1 132 ? 20.425 -25.694 29.455 1.00 17.68 ? 138 ARG   C C   1 
ATOM   2087 O  O   . ARG   B 1 132 ? 20.094 -26.304 30.481 1.00 19.22 ? 138 ARG   C O   1 
ATOM   2088 C  CB  . ARG   B 1 132 ? 21.730 -27.341 28.133 1.00 15.18 ? 138 ARG   C CB  1 
ATOM   2089 C  CG  . ARG   B 1 132 ? 21.724 -28.337 26.982 1.00 15.56 ? 138 ARG   C CG  1 
ATOM   2090 C  CD  . ARG   B 1 132 ? 23.045 -29.077 26.950 1.00 15.69 ? 138 ARG   C CD  1 
ATOM   2091 N  NE  . ARG   B 1 132 ? 24.136 -28.185 26.536 1.00 15.36 ? 138 ARG   C NE  1 
ATOM   2092 C  CZ  . ARG   B 1 132 ? 25.383 -28.591 26.298 1.00 16.01 ? 138 ARG   C CZ  1 
ATOM   2093 N  NH1 . ARG   B 1 132 ? 25.761 -29.826 26.613 1.00 16.32 ? 138 ARG   C NH1 1 
ATOM   2094 N  NH2 . ARG   B 1 132 ? 26.288 -27.741 25.829 1.00 17.11 ? 138 ARG   C NH2 1 
ATOM   2095 N  N   . ASP   B 1 133 ? 20.807 -24.416 29.446 1.00 17.29 ? 139 ASP   C N   1 
ATOM   2096 C  CA  . ASP   B 1 133 ? 20.744 -23.603 30.658 1.00 18.93 ? 139 ASP   C CA  1 
ATOM   2097 C  C   . ASP   B 1 133 ? 19.360 -23.053 30.951 1.00 19.66 ? 139 ASP   C C   1 
ATOM   2098 O  O   . ASP   B 1 133 ? 19.178 -22.490 32.041 1.00 20.90 ? 139 ASP   C O   1 
ATOM   2099 C  CB  . ASP   B 1 133 ? 21.734 -22.448 30.595 1.00 20.74 ? 139 ASP   C CB  1 
ATOM   2100 C  CG  . ASP   B 1 133 ? 21.397 -21.454 29.495 1.00 24.76 ? 139 ASP   C CG  1 
ATOM   2101 O  OD1 . ASP   B 1 133 ? 21.088 -21.914 28.358 1.00 23.52 ? 139 ASP   C OD1 1 
ATOM   2102 O  OD2 . ASP   B 1 133 ? 21.417 -20.215 29.779 1.00 25.21 ? 139 ASP   C OD2 1 
ATOM   2103 N  N   . LEU   B 1 134 ? 18.393 -23.162 30.021 1.00 18.98 ? 140 LEU   C N   1 
ATOM   2104 C  CA  . LEU   B 1 134 ? 17.046 -22.593 30.196 1.00 19.54 ? 140 LEU   C CA  1 
ATOM   2105 C  C   . LEU   B 1 134 ? 16.188 -23.581 30.962 1.00 20.43 ? 140 LEU   C C   1 
ATOM   2106 O  O   . LEU   B 1 134 ? 15.329 -24.288 30.401 1.00 20.56 ? 140 LEU   C O   1 
ATOM   2107 C  CB  . LEU   B 1 134 ? 16.441 -22.289 28.796 1.00 19.53 ? 140 LEU   C CB  1 
ATOM   2108 C  CG  . LEU   B 1 134 ? 17.294 -21.337 27.942 1.00 21.21 ? 140 LEU   C CG  1 
ATOM   2109 C  CD1 . LEU   B 1 134 ? 16.668 -21.157 26.538 1.00 22.24 ? 140 LEU   C CD1 1 
ATOM   2110 C  CD2 . LEU   B 1 134 ? 17.493 -19.973 28.641 1.00 22.01 ? 140 LEU   C CD2 1 
ATOM   2111 N  N   . LEU   B 1 135 ? 16.429 -23.641 32.279 1.00 19.69 ? 141 LEU   C N   1 
ATOM   2112 C  CA  . LEU   B 1 135 ? 15.773 -24.665 33.097 1.00 21.42 ? 141 LEU   C CA  1 
ATOM   2113 C  C   . LEU   B 1 135 ? 14.275 -24.505 33.170 1.00 23.09 ? 141 LEU   C C   1 
ATOM   2114 O  O   . LEU   B 1 135 ? 13.571 -25.506 33.357 1.00 25.11 ? 141 LEU   C O   1 
ATOM   2115 C  CB  . LEU   B 1 135 ? 16.378 -24.748 34.502 1.00 20.99 ? 141 LEU   C CB  1 
ATOM   2116 C  CG  . LEU   B 1 135 ? 17.890 -24.750 34.588 1.00 21.90 ? 141 LEU   C CG  1 
ATOM   2117 C  CD1 . LEU   B 1 135 ? 18.363 -24.896 36.035 1.00 24.20 ? 141 LEU   C CD1 1 
ATOM   2118 C  CD2 . LEU   B 1 135 ? 18.548 -25.829 33.685 1.00 21.47 ? 141 LEU   C CD2 1 
ATOM   2119 N  N   . TRP   B 1 136 ? 13.784 -23.249 33.046 1.00 22.69 ? 142 TRP   C N   1 
ATOM   2120 C  CA  . TRP   B 1 136 ? 12.351 -22.965 33.147 1.00 23.15 ? 142 TRP   C CA  1 
ATOM   2121 C  C   . TRP   B 1 136 ? 11.547 -23.570 31.968 1.00 24.13 ? 142 TRP   C C   1 
ATOM   2122 O  O   . TRP   B 1 136 ? 10.317 -23.606 32.044 1.00 25.54 ? 142 TRP   C O   1 
ATOM   2123 C  CB  . TRP   B 1 136 ? 12.128 -21.445 33.223 1.00 22.76 ? 142 TRP   C CB  1 
ATOM   2124 C  CG  . TRP   B 1 136 ? 12.820 -20.671 32.123 1.00 22.70 ? 142 TRP   C CG  1 
ATOM   2125 C  CD1 . TRP   B 1 136 ? 14.067 -20.118 32.158 1.00 23.28 ? 142 TRP   C CD1 1 
ATOM   2126 C  CD2 . TRP   B 1 136 ? 12.276 -20.363 30.818 1.00 21.92 ? 142 TRP   C CD2 1 
ATOM   2127 N  NE1 . TRP   B 1 136 ? 14.325 -19.467 30.960 1.00 23.63 ? 142 TRP   C NE1 1 
ATOM   2128 C  CE2 . TRP   B 1 136 ? 13.228 -19.594 30.136 1.00 22.78 ? 142 TRP   C CE2 1 
ATOM   2129 C  CE3 . TRP   B 1 136 ? 11.062 -20.664 30.173 1.00 22.33 ? 142 TRP   C CE3 1 
ATOM   2130 C  CZ2 . TRP   B 1 136 ? 13.012 -19.133 28.830 1.00 23.68 ? 142 TRP   C CZ2 1 
ATOM   2131 C  CZ3 . TRP   B 1 136 ? 10.825 -20.146 28.905 1.00 23.96 ? 142 TRP   C CZ3 1 
ATOM   2132 C  CH2 . TRP   B 1 136 ? 11.790 -19.382 28.253 1.00 23.87 ? 142 TRP   C CH2 1 
ATOM   2133 N  N   . LEU   B 1 137 ? 12.216 -24.041 30.888 1.00 23.71 ? 143 LEU   C N   1 
ATOM   2134 C  CA  . LEU   B 1 137 ? 11.460 -24.662 29.782 1.00 24.23 ? 143 LEU   C CA  1 
ATOM   2135 C  C   . LEU   B 1 137 ? 10.738 -25.942 30.268 1.00 28.90 ? 143 LEU   C C   1 
ATOM   2136 O  O   . LEU   B 1 137 ? 9.742  -26.323 29.654 1.00 30.94 ? 143 LEU   C O   1 
ATOM   2137 C  CB  . LEU   B 1 137 ? 12.419 -25.049 28.624 1.00 22.19 ? 143 LEU   C CB  1 
ATOM   2138 C  CG  . LEU   B 1 137 ? 12.940 -23.917 27.769 1.00 21.90 ? 143 LEU   C CG  1 
ATOM   2139 C  CD1 . LEU   B 1 137 ? 13.976 -24.437 26.785 1.00 21.02 ? 143 LEU   C CD1 1 
ATOM   2140 C  CD2 . LEU   B 1 137 ? 11.797 -23.196 26.980 1.00 22.67 ? 143 LEU   C CD2 1 
ATOM   2141 N  N   . ASP   B 1 138 ? 11.289 -26.605 31.306 1.00 31.43 ? 144 ASP   C N   1 
ATOM   2142 C  CA  . ASP   B 1 138 ? 10.851 -27.875 31.909 1.00 35.30 ? 144 ASP   C CA  1 
ATOM   2143 C  C   . ASP   B 1 138 ? 9.716  -27.740 32.895 1.00 39.06 ? 144 ASP   C C   1 
ATOM   2144 O  O   . ASP   B 1 138 ? 9.277  -28.765 33.409 1.00 40.05 ? 144 ASP   C O   1 
ATOM   2145 C  CB  . ASP   B 1 138 ? 11.996 -28.473 32.747 1.00 37.17 ? 144 ASP   C CB  1 
ATOM   2146 C  CG  . ASP   B 1 138 ? 13.135 -29.117 32.006 1.00 40.96 ? 144 ASP   C CG  1 
ATOM   2147 O  OD1 . ASP   B 1 138 ? 13.013 -29.309 30.781 1.00 42.09 ? 144 ASP   C OD1 1 
ATOM   2148 O  OD2 . ASP   B 1 138 ? 14.175 -29.421 32.660 1.00 43.49 ? 144 ASP   C OD2 1 
ATOM   2149 N  N   . GLU   B 1 139 ? 9.376  -26.515 33.315 1.00 40.73 ? 145 GLU   C N   1 
ATOM   2150 C  CA  . GLU   B 1 139 ? 8.350  -26.334 34.340 1.00 43.53 ? 145 GLU   C CA  1 
ATOM   2151 C  C   . GLU   B 1 139 ? 7.133  -25.588 33.822 1.00 45.58 ? 145 GLU   C C   1 
ATOM   2152 O  O   . GLU   B 1 139 ? 6.156  -25.451 34.569 1.00 47.43 ? 145 GLU   C O   1 
ATOM   2153 C  CB  . GLU   B 1 139 ? 8.944  -25.639 35.574 1.00 47.24 ? 145 GLU   C CB  1 
ATOM   2154 C  CG  . GLU   B 1 139 ? 9.472  -24.244 35.298 1.00 53.93 ? 145 GLU   C CG  1 
ATOM   2155 C  CD  . GLU   B 1 139 ? 10.349 -23.660 36.393 1.00 62.88 ? 145 GLU   C CD  1 
ATOM   2156 O  OE1 . GLU   B 1 139 ? 10.318 -22.420 36.585 1.00 64.20 ? 145 GLU   C OE1 1 
ATOM   2157 O  OE2 . GLU   B 1 139 ? 11.076 -24.440 37.051 1.00 65.09 ? 145 GLU   C OE2 1 
HETATM 2158 N  N1  . A1BSJ C 2 .   ? 10.894 14.634  17.498 0.80 25.95 ? 201 A1BSJ A N1  1 
HETATM 2159 C  C4  . A1BSJ C 2 .   ? 6.228  11.415  25.891 0.80 35.05 ? 201 A1BSJ A C4  1 
HETATM 2160 C  C5  . A1BSJ C 2 .   ? 6.720  12.413  25.069 0.80 35.65 ? 201 A1BSJ A C5  1 
HETATM 2161 C  C6  . A1BSJ C 2 .   ? 7.620  12.115  24.049 0.80 35.68 ? 201 A1BSJ A C6  1 
HETATM 2162 C  C7  . A1BSJ C 2 .   ? 8.032  13.164  23.044 0.80 36.48 ? 201 A1BSJ A C7  1 
HETATM 2163 C  C8  . A1BSJ C 2 .   ? 9.374  13.745  23.436 0.80 37.01 ? 201 A1BSJ A C8  1 
HETATM 2164 C  C10 . A1BSJ C 2 .   ? 12.068 15.179  21.753 0.80 32.34 ? 201 A1BSJ A C10 1 
HETATM 2165 C  C13 . A1BSJ C 2 .   ? 10.395 15.521  18.343 0.80 28.08 ? 201 A1BSJ A C13 1 
HETATM 2166 C  C15 . A1BSJ C 2 .   ? 8.944  15.663  21.909 0.80 33.69 ? 201 A1BSJ A C15 1 
HETATM 2167 O  O2  . A1BSJ C 2 .   ? 9.942  16.611  17.983 0.80 27.96 ? 201 A1BSJ A O2  1 
HETATM 2168 C  C12 . A1BSJ C 2 .   ? 10.414 15.125  19.810 0.80 30.33 ? 201 A1BSJ A C12 1 
HETATM 2169 C  C11 . A1BSJ C 2 .   ? 11.539 15.884  20.520 0.80 31.15 ? 201 A1BSJ A C11 1 
HETATM 2170 C  C9  . A1BSJ C 2 .   ? 11.181 15.295  22.972 0.80 33.43 ? 201 A1BSJ A C9  1 
HETATM 2171 C  C14 . A1BSJ C 2 .   ? 9.020  15.339  20.416 0.80 32.27 ? 201 A1BSJ A C14 1 
HETATM 2172 N  N   . A1BSJ C 2 .   ? 9.807  14.828  22.760 0.80 34.63 ? 201 A1BSJ A N   1 
HETATM 2173 O  O1  . A1BSJ C 2 .   ? 10.008 13.261  24.367 0.80 39.12 ? 201 A1BSJ A O1  1 
HETATM 2174 C  C1  . A1BSJ C 2 .   ? 8.056  10.796  23.910 0.80 34.45 ? 201 A1BSJ A C1  1 
HETATM 2175 O  O   . A1BSJ C 2 .   ? 9.015  10.603  22.952 0.80 33.49 ? 201 A1BSJ A O   1 
HETATM 2176 C  C   . A1BSJ C 2 .   ? 9.820  9.431   23.026 0.80 32.72 ? 201 A1BSJ A C   1 
HETATM 2177 C  C3  . A1BSJ C 2 .   ? 6.616  10.111  25.698 0.80 33.70 ? 201 A1BSJ A C3  1 
HETATM 2178 C  C2  . A1BSJ C 2 .   ? 7.535  9.791   24.709 0.80 34.12 ? 201 A1BSJ A C2  1 
HETATM 2179 ZN ZN  . ZN    D 3 .   ? 11.559 -4.690  5.580  1.00 21.44 2 202 ZN    A ZN  1 
HETATM 2180 S  S   . DMS   E 4 .   ? 20.213 0.202   20.730 0.00 39.98 ? 203 DMS   A S   1 
HETATM 2181 O  O   . DMS   E 4 .   ? 18.866 -0.453  20.647 0.00 24.73 ? 203 DMS   A O   1 
HETATM 2182 C  C1  . DMS   E 4 .   ? 20.267 1.141   22.280 0.00 38.84 ? 203 DMS   A C1  1 
HETATM 2183 C  C2  . DMS   E 4 .   ? 20.184 1.649   19.639 0.00 39.24 ? 203 DMS   A C2  1 
HETATM 2184 N  N1  . A1BSJ F 2 .   ? 22.925 -15.880 14.458 0.80 21.35 ? 201 A1BSJ C N1  1 
HETATM 2185 C  C4  . A1BSJ F 2 .   ? 26.636 -19.042 5.759  0.80 38.23 ? 201 A1BSJ C C4  1 
HETATM 2186 C  C5  . A1BSJ F 2 .   ? 26.162 -18.057 6.605  0.80 38.02 ? 201 A1BSJ C C5  1 
HETATM 2187 C  C6  . A1BSJ F 2 .   ? 25.417 -18.385 7.733  0.80 37.79 ? 201 A1BSJ C C6  1 
HETATM 2188 C  C7  . A1BSJ F 2 .   ? 25.088 -17.342 8.774  0.80 37.27 ? 201 A1BSJ C C7  1 
HETATM 2189 C  C8  . A1BSJ F 2 .   ? 23.698 -16.790 8.536  0.80 36.06 ? 201 A1BSJ C C8  1 
HETATM 2190 C  C10 . A1BSJ F 2 .   ? 21.213 -15.355 10.348 0.80 27.94 ? 201 A1BSJ C C10 1 
HETATM 2191 C  C13 . A1BSJ F 2 .   ? 23.181 -14.925 13.578 0.80 23.64 ? 201 A1BSJ C C13 1 
HETATM 2192 C  C15 . A1BSJ F 2 .   ? 24.324 -14.783 9.882  0.80 30.39 ? 201 A1BSJ C C15 1 
HETATM 2193 O  O2  . A1BSJ F 2 .   ? 23.550 -13.786 13.894 0.80 22.52 ? 201 A1BSJ C O2  1 
HETATM 2194 C  C12 . A1BSJ F 2 .   ? 23.041 -15.321 12.120 0.80 26.01 ? 201 A1BSJ C C12 1 
HETATM 2195 C  C11 . A1BSJ F 2 .   ? 21.793 -14.641 11.549 0.80 26.54 ? 201 A1BSJ C C11 1 
HETATM 2196 C  C9  . A1BSJ F 2 .   ? 22.003 -15.135 9.085  0.80 30.21 ? 201 A1BSJ C C9  1 
HETATM 2197 C  C14 . A1BSJ F 2 .   ? 24.351 -14.986 11.396 0.80 27.87 ? 201 A1BSJ C C14 1 
HETATM 2198 N  N   . A1BSJ F 2 .   ? 23.373 -15.648 9.175  0.80 32.09 ? 201 A1BSJ C N   1 
HETATM 2199 O  O1  . A1BSJ F 2 .   ? 22.942 -17.327 7.735  0.80 38.10 ? 201 A1BSJ C O1  1 
HETATM 2200 C  C1  . A1BSJ F 2 .   ? 25.101 -19.726 7.952  0.80 37.70 ? 201 A1BSJ C C1  1 
HETATM 2201 O  O   . A1BSJ F 2 .   ? 24.235 -19.949 8.991  0.80 36.93 ? 201 A1BSJ C O   1 
HETATM 2202 C  C   . A1BSJ F 2 .   ? 23.717 -21.262 9.169  0.80 36.00 ? 201 A1BSJ C C   1 
HETATM 2203 C  C3  . A1BSJ F 2 .   ? 26.381 -20.362 6.027  0.80 37.88 ? 201 A1BSJ C C3  1 
HETATM 2204 C  C2  . A1BSJ F 2 .   ? 25.612 -20.717 7.126  0.80 38.05 ? 201 A1BSJ C C2  1 
HETATM 2205 ZN ZN  . ZN    G 3 .   ? 24.109 -34.695 27.006 1.00 17.44 2 202 ZN    C ZN  1 
HETATM 2206 S  S   . DMS   H 4 .   ? 14.502 -30.830 12.974 0.00 39.98 ? 203 DMS   C S   1 
HETATM 2207 O  O   . DMS   H 4 .   ? 15.994 -30.851 13.118 0.00 24.73 ? 203 DMS   C O   1 
HETATM 2208 C  C1  . DMS   H 4 .   ? 14.126 -30.554 11.222 0.00 38.84 ? 203 DMS   C C1  1 
HETATM 2209 C  C2  . DMS   H 4 .   ? 13.923 -29.209 13.543 0.00 39.24 ? 203 DMS   C C2  1 
HETATM 2210 O  O   . HOH   I 5 .   ? 3.144  8.082   9.428  1.00 53.00 ? 301 HOH   A O   1 
HETATM 2211 O  O   . HOH   I 5 .   ? 33.873 17.988  18.972 1.00 45.63 ? 302 HOH   A O   1 
HETATM 2212 O  O   . HOH   I 5 .   ? 6.212  17.170  21.486 1.00 69.02 ? 303 HOH   A O   1 
HETATM 2213 O  O   . HOH   I 5 .   ? 18.633 -2.313  18.890 1.00 41.42 ? 304 HOH   A O   1 
HETATM 2214 O  O   . HOH   I 5 .   ? 10.911 8.268   4.336  1.00 27.44 ? 305 HOH   A O   1 
HETATM 2215 O  O   . HOH   I 5 .   ? 3.652  -4.394  20.928 1.00 34.91 ? 306 HOH   A O   1 
HETATM 2216 O  O   . HOH   I 5 .   ? 0.836  -2.158  19.620 1.00 44.96 ? 307 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 23.529 22.137  8.103  1.00 28.40 ? 308 HOH   A O   1 
HETATM 2218 O  O   . HOH   I 5 .   ? 12.132 7.620   30.993 1.00 34.12 ? 309 HOH   A O   1 
HETATM 2219 O  O   . HOH   I 5 .   ? 18.517 0.173   27.779 1.00 36.63 ? 310 HOH   A O   1 
HETATM 2220 O  O   . HOH   I 5 .   ? 19.748 9.437   19.132 1.00 17.95 ? 311 HOH   A O   1 
HETATM 2221 O  O   . HOH   I 5 .   ? 0.233  0.132   15.964 1.00 18.43 ? 312 HOH   A O   1 
HETATM 2222 O  O   . HOH   I 5 .   ? 28.313 3.848   3.641  1.00 47.38 ? 313 HOH   A O   1 
HETATM 2223 O  O   . HOH   I 5 .   ? 4.988  7.944   28.189 1.00 41.61 ? 314 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 10.769 4.855   3.251  1.00 30.38 ? 315 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 23.538 0.607   16.605 1.00 31.80 ? 316 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 7.610  19.884  17.418 1.00 32.10 ? 317 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 12.633 9.673   29.612 1.00 33.51 ? 318 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 6.069  -5.341  28.868 1.00 34.56 ? 319 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 31.963 9.304   6.510  1.00 46.18 ? 320 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 13.692 11.276  0.199  1.00 45.01 ? 321 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 25.803 4.802   20.499 1.00 46.19 ? 322 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 17.572 21.560  9.422  1.00 22.61 ? 323 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 3.500  -1.612  2.822  1.00 50.62 ? 324 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? -0.279 15.781  7.183  1.00 54.94 ? 325 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 16.905 -6.720  11.113 1.00 26.07 ? 326 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 21.543 2.700   -1.513 1.00 56.11 ? 327 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 21.131 19.488  17.831 1.00 35.33 ? 328 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 11.186 11.885  11.142 1.00 16.94 ? 329 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 22.242 18.498  19.322 1.00 37.28 ? 330 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 2.547  3.746   27.329 1.00 34.47 ? 331 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 9.073  18.722  19.581 1.00 34.32 ? 332 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 5.531  -6.085  7.176  1.00 45.50 ? 333 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 23.079 -0.837  4.556  1.00 31.97 ? 334 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 30.018 11.719  2.691  1.00 56.90 ? 335 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 6.002  17.879  24.153 1.00 48.48 ? 336 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 11.035 2.651   33.416 1.00 19.30 ? 337 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 17.330 1.254   30.136 1.00 35.29 ? 338 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 29.806 11.786  20.300 1.00 40.94 ? 339 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 14.482 3.003   23.209 1.00 16.31 ? 340 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 29.695 3.971   11.489 1.00 29.61 ? 341 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? 30.547 10.951  14.656 1.00 40.96 ? 342 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 4.990  -1.193  24.125 1.00 27.98 ? 343 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 3.255  0.980   30.798 1.00 41.01 ? 344 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 17.480 19.280  16.977 1.00 19.30 ? 345 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 36.540 16.609  12.177 1.00 35.05 ? 346 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 7.724  20.399  8.163  1.00 58.72 ? 347 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 12.549 -5.086  32.093 1.00 44.20 ? 348 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 14.614 12.683  23.976 1.00 23.56 ? 349 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? -0.106 -5.423  10.829 1.00 46.90 ? 350 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 9.083  2.438   2.668  1.00 30.22 ? 351 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 23.197 14.020  23.868 1.00 56.87 ? 352 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 6.621  4.045   32.891 1.00 28.70 ? 353 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 30.595 20.832  10.904 1.00 34.53 ? 354 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 31.206 18.922  8.967  1.00 37.58 ? 355 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 17.853 5.352   26.737 1.00 29.27 ? 356 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 3.864  6.176   24.728 1.00 23.22 ? 357 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 17.344 2.995   23.272 1.00 23.62 ? 358 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 30.305 4.906   4.401  1.00 43.39 ? 359 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 4.214  -4.834  6.149  1.00 34.81 ? 360 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 13.062 10.775  9.208  1.00 16.26 ? 361 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 14.374 21.400  8.228  1.00 46.40 ? 362 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 6.307  1.651   5.649  1.00 25.89 ? 363 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 34.565 20.682  11.628 1.00 51.15 ? 364 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 13.965 -11.217 3.663  1.00 66.53 ? 365 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 14.681 -4.129  17.213 1.00 26.17 ? 366 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 0.190  4.550   6.332  1.00 29.61 ? 367 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 15.271 -5.135  -0.248 1.00 45.72 ? 368 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 7.538  -7.734  24.145 1.00 36.89 ? 369 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 24.245 18.042  3.785  1.00 52.53 ? 370 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 4.946  7.230   2.665  1.00 43.75 ? 371 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 18.121 9.862   25.726 1.00 26.55 ? 372 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 2.721  9.651   27.876 1.00 42.68 ? 373 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 19.873 -3.053  16.535 1.00 32.34 ? 374 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 9.841  -7.784  7.811  1.00 35.47 ? 375 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 10.076 9.613   31.263 1.00 54.36 ? 376 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 22.044 3.937   23.901 1.00 44.84 ? 377 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 35.004 -0.869  13.239 1.00 66.38 ? 378 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 31.301 3.347   13.609 1.00 39.36 ? 379 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 4.044  -2.129  20.745 1.00 34.54 ? 380 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 9.613  5.043   33.826 1.00 26.36 ? 381 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 6.521  -1.173  -2.957 1.00 72.36 ? 382 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 16.435 -4.417  1.993  1.00 29.53 ? 383 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? -0.925 15.322  12.014 1.00 34.42 ? 384 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 30.612 21.180  16.952 1.00 44.07 ? 385 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 16.847 20.602  19.228 1.00 30.12 ? 386 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 18.966 12.990  1.722  1.00 45.63 ? 387 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 1.726  -1.794  17.309 1.00 24.77 ? 388 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 8.763  -7.433  9.666  1.00 41.41 ? 389 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 11.774 21.881  11.879 1.00 35.18 ? 390 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 30.868 15.485  22.040 1.00 33.08 ? 391 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 3.532  14.035  22.883 1.00 65.70 ? 392 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 34.905 15.802  9.644  1.00 53.85 ? 393 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 14.572 14.902  3.616  1.00 34.51 ? 394 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 21.362 9.365   21.444 1.00 25.87 ? 395 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 32.219 2.187   4.187  1.00 52.63 ? 396 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 7.844  8.777   32.645 1.00 71.83 ? 397 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 19.382 24.024  15.580 1.00 27.93 ? 398 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 23.495 2.987   20.141 1.00 34.09 ? 399 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 22.372 19.405  6.081  1.00 32.14 ? 400 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 12.207 -7.635  13.162 1.00 37.83 ? 401 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 19.420 16.065  26.362 1.00 63.22 ? 402 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 35.989 3.081   4.008  1.00 59.32 ? 403 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 18.580 -4.880  26.956 1.00 65.23 ? 404 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 22.423 -1.743  16.810 1.00 40.88 ? 405 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 30.039 11.280  17.804 1.00 49.59 ? 406 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 27.876 17.047  23.792 1.00 40.49 ? 407 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 2.677  -6.159  14.726 1.00 46.91 ? 408 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 11.340 19.864  4.955  1.00 57.90 ? 409 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 1.838  6.252   28.054 1.00 47.16 ? 410 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 5.491  13.803  20.599 1.00 43.28 ? 411 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 4.344  -1.058  28.832 1.00 52.17 ? 412 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 16.570 -6.784  26.119 1.00 71.54 ? 413 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 18.470 -4.378  19.986 1.00 34.88 ? 414 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 29.147 3.126   20.225 1.00 73.35 ? 415 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 18.356 7.855   28.082 1.00 53.21 ? 416 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 8.879  19.520  29.358 1.00 92.74 ? 417 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 3.851  -2.058  26.534 1.00 44.11 ? 418 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 1.694  1.579   26.300 1.00 36.47 ? 419 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 32.463 22.120  23.992 1.00 65.01 ? 420 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 2.484  12.278  26.917 1.00 54.09 ? 421 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 16.644 11.982  26.090 1.00 44.33 ? 422 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 20.883 22.435  17.764 1.00 32.60 ? 423 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 0.102  12.629  20.590 1.00 51.57 ? 424 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 31.423 11.321  5.161  1.00 58.70 ? 425 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 6.512  2.585   3.103  1.00 37.44 ? 426 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 0.925  -1.290  23.331 1.00 32.02 ? 427 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 32.534 22.053  20.251 1.00 47.60 ? 428 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 9.487  7.767   2.021  1.00 60.53 ? 429 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 3.256  -2.997  22.794 1.00 40.25 ? 430 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 30.077 16.373  25.198 1.00 86.91 ? 431 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 31.772 10.094  0.163  1.00 59.68 ? 432 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 1.686  -4.824  6.894  1.00 54.84 ? 433 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 37.749 7.775   6.683  1.00 88.36 ? 434 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 29.370 0.648   17.014 1.00 74.86 ? 435 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 27.558 0.519   19.281 1.00 56.75 ? 436 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 4.791  -7.724  25.110 1.00 65.56 ? 437 HOH   A O   1 
HETATM 2347 O  O   . HOH   J 5 .   ? 14.329 -7.567  24.852 1.00 33.10 ? 301 HOH   C O   1 
HETATM 2348 O  O   . HOH   J 5 .   ? 31.955 -21.929 22.126 1.00 33.12 ? 302 HOH   C O   1 
HETATM 2349 O  O   . HOH   J 5 .   ? 11.037 -8.421  24.637 1.00 26.61 ? 303 HOH   C O   1 
HETATM 2350 O  O   . HOH   J 5 .   ? 24.160 -26.416 -1.108 1.00 47.73 ? 304 HOH   C O   1 
HETATM 2351 O  O   . HOH   J 5 .   ? 15.955 -10.808 5.299  1.00 45.52 ? 305 HOH   C O   1 
HETATM 2352 O  O   . HOH   J 5 .   ? 5.707  -25.644 37.103 1.00 71.81 ? 306 HOH   C O   1 
HETATM 2353 O  O   . HOH   J 5 .   ? 24.480 -21.893 27.771 1.00 24.82 ? 307 HOH   C O   1 
HETATM 2354 O  O   . HOH   J 5 .   ? 7.311  -26.883 30.388 1.00 46.03 ? 308 HOH   C O   1 
HETATM 2355 O  O   . HOH   J 5 .   ? 18.069 -6.276  3.247  1.00 34.89 ? 309 HOH   C O   1 
HETATM 2356 O  O   . HOH   J 5 .   ? 14.115 -21.536 13.908 1.00 17.41 ? 310 HOH   C O   1 
HETATM 2357 O  O   . HOH   J 5 .   ? 30.467 -35.065 11.073 1.00 33.60 ? 311 HOH   C O   1 
HETATM 2358 O  O   . HOH   J 5 .   ? 0.256  -10.089 22.188 1.00 51.01 ? 312 HOH   C O   1 
HETATM 2359 O  O   . HOH   J 5 .   ? 22.464 -28.462 -0.874 1.00 26.27 ? 313 HOH   C O   1 
HETATM 2360 O  O   . HOH   J 5 .   ? 17.538 -36.749 29.616 1.00 39.94 ? 314 HOH   C O   1 
HETATM 2361 O  O   . HOH   J 5 .   ? 36.073 -30.533 27.753 1.00 40.77 ? 315 HOH   C O   1 
HETATM 2362 O  O   . HOH   J 5 .   ? 22.761 -19.333 31.925 1.00 43.73 ? 316 HOH   C O   1 
HETATM 2363 O  O   . HOH   J 5 .   ? 20.384 -18.661 31.709 1.00 42.60 ? 317 HOH   C O   1 
HETATM 2364 O  O   . HOH   J 5 .   ? 8.338  -21.848 32.939 1.00 44.95 ? 318 HOH   C O   1 
HETATM 2365 O  O   . HOH   J 5 .   ? 11.053 -30.310 17.413 1.00 33.30 ? 319 HOH   C O   1 
HETATM 2366 O  O   . HOH   J 5 .   ? 30.886 -22.413 28.812 1.00 33.64 ? 320 HOH   C O   1 
HETATM 2367 O  O   . HOH   J 5 .   ? 33.976 -15.492 14.723 1.00 43.36 ? 321 HOH   C O   1 
HETATM 2368 O  O   . HOH   J 5 .   ? 24.781 -25.253 28.945 1.00 21.87 ? 322 HOH   C O   1 
HETATM 2369 O  O   . HOH   J 5 .   ? 5.272  -26.977 22.718 1.00 28.11 ? 323 HOH   C O   1 
HETATM 2370 O  O   . HOH   J 5 .   ? 24.065 -11.693 12.240 1.00 26.92 ? 324 HOH   C O   1 
HETATM 2371 O  O   . HOH   J 5 .   ? 14.920 -30.850 5.438  1.00 38.18 ? 325 HOH   C O   1 
HETATM 2372 O  O   . HOH   J 5 .   ? 11.648 -35.245 20.446 1.00 49.16 ? 326 HOH   C O   1 
HETATM 2373 O  O   . HOH   J 5 .   ? 23.614 -12.859 26.814 1.00 59.84 ? 327 HOH   C O   1 
HETATM 2374 O  O   . HOH   J 5 .   ? 15.387 -35.364 5.551  1.00 60.61 ? 328 HOH   C O   1 
HETATM 2375 O  O   . HOH   J 5 .   ? 3.712  -20.160 19.552 1.00 36.13 ? 329 HOH   C O   1 
HETATM 2376 O  O   . HOH   J 5 .   ? 16.838 -9.144  23.296 1.00 20.61 ? 330 HOH   C O   1 
HETATM 2377 O  O   . HOH   J 5 .   ? 7.988  -26.284 13.247 1.00 45.34 ? 331 HOH   C O   1 
HETATM 2378 O  O   . HOH   J 5 .   ? 18.555 -18.045 8.502  1.00 27.59 ? 332 HOH   C O   1 
HETATM 2379 O  O   . HOH   J 5 .   ? 26.346 -27.416 29.603 1.00 23.81 ? 333 HOH   C O   1 
HETATM 2380 O  O   . HOH   J 5 .   ? 23.314 -18.594 21.013 1.00 17.69 ? 334 HOH   C O   1 
HETATM 2381 O  O   . HOH   J 5 .   ? 37.943 -17.861 4.918  1.00 41.40 ? 335 HOH   C O   1 
HETATM 2382 O  O   . HOH   J 5 .   ? 25.810 -10.440 14.307 1.00 26.97 ? 336 HOH   C O   1 
HETATM 2383 O  O   . HOH   J 5 .   ? 29.587 -24.340 7.567  1.00 36.55 ? 337 HOH   C O   1 
HETATM 2384 O  O   . HOH   J 5 .   ? 33.859 -30.464 15.477 1.00 18.27 ? 338 HOH   C O   1 
HETATM 2385 O  O   . HOH   J 5 .   ? 19.350 -27.856 9.436  1.00 18.52 ? 339 HOH   C O   1 
HETATM 2386 O  O   . HOH   J 5 .   ? 11.360 -12.275 13.489 1.00 39.97 ? 340 HOH   C O   1 
HETATM 2387 O  O   . HOH   J 5 .   ? 18.051 -13.181 28.417 1.00 51.17 ? 341 HOH   C O   1 
HETATM 2388 O  O   . HOH   J 5 .   ? 22.178 -5.273  10.457 1.00 32.94 ? 342 HOH   C O   1 
HETATM 2389 O  O   . HOH   J 5 .   ? 16.438 -27.826 9.662  1.00 27.91 ? 343 HOH   C O   1 
HETATM 2390 O  O   . HOH   J 5 .   ? 12.571 -31.312 28.870 1.00 31.24 ? 344 HOH   C O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 3.870  -19.239 13.660 1.00 40.14 ? 345 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 5.359  -18.862 30.831 1.00 56.11 ? 346 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 23.576 -35.468 1.081  1.00 38.04 ? 347 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 20.236 -9.239  24.049 1.00 39.12 ? 348 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 12.456 -11.386 15.219 1.00 31.26 ? 349 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 9.727  -19.813 12.155 1.00 53.26 ? 350 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 16.234 -11.487 15.592 1.00 20.61 ? 351 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 15.074 -21.340 7.120  1.00 39.59 ? 352 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 3.401  -9.782  16.277 1.00 29.59 ? 353 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 18.242 -37.352 22.087 1.00 35.93 ? 354 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 20.188 -21.611 2.487  1.00 39.82 ? 355 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 23.649 -34.858 33.050 1.00 33.24 ? 356 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 31.146 -13.958 6.265  1.00 64.09 ? 357 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? -0.312 -23.965 19.630 1.00 71.67 ? 358 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 26.680 -34.083 32.079 1.00 26.24 ? 359 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 8.151  -32.323 19.028 1.00 39.12 ? 360 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 12.803 -13.974 8.978  1.00 46.33 ? 361 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 21.687 -19.669 23.152 1.00 15.74 ? 362 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 33.619 -32.756 12.242 1.00 36.30 ? 363 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 13.926 -14.500 6.536  1.00 63.80 ? 364 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 4.958  -9.104  22.440 1.00 46.46 ? 365 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 27.836 -36.110 3.454  1.00 44.93 ? 366 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 34.035 -28.357 7.543  1.00 39.64 ? 367 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 30.944 -35.170 25.740 1.00 29.84 ? 368 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 8.191  -31.966 26.868 1.00 54.10 ? 369 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 16.133 -29.783 2.534  1.00 44.96 ? 370 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 35.096 -14.522 18.441 1.00 34.25 ? 371 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 29.126 -28.098 25.246 1.00 20.97 ? 372 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 3.282  -27.750 20.802 1.00 47.07 ? 373 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 15.232 -26.148 6.882  1.00 42.91 ? 374 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 29.009 -31.697 8.116  1.00 28.97 ? 375 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 4.983  -25.664 29.900 1.00 46.36 ? 376 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 21.557 -11.468 5.833  1.00 52.74 ? 377 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 36.835 -29.216 24.021 1.00 24.72 ? 378 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 16.414 -10.172 13.450 1.00 33.85 ? 379 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 13.268 -26.387 37.176 1.00 50.60 ? 380 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 28.149 -17.289 26.679 1.00 27.02 ? 381 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 3.324  -25.184 35.298 1.00 56.96 ? 382 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 19.758 -34.768 15.576 1.00 25.16 ? 383 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 24.088 -14.211 29.103 1.00 46.25 ? 384 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 19.519 -34.636 30.893 1.00 26.56 ? 385 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 29.741 -16.819 7.305  1.00 58.76 ? 386 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 16.443 -17.425 31.316 1.00 42.19 ? 387 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 24.761 -40.078 31.306 1.00 52.68 ? 388 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 32.849 -16.713 26.440 1.00 34.01 ? 389 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 16.740 -11.044 27.288 1.00 47.62 ? 390 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 3.288  -21.089 27.772 1.00 50.09 ? 391 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 24.980 -8.999  21.193 1.00 51.18 ? 392 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 4.033  -29.099 31.020 1.00 69.30 ? 393 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 18.398 -6.617  17.931 1.00 47.98 ? 394 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 20.402 -15.514 28.737 1.00 31.61 ? 395 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 12.301 -11.322 26.921 1.00 30.72 ? 396 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 15.246 -6.600  17.275 1.00 25.90 ? 397 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 5.978  -32.348 20.162 1.00 48.89 ? 398 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 22.395 -8.674  20.256 1.00 40.18 ? 399 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 5.404  -13.805 10.050 1.00 43.73 ? 400 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 33.167 -32.940 14.704 1.00 28.20 ? 401 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 25.989 -37.720 23.032 1.00 33.12 ? 402 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 28.249 -7.221  21.125 1.00 42.05 ? 403 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 10.481 -28.170 13.733 1.00 31.92 ? 404 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 13.094 -35.662 22.687 1.00 41.70 ? 405 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 30.358 -32.496 10.363 1.00 42.51 ? 406 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 2.532  -15.763 11.947 1.00 31.77 ? 407 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 30.700 -27.558 32.457 1.00 56.17 ? 408 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? -1.820 -22.890 26.720 1.00 78.17 ? 409 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 12.198 -21.560 11.853 1.00 27.00 ? 410 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 29.102 -27.452 28.354 1.00 52.24 ? 411 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 30.381 -19.492 12.994 1.00 41.04 ? 412 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 22.501 -38.165 19.616 1.00 39.83 ? 413 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 17.425 -21.018 34.349 1.00 37.49 ? 414 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 17.460 -33.410 14.805 1.00 39.53 ? 415 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 21.198 -41.419 28.496 1.00 59.94 ? 416 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 27.624 -35.628 29.594 1.00 31.47 ? 417 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 13.980 -8.459  14.940 1.00 41.61 ? 418 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 15.286 -21.121 35.274 1.00 44.58 ? 419 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 9.912  -23.409 12.524 1.00 46.03 ? 420 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 26.155 -35.196 0.369  1.00 46.70 ? 421 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 25.757 -7.461  5.878  1.00 61.36 ? 422 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 27.857 -18.885 28.468 1.00 59.38 ? 423 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 17.954 -19.112 32.694 1.00 49.03 ? 424 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 3.832  -23.252 30.592 1.00 57.31 ? 425 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 6.765  -29.630 30.764 1.00 61.40 ? 426 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 16.386 -19.322 6.699  1.00 47.17 ? 427 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 3.771  -30.035 19.529 1.00 61.97 ? 428 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 10.331 -15.184 8.899  1.00 51.58 ? 429 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 0.469  -31.033 31.534 1.00 76.65 ? 430 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 18.973 -39.232 29.527 1.00 52.37 ? 431 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? -0.824 -22.806 29.598 1.00 77.03 ? 432 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 5.564  -28.311 12.923 1.00 73.66 ? 433 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 30.171 -17.363 28.333 1.00 65.15 ? 434 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 18.566 -39.753 21.260 1.00 55.78 ? 435 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 36.198 -23.837 4.144  1.00 50.32 ? 436 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 12.446 -35.260 0.565  1.00 58.26 ? 437 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 26.098 -22.876 29.878 1.00 38.10 ? 438 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 27.898 -38.494 30.136 1.00 69.48 ? 439 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 1.734  -8.411  18.278 1.00 39.79 ? 440 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 37.005 -15.601 3.688  1.00 53.01 ? 441 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 33.714 -5.181  20.860 1.00 56.07 ? 442 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 2.731  -21.659 17.269 1.00 44.96 ? 443 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 11.666 -20.325 9.071  1.00 61.14 ? 444 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 31.591 -5.793  18.570 1.00 74.07 ? 445 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 13.824 -18.483 35.514 1.00 50.19 ? 446 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 30.147 -17.521 4.702  1.00 54.43 ? 447 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 33.995 -9.189  24.581 1.00 65.77 ? 448 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 6.204  -30.336 15.451 1.00 65.06 ? 449 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? -0.835 -9.237  24.593 1.00 68.89 ? 450 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 3.798  -29.339 16.325 1.00 72.27 ? 451 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 24.799 -7.926  26.089 1.00 65.32 ? 452 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? -0.871 -9.375  17.048 1.00 36.06 ? 453 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   ? 0.2876 0.3033 0.2740 -0.0139 -0.0264 -0.0209 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2786 0.2995 0.2813 -0.0116 -0.0305 -0.0176 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2799 0.3047 0.2934 -0.0059 -0.0300 -0.0112 7   SER   A C   
4    O O   . SER   A 1   ? 0.2876 0.3111 0.2949 -0.0046 -0.0288 -0.0085 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3139 0.3376 0.3148 -0.0175 -0.0405 -0.0157 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3668 0.3929 0.3615 -0.0189 -0.0468 -0.0091 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2552 0.2836 0.2843 -0.0031 -0.0297 -0.0094 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2341 0.2644 0.2734 0.0014  -0.0273 -0.0048 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2142 0.2459 0.2657 0.0035  -0.0223 -0.0058 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2202 0.2509 0.2711 0.0025  -0.0197 -0.0093 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1894 0.2225 0.2516 0.0063  -0.0198 -0.0025 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2084 0.2423 0.2800 0.0072  -0.0140 -0.0034 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2097 0.2405 0.2842 0.0094  -0.0070 -0.0021 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2230 0.2522 0.2988 0.0113  -0.0078 0.0007  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2150 0.2549 0.3023 0.0067  -0.0176 -0.0018 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1840 0.2131 0.2591 0.0083  0.0001  -0.0039 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1893 0.2137 0.2656 0.0085  0.0087  -0.0044 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1941 0.2219 0.2880 0.0098  0.0127  -0.0037 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1932 0.2250 0.2912 0.0081  0.0119  -0.0041 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1894 0.2097 0.2517 0.0042  0.0139  -0.0067 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1917 0.2111 0.2405 0.0028  0.0094  -0.0063 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2151 0.2284 0.2747 0.0023  0.0238  -0.0087 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2062 0.2250 0.2449 -0.0022 0.0115  -0.0061 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2030 0.2292 0.3093 0.0130  0.0177  -0.0022 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2059 0.2358 0.3323 0.0146  0.0235  -0.0013 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2218 0.2430 0.3455 0.0134  0.0379  -0.0052 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2498 0.2643 0.3748 0.0157  0.0429  -0.0054 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2030 0.2394 0.3516 0.0194  0.0181  0.0049  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2181 0.2628 0.3672 0.0182  0.0038  0.0084  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2428 0.2861 0.3783 0.0176  -0.0048 0.0098  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2277 0.2806 0.3885 0.0164  -0.0003 0.0095  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2643 0.3132 0.3962 0.0147  -0.0166 0.0115  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2495 0.3081 0.4078 0.0135  -0.0129 0.0114  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2694 0.3255 0.4121 0.0124  -0.0206 0.0120  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3152 0.3750 0.4513 0.0079  -0.0316 0.0124  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2276 0.2473 0.3449 0.0088  0.0449  -0.0085 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2450 0.2548 0.3543 0.0050  0.0596  -0.0135 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2590 0.2719 0.3816 0.0040  0.0684  -0.0142 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2638 0.2833 0.3864 0.0016  0.0634  -0.0125 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2755 0.2791 0.3558 -0.0027 0.0591  -0.0164 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2786 0.2896 0.3530 -0.0055 0.0498  -0.0135 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3052 0.2984 0.3728 -0.0096 0.0738  -0.0219 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2737 0.2820 0.4108 0.0062  0.0821  -0.0164 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2726 0.2842 0.4249 0.0052  0.0925  -0.0171 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2686 0.2951 0.4441 0.0092  0.0816  -0.0106 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2689 0.3021 0.4601 0.0150  0.0714  -0.0054 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2611 0.2924 0.4355 0.0048  0.0816  -0.0104 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2567 0.3011 0.4504 0.0069  0.0706  -0.0049 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2379 0.2838 0.4135 0.0034  0.0568  -0.0041 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2434 0.2959 0.4258 0.0013  0.0516  -0.0020 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2861 0.3356 0.4984 0.0052  0.0806  -0.0043 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3620 0.4129 0.6018 0.0106  0.0930  -0.0036 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3894 0.4497 0.6556 0.0167  0.0858  0.0025  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3839 0.4252 0.6181 0.0078  0.1119  -0.0093 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2163 0.2562 0.3712 0.0032  0.0512  -0.0055 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2026 0.2431 0.3420 0.0007  0.0400  -0.0049 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1889 0.2303 0.3254 0.0044  0.0293  -0.0038 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1918 0.2299 0.3283 0.0074  0.0314  -0.0039 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2161 0.2486 0.3308 -0.0048 0.0441  -0.0071 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2274 0.2582 0.3383 -0.0108 0.0532  -0.0074 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2412 0.2777 0.3628 -0.0122 0.0512  -0.0048 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2639 0.2865 0.3593 -0.0160 0.0644  -0.0105 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2607 0.2955 0.3777 -0.0185 0.0595  -0.0043 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2874 0.3079 0.3764 -0.0231 0.0732  -0.0107 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2906 0.3176 0.3909 -0.0240 0.0707  -0.0071 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3308 0.3559 0.4243 -0.0315 0.0792  -0.0063 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1804 0.2249 0.3132 0.0035  0.0189  -0.0030 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1906 0.2350 0.3161 0.0051  0.0095  -0.0027 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1897 0.2299 0.2979 0.0023  0.0076  -0.0045 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1897 0.2308 0.2996 -0.0002 0.0070  -0.0044 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1941 0.2458 0.3328 0.0053  0.0000  -0.0005 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2427 0.2933 0.3696 0.0042  -0.0096 -0.0015 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2326 0.2900 0.3700 0.0022  -0.0193 0.0009  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2656 0.3201 0.3903 -0.0019 -0.0257 -0.0027 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3107 0.3637 0.4237 -0.0038 -0.0327 -0.0033 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3274 0.3822 0.4401 -0.0015 -0.0354 0.0009  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3049 0.3536 0.4060 -0.0084 -0.0360 -0.0080 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1900 0.2259 0.2839 0.0027  0.0071  -0.0053 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1798 0.2132 0.2615 0.0008  0.0054  -0.0055 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1788 0.2122 0.2565 0.0023  -0.0012 -0.0067 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1774 0.2101 0.2512 0.0040  -0.0030 -0.0067 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1792 0.2085 0.2477 -0.0013 0.0099  -0.0051 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1789 0.2082 0.2399 -0.0035 0.0074  -0.0030 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1887 0.2157 0.2571 -0.0042 0.0183  -0.0054 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1642 0.1975 0.2426 0.0013  -0.0040 -0.0078 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1725 0.2042 0.2453 0.0015  -0.0083 -0.0103 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1644 0.1930 0.2337 0.0012  -0.0063 -0.0110 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1683 0.1971 0.2423 0.0006  -0.0036 -0.0083 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1948 0.2280 0.2736 -0.0004 -0.0134 -0.0125 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2215 0.2595 0.3071 0.0003  -0.0169 -0.0098 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1973 0.2304 0.2858 -0.0022 -0.0119 -0.0128 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1594 0.1853 0.2219 0.0015  -0.0071 -0.0139 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1648 0.1875 0.2291 0.0018  -0.0038 -0.0148 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1698 0.1897 0.2428 0.0002  -0.0036 -0.0171 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1756 0.1943 0.2475 -0.0023 -0.0069 -0.0210 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1785 0.1974 0.2339 0.0017  -0.0028 -0.0193 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1930 0.2140 0.2404 0.0029  -0.0025 -0.0169 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2042 0.2261 0.2441 0.0022  -0.0059 -0.0171 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1864 0.2089 0.2369 0.0043  0.0009  -0.0137 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1536 0.1727 0.2356 0.0010  -0.0006 -0.0138 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1603 0.1755 0.2517 -0.0007 0.0002  -0.0154 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1794 0.1870 0.2671 -0.0027 0.0013  -0.0237 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2105 0.2155 0.3001 -0.0064 -0.0008 -0.0275 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1484 0.1633 0.2505 0.0006  0.0033  -0.0090 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1745 0.1854 0.2875 -0.0014 0.0042  -0.0090 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1771 0.1872 0.3018 0.0004  0.0070  -0.0012 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1998 0.2059 0.3363 -0.0014 0.0081  0.0012  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1911 0.1880 0.3359 -0.0015 0.0117  -0.0036 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2198 0.2100 0.3605 -0.0004 0.0151  -0.0121 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2080 0.2010 0.3644 -0.0033 0.0127  -0.0002 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1824 0.1865 0.2636 -0.0013 0.0048  -0.0268 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2015 0.1962 0.2762 -0.0045 0.0081  -0.0359 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2254 0.2204 0.2855 -0.0098 0.0018  -0.0407 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2760 0.2628 0.3279 -0.0152 0.0030  -0.0487 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2152 0.2053 0.2890 -0.0017 0.0161  -0.0381 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2306 0.2250 0.2920 -0.0010 0.0149  -0.0375 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2311 0.2342 0.2959 0.0027  0.0130  -0.0294 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2437 0.2343 0.2885 -0.0046 0.0154  -0.0438 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2418 0.2457 0.2937 0.0019  0.0127  -0.0311 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2504 0.2474 0.2899 -0.0024 0.0139  -0.0392 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2107 0.2144 0.2681 -0.0091 -0.0048 -0.0357 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2160 0.2224 0.2638 -0.0137 -0.0124 -0.0371 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2163 0.2293 0.2752 -0.0152 -0.0187 -0.0333 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2437 0.2612 0.2996 -0.0187 -0.0262 -0.0320 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2121 0.2227 0.2508 -0.0116 -0.0145 -0.0336 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2406 0.2457 0.2681 -0.0110 -0.0084 -0.0371 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2505 0.2601 0.2699 -0.0094 -0.0111 -0.0327 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2601 0.2558 0.2744 -0.0178 -0.0064 -0.0461 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2113 0.2257 0.2841 -0.0128 -0.0156 -0.0305 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2001 0.2213 0.2849 -0.0141 -0.0197 -0.0268 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2205 0.2404 0.3049 -0.0215 -0.0257 -0.0308 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2306 0.2416 0.3086 -0.0255 -0.0237 -0.0373 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1995 0.2204 0.2963 -0.0120 -0.0145 -0.0237 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2287 0.2574 0.3210 -0.0234 -0.0325 -0.0268 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2450 0.2752 0.3380 -0.0318 -0.0406 -0.0288 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2614 0.2921 0.3695 -0.0344 -0.0393 -0.0288 24  THR   A C   
137  O O   . THR   A 18  ? 0.2582 0.2898 0.3769 -0.0294 -0.0328 -0.0259 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2657 0.3074 0.3638 -0.0326 -0.0499 -0.0220 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2592 0.3101 0.3779 -0.0272 -0.0477 -0.0152 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2897 0.3307 0.3737 -0.0301 -0.0512 -0.0207 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2631 0.2946 0.3726 -0.0435 -0.0467 -0.0311 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2727 0.3061 0.3986 -0.0467 -0.0463 -0.0302 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2311 0.2777 0.3775 -0.0411 -0.0454 -0.0213 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2371 0.2836 0.3952 -0.0391 -0.0391 -0.0195 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3203 0.3549 0.4448 -0.0588 -0.0564 -0.0329 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4467 0.4666 0.5487 -0.0668 -0.0563 -0.0433 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5059 0.5106 0.6040 -0.0673 -0.0466 -0.0511 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4972 0.5152 0.5803 -0.0756 -0.0642 -0.0468 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5342 0.5271 0.6114 -0.0758 -0.0472 -0.0605 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5363 0.5367 0.6018 -0.0818 -0.0579 -0.0584 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2375 0.2944 0.3881 -0.0385 -0.0506 -0.0154 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2269 0.2947 0.3979 -0.0329 -0.0474 -0.0080 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2082 0.2715 0.3769 -0.0251 -0.0357 -0.0078 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2079 0.2753 0.3904 -0.0229 -0.0292 -0.0046 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2615 0.3399 0.4401 -0.0312 -0.0546 -0.0013 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3527 0.4443 0.5577 -0.0336 -0.0587 0.0053  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3469 0.4404 0.5568 -0.0418 -0.0646 0.0042  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4056 0.5058 0.6293 -0.0267 -0.0541 0.0120  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1895 0.2446 0.3400 -0.0218 -0.0328 -0.0110 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1891 0.2402 0.3358 -0.0164 -0.0232 -0.0103 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1844 0.2313 0.3360 -0.0184 -0.0181 -0.0109 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1915 0.2402 0.3489 -0.0166 -0.0114 -0.0074 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1872 0.2308 0.3155 -0.0139 -0.0221 -0.0134 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2291 0.2760 0.3521 -0.0109 -0.0248 -0.0114 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2320 0.2845 0.3648 -0.0079 -0.0224 -0.0072 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2288 0.2717 0.3379 -0.0118 -0.0283 -0.0142 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1872 0.2272 0.3354 -0.0228 -0.0206 -0.0153 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2048 0.2394 0.3588 -0.0246 -0.0158 -0.0150 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2249 0.2664 0.3960 -0.0278 -0.0154 -0.0114 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2319 0.2721 0.4089 -0.0279 -0.0095 -0.0080 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2017 0.2253 0.3492 -0.0284 -0.0169 -0.0215 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2110 0.2264 0.3472 -0.0240 -0.0124 -0.0233 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2405 0.2519 0.3632 -0.0235 -0.0137 -0.0282 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2081 0.2191 0.3473 -0.0204 -0.0061 -0.0193 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2389 0.2441 0.3581 -0.0190 -0.0076 -0.0279 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2289 0.2344 0.3589 -0.0170 -0.0037 -0.0219 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2215 0.2333 0.3707 -0.0202 -0.0026 -0.0129 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2291 0.2311 0.3625 -0.0131 0.0013  -0.0173 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2257 0.2335 0.3755 -0.0170 0.0016  -0.0080 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2339 0.2374 0.3774 -0.0133 0.0031  -0.0099 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2182 0.2681 0.3983 -0.0309 -0.0219 -0.0110 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2313 0.2900 0.4313 -0.0341 -0.0213 -0.0069 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2364 0.3020 0.4449 -0.0290 -0.0132 -0.0016 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2374 0.3089 0.4617 -0.0309 -0.0090 0.0018  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2280 0.2958 0.4377 -0.0390 -0.0315 -0.0063 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2095 0.2746 0.4083 -0.0234 -0.0106 -0.0013 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2100 0.2787 0.4131 -0.0196 -0.0015 0.0019  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2048 0.2646 0.3888 -0.0175 0.0045  0.0010  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1937 0.2532 0.3716 -0.0144 0.0100  0.0016  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2193 0.2947 0.4290 -0.0156 -0.0039 0.0034  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2501 0.3369 0.4823 -0.0180 -0.0102 0.0069  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2503 0.3443 0.5023 -0.0181 -0.0041 0.0102  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2469 0.3357 0.4764 -0.0207 -0.0224 0.0065  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1884 0.2411 0.3646 -0.0197 0.0037  0.0004  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1960 0.2420 0.3568 -0.0184 0.0072  0.0016  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2215 0.2682 0.3788 -0.0199 0.0158  0.0054  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2418 0.2904 0.4077 -0.0234 0.0204  0.0080  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2002 0.2394 0.3601 -0.0204 0.0048  0.0016  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2125 0.2463 0.3618 -0.0194 0.0071  0.0053  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2201 0.2525 0.3577 -0.0154 0.0048  0.0028  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2211 0.2480 0.3760 -0.0210 0.0062  0.0069  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2195 0.2638 0.3625 -0.0183 0.0184  0.0057  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2246 0.2672 0.3578 -0.0219 0.0263  0.0086  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2350 0.2732 0.3554 -0.0243 0.0236  0.0133  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2538 0.2907 0.3704 -0.0295 0.0264  0.0187  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2397 0.2821 0.3658 -0.0199 0.0313  0.0055  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2504 0.2887 0.3603 -0.0254 0.0393  0.0071  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2435 0.2914 0.3873 -0.0172 0.0348  0.0032  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2190 0.2553 0.3342 -0.0206 0.0178  0.0121  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2201 0.2539 0.3274 -0.0220 0.0149  0.0176  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1988 0.2311 0.3077 -0.0169 0.0096  0.0150  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2003 0.2333 0.3074 -0.0136 0.0085  0.0092  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2357 0.2694 0.3262 -0.0261 0.0179  0.0202  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2513 0.2849 0.3340 -0.0279 0.0132  0.0267  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2720 0.3060 0.3534 -0.0329 0.0110  0.0363  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2469 0.2808 0.3236 -0.0250 0.0098  0.0255  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2774 0.3132 0.3549 -0.0329 0.0057  0.0417  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2544 0.2901 0.3286 -0.0282 0.0055  0.0347  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2429 0.2764 0.3172 -0.0204 0.0097  0.0186  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2540 0.2917 0.3240 -0.0270 0.0016  0.0365  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2550 0.2892 0.3232 -0.0193 0.0064  0.0199  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2517 0.2882 0.3186 -0.0225 0.0026  0.0285  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1929 0.2229 0.3061 -0.0165 0.0071  0.0194  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1977 0.2255 0.3123 -0.0119 0.0044  0.0168  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1868 0.2145 0.3041 -0.0120 0.0030  0.0252  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1951 0.2229 0.3177 -0.0152 0.0030  0.0331  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2259 0.2493 0.3496 -0.0098 0.0037  0.0101  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2209 0.2406 0.3569 -0.0120 0.0048  0.0124  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2224 0.2372 0.3676 -0.0107 0.0056  0.0182  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2875 0.3006 0.4415 -0.0133 0.0064  0.0245  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2178 0.2308 0.3633 -0.0071 0.0058  0.0174  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1810 0.2091 0.2969 -0.0087 0.0019  0.0246  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1808 0.2106 0.3039 -0.0082 0.0003  0.0339  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1852 0.2122 0.3152 -0.0025 0.0019  0.0294  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1797 0.2086 0.3007 -0.0011 0.0017  0.0252  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2018 0.2379 0.3128 -0.0129 -0.0027 0.0412  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3045 0.3450 0.4250 -0.0140 -0.0065 0.0540  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3210 0.3599 0.4586 -0.0086 -0.0054 0.0557  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2943 0.3398 0.4053 -0.0209 -0.0102 0.0626  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1837 0.2049 0.3294 0.0004  0.0048  0.0296  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2044 0.2207 0.3570 0.0052  0.0090  0.0239  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1998 0.2162 0.3525 0.0052  0.0091  0.0240  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2115 0.2343 0.3681 0.0074  0.0084  0.0311  36  SER   A C   
244  O O   . SER   A 30  ? 0.2320 0.2537 0.3856 0.0102  0.0115  0.0249  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2365 0.2436 0.4063 0.0072  0.0138  0.0232  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2188 0.2260 0.3891 0.0073  0.0139  0.0234  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2827 0.2837 0.4602 0.0115  0.0204  0.0177  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2356 0.2456 0.4226 0.0077  0.0127  0.0371  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2011 0.2313 0.3637 0.0050  0.0038  0.0446  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2064 0.2449 0.3745 0.0059  0.0016  0.0530  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2104 0.2534 0.3585 0.0033  -0.0008 0.0484  37  SER   A C   
252  O O   . SER   A 31  ? 0.2273 0.2760 0.3791 0.0043  -0.0015 0.0523  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2588 0.3050 0.4372 0.0021  -0.0047 0.0702  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3288 0.3799 0.4871 -0.0059 -0.0106 0.0735  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1830 0.2235 0.3124 0.0002  -0.0016 0.0408  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1688 0.2117 0.2805 -0.0019 -0.0029 0.0361  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1731 0.2102 0.2775 0.0016  0.0007  0.0234  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1728 0.2109 0.2645 0.0008  0.0000  0.0197  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1710 0.2151 0.2671 -0.0084 -0.0054 0.0372  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1738 0.2240 0.2701 -0.0149 -0.0102 0.0502  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2054 0.2546 0.2835 -0.0228 -0.0106 0.0500  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2005 0.2483 0.2616 -0.0251 -0.0091 0.0431  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2232 0.2701 0.2666 -0.0335 -0.0088 0.0436  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2358 0.2839 0.2737 -0.0413 -0.0104 0.0510  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2125 0.2564 0.2425 -0.0351 -0.0066 0.0371  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1584 0.1890 0.2695 0.0045  0.0040  0.0172  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1593 0.1848 0.2614 0.0055  0.0056  0.0062  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1492 0.1762 0.2394 0.0029  0.0025  0.0036  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1651 0.1911 0.2457 0.0033  0.0018  -0.0020 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1695 0.1942 0.2668 0.0077  0.0082  0.0021  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1950 0.2140 0.2815 0.0072  0.0091  -0.0082 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1893 0.2026 0.2780 0.0062  0.0099  -0.0132 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1929 0.2128 0.2683 0.0070  0.0087  -0.0107 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1403 0.1693 0.2318 0.0001  0.0012  0.0080  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1439 0.1738 0.2276 -0.0019 0.0006  0.0053  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1512 0.1799 0.2421 -0.0031 0.0010  0.0038  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1552 0.1830 0.2544 -0.0043 0.0016  0.0078  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1485 0.1815 0.2241 -0.0057 0.0008  0.0104  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1609 0.1954 0.2269 -0.0062 0.0000  0.0114  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1759 0.2115 0.2315 -0.0124 0.0007  0.0154  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1557 0.1880 0.2160 -0.0033 0.0003  0.0046  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1419 0.1713 0.2310 -0.0031 0.0005  -0.0006 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1534 0.1836 0.2507 -0.0048 0.0009  -0.0013 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1656 0.1990 0.2612 -0.0051 0.0024  -0.0020 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1679 0.2016 0.2585 -0.0030 0.0010  -0.0043 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1506 0.1783 0.2538 -0.0048 -0.0019 -0.0064 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1624 0.1918 0.2765 -0.0075 -0.0023 -0.0066 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1808 0.2047 0.3000 -0.0094 -0.0039 -0.0104 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1755 0.2102 0.2923 -0.0076 -0.0050 -0.0083 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1563 0.1914 0.2569 -0.0075 0.0062  0.0001  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1651 0.2025 0.2681 -0.0074 0.0102  -0.0009 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1780 0.2192 0.2966 -0.0082 0.0104  -0.0012 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1865 0.2274 0.3098 -0.0110 0.0113  0.0008  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1820 0.2174 0.2754 -0.0111 0.0172  0.0013  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1974 0.2332 0.2953 -0.0108 0.0244  -0.0010 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1856 0.2182 0.2642 -0.0117 0.0157  0.0022  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1786 0.2237 0.3063 -0.0059 0.0088  -0.0025 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1844 0.2353 0.3298 -0.0068 0.0082  -0.0017 43  SER   A CA  
299  C C   . SER   A 37  ? 0.2062 0.2608 0.3623 -0.0051 0.0155  -0.0006 43  SER   A C   
300  O O   . SER   A 37  ? 0.2040 0.2557 0.3535 -0.0026 0.0195  -0.0014 43  SER   A O   
301  C CB  . SER   A 37  ? 0.2058 0.2598 0.3568 -0.0069 -0.0016 -0.0029 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2123 0.2675 0.3600 -0.0040 -0.0058 -0.0029 43  SER   A OG  
303  N N   . SER   A 38  ? 0.2119 0.2727 0.3865 -0.0064 0.0182  0.0012  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2284 0.2929 0.4179 -0.0042 0.0270  0.0023  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2313 0.3036 0.4392 -0.0002 0.0204  0.0052  44  SER   A C   
306  O O   . SER   A 38  ? 0.2283 0.3057 0.4412 -0.0015 0.0088  0.0067  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2587 0.3266 0.4608 -0.0076 0.0351  0.0036  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2883 0.3629 0.5040 -0.0097 0.0264  0.0056  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2438 0.3165 0.4618 0.0040  0.0278  0.0062  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2673 0.3481 0.5062 0.0082  0.0216  0.0113  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3110 0.3982 0.5794 0.0111  0.0329  0.0145  45  THR   A C   
312  O O   . THR   A 39  ? 0.3221 0.4039 0.5882 0.0101  0.0477  0.0108  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2884 0.3631 0.5158 0.0122  0.0200  0.0111  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3093 0.3762 0.5356 0.0146  0.0352  0.0082  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2900 0.3576 0.4888 0.0098  0.0128  0.0074  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3410 0.4393 0.6367 0.0141  0.0263  0.0216  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3636 0.4694 0.6933 0.0180  0.0371  0.0260  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3911 0.4910 0.7281 0.0250  0.0460  0.0269  46  THR   A C   
319  O O   . THR   A 40  ? 0.4041 0.5015 0.7581 0.0283  0.0634  0.0257  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3866 0.5097 0.7466 0.0171  0.0239  0.0354  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4124 0.5386 0.7681 0.0177  0.0073  0.0405  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3965 0.5243 0.7522 0.0096  0.0173  0.0339  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3890 0.4859 0.7139 0.0269  0.0351  0.0290  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3849 0.4754 0.7165 0.0332  0.0416  0.0308  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4006 0.4734 0.6992 0.0318  0.0525  0.0208  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4030 0.4709 0.6713 0.0267  0.0467  0.0157  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3817 0.4785 0.7167 0.0347  0.0235  0.0394  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4003 0.4635 0.7056 0.0359  0.0682  0.0183  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4275 0.4735 0.7012 0.0330  0.0786  0.0088  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4322 0.4738 0.6856 0.0332  0.0660  0.0100  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4359 0.4823 0.7055 0.0381  0.0576  0.0178  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4700 0.5051 0.7568 0.0363  0.1002  0.0048  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5688 0.5853 0.8211 0.0308  0.1117  -0.0059 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6687 0.6800 0.9019 0.0227  0.1235  -0.0139 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6938 0.7148 0.9390 0.0213  0.1239  -0.0120 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6984 0.6941 0.9007 0.0160  0.1329  -0.0225 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4269 0.4607 0.6462 0.0275  0.0641  0.0036  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4266 0.4566 0.6246 0.0267  0.0532  0.0039  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4180 0.4368 0.6132 0.0295  0.0597  0.0031  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4378 0.4480 0.6420 0.0309  0.0755  -0.0003 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3838 0.4012 0.5648 0.0294  0.0486  0.0054  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3584 0.3662 0.5356 0.0316  0.0510  0.0062  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3524 0.3473 0.4980 0.0257  0.0564  -0.0018 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3473 0.3314 0.4899 0.0264  0.0624  -0.0029 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3592 0.3747 0.5418 0.0344  0.0349  0.0154  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3780 0.3992 0.5327 0.0287  0.0191  0.0143  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3411 0.3373 0.4656 0.0195  0.0543  -0.0064 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3369 0.3246 0.4326 0.0128  0.0556  -0.0116 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3315 0.3094 0.4121 0.0055  0.0690  -0.0193 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3491 0.3290 0.4380 0.0048  0.0762  -0.0210 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3286 0.3251 0.4112 0.0104  0.0422  -0.0097 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3597 0.3624 0.4462 0.0143  0.0297  -0.0041 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3778 0.3750 0.4600 0.0152  0.0291  -0.0027 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2956 0.3079 0.3878 0.0153  0.0208  -0.0014 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3232 0.2918 0.3799 -0.0014 0.0711  -0.0233 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3497 0.3083 0.3838 -0.0118 0.0807  -0.0300 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3223 0.2867 0.3351 -0.0185 0.0691  -0.0277 52  THR   A C   
358  O O   . THR   A 46  ? 0.3304 0.2979 0.3414 -0.0162 0.0599  -0.0244 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4354 0.3772 0.4623 -0.0145 0.0922  -0.0356 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4962 0.4306 0.5391 -0.0115 0.1077  -0.0396 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4717 0.4037 0.4666 -0.0280 0.0953  -0.0412 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2885 0.2545 0.2871 -0.0268 0.0697  -0.0286 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2646 0.2373 0.2482 -0.0327 0.0588  -0.0244 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2791 0.2427 0.2385 -0.0443 0.0616  -0.0273 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.3070 0.2599 0.2534 -0.0525 0.0730  -0.0332 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2574 0.2382 0.2413 -0.0355 0.0558  -0.0210 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2671 0.2558 0.2743 -0.0259 0.0541  -0.0191 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2660 0.2550 0.2408 -0.0399 0.0440  -0.0147 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2617 0.2582 0.2813 -0.0173 0.0430  -0.0153 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2578 0.2253 0.2104 -0.0461 0.0521  -0.0236 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2666 0.2277 0.1967 -0.0585 0.0523  -0.0250 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2865 0.2517 0.2015 -0.0698 0.0494  -0.0218 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2868 0.2636 0.2107 -0.0667 0.0420  -0.0153 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2621 0.2299 0.1931 -0.0570 0.0415  -0.0198 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3116 0.2661 0.2024 -0.0841 0.0555  -0.0263 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3270 0.2854 0.1998 -0.0976 0.0513  -0.0218 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3598 0.3153 0.2121 -0.1108 0.0459  -0.0206 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3922 0.3326 0.2231 -0.1221 0.0552  -0.0289 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3424 0.2896 0.2023 -0.1049 0.0654  -0.0290 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3383 0.2883 0.2219 -0.0914 0.0719  -0.0305 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3452 0.3115 0.2446 -0.0850 0.0603  -0.0205 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3251 0.2931 0.2454 -0.0743 0.0670  -0.0227 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3320 0.3117 0.2715 -0.0655 0.0592  -0.0165 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.3054 0.2955 0.2470 -0.0654 0.0458  -0.0080 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3278 0.3089 0.2859 -0.0574 0.0651  -0.0187 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3425 0.3116 0.2034 -0.1087 0.0319  -0.0112 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3549 0.3234 0.2027 -0.1189 0.0259  -0.0093 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3455 0.3330 0.2055 -0.1179 0.0100  0.0042  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3489 0.3479 0.2281 -0.1079 0.0051  0.0108  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3525 0.3116 0.2068 -0.1111 0.0321  -0.0166 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3190 0.2907 0.2055 -0.0904 0.0260  -0.0114 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.3605 0.3508 0.2127 -0.1271 0.0030  0.0079  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3554 0.3642 0.2237 -0.1253 -0.0107 0.0209  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.3540 0.3643 0.2340 -0.1180 -0.0114 0.0198  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3617 0.3840 0.2482 -0.1222 -0.0209 0.0288  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4168 0.4331 0.2693 -0.1442 -0.0215 0.0307  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5268 0.5318 0.3531 -0.1610 -0.0199 0.0248  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5225 0.5119 0.3426 -0.1576 -0.0088 0.0124  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6210 0.6325 0.4328 -0.1783 -0.0300 0.0331  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3255 0.3249 0.2102 -0.1072 -0.0017 0.0101  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3061 0.3066 0.2009 -0.1005 -0.0024 0.0099  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2883 0.3064 0.2061 -0.0913 -0.0104 0.0195  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2806 0.3056 0.2115 -0.0831 -0.0117 0.0225  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3049 0.2925 0.2038 -0.0896 0.0079  0.0004  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3333 0.2973 0.2107 -0.0984 0.0206  -0.0118 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2752 0.2997 0.1987 -0.0926 -0.0147 0.0238  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2556 0.2948 0.2018 -0.0834 -0.0192 0.0313  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2305 0.2656 0.1818 -0.0758 -0.0147 0.0271  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2244 0.2701 0.1907 -0.0712 -0.0169 0.0325  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2825 0.3374 0.2364 -0.0921 -0.0290 0.0435  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3455 0.4088 0.3027 -0.0961 -0.0352 0.0515  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4099 0.4908 0.3796 -0.1040 -0.0461 0.0659  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4438 0.5277 0.4002 -0.1194 -0.0537 0.0719  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3649 0.4582 0.3612 -0.0942 -0.0468 0.0722  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2350 0.2543 0.1739 -0.0751 -0.0077 0.0180  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2331 0.2472 0.1761 -0.0673 -0.0035 0.0147  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2274 0.2295 0.1684 -0.0595 0.0032  0.0074  60  THR   A C   
418  O O   . THR   A 54  ? 0.2462 0.2403 0.1790 -0.0627 0.0067  0.0030  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2649 0.2723 0.1978 -0.0760 -0.0026 0.0138  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3190 0.3107 0.2348 -0.0837 0.0024  0.0068  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2709 0.2915 0.2072 -0.0852 -0.0099 0.0220  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2151 0.2171 0.1646 -0.0496 0.0046  0.0068  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2034 0.1969 0.1552 -0.0417 0.0091  0.0022  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1962 0.1913 0.1551 -0.0335 0.0083  0.0036  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2040 0.2036 0.1631 -0.0348 0.0066  0.0068  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1875 0.1791 0.1517 -0.0261 0.0097  0.0017  62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1941 0.1864 0.1621 -0.0199 0.0081  0.0036  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1819 0.1799 0.1577 -0.0139 0.0059  0.0029  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1938 0.1897 0.1737 -0.0123 0.0073  0.0008  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2249 0.2054 0.1920 -0.0186 0.0110  0.0034  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2437 0.2255 0.2142 -0.0130 0.0076  0.0071  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2402 0.2136 0.1988 -0.0255 0.0136  0.0036  62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1697 0.1737 0.1469 -0.0111 0.0032  0.0043  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1714 0.1791 0.1544 -0.0066 0.0010  0.0030  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1858 0.1920 0.1664 -0.0042 -0.0018 0.0043  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1921 0.1963 0.1661 -0.0059 -0.0017 0.0066  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1655 0.1811 0.1526 -0.0066 0.0010  0.0023  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1629 0.1818 0.1476 -0.0067 0.0020  0.0028  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1797 0.2006 0.1622 -0.0100 0.0039  0.0053  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1773 0.1971 0.1618 -0.0045 0.0019  0.0003  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.1828 0.2072 0.1652 -0.0102 0.0067  0.0055  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1907 0.2122 0.1721 -0.0054 0.0053  -0.0006 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1956 0.2196 0.1767 -0.0078 0.0082  0.0022  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2357 0.2616 0.2150 -0.0087 0.0134  0.0014  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1820 0.1894 0.1675 -0.0013 -0.0047 0.0036  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1905 0.1977 0.1725 -0.0008 -0.0093 0.0058  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1938 0.2048 0.1698 -0.0024 -0.0095 0.0026  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1897 0.2036 0.1708 -0.0016 -0.0084 -0.0009 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1895 0.1970 0.1813 0.0019  -0.0133 0.0076  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2012 0.2097 0.1887 0.0007  -0.0201 0.0117  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2206 0.2255 0.2024 -0.0005 -0.0222 0.0173  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2229 0.2356 0.2102 -0.0006 -0.0249 0.0102  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2461 0.2523 0.2216 -0.0032 -0.0297 0.0224  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2301 0.2438 0.2100 -0.0041 -0.0323 0.0141  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2561 0.2669 0.2295 -0.0056 -0.0350 0.0206  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3129 0.3252 0.2772 -0.0104 -0.0434 0.0259  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1965 0.2061 0.1612 -0.0052 -0.0098 0.0037  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1925 0.2032 0.1491 -0.0078 -0.0076 -0.0004 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2179 0.2269 0.1641 -0.0111 -0.0138 0.0008  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2297 0.2363 0.1653 -0.0143 -0.0162 0.0051  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2081 0.2187 0.1587 -0.0098 -0.0016 -0.0003 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2399 0.2498 0.1799 -0.0134 0.0048  -0.0062 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2117 0.2219 0.1606 -0.0115 -0.0169 -0.0024 66  SER   A N   
464  C CA  . SER   A 60  ? 0.2309 0.2405 0.1704 -0.0163 -0.0247 -0.0005 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2406 0.2464 0.1588 -0.0234 -0.0227 -0.0031 66  SER   A C   
466  O O   . SER   A 60  ? 0.2614 0.2663 0.1674 -0.0288 -0.0299 0.0022  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2860 0.2979 0.2331 -0.0164 -0.0283 -0.0037 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3701 0.3795 0.3134 -0.0179 -0.0215 -0.0123 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2294 0.2329 0.1438 -0.0236 -0.0122 -0.0101 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2561 0.2549 0.1503 -0.0306 -0.0069 -0.0141 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2582 0.2561 0.1425 -0.0327 -0.0063 -0.0081 67  SER   A C   
472  O O   . SER   A 61  ? 0.2816 0.2753 0.1466 -0.0397 -0.0021 -0.0105 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2791 0.2754 0.1759 -0.0296 0.0057  -0.0233 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2657 0.2661 0.1777 -0.0235 0.0120  -0.0212 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2497 0.2504 0.1458 -0.0278 -0.0099 -0.0007 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2645 0.2636 0.1528 -0.0300 -0.0108 0.0063  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2780 0.2773 0.1725 -0.0283 -0.0216 0.0162  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2982 0.2952 0.1888 -0.0296 -0.0230 0.0233  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2583 0.2589 0.1563 -0.0263 -0.0025 0.0058  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2698 0.2711 0.1657 -0.0275 0.0089  -0.0015 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.2908 0.2883 0.1663 -0.0348 0.0135  -0.0017 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3118 0.3097 0.1881 -0.0355 0.0268  -0.0089 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.3202 0.3145 0.1896 -0.0381 0.0331  -0.0175 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3249 0.3154 0.1840 -0.0413 0.0260  -0.0200 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3290 0.3231 0.2029 -0.0379 0.0472  -0.0236 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2800 0.2822 0.1869 -0.0251 -0.0282 0.0171  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2974 0.3004 0.2170 -0.0218 -0.0364 0.0264  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.3004 0.3002 0.2295 -0.0172 -0.0318 0.0298  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3256 0.3223 0.2561 -0.0173 -0.0357 0.0387  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3524 0.3555 0.2610 -0.0279 -0.0468 0.0356  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4105 0.4174 0.3153 -0.0323 -0.0543 0.0342  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4163 0.4256 0.3175 -0.0375 -0.0679 0.0473  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4321 0.4443 0.3204 -0.0462 -0.0758 0.0458  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4632 0.4727 0.3238 -0.0578 -0.0794 0.0463  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4770 0.4817 0.3217 -0.0612 -0.0759 0.0496  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4657 0.4767 0.3131 -0.0671 -0.0861 0.0432  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2710 0.2709 0.2051 -0.0144 -0.0233 0.0231  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2698 0.2657 0.2093 -0.0125 -0.0186 0.0251  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2441 0.2415 0.1947 -0.0091 -0.0134 0.0195  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2460 0.2478 0.1984 -0.0085 -0.0116 0.0140  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3236 0.3188 0.2504 -0.0169 -0.0132 0.0242  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4309 0.4220 0.3456 -0.0212 -0.0163 0.0317  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5293 0.5207 0.4332 -0.0256 -0.0088 0.0294  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.6142 0.6007 0.5073 -0.0301 -0.0101 0.0373  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6651 0.6519 0.5383 -0.0368 -0.0107 0.0380  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2315 0.2242 0.1881 -0.0080 -0.0105 0.0210  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2217 0.2150 0.1844 -0.0074 -0.0056 0.0162  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2292 0.2229 0.1856 -0.0115 -0.0014 0.0157  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2474 0.2372 0.1977 -0.0141 -0.0008 0.0194  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2093 0.1955 0.1807 -0.0054 -0.0038 0.0172  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2221 0.2087 0.2044 -0.0009 -0.0070 0.0189  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2555 0.2446 0.2464 0.0013  -0.0052 0.0148  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2218 0.2070 0.2093 0.0012  -0.0119 0.0255  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2398 0.2293 0.2419 0.0050  -0.0086 0.0185  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2771 0.2649 0.2784 0.0051  -0.0133 0.0254  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2029 0.2021 0.1625 -0.0124 0.0012  0.0121  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2093 0.2116 0.1669 -0.0167 0.0044  0.0127  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2113 0.2142 0.1731 -0.0195 0.0054  0.0115  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.1977 0.2030 0.1645 -0.0178 0.0047  0.0093  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2103 0.2213 0.1698 -0.0163 0.0065  0.0112  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2351 0.2452 0.1861 -0.0164 0.0073  0.0114  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2692 0.2773 0.2125 -0.0200 0.0095  0.0145  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2285 0.2393 0.1775 -0.0143 0.0064  0.0082  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2836 0.2903 0.2158 -0.0217 0.0106  0.0148  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2444 0.2534 0.1816 -0.0166 0.0075  0.0076  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2905 0.2975 0.2186 -0.0205 0.0097  0.0110  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3368 0.3414 0.2502 -0.0243 0.0112  0.0105  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2088 0.2098 0.1673 -0.0250 0.0069  0.0132  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2185 0.2207 0.1779 -0.0304 0.0069  0.0125  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2329 0.2484 0.2001 -0.0316 0.0056  0.0147  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2576 0.2797 0.2287 -0.0306 0.0070  0.0169  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2347 0.2300 0.1874 -0.0371 0.0083  0.0139  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2388 0.2354 0.1903 -0.0353 0.0091  0.0171  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2081 0.2055 0.1610 -0.0280 0.0081  0.0164  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2000 0.2195 0.1703 -0.0340 0.0037  0.0148  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2135 0.2459 0.1950 -0.0346 0.0018  0.0188  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2074 0.2434 0.1878 -0.0429 -0.0020 0.0221  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2130 0.2408 0.1831 -0.0472 -0.0023 0.0190  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2425 0.2780 0.2319 -0.0274 0.0019  0.0171  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2676 0.3037 0.2600 -0.0212 0.0053  0.0151  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2415 0.2690 0.2251 -0.0259 0.0015  0.0129  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1983 0.2472 0.1901 -0.0461 -0.0048 0.0288  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2086 0.2650 0.2025 -0.0543 -0.0107 0.0347  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1923 0.2579 0.2021 -0.0480 -0.0119 0.0384  75  SER   A C   
545  O O   . SER   A 69  ? 0.2066 0.2779 0.2307 -0.0407 -0.0085 0.0395  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2515 0.3186 0.2526 -0.0620 -0.0142 0.0423  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3618 0.4196 0.3476 -0.0695 -0.0135 0.0391  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1779 0.2425 0.1839 -0.0506 -0.0151 0.0391  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1745 0.2456 0.1955 -0.0442 -0.0158 0.0424  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1851 0.2655 0.2107 -0.0521 -0.0233 0.0520  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2054 0.2839 0.2160 -0.0635 -0.0279 0.0536  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1738 0.2341 0.1880 -0.0372 -0.0115 0.0337  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1773 0.2266 0.1727 -0.0426 -0.0111 0.0283  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1933 0.2315 0.1769 -0.0422 -0.0070 0.0214  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1841 0.2332 0.1756 -0.0470 -0.0133 0.0300  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2116 0.2387 0.1813 -0.0463 -0.0042 0.0160  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2112 0.2491 0.1856 -0.0521 -0.0103 0.0240  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2071 0.2338 0.1721 -0.0510 -0.0051 0.0166  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1807 0.2712 0.2279 -0.0468 -0.0247 0.0593  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1873 0.2879 0.2419 -0.0538 -0.0330 0.0711  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2063 0.2994 0.2461 -0.0573 -0.0346 0.0686  77  SER   A C   
562  O O   . SER   A 71  ? 0.2015 0.2831 0.2317 -0.0517 -0.0284 0.0582  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1891 0.3022 0.2749 -0.0464 -0.0332 0.0807  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2315 0.3374 0.3237 -0.0352 -0.0259 0.0737  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2032 0.3033 0.2405 -0.0678 -0.0432 0.0789  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2206 0.3144 0.2435 -0.0726 -0.0443 0.0778  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2331 0.3274 0.2741 -0.0611 -0.0410 0.0786  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2253 0.3280 0.2916 -0.0530 -0.0409 0.0845  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2738 0.3766 0.2900 -0.0880 -0.0554 0.0910  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3459 0.4446 0.3381 -0.1019 -0.0579 0.0878  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.4290 0.5345 0.4083 -0.1198 -0.0692 0.0995  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.5216 0.6162 0.4689 -0.1348 -0.0683 0.0913  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5721 0.6782 0.5130 -0.1529 -0.0816 0.1044  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2263 0.3113 0.2557 -0.0606 -0.0376 0.0725  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2298 0.3145 0.2761 -0.0506 -0.0346 0.0729  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2312 0.3284 0.2998 -0.0513 -0.0417 0.0888  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2444 0.3481 0.3070 -0.0626 -0.0502 0.0998  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2557 0.3307 0.2842 -0.0542 -0.0317 0.0668  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2827 0.3493 0.2859 -0.0620 -0.0290 0.0583  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2455 0.3195 0.2473 -0.0693 -0.0351 0.0647  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2072 0.3074 0.3013 -0.0400 -0.0381 0.0904  80  SER   A N   
582  C CA  A SER   A 74  ? 0.2138 0.3259 0.3350 -0.0391 -0.0435 0.1063  80  SER   A CA  
583  C CA  B SER   A 74  ? 0.2079 0.3202 0.3298 -0.0388 -0.0434 0.1063  80  SER   A CA  
584  C C   . SER   A 74  ? 0.2077 0.3158 0.3520 -0.0266 -0.0362 0.1041  80  SER   A C   
585  O O   . SER   A 74  ? 0.2080 0.3049 0.3450 -0.0200 -0.0280 0.0900  80  SER   A O   
586  C CB  A SER   A 74  ? 0.2433 0.3679 0.3788 -0.0411 -0.0476 0.1152  80  SER   A CB  
587  C CB  B SER   A 74  ? 0.2207 0.3443 0.3582 -0.0387 -0.0455 0.1130  80  SER   A CB  
588  O OG  A SER   A 74  ? 0.2796 0.4009 0.4236 -0.0314 -0.0383 0.1055  80  SER   A OG  
589  O OG  B SER   A 74  ? 0.2488 0.3733 0.3650 -0.0484 -0.0493 0.1105  80  SER   A OG  
590  N N   . LEU   A 75  ? 0.1859 0.3032 0.3588 -0.0243 -0.0398 0.1191  81  LEU   A N   
591  C CA  . LEU   A 75  ? 0.2028 0.3153 0.4000 -0.0133 -0.0322 0.1181  81  LEU   A CA  
592  C C   . LEU   A 75  ? 0.2066 0.3229 0.4262 -0.0052 -0.0249 0.1167  81  LEU   A C   
593  O O   . LEU   A 75  ? 0.2147 0.3448 0.4547 -0.0069 -0.0298 0.1306  81  LEU   A O   
594  C CB  . LEU   A 75  ? 0.2137 0.3340 0.4321 -0.0156 -0.0396 0.1367  81  LEU   A CB  
595  C CG  . LEU   A 75  ? 0.2543 0.3670 0.4943 -0.0064 -0.0326 0.1363  81  LEU   A CG  
596  C CD1 . LEU   A 75  ? 0.2785 0.3768 0.4965 -0.0062 -0.0280 0.1221  81  LEU   A CD1 
597  C CD2 . LEU   A 75  ? 0.2729 0.3952 0.5373 -0.0090 -0.0412 0.1581  81  LEU   A CD2 
598  N N   . ILE   A 76  ? 0.2170 0.3217 0.4331 0.0027  -0.0133 0.1008  82  ILE   A N   
599  C CA  . ILE   A 76  ? 0.2334 0.3386 0.4632 0.0093  -0.0039 0.0956  82  ILE   A CA  
600  C C   . ILE   A 76  ? 0.2379 0.3324 0.4839 0.0187  0.0084  0.0878  82  ILE   A C   
601  O O   . ILE   A 76  ? 0.2348 0.3169 0.4659 0.0196  0.0113  0.0770  82  ILE   A O   
602  C CB  . ILE   A 76  ? 0.2666 0.3665 0.4672 0.0066  -0.0018 0.0819  82  ILE   A CB  
603  C CG1 . ILE   A 76  ? 0.2855 0.3951 0.4723 -0.0032 -0.0124 0.0894  82  ILE   A CG1 
604  C CG2 . ILE   A 76  ? 0.2786 0.3754 0.4870 0.0130  0.0099  0.0734  82  ILE   A CG2 
605  C CD1 . ILE   A 76  ? 0.3167 0.4205 0.4770 -0.0064 -0.0112 0.0782  82  ILE   A CD1 
606  N N   . PHE   A 77  ? 0.2283 0.3267 0.5049 0.0253  0.0166  0.0925  83  PHE   A N   
607  C CA  . PHE   A 77  ? 0.2493 0.3353 0.5411 0.0335  0.0307  0.0836  83  PHE   A CA  
608  C C   . PHE   A 77  ? 0.2791 0.3518 0.5448 0.0341  0.0401  0.0634  83  PHE   A C   
609  O O   . PHE   A 77  ? 0.2879 0.3639 0.5424 0.0324  0.0418  0.0591  83  PHE   A O   
610  C CB  . PHE   A 77  ? 0.2490 0.3424 0.5819 0.0404  0.0393  0.0935  83  PHE   A CB  
611  C CG  . PHE   A 77  ? 0.2843 0.3622 0.6332 0.0484  0.0560  0.0834  83  PHE   A CG  
612  C CD1 . PHE   A 77  ? 0.3125 0.3824 0.6739 0.0510  0.0566  0.0863  83  PHE   A CD1 
613  C CD2 . PHE   A 77  ? 0.3091 0.3786 0.6564 0.0520  0.0718  0.0694  83  PHE   A CD2 
614  C CE1 . PHE   A 77  ? 0.3351 0.3886 0.7100 0.0573  0.0729  0.0757  83  PHE   A CE1 
615  C CE2 . PHE   A 77  ? 0.3272 0.3804 0.6869 0.0578  0.0886  0.0587  83  PHE   A CE2 
616  C CZ  . PHE   A 77  ? 0.3329 0.3779 0.7066 0.0605  0.0892  0.0616  83  PHE   A CZ  
617  N N   . VAL   A 78  ? 0.2963 0.3539 0.5519 0.0355  0.0454  0.0516  84  VAL   A N   
618  C CA  . VAL   A 78  ? 0.3209 0.3656 0.5511 0.0347  0.0530  0.0333  84  VAL   A CA  
619  C C   . VAL   A 78  ? 0.3545 0.3853 0.5991 0.0396  0.0677  0.0246  84  VAL   A C   
620  O O   . VAL   A 78  ? 0.3682 0.3932 0.6260 0.0415  0.0682  0.0271  84  VAL   A O   
621  C CB  . VAL   A 78  ? 0.3295 0.3692 0.5296 0.0293  0.0438  0.0267  84  VAL   A CB  
622  C CG1 . VAL   A 78  ? 0.3595 0.3865 0.5363 0.0279  0.0501  0.0098  84  VAL   A CG1 
623  C CG2 . VAL   A 78  ? 0.3242 0.3750 0.5093 0.0242  0.0319  0.0335  84  VAL   A CG2 
624  N N   . GLU   A 79  ? 0.3734 0.3980 0.6152 0.0410  0.0804  0.0143  85  GLU   A N   
625  C CA  . GLU   A 79  ? 0.3990 0.4083 0.6525 0.0447  0.0976  0.0039  85  GLU   A CA  
626  C C   . GLU   A 79  ? 0.4222 0.4153 0.6538 0.0407  0.0980  -0.0094 85  GLU   A C   
627  O O   . GLU   A 79  ? 0.4296 0.4237 0.6334 0.0352  0.0866  -0.0129 85  GLU   A O   
628  C CB  . GLU   A 79  ? 0.4533 0.4592 0.7020 0.0449  0.1117  -0.0055 85  GLU   A CB  
629  C CG  . GLU   A 79  ? 0.5667 0.5779 0.7837 0.0391  0.1045  -0.0095 85  GLU   A CG  
630  C CD  . GLU   A 79  ? 0.6768 0.7068 0.9031 0.0394  0.0959  0.0043  85  GLU   A CD  
631  O OE1 . GLU   A 79  ? 0.6994 0.7357 0.9468 0.0428  0.1054  0.0084  85  GLU   A OE1 
632  O OE2 . GLU   A 79  ? 0.6850 0.7233 0.8983 0.0358  0.0801  0.0111  85  GLU   A OE2 
633  N N   . ALA   A 80  ? 0.4329 0.4109 0.6778 0.0432  0.1112  -0.0168 86  ALA   A N   
634  C CA  . ALA   A 80  ? 0.4507 0.4126 0.6760 0.0382  0.1121  -0.0298 86  ALA   A CA  
635  C C   . ALA   A 80  ? 0.4673 0.4227 0.6541 0.0305  0.1117  -0.0446 86  ALA   A C   
636  O O   . ALA   A 80  ? 0.4789 0.4352 0.6567 0.0297  0.1185  -0.0491 86  ALA   A O   
637  C CB  . ALA   A 80  ? 0.4531 0.3978 0.6991 0.0414  0.1293  -0.0368 86  ALA   A CB  
638  N N   . SER   A 81  ? 0.4621 0.4123 0.6267 0.0243  0.1025  -0.0504 87  SER   A N   
639  C CA  . SER   A 81  ? 0.4678 0.4122 0.5971 0.0160  0.0999  -0.0627 87  SER   A CA  
640  C C   . SER   A 81  ? 0.4759 0.4054 0.5948 0.0099  0.1005  -0.0732 87  SER   A C   
641  O O   . SER   A 81  ? 0.4693 0.3929 0.6087 0.0129  0.1040  -0.0710 87  SER   A O   
642  C CB  . SER   A 81  ? 0.4875 0.4465 0.6008 0.0140  0.0830  -0.0552 87  SER   A CB  
643  O OG  . SER   A 81  ? 0.4973 0.4608 0.6138 0.0136  0.0713  -0.0492 87  SER   A OG  
644  N N   . GLU   A 82  ? 0.4929 0.4163 0.5804 0.0007  0.0968  -0.0838 88  GLU   A N   
645  C CA  . GLU   A 82  ? 0.5119 0.4236 0.5864 -0.0072 0.0940  -0.0930 88  GLU   A CA  
646  C C   . GLU   A 82  ? 0.4909 0.4126 0.5762 -0.0054 0.0797  -0.0827 88  GLU   A C   
647  O O   . GLU   A 82  ? 0.5060 0.4194 0.5906 -0.0100 0.0781  -0.0873 88  GLU   A O   
648  C CB  . GLU   A 82  ? 0.5784 0.4874 0.6170 -0.0182 0.0877  -0.1019 88  GLU   A CB  
649  C CG  . GLU   A 82  ? 0.6891 0.5941 0.7106 -0.0210 0.0973  -0.1086 88  GLU   A CG  
650  C CD  . GLU   A 82  ? 0.7872 0.7087 0.8037 -0.0177 0.0882  -0.0986 88  GLU   A CD  
651  O OE1 . GLU   A 82  ? 0.8300 0.7544 0.8210 -0.0251 0.0783  -0.0998 88  GLU   A OE1 
652  O OE2 . GLU   A 82  ? 0.7893 0.7208 0.8277 -0.0084 0.0906  -0.0889 88  GLU   A OE2 
653  N N   . TYR   A 83  ? 0.4593 0.3981 0.5523 0.0001  0.0695  -0.0694 89  TYR   A N   
654  C CA  . TYR   A 83  ? 0.4305 0.3788 0.5301 0.0009  0.0572  -0.0603 89  TYR   A CA  
655  C C   . TYR   A 83  ? 0.3969 0.3497 0.5243 0.0078  0.0583  -0.0488 89  TYR   A C   
656  O O   . TYR   A 83  ? 0.3883 0.3436 0.5217 0.0069  0.0516  -0.0439 89  TYR   A O   
657  C CB  . TYR   A 83  ? 0.4229 0.3854 0.5098 0.0007  0.0457  -0.0540 89  TYR   A CB  
658  C CG  . TYR   A 83  ? 0.4411 0.4011 0.5017 -0.0065 0.0418  -0.0622 89  TYR   A CG  
659  C CD1 . TYR   A 83  ? 0.4611 0.4212 0.5089 -0.0071 0.0457  -0.0651 89  TYR   A CD1 
660  C CD2 . TYR   A 83  ? 0.4535 0.4124 0.5031 -0.0132 0.0333  -0.0656 89  TYR   A CD2 
661  C CE1 . TYR   A 83  ? 0.4848 0.4435 0.5078 -0.0143 0.0406  -0.0704 89  TYR   A CE1 
662  C CE2 . TYR   A 83  ? 0.4732 0.4316 0.5001 -0.0204 0.0276  -0.0707 89  TYR   A CE2 
663  C CZ  . TYR   A 83  ? 0.5001 0.4579 0.5129 -0.0211 0.0313  -0.0730 89  TYR   A CZ  
664  O OH  . TYR   A 83  ? 0.5398 0.4974 0.5293 -0.0291 0.0247  -0.0762 89  TYR   A OH  
665  N N   . TYR   A 84  ? 0.3818 0.3370 0.5267 0.0142  0.0659  -0.0431 90  TYR   A N   
666  C CA  . TYR   A 84  ? 0.3709 0.3324 0.5433 0.0201  0.0650  -0.0294 90  TYR   A CA  
667  C C   . TYR   A 84  ? 0.4031 0.3587 0.6005 0.0261  0.0784  -0.0278 90  TYR   A C   
668  O O   . TYR   A 84  ? 0.4153 0.3686 0.6099 0.0273  0.0873  -0.0336 90  TYR   A O   
669  C CB  . TYR   A 84  ? 0.3369 0.3162 0.5098 0.0220  0.0546  -0.0162 90  TYR   A CB  
670  C CG  . TYR   A 84  ? 0.2985 0.2850 0.4529 0.0175  0.0423  -0.0147 90  TYR   A CG  
671  C CD1 . TYR   A 84  ? 0.2966 0.2849 0.4564 0.0160  0.0362  -0.0087 90  TYR   A CD1 
672  C CD2 . TYR   A 84  ? 0.2874 0.2793 0.4213 0.0151  0.0375  -0.0180 90  TYR   A CD2 
673  C CE1 . TYR   A 84  ? 0.2796 0.2742 0.4247 0.0122  0.0271  -0.0078 90  TYR   A CE1 
674  C CE2 . TYR   A 84  ? 0.2678 0.2660 0.3887 0.0119  0.0278  -0.0161 90  TYR   A CE2 
675  C CZ  . TYR   A 84  ? 0.2669 0.2665 0.3938 0.0106  0.0232  -0.0113 90  TYR   A CZ  
676  O OH  . TYR   A 84  ? 0.2385 0.2435 0.3544 0.0076  0.0160  -0.0103 90  TYR   A OH  
677  N N   . PRO   A 85  ? 0.4162 0.3712 0.6410 0.0303  0.0798  -0.0177 91  PRO   A N   
678  C CA  . PRO   A 85  ? 0.4218 0.3748 0.6776 0.0376  0.0918  -0.0121 91  PRO   A CA  
679  C C   . PRO   A 85  ? 0.4241 0.3957 0.6880 0.0410  0.0862  0.0008  91  PRO   A C   
680  O O   . PRO   A 85  ? 0.4357 0.4203 0.6834 0.0377  0.0727  0.0068  91  PRO   A O   
681  C CB  . PRO   A 85  ? 0.4231 0.3741 0.7051 0.0404  0.0900  -0.0006 91  PRO   A CB  
682  C CG  . PRO   A 85  ? 0.4345 0.3962 0.7000 0.0353  0.0731  0.0065  91  PRO   A CG  
683  C CD  . PRO   A 85  ? 0.4213 0.3792 0.6522 0.0288  0.0703  -0.0088 91  PRO   A CD  
684  N N   . ALA   A 86  ? 0.4075 0.3806 0.6989 0.0475  0.0967  0.0061  92  ALA   A N   
685  C CA  . ALA   A 86  ? 0.3976 0.3894 0.7027 0.0504  0.0913  0.0204  92  ALA   A CA  
686  C C   . ALA   A 86  ? 0.3758 0.3815 0.6910 0.0494  0.0752  0.0394  92  ALA   A C   
687  O O   . ALA   A 86  ? 0.3739 0.3743 0.7060 0.0509  0.0750  0.0455  92  ALA   A O   
688  C CB  . ALA   A 86  ? 0.3988 0.3893 0.7402 0.0582  0.1065  0.0245  92  ALA   A CB  
689  N N   . ARG   A 87  ? 0.3546 0.3753 0.6533 0.0450  0.0617  0.0464  93  ARG   A N   
690  C CA  . ARG   A 87  ? 0.3234 0.3552 0.6242 0.0415  0.0470  0.0623  93  ARG   A CA  
691  C C   . ARG   A 87  ? 0.3027 0.3510 0.5905 0.0367  0.0354  0.0705  93  ARG   A C   
692  O O   . ARG   A 87  ? 0.3165 0.3665 0.5919 0.0364  0.0385  0.0630  93  ARG   A O   
693  C CB  . ARG   A 87  ? 0.3259 0.3486 0.6035 0.0366  0.0423  0.0542  93  ARG   A CB  
694  C CG  . ARG   A 87  ? 0.3410 0.3645 0.5824 0.0312  0.0373  0.0427  93  ARG   A CG  
695  C CD  . ARG   A 87  ? 0.3378 0.3496 0.5589 0.0279  0.0379  0.0293  93  ARG   A CD  
696  N NE  . ARG   A 87  ? 0.3222 0.3394 0.5168 0.0224  0.0284  0.0271  93  ARG   A NE  
697  C CZ  . ARG   A 87  ? 0.3067 0.3264 0.4819 0.0207  0.0273  0.0201  93  ARG   A CZ  
698  N NH1 . ARG   A 87  ? 0.2863 0.3094 0.4414 0.0164  0.0200  0.0184  93  ARG   A NH1 
699  N NH2 . ARG   A 87  ? 0.3050 0.3236 0.4821 0.0234  0.0341  0.0156  93  ARG   A NH2 
700  N N   . TYR   A 88  ? 0.2799 0.3387 0.5681 0.0319  0.0225  0.0853  94  TYR   A N   
701  C CA  . TYR   A 88  ? 0.2783 0.3498 0.5487 0.0251  0.0116  0.0912  94  TYR   A CA  
702  C C   . TYR   A 88  ? 0.2637 0.3290 0.4992 0.0192  0.0073  0.0803  94  TYR   A C   
703  O O   . TYR   A 88  ? 0.2797 0.3397 0.5109 0.0172  0.0049  0.0806  94  TYR   A O   
704  C CB  . TYR   A 88  ? 0.2828 0.3687 0.5692 0.0208  -0.0001 0.1130  94  TYR   A CB  
705  C CG  . TYR   A 88  ? 0.2889 0.3847 0.6122 0.0263  0.0027  0.1258  94  TYR   A CG  
706  C CD1 . TYR   A 88  ? 0.3007 0.3928 0.6590 0.0338  0.0096  0.1329  94  TYR   A CD1 
707  C CD2 . TYR   A 88  ? 0.2983 0.4066 0.6237 0.0243  -0.0001 0.1302  94  TYR   A CD2 
708  C CE1 . TYR   A 88  ? 0.3094 0.4108 0.7062 0.0400  0.0140  0.1448  94  TYR   A CE1 
709  C CE2 . TYR   A 88  ? 0.3105 0.4295 0.6735 0.0296  0.0031  0.1427  94  TYR   A CE2 
710  C CZ  . TYR   A 88  ? 0.3216 0.4373 0.7213 0.0379  0.0106  0.1500  94  TYR   A CZ  
711  O OH  . TYR   A 88  ? 0.3535 0.4802 0.7948 0.0440  0.0151  0.1629  94  TYR   A OH  
712  N N   . GLN   A 89  ? 0.2292 0.2946 0.4423 0.0170  0.0074  0.0706  95  GLN   A N   
713  C CA  . GLN   A 89  ? 0.2015 0.2622 0.3846 0.0118  0.0035  0.0616  95  GLN   A CA  
714  C C   . GLN   A 89  ? 0.1858 0.2569 0.3578 0.0038  -0.0067 0.0718  95  GLN   A C   
715  O O   . GLN   A 89  ? 0.2081 0.2884 0.3840 0.0020  -0.0096 0.0783  95  GLN   A O   
716  C CB  . GLN   A 89  ? 0.2098 0.2639 0.3754 0.0134  0.0090  0.0464  95  GLN   A CB  
717  C CG  . GLN   A 89  ? 0.2188 0.2697 0.3576 0.0086  0.0047  0.0391  95  GLN   A CG  
718  C CD  . GLN   A 89  ? 0.2471 0.2898 0.3720 0.0106  0.0094  0.0251  95  GLN   A CD  
719  O OE1 . GLN   A 89  ? 0.2551 0.2905 0.3858 0.0141  0.0160  0.0180  95  GLN   A OE1 
720  N NE2 . GLN   A 89  ? 0.1923 0.2353 0.2980 0.0075  0.0063  0.0210  95  GLN   A NE2 
721  N N   . SER   A 90  ? 0.1740 0.2436 0.3323 -0.0018 -0.0116 0.0734  96  SER   A N   
722  C CA  . SER   A 90  ? 0.1762 0.2528 0.3196 -0.0114 -0.0200 0.0814  96  SER   A CA  
723  C C   . SER   A 90  ? 0.1947 0.2666 0.3105 -0.0151 -0.0189 0.0697  96  SER   A C   
724  O O   . SER   A 90  ? 0.1926 0.2562 0.3015 -0.0104 -0.0131 0.0568  96  SER   A O   
725  C CB  . SER   A 90  ? 0.1993 0.2762 0.3425 -0.0166 -0.0245 0.0903  96  SER   A CB  
726  O OG  . SER   A 90  ? 0.2285 0.2955 0.3609 -0.0153 -0.0198 0.0794  96  SER   A OG  
727  N N   . HIS   A 91  ? 0.1866 0.2635 0.2872 -0.0243 -0.0247 0.0747  97  HIS   A N   
728  C CA  . HIS   A 91  ? 0.1847 0.2561 0.2603 -0.0289 -0.0231 0.0649  97  HIS   A CA  
729  C C   . HIS   A 91  ? 0.1790 0.2471 0.2540 -0.0223 -0.0181 0.0549  97  HIS   A C   
730  O O   . HIS   A 91  ? 0.1855 0.2462 0.2461 -0.0216 -0.0144 0.0447  97  HIS   A O   
731  C CB  . HIS   A 91  ? 0.2059 0.2690 0.2687 -0.0304 -0.0196 0.0580  97  HIS   A CB  
732  C CG  . HIS   A 91  ? 0.2445 0.3101 0.3040 -0.0385 -0.0238 0.0677  97  HIS   A CG  
733  N ND1 . HIS   A 91  ? 0.2833 0.3482 0.3208 -0.0502 -0.0260 0.0695  97  HIS   A ND1 
734  C CD2 . HIS   A 91  ? 0.2522 0.3203 0.3270 -0.0371 -0.0260 0.0764  97  HIS   A CD2 
735  C CE1 . HIS   A 91  ? 0.2863 0.3540 0.3247 -0.0562 -0.0299 0.0795  97  HIS   A CE1 
736  N NE2 . HIS   A 91  ? 0.2753 0.3451 0.3370 -0.0482 -0.0302 0.0844  97  HIS   A NE2 
737  N N   . LEU   A 92  ? 0.1635 0.2375 0.2548 -0.0181 -0.0178 0.0590  98  LEU   A N   
738  C CA  . LEU   A 92  ? 0.1609 0.2319 0.2511 -0.0128 -0.0126 0.0503  98  LEU   A CA  
739  C C   . LEU   A 92  ? 0.1625 0.2395 0.2470 -0.0180 -0.0156 0.0540  98  LEU   A C   
740  O O   . LEU   A 92  ? 0.1698 0.2567 0.2633 -0.0230 -0.0213 0.0657  98  LEU   A O   
741  C CB  . LEU   A 92  ? 0.1687 0.2405 0.2813 -0.0044 -0.0072 0.0506  98  LEU   A CB  
742  C CG  . LEU   A 92  ? 0.1949 0.2624 0.3060 0.0007  -0.0001 0.0411  98  LEU   A CG  
743  C CD1 . LEU   A 92  ? 0.1981 0.2551 0.2909 0.0020  0.0024  0.0286  98  LEU   A CD1 
744  C CD2 . LEU   A 92  ? 0.2193 0.2863 0.3534 0.0077  0.0073  0.0414  98  LEU   A CD2 
745  N N   . MET   A 93  ? 0.1708 0.2418 0.2409 -0.0174 -0.0123 0.0448  99  MET   A N   
746  C CA  . MET   A 93  ? 0.1691 0.2439 0.2326 -0.0226 -0.0143 0.0470  99  MET   A CA  
747  C C   . MET   A 93  ? 0.1717 0.2460 0.2413 -0.0164 -0.0086 0.0422  99  MET   A C   
748  O O   . MET   A 93  ? 0.1773 0.2431 0.2400 -0.0114 -0.0037 0.0328  99  MET   A O   
749  C CB  . MET   A 93  ? 0.1956 0.2620 0.2355 -0.0284 -0.0147 0.0405  99  MET   A CB  
750  C CG  . MET   A 93  ? 0.2094 0.2746 0.2398 -0.0359 -0.0184 0.0437  99  MET   A CG  
751  S SD  . MET   A 93  ? 0.2654 0.3180 0.2705 -0.0418 -0.0149 0.0344  99  MET   A SD  
752  C CE  . MET   A 93  ? 0.2837 0.3281 0.2932 -0.0299 -0.0083 0.0241  99  MET   A CE  
753  N N   . LEU   A 94  ? 0.1509 0.2344 0.2326 -0.0176 -0.0091 0.0490  100 LEU   A N   
754  C CA  . LEU   A 94  ? 0.1654 0.2479 0.2519 -0.0125 -0.0019 0.0442  100 LEU   A CA  
755  C C   . LEU   A 94  ? 0.1597 0.2417 0.2329 -0.0176 -0.0027 0.0428  100 LEU   A C   
756  O O   . LEU   A 94  ? 0.1676 0.2544 0.2361 -0.0257 -0.0090 0.0489  100 LEU   A O   
757  C CB  . LEU   A 94  ? 0.1834 0.2764 0.2977 -0.0086 0.0015  0.0520  100 LEU   A CB  
758  C CG  . LEU   A 94  ? 0.2363 0.3290 0.3690 -0.0024 0.0046  0.0538  100 LEU   A CG  
759  C CD1 . LEU   A 94  ? 0.2413 0.3432 0.4047 0.0024  0.0107  0.0609  100 LEU   A CD1 
760  C CD2 . LEU   A 94  ? 0.2634 0.3430 0.3855 0.0028  0.0110  0.0412  100 LEU   A CD2 
761  N N   . ALA   A 95  ? 0.1709 0.2468 0.2374 -0.0139 0.0036  0.0354  101 ALA   A N   
762  C CA  . ALA   A 95  ? 0.1629 0.2376 0.2186 -0.0181 0.0040  0.0344  101 ALA   A CA  
763  C C   . ALA   A 95  ? 0.1693 0.2436 0.2293 -0.0137 0.0122  0.0309  101 ALA   A C   
764  O O   . ALA   A 95  ? 0.1761 0.2472 0.2413 -0.0079 0.0179  0.0263  101 ALA   A O   
765  C CB  . ALA   A 95  ? 0.1847 0.2475 0.2179 -0.0200 0.0023  0.0275  101 ALA   A CB  
766  N N   . VAL   A 96  ? 0.1634 0.2402 0.2207 -0.0174 0.0135  0.0328  102 VAL   A N   
767  C CA  . VAL   A 96  ? 0.1716 0.2463 0.2282 -0.0147 0.0222  0.0288  102 VAL   A CA  
768  C C   . VAL   A 96  ? 0.2064 0.2681 0.2389 -0.0149 0.0219  0.0212  102 VAL   A C   
769  O O   . VAL   A 96  ? 0.2345 0.2918 0.2544 -0.0191 0.0170  0.0218  102 VAL   A O   
770  C CB  . VAL   A 96  ? 0.1791 0.2631 0.2448 -0.0191 0.0237  0.0352  102 VAL   A CB  
771  C CG1 . VAL   A 96  ? 0.1910 0.2718 0.2527 -0.0174 0.0338  0.0307  102 VAL   A CG1 
772  C CG2 . VAL   A 96  ? 0.1746 0.2732 0.2679 -0.0186 0.0226  0.0446  102 VAL   A CG2 
773  N N   . GLY   A 97  ? 0.2007 0.2563 0.2282 -0.0109 0.0271  0.0148  103 GLY   A N   
774  C CA  . GLY   A 97  ? 0.2256 0.2705 0.2327 -0.0112 0.0256  0.0094  103 GLY   A CA  
775  C C   . GLY   A 97  ? 0.2315 0.2714 0.2349 -0.0083 0.0310  0.0027  103 GLY   A C   
776  O O   . GLY   A 97  ? 0.2490 0.2915 0.2656 -0.0052 0.0359  0.0011  103 GLY   A O   
777  N N   . HIS   A 98  ? 0.2345 0.2665 0.2195 -0.0101 0.0305  -0.0009 104 HIS   A N   
778  C CA  . HIS   A 98  ? 0.2370 0.2631 0.2134 -0.0100 0.0346  -0.0077 104 HIS   A CA  
779  C C   . HIS   A 98  ? 0.2418 0.2650 0.2194 -0.0076 0.0293  -0.0106 104 HIS   A C   
780  O O   . HIS   A 98  ? 0.2442 0.2666 0.2193 -0.0073 0.0211  -0.0081 104 HIS   A O   
781  C CB  . HIS   A 98  ? 0.2420 0.2614 0.1963 -0.0146 0.0336  -0.0088 104 HIS   A CB  
782  C CG  . HIS   A 98  ? 0.2603 0.2730 0.2017 -0.0170 0.0374  -0.0161 104 HIS   A CG  
783  N ND1 . HIS   A 98  ? 0.2869 0.2982 0.2302 -0.0177 0.0496  -0.0218 104 HIS   A ND1 
784  C CD2 . HIS   A 98  ? 0.2666 0.2737 0.1943 -0.0194 0.0307  -0.0185 104 HIS   A CD2 
785  C CE1 . HIS   A 98  ? 0.3014 0.3047 0.2293 -0.0214 0.0505  -0.0288 104 HIS   A CE1 
786  N NE2 . HIS   A 98  ? 0.2853 0.2867 0.2031 -0.0229 0.0382  -0.0264 104 HIS   A NE2 
787  N N   . SER   A 99  ? 0.2468 0.2673 0.2276 -0.0065 0.0347  -0.0164 105 SER   A N   
788  C CA  . SER   A 99  ? 0.2472 0.2640 0.2278 -0.0055 0.0306  -0.0201 105 SER   A CA  
789  C C   . SER   A 99  ? 0.2882 0.2981 0.2640 -0.0071 0.0392  -0.0287 105 SER   A C   
790  O O   . SER   A 99  ? 0.3083 0.3180 0.2901 -0.0066 0.0502  -0.0310 105 SER   A O   
791  C CB  . SER   A 99  ? 0.2538 0.2758 0.2524 -0.0014 0.0272  -0.0163 105 SER   A CB  
792  O OG  . SER   A 99  ? 0.2798 0.3057 0.2962 0.0014  0.0346  -0.0153 105 SER   A OG  
793  N N   . GLU   A 100 ? 0.2778 0.2817 0.2418 -0.0101 0.0345  -0.0332 106 GLU   A N   
794  C CA  . GLU   A 100 ? 0.2958 0.2908 0.2508 -0.0139 0.0398  -0.0425 106 GLU   A CA  
795  C C   . GLU   A 100 ? 0.3209 0.3155 0.2842 -0.0123 0.0334  -0.0434 106 GLU   A C   
796  O O   . GLU   A 100 ? 0.3263 0.3267 0.2968 -0.0095 0.0243  -0.0370 106 GLU   A O   
797  C CB  . GLU   A 100 ? 0.3251 0.3143 0.2526 -0.0223 0.0366  -0.0454 106 GLU   A CB  
798  C CG  . GLU   A 100 ? 0.3519 0.3405 0.2706 -0.0246 0.0447  -0.0452 106 GLU   A CG  
799  C CD  . GLU   A 100 ? 0.3790 0.3619 0.2689 -0.0339 0.0416  -0.0467 106 GLU   A CD  
800  O OE1 . GLU   A 100 ? 0.4133 0.3891 0.2871 -0.0408 0.0395  -0.0528 106 GLU   A OE1 
801  O OE2 . GLU   A 100 ? 0.3519 0.3375 0.2348 -0.0353 0.0407  -0.0410 106 GLU   A OE2 
802  N N   . PRO   A 101 ? 0.3434 0.3301 0.3067 -0.0143 0.0393  -0.0515 107 PRO   A N   
803  C CA  . PRO   A 101 ? 0.3387 0.3253 0.3128 -0.0127 0.0339  -0.0517 107 PRO   A CA  
804  C C   . PRO   A 101 ? 0.3415 0.3323 0.3101 -0.0147 0.0199  -0.0473 107 PRO   A C   
805  O O   . PRO   A 101 ? 0.3467 0.3432 0.3300 -0.0104 0.0147  -0.0421 107 PRO   A O   
806  C CB  . PRO   A 101 ? 0.3625 0.3370 0.3302 -0.0174 0.0427  -0.0629 107 PRO   A CB  
807  C CG  . PRO   A 101 ? 0.3778 0.3478 0.3438 -0.0172 0.0571  -0.0673 107 PRO   A CG  
808  C CD  . PRO   A 101 ? 0.3540 0.3311 0.3103 -0.0177 0.0532  -0.0610 107 PRO   A CD  
809  N N   . GLY   A 102 ? 0.3207 0.3095 0.2694 -0.0213 0.0140  -0.0482 108 GLY   A N   
810  C CA  . GLY   A 102 ? 0.2943 0.2880 0.2401 -0.0233 0.0009  -0.0426 108 GLY   A CA  
811  C C   . GLY   A 102 ? 0.2607 0.2626 0.2170 -0.0173 -0.0041 -0.0331 108 GLY   A C   
812  O O   . GLY   A 102 ? 0.2642 0.2704 0.2237 -0.0172 -0.0132 -0.0277 108 GLY   A O   
813  N N   . ASP   A 103 ? 0.2384 0.2421 0.2000 -0.0130 0.0024  -0.0310 109 ASP   A N   
814  C CA  . ASP   A 103 ? 0.2131 0.2227 0.1832 -0.0087 -0.0010 -0.0235 109 ASP   A CA  
815  C C   . ASP   A 103 ? 0.2056 0.2189 0.1925 -0.0043 -0.0021 -0.0214 109 ASP   A C   
816  O O   . ASP   A 103 ? 0.2008 0.2173 0.1928 -0.0020 -0.0050 -0.0163 109 ASP   A O   
817  C CB  . ASP   A 103 ? 0.2112 0.2219 0.1807 -0.0073 0.0052  -0.0216 109 ASP   A CB  
818  C CG  . ASP   A 103 ? 0.2427 0.2505 0.1948 -0.0118 0.0049  -0.0212 109 ASP   A CG  
819  O OD1 . ASP   A 103 ? 0.2496 0.2567 0.1932 -0.0145 -0.0031 -0.0182 109 ASP   A OD1 
820  O OD2 . ASP   A 103 ? 0.2370 0.2437 0.1849 -0.0128 0.0130  -0.0231 109 ASP   A OD2 
821  N N   . CYS   A 104 ? 0.2087 0.2206 0.2034 -0.0038 0.0005  -0.0252 110 CYS   A N   
822  C CA  . CYS   A 104 ? 0.1945 0.2098 0.2039 -0.0006 -0.0006 -0.0225 110 CYS   A CA  
823  C C   . CYS   A 104 ? 0.1925 0.2103 0.2036 -0.0008 -0.0076 -0.0195 110 CYS   A C   
824  O O   . CYS   A 104 ? 0.2195 0.2365 0.2247 -0.0037 -0.0127 -0.0205 110 CYS   A O   
825  C CB  . CYS   A 104 ? 0.2001 0.2122 0.2176 -0.0006 0.0032  -0.0267 110 CYS   A CB  
826  S SG  . CYS   A 104 ? 0.2404 0.2512 0.2668 0.0021  0.0132  -0.0274 110 CYS   A SG  
827  N N   . GLY   A 105 ? 0.1715 0.1925 0.1903 0.0016  -0.0076 -0.0153 111 GLY   A N   
828  C CA  . GLY   A 105 ? 0.1714 0.1944 0.1950 0.0022  -0.0116 -0.0126 111 GLY   A CA  
829  C C   . GLY   A 105 ? 0.1836 0.2063 0.2032 0.0031  -0.0122 -0.0089 111 GLY   A C   
830  O O   . GLY   A 105 ? 0.1865 0.2099 0.2127 0.0045  -0.0127 -0.0064 111 GLY   A O   
831  N N   . GLY   A 106 ? 0.1761 0.1970 0.1860 0.0022  -0.0110 -0.0087 112 GLY   A N   
832  C CA  . GLY   A 106 ? 0.1704 0.1896 0.1767 0.0026  -0.0108 -0.0052 112 GLY   A CA  
833  C C   . GLY   A 106 ? 0.1739 0.1927 0.1845 0.0031  -0.0068 -0.0042 112 GLY   A C   
834  O O   . GLY   A 106 ? 0.1719 0.1928 0.1842 0.0022  -0.0042 -0.0048 112 GLY   A O   
835  N N   . ILE   A 107 ? 0.1621 0.1780 0.1750 0.0038  -0.0060 -0.0023 113 ILE   A N   
836  C CA  . ILE   A 107 ? 0.1537 0.1672 0.1672 0.0024  -0.0011 -0.0027 113 ILE   A CA  
837  C C   . ILE   A 107 ? 0.1663 0.1771 0.1706 -0.0008 0.0011  -0.0019 113 ILE   A C   
838  O O   . ILE   A 107 ? 0.1778 0.1857 0.1775 -0.0007 0.0003  -0.0005 113 ILE   A O   
839  C CB  . ILE   A 107 ? 0.1887 0.1986 0.2103 0.0043  0.0014  -0.0023 113 ILE   A CB  
840  C CG1 . ILE   A 107 ? 0.1968 0.2113 0.2296 0.0063  -0.0002 -0.0028 113 ILE   A CG1 
841  C CG2 . ILE   A 107 ? 0.2272 0.2308 0.2451 0.0014  0.0084  -0.0040 113 ILE   A CG2 
842  C CD1 . ILE   A 107 ? 0.2230 0.2357 0.2693 0.0092  0.0028  -0.0014 113 ILE   A CD1 
843  N N   . LEU   A 108 ? 0.1548 0.1667 0.1566 -0.0045 0.0033  -0.0021 114 LEU   A N   
844  C CA  . LEU   A 108 ? 0.1608 0.1706 0.1541 -0.0097 0.0049  -0.0010 114 LEU   A CA  
845  C C   . LEU   A 108 ? 0.1960 0.1982 0.1852 -0.0132 0.0098  -0.0033 114 LEU   A C   
846  O O   . LEU   A 108 ? 0.1932 0.1958 0.1848 -0.0141 0.0118  -0.0045 114 LEU   A O   
847  C CB  . LEU   A 108 ? 0.1576 0.1748 0.1518 -0.0128 0.0030  0.0016  114 LEU   A CB  
848  C CG  . LEU   A 108 ? 0.1789 0.1964 0.1654 -0.0202 0.0029  0.0042  114 LEU   A CG  
849  C CD1 . LEU   A 108 ? 0.1973 0.2137 0.1802 -0.0206 0.0028  0.0051  114 LEU   A CD1 
850  C CD2 . LEU   A 108 ? 0.1921 0.2191 0.1840 -0.0232 -0.0004 0.0093  114 LEU   A CD2 
851  N N   . ARG   A 109 ? 0.1932 0.1875 0.1761 -0.0156 0.0128  -0.0041 115 ARG   A N   
852  C CA  . ARG   A 109 ? 0.2001 0.1843 0.1779 -0.0196 0.0197  -0.0078 115 ARG   A CA  
853  C C   . ARG   A 109 ? 0.2145 0.1936 0.1791 -0.0281 0.0210  -0.0083 115 ARG   A C   
854  O O   . ARG   A 109 ? 0.2329 0.2133 0.1953 -0.0286 0.0180  -0.0058 115 ARG   A O   
855  C CB  . ARG   A 109 ? 0.2353 0.2114 0.2211 -0.0139 0.0236  -0.0085 115 ARG   A CB  
856  C CG  . ARG   A 109 ? 0.3014 0.2825 0.3019 -0.0064 0.0216  -0.0071 115 ARG   A CG  
857  C CD  . ARG   A 109 ? 0.3266 0.3015 0.3379 -0.0010 0.0238  -0.0051 115 ARG   A CD  
858  N NE  . ARG   A 109 ? 0.3961 0.3619 0.4123 -0.0015 0.0340  -0.0090 115 ARG   A NE  
859  C CZ  . ARG   A 109 ? 0.3978 0.3661 0.4265 0.0017  0.0373  -0.0099 115 ARG   A CZ  
860  N NH1 . ARG   A 109 ? 0.3590 0.3384 0.3977 0.0059  0.0299  -0.0064 115 ARG   A NH1 
861  N NH2 . ARG   A 109 ? 0.3954 0.3547 0.4257 -0.0003 0.0489  -0.0148 115 ARG   A NH2 
862  N N   . CYS   A 110 ? 0.2258 0.1971 0.1809 -0.0354 0.0268  -0.0123 116 CYS   A N   
863  C CA  . CYS   A 110 ? 0.2497 0.2124 0.1900 -0.0454 0.0295  -0.0144 116 CYS   A CA  
864  C C   . CYS   A 110 ? 0.2715 0.2173 0.2093 -0.0461 0.0409  -0.0212 116 CYS   A C   
865  O O   . CYS   A 110 ? 0.2764 0.2198 0.2272 -0.0378 0.0455  -0.0225 116 CYS   A O   
866  C CB  . CYS   A 110 ? 0.2607 0.2283 0.1885 -0.0564 0.0262  -0.0131 116 CYS   A CB  
867  S SG  . CYS   A 110 ? 0.2650 0.2271 0.1862 -0.0608 0.0335  -0.0179 116 CYS   A SG  
868  N N   . GLN   A 111 ? 0.2999 0.2334 0.2223 -0.0564 0.0462  -0.0256 117 GLN   A N   
869  C CA  . GLN   A 111 ? 0.3274 0.2423 0.2480 -0.0574 0.0595  -0.0331 117 GLN   A CA  
870  C C   . GLN   A 111 ? 0.3348 0.2456 0.2557 -0.0578 0.0684  -0.0383 117 GLN   A C   
871  O O   . GLN   A 111 ? 0.3500 0.2467 0.2766 -0.0553 0.0812  -0.0442 117 GLN   A O   
872  C CB  . GLN   A 111 ? 0.3770 0.2777 0.2778 -0.0708 0.0641  -0.0382 117 GLN   A CB  
873  C CG  . GLN   A 111 ? 0.4555 0.3576 0.3341 -0.0861 0.0625  -0.0405 117 GLN   A CG  
874  C CD  . GLN   A 111 ? 0.5964 0.4878 0.4542 -0.1013 0.0634  -0.0440 117 GLN   A CD  
875  O OE1 . GLN   A 111 ? 0.6491 0.5512 0.5025 -0.1070 0.0523  -0.0377 117 GLN   A OE1 
876  N NE2 . GLN   A 111 ? 0.5973 0.4674 0.4430 -0.1084 0.0772  -0.0541 117 GLN   A NE2 
877  N N   . HIS   A 112 ? 0.3177 0.2398 0.2335 -0.0614 0.0630  -0.0361 118 HIS   A N   
878  C CA  . HIS   A 112 ? 0.3183 0.2373 0.2319 -0.0635 0.0713  -0.0404 118 HIS   A CA  
879  C C   . HIS   A 112 ? 0.3066 0.2351 0.2429 -0.0508 0.0703  -0.0373 118 HIS   A C   
880  O O   . HIS   A 112 ? 0.3158 0.2408 0.2548 -0.0509 0.0794  -0.0411 118 HIS   A O   
881  C CB  . HIS   A 112 ? 0.3217 0.2463 0.2150 -0.0769 0.0662  -0.0390 118 HIS   A CB  
882  C CG  . HIS   A 112 ? 0.3564 0.2731 0.2260 -0.0920 0.0654  -0.0414 118 HIS   A CG  
883  N ND1 . HIS   A 112 ? 0.3711 0.2999 0.2359 -0.0972 0.0516  -0.0335 118 HIS   A ND1 
884  C CD2 . HIS   A 112 ? 0.4010 0.2985 0.2508 -0.1037 0.0772  -0.0508 118 HIS   A CD2 
885  C CE1 . HIS   A 112 ? 0.4167 0.3348 0.2596 -0.1121 0.0539  -0.0376 118 HIS   A CE1 
886  N NE2 . HIS   A 112 ? 0.4240 0.3222 0.2558 -0.1168 0.0693  -0.0486 118 HIS   A NE2 
887  N N   . GLY   A 113 ? 0.2704 0.2111 0.2217 -0.0411 0.0597  -0.0304 119 GLY   A N   
888  C CA  . GLY   A 113 ? 0.2591 0.2091 0.2302 -0.0307 0.0572  -0.0272 119 GLY   A CA  
889  C C   . GLY   A 113 ? 0.2319 0.1973 0.2075 -0.0271 0.0440  -0.0206 119 GLY   A C   
890  O O   . GLY   A 113 ? 0.2446 0.2140 0.2134 -0.0294 0.0369  -0.0175 119 GLY   A O   
891  N N   . VAL   A 114 ? 0.2138 0.1876 0.2021 -0.0215 0.0417  -0.0187 120 VAL   A N   
892  C CA  . VAL   A 114 ? 0.2065 0.1928 0.2003 -0.0179 0.0310  -0.0136 120 VAL   A CA  
893  C C   . VAL   A 114 ? 0.1995 0.1911 0.1823 -0.0253 0.0269  -0.0112 120 VAL   A C   
894  O O   . VAL   A 114 ? 0.2164 0.2067 0.1929 -0.0312 0.0306  -0.0122 120 VAL   A O   
895  C CB  . VAL   A 114 ? 0.2026 0.1950 0.2130 -0.0111 0.0299  -0.0126 120 VAL   A CB  
896  C CG1 . VAL   A 114 ? 0.2122 0.2149 0.2261 -0.0090 0.0208  -0.0090 120 VAL   A CG1 
897  C CG2 . VAL   A 114 ? 0.2158 0.2058 0.2400 -0.0039 0.0310  -0.0121 120 VAL   A CG2 
898  N N   . VAL   A 115 ? 0.1949 0.1931 0.1767 -0.0251 0.0195  -0.0072 121 VAL   A N   
899  C CA  . VAL   A 115 ? 0.1948 0.2002 0.1715 -0.0310 0.0142  -0.0025 121 VAL   A CA  
900  C C   . VAL   A 115 ? 0.1975 0.2123 0.1873 -0.0254 0.0093  0.0012  121 VAL   A C   
901  O O   . VAL   A 115 ? 0.1907 0.2103 0.1810 -0.0291 0.0069  0.0053  121 VAL   A O   
902  C CB  . VAL   A 115 ? 0.2103 0.2177 0.1817 -0.0341 0.0102  0.0002  121 VAL   A CB  
903  C CG1 . VAL   A 115 ? 0.2191 0.2370 0.1919 -0.0386 0.0035  0.0075  121 VAL   A CG1 
904  C CG2 . VAL   A 115 ? 0.2173 0.2143 0.1743 -0.0415 0.0150  -0.0035 121 VAL   A CG2 
905  N N   . GLY   A 116 ? 0.1762 0.1929 0.1756 -0.0176 0.0075  0.0002  122 GLY   A N   
906  C CA  . GLY   A 116 ? 0.1809 0.2040 0.1912 -0.0132 0.0041  0.0021  122 GLY   A CA  
907  C C   . GLY   A 116 ? 0.1616 0.1849 0.1774 -0.0069 0.0026  -0.0002 122 GLY   A C   
908  O O   . GLY   A 116 ? 0.1585 0.1776 0.1716 -0.0053 0.0036  -0.0023 122 GLY   A O   
909  N N   . ILE   A 117 ? 0.1545 0.1816 0.1779 -0.0040 0.0005  0.0002  123 ILE   A N   
910  C CA  . ILE   A 117 ? 0.1493 0.1756 0.1746 -0.0001 -0.0009 -0.0028 123 ILE   A CA  
911  C C   . ILE   A 117 ? 0.1533 0.1819 0.1803 0.0008  -0.0008 -0.0025 123 ILE   A C   
912  O O   . ILE   A 117 ? 0.1438 0.1758 0.1776 0.0003  -0.0001 0.0004  123 ILE   A O   
913  C CB  . ILE   A 117 ? 0.1778 0.2040 0.2103 0.0019  -0.0021 -0.0051 123 ILE   A CB  
914  C CG1 . ILE   A 117 ? 0.1917 0.2201 0.2319 0.0012  -0.0014 -0.0038 123 ILE   A CG1 
915  C CG2 . ILE   A 117 ? 0.2073 0.2316 0.2414 0.0024  -0.0014 -0.0055 123 ILE   A CG2 
916  C CD1 . ILE   A 117 ? 0.2219 0.2499 0.2696 0.0025  -0.0029 -0.0067 123 ILE   A CD1 
917  N N   . VAL   A 118 ? 0.1472 0.1741 0.1690 0.0019  -0.0009 -0.0048 124 VAL   A N   
918  C CA  . VAL   A 118 ? 0.1438 0.1717 0.1675 0.0026  0.0019  -0.0059 124 VAL   A CA  
919  C C   . VAL   A 118 ? 0.1501 0.1774 0.1830 0.0041  0.0034  -0.0081 124 VAL   A C   
920  O O   . VAL   A 118 ? 0.1547 0.1795 0.1872 0.0041  0.0012  -0.0111 124 VAL   A O   
921  C CB  . VAL   A 118 ? 0.1621 0.1867 0.1756 0.0022  0.0021  -0.0091 124 VAL   A CB  
922  C CG1 . VAL   A 118 ? 0.1661 0.1900 0.1807 0.0025  0.0075  -0.0120 124 VAL   A CG1 
923  C CG2 . VAL   A 118 ? 0.1804 0.2046 0.1860 0.0008  0.0011  -0.0062 124 VAL   A CG2 
924  N N   . SER   A 119 ? 0.1475 0.1773 0.1904 0.0052  0.0069  -0.0057 125 SER   A N   
925  C CA  . SER   A 119 ? 0.1594 0.1873 0.2135 0.0068  0.0094  -0.0072 125 SER   A CA  
926  C C   . SER   A 119 ? 0.1865 0.2127 0.2482 0.0088  0.0166  -0.0091 125 SER   A C   
927  O O   . SER   A 119 ? 0.2223 0.2430 0.2895 0.0098  0.0207  -0.0138 125 SER   A O   
928  C CB  . SER   A 119 ? 0.1828 0.2152 0.2474 0.0065  0.0071  -0.0001 125 SER   A CB  
929  O OG  . SER   A 119 ? 0.1973 0.2278 0.2754 0.0083  0.0096  0.0003  125 SER   A OG  
930  N N   . THR   A 120 ? 0.1892 0.2200 0.2528 0.0091  0.0190  -0.0056 126 THR   A N   
931  C CA  . THR   A 120 ? 0.2025 0.2324 0.2770 0.0115  0.0279  -0.0070 126 THR   A CA  
932  C C   . THR   A 120 ? 0.2190 0.2505 0.2838 0.0100  0.0307  -0.0081 126 THR   A C   
933  O O   . THR   A 120 ? 0.2027 0.2360 0.2547 0.0075  0.0250  -0.0064 126 THR   A O   
934  C CB  . THR   A 120 ? 0.2408 0.2784 0.3394 0.0141  0.0288  0.0028  126 THR   A CB  
935  O OG1 . THR   A 120 ? 0.2696 0.3168 0.3695 0.0121  0.0243  0.0111  126 THR   A OG1 
936  C CG2 . THR   A 120 ? 0.2668 0.3042 0.3749 0.0147  0.0249  0.0066  126 THR   A CG2 
937  N N   . GLY   A 121 ? 0.2378 0.2683 0.3106 0.0117  0.0403  -0.0101 127 GLY   A N   
938  C CA  . GLY   A 121 ? 0.2474 0.2805 0.3135 0.0100  0.0438  -0.0100 127 GLY   A CA  
939  C C   . GLY   A 121 ? 0.2586 0.2881 0.3328 0.0117  0.0574  -0.0149 127 GLY   A C   
940  O O   . GLY   A 121 ? 0.2678 0.2933 0.3563 0.0148  0.0642  -0.0173 127 GLY   A O   
941  N N   . GLY   A 122 ? 0.2835 0.3131 0.3475 0.0093  0.0620  -0.0167 128 GLY   A N   
942  C CA  . GLY   A 122 ? 0.3013 0.3266 0.3690 0.0096  0.0769  -0.0225 128 GLY   A CA  
943  C C   . GLY   A 122 ? 0.2999 0.3357 0.3805 0.0102  0.0807  -0.0152 128 GLY   A C   
944  O O   . GLY   A 122 ? 0.2971 0.3445 0.3928 0.0114  0.0728  -0.0046 128 GLY   A O   
945  N N   . ASN   A 123 ? 0.2997 0.3316 0.3741 0.0083  0.0930  -0.0208 129 ASN   A N   
946  C CA  . ASN   A 123 ? 0.3023 0.3440 0.3912 0.0086  0.0994  -0.0147 129 ASN   A CA  
947  C C   . ASN   A 123 ? 0.2791 0.3313 0.3652 0.0059  0.0869  -0.0049 129 ASN   A C   
948  O O   . ASN   A 123 ? 0.2775 0.3422 0.3853 0.0068  0.0875  0.0042  129 ASN   A O   
949  C CB  . ASN   A 123 ? 0.3425 0.3915 0.4694 0.0151  0.1087  -0.0094 129 ASN   A CB  
950  C CG  . ASN   A 123 ? 0.4329 0.4691 0.5624 0.0171  0.1263  -0.0209 129 ASN   A CG  
951  O OD1 . ASN   A 123 ? 0.4803 0.5069 0.5889 0.0127  0.1369  -0.0308 129 ASN   A OD1 
952  N ND2 . ASN   A 123 ? 0.4360 0.4702 0.5888 0.0227  0.1299  -0.0201 129 ASN   A ND2 
953  N N   . GLY   A 124 ? 0.2496 0.2965 0.3092 0.0018  0.0767  -0.0070 130 GLY   A N   
954  C CA  . GLY   A 124 ? 0.2267 0.2799 0.2803 -0.0016 0.0660  0.0005  130 GLY   A CA  
955  C C   . GLY   A 124 ? 0.1973 0.2572 0.2616 -0.0005 0.0543  0.0078  130 GLY   A C   
956  O O   . GLY   A 124 ? 0.2223 0.2869 0.2829 -0.0042 0.0464  0.0137  130 GLY   A O   
957  N N   . LEU   A 125 ? 0.1812 0.2390 0.2536 0.0031  0.0527  0.0064  131 LEU   A N   
958  C CA  . LEU   A 125 ? 0.1692 0.2315 0.2471 0.0030  0.0417  0.0126  131 LEU   A CA  
959  C C   . LEU   A 125 ? 0.1743 0.2268 0.2342 0.0028  0.0361  0.0064  131 LEU   A C   
960  O O   . LEU   A 125 ? 0.1987 0.2424 0.2487 0.0038  0.0407  -0.0019 131 LEU   A O   
961  C CB  . LEU   A 125 ? 0.1705 0.2399 0.2760 0.0070  0.0433  0.0188  131 LEU   A CB  
962  C CG  . LEU   A 125 ? 0.1969 0.2797 0.3275 0.0072  0.0464  0.0286  131 LEU   A CG  
963  C CD1 . LEU   A 125 ? 0.2213 0.3088 0.3825 0.0129  0.0516  0.0336  131 LEU   A CD1 
964  C CD2 . LEU   A 125 ? 0.1898 0.2825 0.3191 0.0011  0.0345  0.0385  131 LEU   A CD2 
965  N N   . VAL   A 126 ? 0.1543 0.2088 0.2110 0.0009  0.0266  0.0106  132 VAL   A N   
966  C CA  . VAL   A 126 ? 0.1574 0.2047 0.2029 0.0013  0.0219  0.0061  132 VAL   A CA  
967  C C   . VAL   A 126 ? 0.1611 0.2134 0.2164 0.0008  0.0158  0.0122  132 VAL   A C   
968  O O   . VAL   A 126 ? 0.1735 0.2324 0.2319 -0.0029 0.0117  0.0192  132 VAL   A O   
969  C CB  . VAL   A 126 ? 0.1686 0.2096 0.1937 -0.0013 0.0180  0.0030  132 VAL   A CB  
970  C CG1 . VAL   A 126 ? 0.2023 0.2467 0.2239 -0.0053 0.0139  0.0083  132 VAL   A CG1 
971  C CG2 . VAL   A 126 ? 0.1748 0.2105 0.1938 -0.0004 0.0133  -0.0004 132 VAL   A CG2 
972  N N   . GLY   A 127 ? 0.1627 0.2116 0.2218 0.0032  0.0154  0.0098  133 GLY   A N   
973  C CA  . GLY   A 127 ? 0.1602 0.2131 0.2273 0.0021  0.0103  0.0159  133 GLY   A CA  
974  C C   . GLY   A 127 ? 0.1598 0.2068 0.2146 0.0009  0.0064  0.0120  133 GLY   A C   
975  O O   . GLY   A 127 ? 0.1693 0.2099 0.2181 0.0030  0.0079  0.0051  133 GLY   A O   
976  N N   . PHE   A 128 ? 0.1576 0.2067 0.2081 -0.0033 0.0016  0.0163  134 PHE   A N   
977  C CA  . PHE   A 128 ? 0.1531 0.1967 0.1935 -0.0045 -0.0003 0.0128  134 PHE   A CA  
978  C C   . PHE   A 128 ? 0.1579 0.2040 0.2047 -0.0065 -0.0025 0.0174  134 PHE   A C   
979  O O   . PHE   A 128 ? 0.1626 0.2146 0.2131 -0.0106 -0.0054 0.0250  134 PHE   A O   
980  C CB  . PHE   A 128 ? 0.1469 0.1882 0.1739 -0.0093 -0.0017 0.0127  134 PHE   A CB  
981  C CG  . PHE   A 128 ? 0.1608 0.2002 0.1814 -0.0087 -0.0002 0.0104  134 PHE   A CG  
982  C CD1 . PHE   A 128 ? 0.1572 0.1904 0.1711 -0.0059 0.0009  0.0051  134 PHE   A CD1 
983  C CD2 . PHE   A 128 ? 0.1748 0.2193 0.1969 -0.0118 -0.0005 0.0148  134 PHE   A CD2 
984  C CE1 . PHE   A 128 ? 0.1720 0.2031 0.1792 -0.0061 0.0019  0.0042  134 PHE   A CE1 
985  C CE2 . PHE   A 128 ? 0.1837 0.2260 0.1993 -0.0120 0.0013  0.0131  134 PHE   A CE2 
986  C CZ  . PHE   A 128 ? 0.1825 0.2176 0.1900 -0.0090 0.0026  0.0078  134 PHE   A CZ  
987  N N   . ALA   A 129 ? 0.1449 0.1867 0.1921 -0.0044 -0.0017 0.0133  135 ALA   A N   
988  C CA  . ALA   A 129 ? 0.1491 0.1920 0.1999 -0.0068 -0.0032 0.0171  135 ALA   A CA  
989  C C   . ALA   A 129 ? 0.1549 0.1956 0.1918 -0.0127 -0.0036 0.0169  135 ALA   A C   
990  O O   . ALA   A 129 ? 0.1562 0.1916 0.1862 -0.0116 -0.0013 0.0109  135 ALA   A O   
991  C CB  . ALA   A 129 ? 0.1549 0.1937 0.2112 -0.0031 -0.0015 0.0122  135 ALA   A CB  
992  N N   . ASP   A 130 ? 0.1528 0.1970 0.1858 -0.0195 -0.0062 0.0237  136 ASP   A N   
993  C CA  . ASP   A 130 ? 0.1698 0.2098 0.1868 -0.0269 -0.0050 0.0222  136 ASP   A CA  
994  C C   . ASP   A 130 ? 0.1853 0.2209 0.2010 -0.0270 -0.0014 0.0189  136 ASP   A C   
995  O O   . ASP   A 130 ? 0.1869 0.2252 0.2128 -0.0251 -0.0024 0.0220  136 ASP   A O   
996  C CB  . ASP   A 130 ? 0.2100 0.2555 0.2217 -0.0363 -0.0098 0.0312  136 ASP   A CB  
997  C CG  . ASP   A 130 ? 0.2882 0.3278 0.2792 -0.0465 -0.0079 0.0289  136 ASP   A CG  
998  O OD1 . ASP   A 130 ? 0.2853 0.3184 0.2674 -0.0466 -0.0040 0.0221  136 ASP   A OD1 
999  O OD2 . ASP   A 130 ? 0.3363 0.3766 0.3196 -0.0547 -0.0094 0.0335  136 ASP   A OD2 
1000 N N   . VAL   A 131 ? 0.1815 0.2101 0.1861 -0.0295 0.0038  0.0129  137 VAL   A N   
1001 C CA  . VAL   A 131 ? 0.1768 0.2016 0.1806 -0.0308 0.0089  0.0101  137 VAL   A CA  
1002 C C   . VAL   A 131 ? 0.1975 0.2165 0.1834 -0.0410 0.0137  0.0088  137 VAL   A C   
1003 O O   . VAL   A 131 ? 0.2060 0.2209 0.1896 -0.0432 0.0202  0.0058  137 VAL   A O   
1004 C CB  . VAL   A 131 ? 0.1882 0.2097 0.2009 -0.0231 0.0131  0.0034  137 VAL   A CB  
1005 C CG1 . VAL   A 131 ? 0.1870 0.2129 0.2137 -0.0154 0.0084  0.0038  137 VAL   A CG1 
1006 C CG2 . VAL   A 131 ? 0.1958 0.2110 0.2017 -0.0226 0.0168  -0.0013 137 VAL   A CG2 
1007 N N   . ARG   A 132 ? 0.2044 0.2225 0.1769 -0.0483 0.0114  0.0106  138 ARG   A N   
1008 C CA  . ARG   A 132 ? 0.2039 0.2138 0.1556 -0.0597 0.0170  0.0075  138 ARG   A CA  
1009 C C   . ARG   A 132 ? 0.2544 0.2653 0.1960 -0.0695 0.0169  0.0120  138 ARG   A C   
1010 O O   . ARG   A 132 ? 0.2936 0.2955 0.2172 -0.0788 0.0247  0.0071  138 ARG   A O   
1011 C CB  . ARG   A 132 ? 0.2285 0.2373 0.1678 -0.0666 0.0133  0.0085  138 ARG   A CB  
1012 C CG  . ARG   A 132 ? 0.2372 0.2422 0.1827 -0.0585 0.0155  0.0031  138 ARG   A CG  
1013 C CD  . ARG   A 132 ? 0.2466 0.2517 0.1811 -0.0661 0.0113  0.0053  138 ARG   A CD  
1014 N NE  . ARG   A 132 ? 0.2408 0.2592 0.1854 -0.0653 0.0010  0.0150  138 ARG   A NE  
1015 C CZ  . ARG   A 132 ? 0.2565 0.2794 0.1986 -0.0702 -0.0045 0.0194  138 ARG   A CZ  
1016 N NH1 . ARG   A 132 ? 0.2713 0.2856 0.1975 -0.0780 -0.0016 0.0146  138 ARG   A NH1 
1017 N NH2 . ARG   A 132 ? 0.2557 0.2914 0.2126 -0.0674 -0.0122 0.0284  138 ARG   A NH2 
1018 N N   . ASP   A 133 ? 0.2526 0.2733 0.2047 -0.0683 0.0088  0.0215  139 ASP   A N   
1019 C CA  . ASP   A 133 ? 0.2760 0.2984 0.2195 -0.0779 0.0076  0.0280  139 ASP   A CA  
1020 C C   . ASP   A 133 ? 0.2724 0.2912 0.2219 -0.0743 0.0154  0.0240  139 ASP   A C   
1021 O O   . ASP   A 133 ? 0.2843 0.3026 0.2238 -0.0831 0.0167  0.0281  139 ASP   A O   
1022 C CB  . ASP   A 133 ? 0.2869 0.3210 0.2421 -0.0782 -0.0042 0.0416  139 ASP   A CB  
1023 C CG  . ASP   A 133 ? 0.3120 0.3512 0.2935 -0.0643 -0.0059 0.0429  139 ASP   A CG  
1024 O OD1 . ASP   A 133 ? 0.2894 0.3264 0.2800 -0.0544 -0.0029 0.0352  139 ASP   A OD1 
1025 O OD2 . ASP   A 133 ? 0.3553 0.3997 0.3476 -0.0641 -0.0102 0.0517  139 ASP   A OD2 
1026 N N   . LEU   A 134 ? 0.2521 0.2695 0.2178 -0.0623 0.0200  0.0172  140 LEU   A N   
1027 C CA  . LEU   A 134 ? 0.2438 0.2599 0.2198 -0.0583 0.0266  0.0142  140 LEU   A CA  
1028 C C   . LEU   A 134 ? 0.2600 0.2664 0.2243 -0.0630 0.0395  0.0055  140 LEU   A C   
1029 O O   . LEU   A 134 ? 0.2488 0.2514 0.2229 -0.0555 0.0462  -0.0019 140 LEU   A O   
1030 C CB  . LEU   A 134 ? 0.2308 0.2507 0.2295 -0.0450 0.0242  0.0117  140 LEU   A CB  
1031 C CG  . LEU   A 134 ? 0.2413 0.2684 0.2518 -0.0402 0.0142  0.0184  140 LEU   A CG  
1032 C CD1 . LEU   A 134 ? 0.2317 0.2602 0.2592 -0.0293 0.0130  0.0140  140 LEU   A CD1 
1033 C CD2 . LEU   A 134 ? 0.2479 0.2793 0.2624 -0.0442 0.0102  0.0274  140 LEU   A CD2 
1034 N N   . LEU   A 135 ? 0.2808 0.2827 0.2237 -0.0762 0.0436  0.0066  141 LEU   A N   
1035 C CA  . LEU   A 135 ? 0.3134 0.3035 0.2420 -0.0823 0.0583  -0.0030 141 LEU   A CA  
1036 C C   . LEU   A 135 ? 0.3231 0.3115 0.2679 -0.0758 0.0696  -0.0082 141 LEU   A C   
1037 O O   . LEU   A 135 ? 0.3334 0.3130 0.2786 -0.0745 0.0826  -0.0173 141 LEU   A O   
1038 C CB  . LEU   A 135 ? 0.3362 0.3205 0.2342 -0.1002 0.0608  -0.0013 141 LEU   A CB  
1039 C CG  . LEU   A 135 ? 0.3652 0.3538 0.2480 -0.1091 0.0478  0.0065  141 LEU   A CG  
1040 C CD1 . LEU   A 135 ? 0.4001 0.3814 0.2487 -0.1295 0.0512  0.0071  141 LEU   A CD1 
1041 C CD2 . LEU   A 135 ? 0.3672 0.3535 0.2522 -0.1040 0.0453  0.0020  141 LEU   A CD2 
1042 N N   . TRP   A 136 ? 0.3086 0.3053 0.2688 -0.0717 0.0650  -0.0023 142 TRP   A N   
1043 C CA  . TRP   A 136 ? 0.3180 0.3154 0.2957 -0.0664 0.0743  -0.0056 142 TRP   A CA  
1044 C C   . TRP   A 136 ? 0.3207 0.3198 0.3223 -0.0532 0.0757  -0.0106 142 TRP   A C   
1045 O O   . TRP   A 136 ? 0.3313 0.3310 0.3495 -0.0489 0.0846  -0.0138 142 TRP   A O   
1046 C CB  . TRP   A 136 ? 0.3108 0.3164 0.2989 -0.0662 0.0675  0.0026  142 TRP   A CB  
1047 C CG  . TRP   A 136 ? 0.2941 0.3076 0.2943 -0.0592 0.0524  0.0093  142 TRP   A CG  
1048 C CD1 . TRP   A 136 ? 0.2904 0.3072 0.2821 -0.0634 0.0418  0.0176  142 TRP   A CD1 
1049 C CD2 . TRP   A 136 ? 0.2779 0.2966 0.3015 -0.0474 0.0474  0.0081  142 TRP   A CD2 
1050 N NE1 . TRP   A 136 ? 0.2859 0.3087 0.2957 -0.0541 0.0324  0.0208  142 TRP   A NE1 
1051 C CE2 . TRP   A 136 ? 0.2818 0.3053 0.3091 -0.0450 0.0356  0.0145  142 TRP   A CE2 
1052 C CE3 . TRP   A 136 ? 0.2836 0.3038 0.3261 -0.0394 0.0517  0.0029  142 TRP   A CE3 
1053 C CZ2 . TRP   A 136 ? 0.2818 0.3092 0.3272 -0.0356 0.0294  0.0139  142 TRP   A CZ2 
1054 C CZ3 . TRP   A 136 ? 0.2826 0.3083 0.3426 -0.0311 0.0432  0.0037  142 TRP   A CZ3 
1055 C CH2 . TRP   A 136 ? 0.2776 0.3058 0.3372 -0.0297 0.0329  0.0084  142 TRP   A CH2 
1056 N N   . LEU   A 137 ? 0.3030 0.3040 0.3079 -0.0469 0.0667  -0.0102 143 LEU   A N   
1057 C CA  . LEU   A 137 ? 0.3093 0.3120 0.3348 -0.0357 0.0668  -0.0134 143 LEU   A CA  
1058 C C   . LEU   A 137 ? 0.3720 0.3657 0.3992 -0.0355 0.0816  -0.0206 143 LEU   A C   
1059 O O   . LEU   A 137 ? 0.3716 0.3678 0.4210 -0.0267 0.0841  -0.0218 143 LEU   A O   
1060 C CB  . LEU   A 137 ? 0.2861 0.2906 0.3102 -0.0311 0.0561  -0.0119 143 LEU   A CB  
1061 C CG  . LEU   A 137 ? 0.2599 0.2729 0.2901 -0.0278 0.0433  -0.0061 143 LEU   A CG  
1062 C CD1 . LEU   A 137 ? 0.2691 0.2824 0.2950 -0.0248 0.0358  -0.0056 143 LEU   A CD1 
1063 C CD2 . LEU   A 137 ? 0.2547 0.2742 0.3074 -0.0204 0.0403  -0.0054 143 LEU   A CD2 
1064 N N   . ASP   A 138 ? 0.4238 0.4068 0.4274 -0.0455 0.0909  -0.0251 144 ASP   A N   
1065 C CA  . ASP   A 138 ? 0.4910 0.4614 0.4908 -0.0476 0.1072  -0.0335 144 ASP   A CA  
1066 C C   . ASP   A 138 ? 0.5455 0.5127 0.5542 -0.0490 0.1234  -0.0375 144 ASP   A C   
1067 O O   . ASP   A 138 ? 0.5660 0.5214 0.5730 -0.0506 0.1394  -0.0452 144 ASP   A O   
1068 C CB  . ASP   A 138 ? 0.5410 0.4999 0.5072 -0.0610 0.1109  -0.0374 144 ASP   A CB  
1069 C CG  . ASP   A 138 ? 0.6333 0.5907 0.5901 -0.0609 0.1010  -0.0364 144 ASP   A CG  
1070 O OD1 . ASP   A 138 ? 0.6443 0.6074 0.6201 -0.0496 0.0937  -0.0340 144 ASP   A OD1 
1071 O OD2 . ASP   A 138 ? 0.7005 0.6514 0.6300 -0.0732 0.1003  -0.0376 144 ASP   A OD2 
1072 N N   . GLU   A 139 ? 0.5696 0.5456 0.5864 -0.0496 0.1211  -0.0329 145 GLU   A N   
1073 C CA  . GLU   A 139 ? 0.6064 0.5805 0.6334 -0.0512 0.1373  -0.0363 145 GLU   A CA  
1074 C C   . GLU   A 139 ? 0.6138 0.6019 0.6657 -0.0452 0.1306  -0.0296 145 GLU   A C   
1075 O O   . GLU   A 139 ? 0.6265 0.6230 0.6776 -0.0443 0.1147  -0.0229 145 GLU   A O   
1076 C CB  . GLU   A 139 ? 0.6658 0.6296 0.6612 -0.0669 0.1488  -0.0402 145 GLU   A CB  
1077 C CG  . GLU   A 139 ? 0.7493 0.7196 0.7272 -0.0754 0.1360  -0.0319 145 GLU   A CG  
1078 C CD  . GLU   A 139 ? 0.8675 0.8341 0.8158 -0.0846 0.1254  -0.0296 145 GLU   A CD  
1079 O OE1 . GLU   A 139 ? 0.8957 0.8649 0.8256 -0.0949 0.1184  -0.0228 145 GLU   A OE1 
1080 O OE2 . GLU   A 139 ? 0.9039 0.8654 0.8487 -0.0818 0.1238  -0.0334 145 GLU   A OE2 
1081 N N   . SER   B 1   ? 0.3580 0.3485 0.3296 -0.0012 -0.0294 0.0276  7   SER   C N   
1082 C CA  . SER   B 1   ? 0.3538 0.3501 0.3427 -0.0043 -0.0327 0.0267  7   SER   C CA  
1083 C C   . SER   B 1   ? 0.3356 0.3358 0.3320 -0.0067 -0.0318 0.0233  7   SER   C C   
1084 O O   . SER   B 1   ? 0.3477 0.3443 0.3353 -0.0059 -0.0312 0.0211  7   SER   C O   
1085 C CB  . SER   B 1   ? 0.4000 0.3929 0.3896 -0.0034 -0.0425 0.0269  7   SER   C CB  
1086 O OG  . SER   B 1   ? 0.4649 0.4522 0.4459 -0.0023 -0.0491 0.0233  7   SER   C OG  
1087 N N   . GLY   B 2   ? 0.3021 0.3090 0.3141 -0.0090 -0.0313 0.0234  8   GLY   C N   
1088 C CA  . GLY   B 2   ? 0.2822 0.2926 0.3016 -0.0109 -0.0296 0.0219  8   GLY   C CA  
1089 C C   . GLY   B 2   ? 0.2564 0.2752 0.2887 -0.0117 -0.0247 0.0228  8   GLY   C C   
1090 O O   . GLY   B 2   ? 0.2764 0.2981 0.3106 -0.0105 -0.0215 0.0232  8   GLY   C O   
1091 N N   . ALA   B 3   ? 0.2357 0.2580 0.2768 -0.0131 -0.0237 0.0233  9   ALA   C N   
1092 C CA  . ALA   B 3   ? 0.2355 0.2658 0.2866 -0.0126 -0.0182 0.0243  9   ALA   C CA  
1093 C C   . ALA   B 3   ? 0.2240 0.2558 0.2766 -0.0130 -0.0142 0.0254  9   ALA   C C   
1094 O O   . ALA   B 3   ? 0.2402 0.2673 0.2923 -0.0150 -0.0171 0.0259  9   ALA   C O   
1095 C CB  . ALA   B 3   ? 0.2339 0.2689 0.2994 -0.0134 -0.0208 0.0259  9   ALA   C CB  
1096 N N   . ILE   B 4   ? 0.2003 0.2380 0.2552 -0.0107 -0.0079 0.0259  10  ILE   C N   
1097 C CA  . ILE   B 4   ? 0.1925 0.2323 0.2485 -0.0100 -0.0029 0.0285  10  ILE   C CA  
1098 C C   . ILE   B 4   ? 0.2059 0.2529 0.2759 -0.0100 0.0006  0.0319  10  ILE   C C   
1099 O O   . ILE   B 4   ? 0.1983 0.2507 0.2727 -0.0078 0.0021  0.0308  10  ILE   C O   
1100 C CB  . ILE   B 4   ? 0.1906 0.2316 0.2364 -0.0057 0.0017  0.0263  10  ILE   C CB  
1101 C CG1 . ILE   B 4   ? 0.2064 0.2419 0.2416 -0.0055 -0.0012 0.0226  10  ILE   C CG1 
1102 C CG2 . ILE   B 4   ? 0.2139 0.2559 0.2580 -0.0040 0.0069  0.0299  10  ILE   C CG2 
1103 C CD1 . ILE   B 4   ? 0.2286 0.2668 0.2579 -0.0010 0.0016  0.0190  10  ILE   C CD1 
1104 N N   . TYR   B 5   ? 0.2119 0.2593 0.2909 -0.0125 0.0023  0.0365  11  TYR   C N   
1105 C CA  . TYR   B 5   ? 0.2157 0.2711 0.3109 -0.0126 0.0071  0.0409  11  TYR   C CA  
1106 C C   . TYR   B 5   ? 0.2369 0.2946 0.3294 -0.0101 0.0162  0.0458  11  TYR   C C   
1107 O O   . TYR   B 5   ? 0.2569 0.3095 0.3493 -0.0124 0.0165  0.0493  11  TYR   C O   
1108 C CB  . TYR   B 5   ? 0.2168 0.2712 0.3291 -0.0180 0.0011  0.0430  11  TYR   C CB  
1109 C CG  . TYR   B 5   ? 0.2097 0.2617 0.3232 -0.0192 -0.0083 0.0386  11  TYR   C CG  
1110 C CD1 . TYR   B 5   ? 0.2196 0.2785 0.3443 -0.0181 -0.0088 0.0382  11  TYR   C CD1 
1111 C CD2 . TYR   B 5   ? 0.2394 0.2822 0.3410 -0.0203 -0.0162 0.0348  11  TYR   C CD2 
1112 C CE1 . TYR   B 5   ? 0.2525 0.3084 0.3767 -0.0184 -0.0176 0.0349  11  TYR   C CE1 
1113 C CE2 . TYR   B 5   ? 0.2595 0.2994 0.3591 -0.0203 -0.0242 0.0317  11  TYR   C CE2 
1114 C CZ  . TYR   B 5   ? 0.2762 0.3223 0.3870 -0.0194 -0.0252 0.0320  11  TYR   C CZ  
1115 O OH  . TYR   B 5   ? 0.3210 0.3632 0.4280 -0.0187 -0.0332 0.0297  11  TYR   C OH  
1116 N N   . VAL   B 6   ? 0.2443 0.3086 0.3328 -0.0045 0.0235  0.0461  12  VAL   C N   
1117 C CA  . VAL   B 6   ? 0.2614 0.3275 0.3429 -0.0002 0.0327  0.0509  12  VAL   C CA  
1118 C C   . VAL   B 6   ? 0.2681 0.3443 0.3590 0.0036  0.0414  0.0544  12  VAL   C C   
1119 O O   . VAL   B 6   ? 0.2564 0.3372 0.3471 0.0070  0.0407  0.0494  12  VAL   C O   
1120 C CB  . VAL   B 6   ? 0.2901 0.3520 0.3497 0.0053  0.0322  0.0460  12  VAL   C CB  
1121 C CG1 . VAL   B 6   ? 0.3011 0.3653 0.3563 0.0084  0.0285  0.0382  12  VAL   C CG1 
1122 C CG2 . VAL   B 6   ? 0.3036 0.3673 0.3532 0.0116  0.0413  0.0508  12  VAL   C CG2 
1123 N N   . GLY   B 7   ? 0.2807 0.3606 0.3827 0.0027  0.0496  0.0631  13  GLY   C N   
1124 C CA  . GLY   B 7   ? 0.2921 0.3829 0.4046 0.0067  0.0595  0.0672  13  GLY   C CA  
1125 C C   . GLY   B 7   ? 0.2915 0.3883 0.4223 0.0040  0.0546  0.0635  13  GLY   C C   
1126 O O   . GLY   B 7   ? 0.3000 0.3938 0.4442 -0.0030 0.0460  0.0628  13  GLY   C O   
1127 N N   . ASN   B 8   ? 0.2860 0.3900 0.4153 0.0103  0.0582  0.0598  14  ASN   C N   
1128 C CA  . ASN   B 8   ? 0.2744 0.3833 0.4203 0.0085  0.0526  0.0559  14  ASN   C CA  
1129 C C   . ASN   B 8   ? 0.2438 0.3468 0.3769 0.0099  0.0429  0.0465  14  ASN   C C   
1130 O O   . ASN   B 8   ? 0.2290 0.3363 0.3686 0.0125  0.0409  0.0422  14  ASN   C O   
1131 C CB  . ASN   B 8   ? 0.3173 0.4383 0.4760 0.0139  0.0626  0.0585  14  ASN   C CB  
1132 C CG  . ASN   B 8   ? 0.4037 0.5317 0.5838 0.0105  0.0713  0.0686  14  ASN   C CG  
1133 O OD1 . ASN   B 8   ? 0.4282 0.5571 0.6307 0.0030  0.0656  0.0709  14  ASN   C OD1 
1134 N ND2 . ASN   B 8   ? 0.4286 0.5613 0.6023 0.0163  0.0851  0.0751  14  ASN   C ND2 
1135 N N   . TYR   B 9   ? 0.2324 0.3258 0.3496 0.0078  0.0370  0.0438  15  TYR   C N   
1136 C CA  . TYR   B 9   ? 0.2146 0.3022 0.3209 0.0085  0.0289  0.0361  15  TYR   C CA  
1137 C C   . TYR   B 9   ? 0.1975 0.2767 0.3027 0.0019  0.0196  0.0354  15  TYR   C C   
1138 O O   . TYR   B 9   ? 0.2089 0.2841 0.3134 -0.0019 0.0192  0.0390  15  TYR   C O   
1139 C CB  . TYR   B 9   ? 0.2262 0.3105 0.3122 0.0142  0.0312  0.0323  15  TYR   C CB  
1140 C CG  . TYR   B 9   ? 0.2518 0.3425 0.3327 0.0229  0.0390  0.0309  15  TYR   C CG  
1141 C CD1 . TYR   B 9   ? 0.2742 0.3706 0.3635 0.0266  0.0393  0.0271  15  TYR   C CD1 
1142 C CD2 . TYR   B 9   ? 0.2767 0.3676 0.3437 0.0283  0.0461  0.0334  15  TYR   C CD2 
1143 C CE1 . TYR   B 9   ? 0.2943 0.3964 0.3776 0.0358  0.0464  0.0249  15  TYR   C CE1 
1144 C CE2 . TYR   B 9   ? 0.2946 0.3910 0.3539 0.0378  0.0533  0.0318  15  TYR   C CE2 
1145 C CZ  . TYR   B 9   ? 0.3179 0.4200 0.3851 0.0417  0.0535  0.0271  15  TYR   C CZ  
1146 O OH  . TYR   B 9   ? 0.3548 0.4618 0.4126 0.0523  0.0604  0.0243  15  TYR   C OH  
1147 N N   . ARG   B 10  ? 0.1798 0.2557 0.2842 0.0011  0.0124  0.0308  16  ARG   C N   
1148 C CA  . ARG   B 10  ? 0.1826 0.2501 0.2818 -0.0034 0.0041  0.0296  16  ARG   C CA  
1149 C C   . ARG   B 10  ? 0.1835 0.2467 0.2697 -0.0008 0.0026  0.0247  16  ARG   C C   
1150 O O   . ARG   B 10  ? 0.1888 0.2546 0.2776 0.0024  0.0027  0.0216  16  ARG   C O   
1151 C CB  . ARG   B 10  ? 0.1776 0.2452 0.2893 -0.0062 -0.0028 0.0300  16  ARG   C CB  
1152 C CG  . ARG   B 10  ? 0.2092 0.2683 0.3126 -0.0083 -0.0110 0.0281  16  ARG   C CG  
1153 C CD  . ARG   B 10  ? 0.2113 0.2700 0.3259 -0.0100 -0.0188 0.0289  16  ARG   C CD  
1154 N NE  . ARG   B 10  ? 0.2387 0.2912 0.3454 -0.0091 -0.0245 0.0274  16  ARG   C NE  
1155 C CZ  . ARG   B 10  ? 0.3064 0.3506 0.4031 -0.0105 -0.0310 0.0275  16  ARG   C CZ  
1156 N NH1 . ARG   B 10  ? 0.3186 0.3591 0.4117 -0.0130 -0.0339 0.0276  16  ARG   C NH1 
1157 N NH2 . ARG   B 10  ? 0.2902 0.3291 0.3798 -0.0090 -0.0345 0.0275  16  ARG   C NH2 
1158 N N   . VAL   B 11  ? 0.1753 0.2326 0.2493 -0.0020 0.0015  0.0237  17  VAL   C N   
1159 C CA  . VAL   B 11  ? 0.1804 0.2342 0.2452 -0.0001 0.0003  0.0194  17  VAL   C CA  
1160 C C   . VAL   B 11  ? 0.1802 0.2275 0.2418 -0.0036 -0.0050 0.0197  17  VAL   C C   
1161 O O   . VAL   B 11  ? 0.1943 0.2373 0.2514 -0.0063 -0.0070 0.0215  17  VAL   C O   
1162 C CB  . VAL   B 11  ? 0.2006 0.2531 0.2544 0.0020  0.0033  0.0182  17  VAL   C CB  
1163 C CG1 . VAL   B 11  ? 0.2075 0.2582 0.2564 0.0042  0.0018  0.0130  17  VAL   C CG1 
1164 C CG2 . VAL   B 11  ? 0.2175 0.2753 0.2708 0.0060  0.0093  0.0197  17  VAL   C CG2 
1165 N N   . VAL   B 12  ? 0.1668 0.2126 0.2305 -0.0031 -0.0073 0.0182  18  VAL   C N   
1166 C CA  . VAL   B 12  ? 0.1685 0.2079 0.2275 -0.0054 -0.0111 0.0197  18  VAL   C CA  
1167 C C   . VAL   B 12  ? 0.1642 0.2015 0.2214 -0.0044 -0.0100 0.0177  18  VAL   C C   
1168 O O   . VAL   B 12  ? 0.1684 0.2090 0.2304 -0.0019 -0.0083 0.0143  18  VAL   C O   
1169 C CB  . VAL   B 12  ? 0.1848 0.2232 0.2506 -0.0062 -0.0158 0.0221  18  VAL   C CB  
1170 C CG1 . VAL   B 12  ? 0.2192 0.2594 0.2898 -0.0080 -0.0183 0.0239  18  VAL   C CG1 
1171 C CG2 . VAL   B 12  ? 0.1736 0.2163 0.2501 -0.0037 -0.0152 0.0206  18  VAL   C CG2 
1172 N N   . ASN   B 13  ? 0.1628 0.1943 0.2137 -0.0059 -0.0110 0.0198  19  ASN   C N   
1173 C CA  . ASN   B 13  ? 0.1702 0.1999 0.2237 -0.0056 -0.0095 0.0195  19  ASN   C CA  
1174 C C   . ASN   B 13  ? 0.1770 0.2070 0.2407 -0.0047 -0.0117 0.0200  19  ASN   C C   
1175 O O   . ASN   B 13  ? 0.1877 0.2157 0.2518 -0.0051 -0.0150 0.0231  19  ASN   C O   
1176 C CB  . ASN   B 13  ? 0.1843 0.2078 0.2293 -0.0069 -0.0090 0.0235  19  ASN   C CB  
1177 C CG  . ASN   B 13  ? 0.2079 0.2306 0.2432 -0.0071 -0.0067 0.0225  19  ASN   C CG  
1178 O OD1 . ASN   B 13  ? 0.1965 0.2169 0.2236 -0.0073 -0.0088 0.0231  19  ASN   C OD1 
1179 N ND2 . ASN   B 13  ? 0.1962 0.2207 0.2343 -0.0067 -0.0031 0.0204  19  ASN   C ND2 
1180 N N   . ARG   B 14  ? 0.1625 0.1944 0.2350 -0.0032 -0.0108 0.0164  20  ARG   C N   
1181 C CA  . ARG   B 14  ? 0.1634 0.1949 0.2466 -0.0019 -0.0132 0.0162  20  ARG   C CA  
1182 C C   . ARG   B 14  ? 0.1742 0.1990 0.2570 -0.0035 -0.0149 0.0225  20  ARG   C C   
1183 O O   . ARG   B 14  ? 0.1876 0.2114 0.2748 -0.0026 -0.0183 0.0244  20  ARG   C O   
1184 C CB  . ARG   B 14  ? 0.1692 0.2021 0.2619 0.0001  -0.0130 0.0105  20  ARG   C CB  
1185 C CG  . ARG   B 14  ? 0.1841 0.2167 0.2886 0.0026  -0.0159 0.0083  20  ARG   C CG  
1186 C CD  . ARG   B 14  ? 0.1838 0.2159 0.2980 0.0042  -0.0169 0.0021  20  ARG   C CD  
1187 N NE  . ARG   B 14  ? 0.1826 0.2140 0.3086 0.0076  -0.0203 -0.0022 20  ARG   C NE  
1188 C CZ  . ARG   B 14  ? 0.2063 0.2318 0.3428 0.0063  -0.0226 0.0010  20  ARG   C CZ  
1189 N NH1 . ARG   B 14  ? 0.2258 0.2458 0.3606 0.0021  -0.0211 0.0094  20  ARG   C NH1 
1190 N NH2 . ARG   B 14  ? 0.1997 0.2242 0.3475 0.0100  -0.0262 -0.0041 20  ARG   C NH2 
1191 N N   . HIS   B 15  ? 0.1765 0.1968 0.2527 -0.0054 -0.0124 0.0264  21  HIS   C N   
1192 C CA  . HIS   B 15  ? 0.1924 0.2055 0.2655 -0.0059 -0.0130 0.0336  21  HIS   C CA  
1193 C C   . HIS   B 15  ? 0.2041 0.2143 0.2655 -0.0053 -0.0170 0.0371  21  HIS   C C   
1194 O O   . HIS   B 15  ? 0.2319 0.2358 0.2892 -0.0044 -0.0191 0.0427  21  HIS   C O   
1195 C CB  . HIS   B 15  ? 0.1929 0.2024 0.2634 -0.0074 -0.0077 0.0375  21  HIS   C CB  
1196 C CG  . HIS   B 15  ? 0.2178 0.2271 0.2736 -0.0077 -0.0047 0.0384  21  HIS   C CG  
1197 N ND1 . HIS   B 15  ? 0.2118 0.2264 0.2676 -0.0080 -0.0027 0.0329  21  HIS   C ND1 
1198 C CD2 . HIS   B 15  ? 0.2481 0.2521 0.2884 -0.0068 -0.0040 0.0436  21  HIS   C CD2 
1199 C CE1 . HIS   B 15  ? 0.2380 0.2504 0.2800 -0.0078 -0.0006 0.0350  21  HIS   C CE1 
1200 N NE2 . HIS   B 15  ? 0.2681 0.2742 0.2996 -0.0068 -0.0014 0.0409  21  HIS   C NE2 
1201 N N   . LEU   B 16  ? 0.1989 0.2132 0.2555 -0.0054 -0.0185 0.0337  22  LEU   C N   
1202 C CA  . LEU   B 16  ? 0.2075 0.2193 0.2562 -0.0049 -0.0238 0.0356  22  LEU   C CA  
1203 C C   . LEU   B 16  ? 0.2163 0.2338 0.2766 -0.0045 -0.0280 0.0330  22  LEU   C C   
1204 O O   . LEU   B 16  ? 0.2321 0.2489 0.2904 -0.0044 -0.0333 0.0336  22  LEU   C O   
1205 C CB  . LEU   B 16  ? 0.2279 0.2389 0.2643 -0.0057 -0.0229 0.0343  22  LEU   C CB  
1206 C CG  . LEU   B 16  ? 0.2529 0.2589 0.2771 -0.0053 -0.0183 0.0370  22  LEU   C CG  
1207 C CD1 . LEU   B 16  ? 0.2759 0.2810 0.2884 -0.0053 -0.0181 0.0345  22  LEU   C CD1 
1208 C CD2 . LEU   B 16  ? 0.2743 0.2723 0.2894 -0.0032 -0.0197 0.0434  22  LEU   C CD2 
1209 N N   . ALA   B 17  ? 0.1957 0.2190 0.2687 -0.0037 -0.0256 0.0297  23  ALA   C N   
1210 C CA  . ALA   B 17  ? 0.2027 0.2327 0.2873 -0.0026 -0.0276 0.0275  23  ALA   C CA  
1211 C C   . ALA   B 17  ? 0.2136 0.2408 0.3031 -0.0013 -0.0342 0.0305  23  ALA   C C   
1212 O O   . ALA   B 17  ? 0.2276 0.2482 0.3149 -0.0004 -0.0359 0.0336  23  ALA   C O   
1213 C CB  . ALA   B 17  ? 0.2005 0.2357 0.2951 -0.0003 -0.0239 0.0231  23  ALA   C CB  
1214 N N   . THR   B 18  ? 0.2188 0.2506 0.3157 -0.0013 -0.0379 0.0300  24  THR   C N   
1215 C CA  . THR   B 18  ? 0.2242 0.2543 0.3275 0.0003  -0.0455 0.0321  24  THR   C CA  
1216 C C   . THR   B 18  ? 0.2284 0.2640 0.3486 0.0031  -0.0451 0.0303  24  THR   C C   
1217 O O   . THR   B 18  ? 0.2172 0.2587 0.3434 0.0041  -0.0389 0.0268  24  THR   C O   
1218 C CB  . THR   B 18  ? 0.2389 0.2718 0.3455 -0.0011 -0.0506 0.0317  24  THR   C CB  
1219 O OG1 . THR   B 18  ? 0.2495 0.2931 0.3711 -0.0017 -0.0460 0.0293  24  THR   C OG1 
1220 C CG2 . THR   B 18  ? 0.2474 0.2745 0.3379 -0.0032 -0.0516 0.0322  24  THR   C CG2 
1221 N N   . HIS   B 19  ? 0.2260 0.2602 0.3543 0.0053  -0.0524 0.0321  25  HIS   C N   
1222 C CA  . HIS   B 19  ? 0.2241 0.2644 0.3700 0.0086  -0.0522 0.0298  25  HIS   C CA  
1223 C C   . HIS   B 19  ? 0.2140 0.2668 0.3725 0.0086  -0.0471 0.0263  25  HIS   C C   
1224 O O   . HIS   B 19  ? 0.2219 0.2808 0.3894 0.0115  -0.0419 0.0230  25  HIS   C O   
1225 C CB  . HIS   B 19  ? 0.2702 0.3078 0.4235 0.0110  -0.0619 0.0324  25  HIS   C CB  
1226 C CG  . HIS   B 19  ? 0.3774 0.4022 0.5182 0.0122  -0.0666 0.0372  25  HIS   C CG  
1227 N ND1 . HIS   B 19  ? 0.4271 0.4469 0.5693 0.0138  -0.0637 0.0381  25  HIS   C ND1 
1228 C CD2 . HIS   B 19  ? 0.4239 0.4401 0.5518 0.0127  -0.0740 0.0416  25  HIS   C CD2 
1229 C CE1 . HIS   B 19  ? 0.4458 0.4542 0.5765 0.0148  -0.0683 0.0442  25  HIS   C CE1 
1230 N NE2 . HIS   B 19  ? 0.4538 0.4596 0.5738 0.0146  -0.0743 0.0465  25  HIS   C NE2 
1231 N N   . ASN   B 20  ? 0.2152 0.2712 0.3740 0.0056  -0.0482 0.0273  26  ASN   C N   
1232 C CA  . ASN   B 20  ? 0.2105 0.2781 0.3822 0.0052  -0.0421 0.0258  26  ASN   C CA  
1233 C C   . ASN   B 20  ? 0.1985 0.2686 0.3619 0.0056  -0.0321 0.0238  26  ASN   C C   
1234 O O   . ASN   B 20  ? 0.1929 0.2719 0.3651 0.0083  -0.0251 0.0220  26  ASN   C O   
1235 C CB  . ASN   B 20  ? 0.2550 0.3245 0.4315 0.0015  -0.0461 0.0276  26  ASN   C CB  
1236 C CG  . ASN   B 20  ? 0.3708 0.4511 0.5720 0.0028  -0.0469 0.0276  26  ASN   C CG  
1237 O OD1 . ASN   B 20  ? 0.3758 0.4570 0.5871 0.0060  -0.0520 0.0270  26  ASN   C OD1 
1238 N ND2 . ASN   B 20  ? 0.4101 0.4991 0.6226 0.0007  -0.0409 0.0286  26  ASN   C ND2 
1239 N N   . ASP   B 21  ? 0.2030 0.2654 0.3488 0.0034  -0.0313 0.0240  27  ASP   C N   
1240 C CA  . ASP   B 21  ? 0.2027 0.2668 0.3403 0.0044  -0.0233 0.0214  27  ASP   C CA  
1241 C C   . ASP   B 21  ? 0.1966 0.2627 0.3388 0.0093  -0.0206 0.0174  27  ASP   C C   
1242 O O   . ASP   B 21  ? 0.2017 0.2743 0.3455 0.0127  -0.0143 0.0144  27  ASP   C O   
1243 C CB  . ASP   B 21  ? 0.1883 0.2435 0.3087 0.0018  -0.0239 0.0220  27  ASP   C CB  
1244 C CG  . ASP   B 21  ? 0.2112 0.2645 0.3246 -0.0019 -0.0250 0.0243  27  ASP   C CG  
1245 O OD1 . ASP   B 21  ? 0.2393 0.2987 0.3585 -0.0027 -0.0216 0.0247  27  ASP   C OD1 
1246 O OD2 . ASP   B 21  ? 0.2185 0.2638 0.3207 -0.0038 -0.0290 0.0258  27  ASP   C OD2 
1247 N N   . TRP   B 22  ? 0.2023 0.2623 0.3466 0.0103  -0.0258 0.0173  28  TRP   C N   
1248 C CA  . TRP   B 22  ? 0.2052 0.2654 0.3553 0.0149  -0.0247 0.0128  28  TRP   C CA  
1249 C C   . TRP   B 22  ? 0.2169 0.2866 0.3821 0.0198  -0.0228 0.0103  28  TRP   C C   
1250 O O   . TRP   B 22  ? 0.2296 0.3026 0.3973 0.0250  -0.0190 0.0048  28  TRP   C O   
1251 C CB  . TRP   B 22  ? 0.1963 0.2465 0.3464 0.0144  -0.0306 0.0147  28  TRP   C CB  
1252 C CG  . TRP   B 22  ? 0.1934 0.2362 0.3324 0.0118  -0.0294 0.0151  28  TRP   C CG  
1253 C CD1 . TRP   B 22  ? 0.2021 0.2381 0.3302 0.0078  -0.0308 0.0202  28  TRP   C CD1 
1254 C CD2 . TRP   B 22  ? 0.1847 0.2265 0.3238 0.0136  -0.0268 0.0097  28  TRP   C CD2 
1255 N NE1 . TRP   B 22  ? 0.2161 0.2479 0.3391 0.0065  -0.0281 0.0190  28  TRP   C NE1 
1256 C CE2 . TRP   B 22  ? 0.2024 0.2374 0.3332 0.0098  -0.0264 0.0125  28  TRP   C CE2 
1257 C CE3 . TRP   B 22  ? 0.1957 0.2416 0.3414 0.0187  -0.0252 0.0024  28  TRP   C CE3 
1258 C CZ2 . TRP   B 22  ? 0.2033 0.2364 0.3349 0.0102  -0.0249 0.0081  28  TRP   C CZ2 
1259 C CZ3 . TRP   B 22  ? 0.1983 0.2411 0.3424 0.0196  -0.0247 -0.0027 28  TRP   C CZ3 
1260 C CH2 . TRP   B 22  ? 0.2015 0.2382 0.3401 0.0150  -0.0249 0.0002  28  TRP   C CH2 
1261 N N   . ALA   B 23  ? 0.2080 0.2820 0.3835 0.0187  -0.0255 0.0137  29  ALA   C N   
1262 C CA  . ALA   B 23  ? 0.2121 0.2966 0.4047 0.0232  -0.0228 0.0119  29  ALA   C CA  
1263 C C   . ALA   B 23  ? 0.2299 0.3246 0.4227 0.0250  -0.0127 0.0111  29  ALA   C C   
1264 O O   . ALA   B 23  ? 0.2586 0.3628 0.4631 0.0302  -0.0074 0.0091  29  ALA   C O   
1265 C CB  . ALA   B 23  ? 0.1998 0.2866 0.4060 0.0212  -0.0294 0.0159  29  ALA   C CB  
1266 N N   . ASN   B 24  ? 0.2017 0.2948 0.3824 0.0209  -0.0096 0.0134  30  ASN   C N   
1267 C CA  . ASN   B 24  ? 0.1878 0.2888 0.3666 0.0224  0.0001  0.0143  30  ASN   C CA  
1268 C C   . ASN   B 24  ? 0.2019 0.2977 0.3610 0.0237  0.0032  0.0111  30  ASN   C C   
1269 O O   . ASN   B 24  ? 0.2038 0.3006 0.3544 0.0223  0.0082  0.0134  30  ASN   C O   
1270 C CB  . ASN   B 24  ? 0.1911 0.2944 0.3752 0.0164  -0.0001 0.0203  30  ASN   C CB  
1271 C CG  . ASN   B 24  ? 0.2370 0.3472 0.4437 0.0157  -0.0032 0.0226  30  ASN   C CG  
1272 O OD1 . ASN   B 24  ? 0.2225 0.3439 0.4440 0.0192  0.0039  0.0234  30  ASN   C OD1 
1273 N ND2 . ASN   B 24  ? 0.2427 0.3466 0.4522 0.0119  -0.0141 0.0237  30  ASN   C ND2 
1274 N N   . LEU   B 25  ? 0.2027 0.2928 0.3566 0.0268  -0.0001 0.0058  31  LEU   C N   
1275 C CA  . LEU   B 25  ? 0.2120 0.2969 0.3506 0.0280  0.0007  0.0018  31  LEU   C CA  
1276 C C   . LEU   B 25  ? 0.2222 0.3131 0.3528 0.0345  0.0087  -0.0013 31  LEU   C C   
1277 O O   . LEU   B 25  ? 0.2385 0.3358 0.3745 0.0413  0.0127  -0.0045 31  LEU   C O   
1278 C CB  . LEU   B 25  ? 0.2133 0.2913 0.3539 0.0299  -0.0053 -0.0033 31  LEU   C CB  
1279 C CG  . LEU   B 25  ? 0.2133 0.2859 0.3428 0.0314  -0.0062 -0.0087 31  LEU   C CG  
1280 C CD1 . LEU   B 25  ? 0.2315 0.2987 0.3515 0.0247  -0.0074 -0.0046 31  LEU   C CD1 
1281 C CD2 . LEU   B 25  ? 0.2167 0.2831 0.3534 0.0334  -0.0120 -0.0137 31  LEU   C CD2 
1282 N N   . VAL   B 26  ? 0.2075 0.2960 0.3239 0.0332  0.0109  -0.0006 32  VAL   C N   
1283 C CA  . VAL   B 26  ? 0.2176 0.3095 0.3218 0.0401  0.0174  -0.0035 32  VAL   C CA  
1284 C C   . VAL   B 26  ? 0.2304 0.3156 0.3242 0.0432  0.0123  -0.0115 32  VAL   C C   
1285 O O   . VAL   B 26  ? 0.2536 0.3402 0.3418 0.0517  0.0132  -0.0187 32  VAL   C O   
1286 C CB  . VAL   B 26  ? 0.2354 0.3289 0.3322 0.0369  0.0229  0.0034  32  VAL   C CB  
1287 C CG1 . VAL   B 26  ? 0.2513 0.3462 0.3316 0.0445  0.0288  0.0010  32  VAL   C CG1 
1288 C CG2 . VAL   B 26  ? 0.2411 0.3418 0.3523 0.0339  0.0278  0.0109  32  VAL   C CG2 
1289 N N   . TRP   B 27  ? 0.2011 0.2791 0.2929 0.0368  0.0066  -0.0107 33  TRP   C N   
1290 C CA  . TRP   B 27  ? 0.2030 0.2753 0.2886 0.0385  0.0017  -0.0174 33  TRP   C CA  
1291 C C   . TRP   B 27  ? 0.2011 0.2667 0.2909 0.0306  -0.0034 -0.0146 33  TRP   C C   
1292 O O   . TRP   B 27  ? 0.2031 0.2679 0.2921 0.0245  -0.0024 -0.0076 33  TRP   C O   
1293 C CB  . TRP   B 27  ? 0.2186 0.2920 0.2884 0.0424  0.0050  -0.0187 33  TRP   C CB  
1294 C CG  . TRP   B 27  ? 0.2263 0.2943 0.2906 0.0432  -0.0007 -0.0250 33  TRP   C CG  
1295 C CD1 . TRP   B 27  ? 0.2562 0.3227 0.3186 0.0502  -0.0053 -0.0349 33  TRP   C CD1 
1296 C CD2 . TRP   B 27  ? 0.2130 0.2769 0.2746 0.0372  -0.0029 -0.0223 33  TRP   C CD2 
1297 N NE1 . TRP   B 27  ? 0.2595 0.3216 0.3201 0.0483  -0.0105 -0.0383 33  TRP   C NE1 
1298 C CE2 . TRP   B 27  ? 0.2379 0.2987 0.2979 0.0404  -0.0084 -0.0304 33  TRP   C CE2 
1299 C CE3 . TRP   B 27  ? 0.2161 0.2786 0.2767 0.0299  -0.0010 -0.0145 33  TRP   C CE3 
1300 C CZ2 . TRP   B 27  ? 0.2316 0.2893 0.2903 0.0364  -0.0111 -0.0301 33  TRP   C CZ2 
1301 C CZ3 . TRP   B 27  ? 0.2303 0.2889 0.2873 0.0265  -0.0035 -0.0145 33  TRP   C CZ3 
1302 C CH2 . TRP   B 27  ? 0.2280 0.2848 0.2850 0.0296  -0.0080 -0.0219 33  TRP   C CH2 
1303 N N   . GLU   B 28  ? 0.1936 0.2541 0.2882 0.0309  -0.0088 -0.0199 34  GLU   C N   
1304 C CA  . GLU   B 28  ? 0.1928 0.2473 0.2908 0.0240  -0.0120 -0.0166 34  GLU   C CA  
1305 C C   . GLU   B 28  ? 0.1917 0.2426 0.2921 0.0255  -0.0161 -0.0235 34  GLU   C C   
1306 O O   . GLU   B 28  ? 0.1993 0.2506 0.3031 0.0316  -0.0190 -0.0316 34  GLU   C O   
1307 C CB  . GLU   B 28  ? 0.2008 0.2517 0.3093 0.0200  -0.0143 -0.0117 34  GLU   C CB  
1308 C CG  . GLU   B 28  ? 0.2091 0.2593 0.3292 0.0242  -0.0174 -0.0164 34  GLU   C CG  
1309 C CD  . GLU   B 28  ? 0.2369 0.2811 0.3657 0.0247  -0.0223 -0.0218 34  GLU   C CD  
1310 O OE1 . GLU   B 28  ? 0.2855 0.3293 0.4218 0.0301  -0.0253 -0.0289 34  GLU   C OE1 
1311 O OE2 . GLU   B 28  ? 0.2172 0.2570 0.3468 0.0197  -0.0231 -0.0190 34  GLU   C OE2 
1312 N N   . ASP   B 29  ? 0.1794 0.2271 0.2794 0.0205  -0.0167 -0.0208 35  ASP   C N   
1313 C CA  . ASP   B 29  ? 0.1769 0.2219 0.2836 0.0212  -0.0208 -0.0270 35  ASP   C CA  
1314 C C   . ASP   B 29  ? 0.1837 0.2242 0.2978 0.0140  -0.0203 -0.0208 35  ASP   C C   
1315 O O   . ASP   B 29  ? 0.1844 0.2251 0.2909 0.0105  -0.0171 -0.0156 35  ASP   C O   
1316 C CB  . ASP   B 29  ? 0.1870 0.2349 0.2826 0.0250  -0.0208 -0.0318 35  ASP   C CB  
1317 C CG  . ASP   B 29  ? 0.2697 0.3158 0.3740 0.0269  -0.0267 -0.0400 35  ASP   C CG  
1318 O OD1 . ASP   B 29  ? 0.2967 0.3393 0.4160 0.0223  -0.0288 -0.0390 35  ASP   C OD1 
1319 O OD2 . ASP   B 29  ? 0.2844 0.3325 0.3804 0.0329  -0.0292 -0.0469 35  ASP   C OD2 
1320 N N   . SER   B 30  ? 0.1745 0.2105 0.3035 0.0124  -0.0231 -0.0207 36  SER   C N   
1321 C CA  A SER   B 30  ? 0.1893 0.2207 0.3258 0.0063  -0.0214 -0.0135 36  SER   C CA  
1322 C CA  B SER   B 30  ? 0.1844 0.2158 0.3210 0.0063  -0.0214 -0.0135 36  SER   C CA  
1323 C C   . SER   B 30  ? 0.1985 0.2309 0.3376 0.0043  -0.0205 -0.0149 36  SER   C C   
1324 O O   . SER   B 30  ? 0.2212 0.2524 0.3573 0.0000  -0.0161 -0.0075 36  SER   C O   
1325 C CB  A SER   B 30  ? 0.2230 0.2488 0.3763 0.0056  -0.0246 -0.0132 36  SER   C CB  
1326 C CB  B SER   B 30  ? 0.2045 0.2303 0.3583 0.0055  -0.0246 -0.0134 36  SER   C CB  
1327 O OG  A SER   B 30  ? 0.2627 0.2838 0.4242 0.0002  -0.0219 -0.0054 36  SER   C OG  
1328 O OG  B SER   B 30  ? 0.2146 0.2401 0.3813 0.0086  -0.0300 -0.0233 36  SER   C OG  
1329 N N   . SER   B 31  ? 0.1717 0.2067 0.3154 0.0082  -0.0249 -0.0246 37  SER   C N   
1330 C CA  . SER   B 31  ? 0.1735 0.2102 0.3220 0.0067  -0.0251 -0.0267 37  SER   C CA  
1331 C C   . SER   B 31  ? 0.1965 0.2364 0.3278 0.0064  -0.0207 -0.0232 37  SER   C C   
1332 O O   . SER   B 31  ? 0.2176 0.2589 0.3529 0.0043  -0.0193 -0.0226 37  SER   C O   
1333 C CB  . SER   B 31  ? 0.2315 0.2697 0.3887 0.0119  -0.0327 -0.0390 37  SER   C CB  
1334 O OG  . SER   B 31  ? 0.2944 0.3361 0.4340 0.0183  -0.0342 -0.0446 37  SER   C OG  
1335 N N   . ARG   B 32  ? 0.1618 0.2030 0.2766 0.0083  -0.0186 -0.0211 38  ARG   C N   
1336 C CA  . ARG   B 32  ? 0.1657 0.2089 0.2652 0.0078  -0.0149 -0.0175 38  ARG   C CA  
1337 C C   . ARG   B 32  ? 0.1621 0.2028 0.2544 0.0034  -0.0104 -0.0082 38  ARG   C C   
1338 O O   . ARG   B 32  ? 0.1703 0.2114 0.2514 0.0026  -0.0079 -0.0052 38  ARG   C O   
1339 C CB  . ARG   B 32  ? 0.1643 0.2106 0.2504 0.0133  -0.0156 -0.0212 38  ARG   C CB  
1340 C CG  . ARG   B 32  ? 0.1740 0.2221 0.2618 0.0194  -0.0207 -0.0309 38  ARG   C CG  
1341 C CD  . ARG   B 32  ? 0.1907 0.2412 0.2629 0.0261  -0.0203 -0.0337 38  ARG   C CD  
1342 N NE  . ARG   B 32  ? 0.1747 0.2260 0.2337 0.0253  -0.0162 -0.0284 38  ARG   C NE  
1343 C CZ  . ARG   B 32  ? 0.2014 0.2540 0.2467 0.0312  -0.0158 -0.0301 38  ARG   C CZ  
1344 N NH1 . ARG   B 32  ? 0.2204 0.2743 0.2614 0.0391  -0.0191 -0.0374 38  ARG   C NH1 
1345 N NH2 . ARG   B 32  ? 0.2081 0.2602 0.2435 0.0299  -0.0125 -0.0248 38  ARG   C NH2 
1346 N N   . ASP   B 33  ? 0.1578 0.1954 0.2557 0.0013  -0.0103 -0.0040 39  ASP   C N   
1347 C CA  . ASP   B 33  ? 0.1543 0.1891 0.2439 -0.0015 -0.0079 0.0039  39  ASP   C CA  
1348 C C   . ASP   B 33  ? 0.1475 0.1848 0.2260 0.0001  -0.0079 0.0041  39  ASP   C C   
1349 O O   . ASP   B 33  ? 0.1554 0.1909 0.2249 -0.0020 -0.0066 0.0089  39  ASP   C O   
1350 C CB  . ASP   B 33  ? 0.1597 0.1918 0.2442 -0.0047 -0.0041 0.0095  39  ASP   C CB  
1351 C CG  . ASP   B 33  ? 0.1747 0.2024 0.2493 -0.0064 -0.0031 0.0168  39  ASP   C CG  
1352 O OD1 . ASP   B 33  ? 0.1870 0.2122 0.2651 -0.0064 -0.0052 0.0195  39  ASP   C OD1 
1353 O OD2 . ASP   B 33  ? 0.1838 0.2102 0.2467 -0.0071 -0.0009 0.0194  39  ASP   C OD2 
1354 N N   . LEU   B 34  ? 0.1416 0.1827 0.2214 0.0040  -0.0092 -0.0008 40  LEU   C N   
1355 C CA  . LEU   B 34  ? 0.1476 0.1917 0.2199 0.0053  -0.0078 0.0007  40  LEU   C CA  
1356 C C   . LEU   B 34  ? 0.1597 0.2061 0.2383 0.0073  -0.0086 0.0004  40  LEU   C C   
1357 O O   . LEU   B 34  ? 0.1607 0.2076 0.2468 0.0104  -0.0105 -0.0044 40  LEU   C O   
1358 C CB  . LEU   B 34  ? 0.1559 0.2036 0.2210 0.0093  -0.0065 -0.0035 40  LEU   C CB  
1359 C CG  . LEU   B 34  ? 0.1668 0.2131 0.2243 0.0081  -0.0056 -0.0031 40  LEU   C CG  
1360 C CD1 . LEU   B 34  ? 0.1803 0.2296 0.2297 0.0134  -0.0048 -0.0067 40  LEU   C CD1 
1361 C CD2 . LEU   B 34  ? 0.1707 0.2145 0.2221 0.0039  -0.0040 0.0033  40  LEU   C CD2 
1362 N N   . LEU   B 35  ? 0.1458 0.1940 0.2224 0.0062  -0.0075 0.0046  41  LEU   C N   
1363 C CA  . LEU   B 35  ? 0.1568 0.2088 0.2406 0.0086  -0.0074 0.0045  41  LEU   C CA  
1364 C C   . LEU   B 35  ? 0.1542 0.2110 0.2350 0.0088  -0.0040 0.0074  41  LEU   C C   
1365 O O   . LEU   B 35  ? 0.1728 0.2274 0.2486 0.0050  -0.0040 0.0113  41  LEU   C O   
1366 C CB  . LEU   B 35  ? 0.1681 0.2168 0.2593 0.0062  -0.0110 0.0080  41  LEU   C CB  
1367 C CG  . LEU   B 35  ? 0.1760 0.2292 0.2776 0.0091  -0.0116 0.0075  41  LEU   C CG  
1368 C CD1 . LEU   B 35  ? 0.1787 0.2270 0.2888 0.0088  -0.0162 0.0085  41  LEU   C CD1 
1369 C CD2 . LEU   B 35  ? 0.1975 0.2543 0.3011 0.0071  -0.0112 0.0122  41  LEU   C CD2 
1370 N N   . VAL   B 36  ? 0.1498 0.2128 0.2338 0.0134  -0.0006 0.0056  42  VAL   C N   
1371 C CA  . VAL   B 36  ? 0.1638 0.2321 0.2480 0.0137  0.0043  0.0096  42  VAL   C CA  
1372 C C   . VAL   B 36  ? 0.1717 0.2456 0.2693 0.0151  0.0051  0.0108  42  VAL   C C   
1373 O O   . VAL   B 36  ? 0.1711 0.2473 0.2731 0.0199  0.0051  0.0064  42  VAL   C O   
1374 C CB  . VAL   B 36  ? 0.1726 0.2440 0.2469 0.0193  0.0098  0.0074  42  VAL   C CB  
1375 C CG1 . VAL   B 36  ? 0.1856 0.2627 0.2622 0.0197  0.0164  0.0133  42  VAL   C CG1 
1376 C CG2 . VAL   B 36  ? 0.1845 0.2506 0.2471 0.0182  0.0080  0.0059  42  VAL   C CG2 
1377 N N   . SER   B 37  ? 0.1673 0.2432 0.2726 0.0111  0.0049  0.0161  43  SER   C N   
1378 C CA  . SER   B 37  ? 0.1821 0.2646 0.3031 0.0121  0.0056  0.0178  43  SER   C CA  
1379 C C   . SER   B 37  ? 0.1989 0.2888 0.3264 0.0120  0.0127  0.0226  43  SER   C C   
1380 O O   . SER   B 37  ? 0.2019 0.2899 0.3221 0.0098  0.0154  0.0256  43  SER   C O   
1381 C CB  . SER   B 37  ? 0.1806 0.2591 0.3095 0.0077  -0.0026 0.0196  43  SER   C CB  
1382 O OG  . SER   B 37  ? 0.2130 0.2872 0.3389 0.0023  -0.0059 0.0233  43  SER   C OG  
1383 N N   . SER   B 38  ? 0.2081 0.3066 0.3509 0.0147  0.0162  0.0237  44  SER   C N   
1384 C CA  . SER   B 38  ? 0.2390 0.3456 0.3914 0.0146  0.0244  0.0295  44  SER   C CA  
1385 C C   . SER   B 38  ? 0.2602 0.3673 0.4294 0.0075  0.0193  0.0342  44  SER   C C   
1386 O O   . SER   B 38  ? 0.2658 0.3705 0.4430 0.0051  0.0104  0.0325  44  SER   C O   
1387 C CB  . SER   B 38  ? 0.2567 0.3736 0.4183 0.0217  0.0324  0.0286  44  SER   C CB  
1388 O OG  . SER   B 38  ? 0.3008 0.4198 0.4774 0.0217  0.0264  0.0262  44  SER   C OG  
1389 N N   . THR   B 39  ? 0.2766 0.3863 0.4513 0.0045  0.0245  0.0401  45  THR   C N   
1390 C CA  . THR   B 39  ? 0.3054 0.4156 0.4985 -0.0022 0.0194  0.0441  45  THR   C CA  
1391 C C   . THR   B 39  ? 0.3342 0.4562 0.5492 -0.0019 0.0293  0.0504  45  THR   C C   
1392 O O   . THR   B 39  ? 0.3374 0.4652 0.5476 0.0034  0.0414  0.0530  45  THR   C O   
1393 C CB  . THR   B 39  ? 0.3249 0.4254 0.5070 -0.0074 0.0154  0.0456  45  THR   C CB  
1394 O OG1 . THR   B 39  ? 0.3467 0.4491 0.5244 -0.0063 0.0259  0.0506  45  THR   C OG1 
1395 C CG2 . THR   B 39  ? 0.3322 0.4221 0.4916 -0.0070 0.0088  0.0403  45  THR   C CG2 
1396 N N   . THR   B 40  ? 0.3573 0.4825 0.5964 -0.0072 0.0242  0.0532  46  THR   C N   
1397 C CA  . THR   B 40  ? 0.3786 0.5153 0.6437 -0.0082 0.0335  0.0602  46  THR   C CA  
1398 C C   . THR   B 40  ? 0.4056 0.5383 0.6731 -0.0137 0.0366  0.0667  46  THR   C C   
1399 O O   . THR   B 40  ? 0.4195 0.5597 0.6979 -0.0129 0.0494  0.0744  46  THR   C O   
1400 C CB  . THR   B 40  ? 0.3948 0.5383 0.6891 -0.0107 0.0255  0.0592  46  THR   C CB  
1401 O OG1 . THR   B 40  ? 0.4285 0.5616 0.7215 -0.0162 0.0096  0.0556  46  THR   C OG1 
1402 C CG2 . THR   B 40  ? 0.3945 0.5433 0.6895 -0.0043 0.0250  0.0543  46  THR   C CG2 
1403 N N   . ALA   B 41  ? 0.4140 0.5346 0.6715 -0.0186 0.0254  0.0639  47  ALA   C N   
1404 C CA  . ALA   B 41  ? 0.4224 0.5373 0.6819 -0.0237 0.0265  0.0690  47  ALA   C CA  
1405 C C   . ALA   B 41  ? 0.4345 0.5429 0.6649 -0.0200 0.0340  0.0701  47  ALA   C C   
1406 O O   . ALA   B 41  ? 0.4466 0.5509 0.6536 -0.0157 0.0320  0.0643  47  ALA   C O   
1407 C CB  . ALA   B 41  ? 0.4305 0.5349 0.6917 -0.0294 0.0102  0.0642  47  ALA   C CB  
1408 N N   . GLN   B 42  ? 0.4297 0.5368 0.6631 -0.0219 0.0419  0.0777  48  GLN   C N   
1409 C CA  . GLN   B 42  ? 0.4394 0.5402 0.6468 -0.0181 0.0485  0.0796  48  GLN   C CA  
1410 C C   . GLN   B 42  ? 0.4251 0.5123 0.6164 -0.0213 0.0370  0.0743  48  GLN   C C   
1411 O O   . GLN   B 42  ? 0.4385 0.5202 0.6427 -0.0276 0.0290  0.0747  48  GLN   C O   
1412 C CB  . GLN   B 42  ? 0.4812 0.5852 0.6980 -0.0183 0.0619  0.0912  48  GLN   C CB  
1413 C CG  . GLN   B 42  ? 0.5692 0.6667 0.7581 -0.0130 0.0690  0.0939  48  GLN   C CG  
1414 C CD  . GLN   B 42  ? 0.6691 0.7737 0.8411 -0.0031 0.0803  0.0943  48  GLN   C CD  
1415 O OE1 . GLN   B 42  ? 0.6931 0.8080 0.8746 0.0001  0.0844  0.0929  48  GLN   C OE1 
1416 N NE2 . GLN   B 42  ? 0.6970 0.7958 0.8430 0.0027  0.0850  0.0955  48  GLN   C NE2 
1417 N N   . GLY   B 43  ? 0.3902 0.4724 0.5548 -0.0167 0.0356  0.0687  49  GLY   C N   
1418 C CA  . GLY   B 43  ? 0.3794 0.4499 0.5272 -0.0185 0.0265  0.0636  49  GLY   C CA  
1419 C C   . GLY   B 43  ? 0.3644 0.4290 0.5017 -0.0177 0.0320  0.0686  49  GLY   C C   
1420 O O   . GLY   B 43  ? 0.3694 0.4384 0.5010 -0.0129 0.0430  0.0739  49  GLY   C O   
1421 N N   . CYS   B 44  ? 0.3492 0.4036 0.4827 -0.0214 0.0244  0.0668  50  CYS   C N   
1422 C CA  . CYS   B 44  ? 0.3554 0.4033 0.4813 -0.0208 0.0288  0.0720  50  CYS   C CA  
1423 C C   . CYS   B 44  ? 0.3362 0.3759 0.4375 -0.0175 0.0249  0.0665  50  CYS   C C   
1424 O O   . CYS   B 44  ? 0.3519 0.3847 0.4475 -0.0172 0.0265  0.0700  50  CYS   C O   
1425 C CB  . CYS   B 44  ? 0.3967 0.4394 0.5429 -0.0276 0.0252  0.0766  50  CYS   C CB  
1426 S SG  . CYS   B 44  ? 0.5203 0.5739 0.7006 -0.0317 0.0319  0.0852  50  CYS   C SG  
1427 N N   . ASP   B 45  ? 0.2873 0.3275 0.3760 -0.0151 0.0201  0.0584  51  ASP   C N   
1428 C CA  . ASP   B 45  ? 0.2755 0.3092 0.3438 -0.0119 0.0172  0.0534  51  ASP   C CA  
1429 C C   . ASP   B 45  ? 0.2821 0.3180 0.3369 -0.0052 0.0253  0.0561  51  ASP   C C   
1430 O O   . ASP   B 45  ? 0.2984 0.3421 0.3543 -0.0016 0.0320  0.0583  51  ASP   C O   
1431 C CB  . ASP   B 45  ? 0.3000 0.3343 0.3604 -0.0109 0.0113  0.0451  51  ASP   C CB  
1432 C CG  . ASP   B 45  ? 0.3739 0.4042 0.4409 -0.0156 0.0024  0.0417  51  ASP   C CG  
1433 O OD1 . ASP   B 45  ? 0.4078 0.4327 0.4826 -0.0193 -0.0014 0.0435  51  ASP   C OD1 
1434 O OD2 . ASP   B 45  ? 0.3640 0.3959 0.4283 -0.0151 -0.0012 0.0372  51  ASP   C OD2 
1435 N N   . THR   B 46  ? 0.2651 0.2941 0.3072 -0.0030 0.0244  0.0558  52  THR   C N   
1436 C CA  . THR   B 46  ? 0.2777 0.3075 0.3044 0.0044  0.0299  0.0573  52  THR   C CA  
1437 C C   . THR   B 46  ? 0.2649 0.2945 0.2787 0.0079  0.0247  0.0481  52  THR   C C   
1438 O O   . THR   B 46  ? 0.2715 0.2958 0.2836 0.0054  0.0184  0.0436  52  THR   C O   
1439 C CB  . THR   B 46  ? 0.3310 0.3526 0.3528 0.0051  0.0314  0.0631  52  THR   C CB  
1440 O OG1 . THR   B 46  ? 0.3732 0.3952 0.4098 0.0015  0.0373  0.0729  52  THR   C OG1 
1441 C CG2 . THR   B 46  ? 0.3441 0.3650 0.3469 0.0137  0.0350  0.0637  52  THR   C CG2 
1442 N N   . ILE   B 47  ? 0.2525 0.2878 0.2582 0.0141  0.0275  0.0452  53  ILE   C N   
1443 C CA  . ILE   B 47  ? 0.2384 0.2739 0.2348 0.0177  0.0225  0.0365  53  ILE   C CA  
1444 C C   . ILE   B 47  ? 0.2326 0.2635 0.2148 0.0235  0.0218  0.0361  53  ILE   C C   
1445 O O   . ILE   B 47  ? 0.2487 0.2793 0.2225 0.0288  0.0271  0.0415  53  ILE   C O   
1446 C CB  . ILE   B 47  ? 0.2453 0.2880 0.2407 0.0222  0.0241  0.0323  53  ILE   C CB  
1447 C CG1 . ILE   B 47  ? 0.2638 0.3115 0.2737 0.0177  0.0254  0.0335  53  ILE   C CG1 
1448 C CG2 . ILE   B 47  ? 0.2506 0.2932 0.2410 0.0249  0.0180  0.0231  53  ILE   C CG2 
1449 C CD1 . ILE   B 47  ? 0.2872 0.3322 0.3057 0.0107  0.0187  0.0305  53  ILE   C CD1 
1450 N N   . ALA   B 48  ? 0.2217 0.2491 0.2012 0.0229  0.0157  0.0304  54  ALA   C N   
1451 C CA  . ALA   B 48  ? 0.2078 0.2313 0.1752 0.0288  0.0137  0.0288  54  ALA   C CA  
1452 C C   . ALA   B 48  ? 0.2165 0.2445 0.1744 0.0371  0.0132  0.0240  54  ALA   C C   
1453 O O   . ALA   B 48  ? 0.2121 0.2451 0.1747 0.0371  0.0114  0.0182  54  ALA   C O   
1454 C CB  . ALA   B 48  ? 0.2085 0.2293 0.1784 0.0264  0.0075  0.0227  54  ALA   C CB  
1455 N N   . ARG   B 49  ? 0.2143 0.2393 0.1582 0.0448  0.0140  0.0262  55  ARG   C N   
1456 C CA  . ARG   B 49  ? 0.2201 0.2480 0.1520 0.0544  0.0119  0.0205  55  ARG   C CA  
1457 C C   . ARG   B 49  ? 0.2340 0.2570 0.1577 0.0591  0.0056  0.0172  55  ARG   C C   
1458 O O   . ARG   B 49  ? 0.2691 0.2870 0.1806 0.0642  0.0074  0.0230  55  ARG   C O   
1459 C CB  . ARG   B 49  ? 0.2329 0.2619 0.1532 0.0609  0.0199  0.0275  55  ARG   C CB  
1460 C CG  . ARG   B 49  ? 0.2396 0.2741 0.1715 0.0558  0.0266  0.0313  55  ARG   C CG  
1461 C CD  . ARG   B 49  ? 0.2648 0.3054 0.2052 0.0547  0.0228  0.0222  55  ARG   C CD  
1462 N NE  . ARG   B 49  ? 0.2750 0.3207 0.2261 0.0508  0.0294  0.0267  55  ARG   C NE  
1463 C CZ  . ARG   B 49  ? 0.2813 0.3314 0.2444 0.0471  0.0271  0.0216  55  ARG   C CZ  
1464 N NH1 . ARG   B 49  ? 0.2531 0.3029 0.2190 0.0467  0.0193  0.0123  55  ARG   C NH1 
1465 N NH2 . ARG   B 49  ? 0.3024 0.3573 0.2759 0.0441  0.0327  0.0259  55  ARG   C NH2 
1466 N N   . CYS   B 50  ? 0.2246 0.2494 0.1564 0.0574  -0.0017 0.0081  56  CYS   C N   
1467 C CA  . CYS   B 50  ? 0.2274 0.2487 0.1569 0.0602  -0.0078 0.0048  56  CYS   C CA  
1468 C C   . CYS   B 50  ? 0.2390 0.2649 0.1800 0.0593  -0.0149 -0.0058 56  CYS   C C   
1469 O O   . CYS   B 50  ? 0.2216 0.2522 0.1727 0.0554  -0.0147 -0.0094 56  CYS   C O   
1470 C CB  . CYS   B 50  ? 0.2458 0.2616 0.1801 0.0537  -0.0054 0.0111  56  CYS   C CB  
1471 S SG  . CYS   B 50  ? 0.2259 0.2444 0.1784 0.0426  -0.0049 0.0087  56  CYS   C SG  
1472 N N   . ASP   B 51  ? 0.2386 0.2627 0.1808 0.0619  -0.0206 -0.0096 57  ASP   C N   
1473 C CA  . ASP   B 51  ? 0.2407 0.2695 0.1975 0.0604  -0.0263 -0.0184 57  ASP   C CA  
1474 C C   . ASP   B 51  ? 0.2450 0.2723 0.2109 0.0550  -0.0252 -0.0170 57  ASP   C C   
1475 O O   . ASP   B 51  ? 0.2461 0.2764 0.2221 0.0560  -0.0297 -0.0230 57  ASP   C O   
1476 C CB  . ASP   B 51  ? 0.2637 0.2939 0.2172 0.0698  -0.0354 -0.0267 57  ASP   C CB  
1477 C CG  . ASP   B 51  ? 0.3375 0.3623 0.2793 0.0764  -0.0386 -0.0246 57  ASP   C CG  
1478 O OD1 . ASP   B 51  ? 0.3556 0.3748 0.2921 0.0737  -0.0335 -0.0163 57  ASP   C OD1 
1479 O OD2 . ASP   B 51  ? 0.4147 0.4404 0.3540 0.0846  -0.0474 -0.0317 57  ASP   C OD2 
1480 N N   . CYS   B 52  ? 0.2189 0.2417 0.1827 0.0493  -0.0194 -0.0095 58  CYS   C N   
1481 C CA  . CYS   B 52  ? 0.1983 0.2189 0.1689 0.0450  -0.0184 -0.0090 58  CYS   C CA  
1482 C C   . CYS   B 52  ? 0.1902 0.2170 0.1755 0.0411  -0.0185 -0.0143 58  CYS   C C   
1483 O O   . CYS   B 52  ? 0.1938 0.2249 0.1851 0.0379  -0.0172 -0.0155 58  CYS   C O   
1484 C CB  . CYS   B 52  ? 0.2109 0.2259 0.1785 0.0393  -0.0133 -0.0016 58  CYS   C CB  
1485 S SG  . CYS   B 52  ? 0.2497 0.2555 0.2046 0.0426  -0.0122 0.0065  58  CYS   C SG  
1486 N N   . GLN   B 53  ? 0.1837 0.2105 0.1751 0.0411  -0.0193 -0.0168 59  GLN   C N   
1487 C CA  . GLN   B 53  ? 0.1824 0.2147 0.1877 0.0372  -0.0172 -0.0199 59  GLN   C CA  
1488 C C   . GLN   B 53  ? 0.1791 0.2072 0.1829 0.0342  -0.0132 -0.0173 59  GLN   C C   
1489 O O   . GLN   B 53  ? 0.1876 0.2196 0.2008 0.0329  -0.0106 -0.0196 59  GLN   C O   
1490 C CB  . GLN   B 53  ? 0.1880 0.2269 0.2064 0.0410  -0.0214 -0.0269 59  GLN   C CB  
1491 C CG  . GLN   B 53  ? 0.2014 0.2452 0.2258 0.0428  -0.0259 -0.0315 59  GLN   C CG  
1492 C CD  . GLN   B 53  ? 0.2384 0.2889 0.2794 0.0462  -0.0313 -0.0390 59  GLN   C CD  
1493 O OE1 . GLN   B 53  ? 0.2873 0.3380 0.3256 0.0531  -0.0391 -0.0438 59  GLN   C OE1 
1494 N NE2 . GLN   B 53  ? 0.2160 0.2718 0.2745 0.0418  -0.0272 -0.0398 59  GLN   C NE2 
1495 N N   . THR   B 54  ? 0.1920 0.2121 0.1844 0.0336  -0.0125 -0.0126 60  THR   C N   
1496 C CA  . THR   B 54  ? 0.1984 0.2133 0.1882 0.0310  -0.0100 -0.0110 60  THR   C CA  
1497 C C   . THR   B 54  ? 0.1960 0.2051 0.1790 0.0268  -0.0089 -0.0055 60  THR   C C   
1498 O O   . THR   B 54  ? 0.2182 0.2259 0.1971 0.0272  -0.0096 -0.0020 60  THR   C O   
1499 C CB  . THR   B 54  ? 0.2592 0.2687 0.2458 0.0353  -0.0122 -0.0123 60  THR   C CB  
1500 O OG1 . THR   B 54  ? 0.3058 0.3089 0.2841 0.0376  -0.0150 -0.0085 60  THR   C OG1 
1501 C CG2 . THR   B 54  ? 0.2591 0.2749 0.2546 0.0400  -0.0138 -0.0179 60  THR   C CG2 
1502 N N   . GLY   B 55  ? 0.1876 0.1944 0.1701 0.0230  -0.0069 -0.0050 61  GLY   C N   
1503 C CA  . GLY   B 55  ? 0.1846 0.1864 0.1636 0.0188  -0.0071 -0.0007 61  GLY   C CA  
1504 C C   . GLY   B 55  ? 0.1804 0.1786 0.1571 0.0165  -0.0066 -0.0017 61  GLY   C C   
1505 O O   . GLY   B 55  ? 0.2016 0.1997 0.1772 0.0189  -0.0056 -0.0052 61  GLY   C O   
1506 N N   . VAL   B 56  ? 0.1808 0.1762 0.1567 0.0124  -0.0076 0.0012  62  VAL   C N   
1507 C CA  . VAL   B 56  ? 0.1877 0.1783 0.1591 0.0111  -0.0089 -0.0002 62  VAL   C CA  
1508 C C   . VAL   B 56  ? 0.1829 0.1771 0.1566 0.0076  -0.0082 0.0021  62  VAL   C C   
1509 O O   . VAL   B 56  ? 0.1851 0.1812 0.1638 0.0049  -0.0089 0.0054  62  VAL   C O   
1510 C CB  . VAL   B 56  ? 0.2074 0.1881 0.1764 0.0103  -0.0138 0.0002  62  VAL   C CB  
1511 C CG1 . VAL   B 56  ? 0.2378 0.2126 0.2010 0.0097  -0.0172 -0.0024 62  VAL   C CG1 
1512 C CG2 . VAL   B 56  ? 0.2187 0.1946 0.1856 0.0142  -0.0148 -0.0019 62  VAL   C CG2 
1513 N N   . TYR   B 57  ? 0.1884 0.1832 0.1582 0.0079  -0.0067 0.0009  63  TYR   C N   
1514 C CA  . TYR   B 57  ? 0.1840 0.1807 0.1552 0.0049  -0.0070 0.0035  63  TYR   C CA  
1515 C C   . TYR   B 57  ? 0.2042 0.1941 0.1667 0.0051  -0.0106 0.0027  63  TYR   C C   
1516 O O   . TYR   B 57  ? 0.2141 0.1988 0.1677 0.0085  -0.0112 -0.0005 63  TYR   C O   
1517 C CB  . TYR   B 57  ? 0.1766 0.1809 0.1526 0.0050  -0.0019 0.0044  63  TYR   C CB  
1518 C CG  . TYR   B 57  ? 0.1907 0.1947 0.1611 0.0074  0.0022  0.0037  63  TYR   C CG  
1519 C CD1 . TYR   B 57  ? 0.2196 0.2247 0.1892 0.0109  0.0054  0.0010  63  TYR   C CD1 
1520 C CD2 . TYR   B 57  ? 0.2002 0.2030 0.1662 0.0069  0.0034  0.0064  63  TYR   C CD2 
1521 C CE1 . TYR   B 57  ? 0.2383 0.2445 0.2042 0.0135  0.0111  0.0012  63  TYR   C CE1 
1522 C CE2 . TYR   B 57  ? 0.2269 0.2296 0.1868 0.0098  0.0089  0.0072  63  TYR   C CE2 
1523 C CZ  . TYR   B 57  ? 0.2446 0.2493 0.2048 0.0130  0.0133  0.0047  63  TYR   C CZ  
1524 O OH  . TYR   B 57  ? 0.2774 0.2831 0.2326 0.0164  0.0204  0.0062  63  TYR   C OH  
1525 N N   . TYR   B 58  ? 0.2097 0.1993 0.1743 0.0024  -0.0137 0.0050  64  TYR   C N   
1526 C CA  . TYR   B 58  ? 0.2101 0.1930 0.1659 0.0032  -0.0187 0.0039  64  TYR   C CA  
1527 C C   . TYR   B 58  ? 0.2275 0.2121 0.1761 0.0052  -0.0148 0.0055  64  TYR   C C   
1528 O O   . TYR   B 58  ? 0.2206 0.2111 0.1765 0.0031  -0.0117 0.0089  64  TYR   C O   
1529 C CB  . TYR   B 58  ? 0.2191 0.2007 0.1826 -0.0005 -0.0252 0.0054  64  TYR   C CB  
1530 C CG  . TYR   B 58  ? 0.2528 0.2268 0.2067 0.0013  -0.0325 0.0030  64  TYR   C CG  
1531 C CD1 . TYR   B 58  ? 0.2770 0.2423 0.2220 0.0042  -0.0378 -0.0019 64  TYR   C CD1 
1532 C CD2 . TYR   B 58  ? 0.2847 0.2597 0.2379 0.0009  -0.0348 0.0052  64  TYR   C CD2 
1533 C CE1 . TYR   B 58  ? 0.3158 0.2733 0.2496 0.0073  -0.0456 -0.0053 64  TYR   C CE1 
1534 C CE2 . TYR   B 58  ? 0.3000 0.2674 0.2420 0.0038  -0.0425 0.0027  64  TYR   C CE2 
1535 C CZ  . TYR   B 58  ? 0.3222 0.2809 0.2540 0.0072  -0.0481 -0.0029 64  TYR   C CZ  
1536 O OH  . TYR   B 58  ? 0.3591 0.3094 0.2778 0.0112  -0.0570 -0.0065 64  TYR   C OH  
1537 N N   . CYS   B 59  ? 0.2350 0.2140 0.1691 0.0097  -0.0146 0.0034  65  CYS   C N   
1538 C CA  . CYS   B 59  ? 0.2405 0.2200 0.1654 0.0125  -0.0096 0.0063  65  CYS   C CA  
1539 C C   . CYS   B 59  ? 0.2656 0.2368 0.1766 0.0151  -0.0170 0.0055  65  CYS   C C   
1540 O O   . CYS   B 59  ? 0.2859 0.2495 0.1825 0.0198  -0.0207 0.0011  65  CYS   C O   
1541 C CB  . CYS   B 59  ? 0.2481 0.2285 0.1661 0.0170  -0.0021 0.0049  65  CYS   C CB  
1542 S SG  . CYS   B 59  ? 0.2941 0.2744 0.1995 0.0215  0.0062  0.0098  65  CYS   C SG  
1543 N N   . SER   B 60  ? 0.2658 0.2381 0.1809 0.0126  -0.0199 0.0092  66  SER   C N   
1544 C CA  . SER   B 60  ? 0.3058 0.2705 0.2093 0.0153  -0.0286 0.0083  66  SER   C CA  
1545 C C   . SER   B 60  ? 0.3207 0.2792 0.2015 0.0225  -0.0260 0.0088  66  SER   C C   
1546 O O   . SER   B 60  ? 0.3351 0.2848 0.2007 0.0272  -0.0344 0.0043  66  SER   C O   
1547 C CB  . SER   B 60  ? 0.3666 0.3344 0.2806 0.0117  -0.0321 0.0124  66  SER   C CB  
1548 O OG  . SER   B 60  ? 0.4344 0.4058 0.3478 0.0121  -0.0241 0.0183  66  SER   C OG  
1549 N N   . SER   B 61  ? 0.3071 0.2699 0.1854 0.0241  -0.0143 0.0136  67  SER   C N   
1550 C CA  . SER   B 61  ? 0.3343 0.2920 0.1903 0.0317  -0.0090 0.0156  67  SER   C CA  
1551 C C   . SER   B 61  ? 0.3479 0.3009 0.1897 0.0377  -0.0085 0.0092  67  SER   C C   
1552 O O   . SER   B 61  ? 0.3744 0.3222 0.1944 0.0456  -0.0047 0.0098  67  SER   C O   
1553 C CB  . SER   B 61  ? 0.3423 0.3064 0.2034 0.0311  0.0041  0.0237  67  SER   C CB  
1554 O OG  . SER   B 61  ? 0.3409 0.3129 0.2163 0.0286  0.0122  0.0228  67  SER   C OG  
1555 N N   . ARG   B 62  ? 0.3232 0.2771 0.1757 0.0350  -0.0125 0.0031  68  ARG   C N   
1556 C CA  . ARG   B 62  ? 0.3255 0.2735 0.1661 0.0406  -0.0145 -0.0041 68  ARG   C CA  
1557 C C   . ARG   B 62  ? 0.3491 0.2899 0.1931 0.0388  -0.0289 -0.0115 68  ARG   C C   
1558 O O   . ARG   B 62  ? 0.3777 0.3119 0.2136 0.0432  -0.0328 -0.0185 68  ARG   C O   
1559 C CB  . ARG   B 62  ? 0.3285 0.2838 0.1798 0.0399  -0.0048 -0.0045 68  ARG   C CB  
1560 C CG  . ARG   B 62  ? 0.3512 0.3137 0.2017 0.0420  0.0094  0.0020  68  ARG   C CG  
1561 C CD  . ARG   B 62  ? 0.3728 0.3294 0.1983 0.0521  0.0142  0.0006  68  ARG   C CD  
1562 N NE  . ARG   B 62  ? 0.4151 0.3791 0.2419 0.0542  0.0294  0.0079  68  ARG   C NE  
1563 C CZ  . ARG   B 62  ? 0.4649 0.4294 0.2861 0.0547  0.0354  0.0164  68  ARG   C CZ  
1564 N NH1 . ARG   B 62  ? 0.4665 0.4244 0.2787 0.0541  0.0266  0.0182  68  ARG   C NH1 
1565 N NH2 . ARG   B 62  ? 0.4616 0.4329 0.2870 0.0563  0.0501  0.0235  68  ARG   C NH2 
1566 N N   . ARG   B 63  ? 0.3439 0.2859 0.2019 0.0324  -0.0365 -0.0097 69  ARG   C N   
1567 C CA  . ARG   B 63  ? 0.3627 0.2998 0.2309 0.0291  -0.0488 -0.0150 69  ARG   C CA  
1568 C C   . ARG   B 63  ? 0.3752 0.3123 0.2524 0.0276  -0.0473 -0.0185 69  ARG   C C   
1569 O O   . ARG   B 63  ? 0.4020 0.3306 0.2768 0.0296  -0.0558 -0.0252 69  ARG   C O   
1570 C CB  . ARG   B 63  ? 0.3956 0.3209 0.2473 0.0349  -0.0615 -0.0216 69  ARG   C CB  
1571 C CG  . ARG   B 63  ? 0.4575 0.3822 0.3049 0.0352  -0.0667 -0.0182 69  ARG   C CG  
1572 C CD  . ARG   B 63  ? 0.5567 0.4696 0.3907 0.0409  -0.0820 -0.0260 69  ARG   C CD  
1573 N NE  . ARG   B 63  ? 0.6408 0.5506 0.4595 0.0455  -0.0859 -0.0234 69  ARG   C NE  
1574 C CZ  . ARG   B 63  ? 0.7122 0.6125 0.5022 0.0558  -0.0901 -0.0271 69  ARG   C CZ  
1575 N NH1 . ARG   B 63  ? 0.7244 0.6178 0.4980 0.0627  -0.0901 -0.0342 69  ARG   C NH1 
1576 N NH2 . ARG   B 63  ? 0.7188 0.6161 0.4948 0.0602  -0.0938 -0.0235 69  ARG   C NH2 
1577 N N   . LYS   B 64  ? 0.3481 0.2944 0.2355 0.0248  -0.0366 -0.0143 70  LYS   C N   
1578 C CA  . LYS   B 64  ? 0.3358 0.2821 0.2298 0.0247  -0.0346 -0.0171 70  LYS   C CA  
1579 C C   . LYS   B 64  ? 0.2940 0.2502 0.2054 0.0191  -0.0281 -0.0121 70  LYS   C C   
1580 O O   . LYS   B 64  ? 0.2852 0.2491 0.2007 0.0171  -0.0221 -0.0071 70  LYS   C O   
1581 C CB  . LYS   B 64  ? 0.3969 0.3432 0.2771 0.0319  -0.0266 -0.0196 70  LYS   C CB  
1582 C CG  . LYS   B 64  ? 0.5481 0.4833 0.4102 0.0395  -0.0323 -0.0273 70  LYS   C CG  
1583 C CD  . LYS   B 64  ? 0.6649 0.6031 0.5160 0.0465  -0.0215 -0.0281 70  LYS   C CD  
1584 C CE  . LYS   B 64  ? 0.7552 0.6833 0.5903 0.0550  -0.0259 -0.0370 70  LYS   C CE  
1585 N NZ  . LYS   B 64  ? 0.8044 0.7277 0.6144 0.0637  -0.0241 -0.0385 70  LYS   C NZ  
1586 N N   . HIS   B 65  ? 0.2781 0.2333 0.1980 0.0178  -0.0291 -0.0137 71  HIS   C N   
1587 C CA  . HIS   B 65  ? 0.2581 0.2217 0.1909 0.0146  -0.0232 -0.0098 71  HIS   C CA  
1588 C C   . HIS   B 65  ? 0.2714 0.2375 0.2008 0.0192  -0.0168 -0.0121 71  HIS   C C   
1589 O O   . HIS   B 65  ? 0.3155 0.2750 0.2365 0.0239  -0.0186 -0.0171 71  HIS   C O   
1590 C CB  . HIS   B 65  ? 0.2429 0.2036 0.1870 0.0110  -0.0279 -0.0090 71  HIS   C CB  
1591 C CG  . HIS   B 65  ? 0.2653 0.2248 0.2173 0.0062  -0.0337 -0.0065 71  HIS   C CG  
1592 N ND1 . HIS   B 65  ? 0.2780 0.2453 0.2417 0.0018  -0.0307 -0.0011 71  HIS   C ND1 
1593 C CD2 . HIS   B 65  ? 0.2828 0.2344 0.2341 0.0056  -0.0426 -0.0094 71  HIS   C CD2 
1594 C CE1 . HIS   B 65  ? 0.2637 0.2282 0.2344 -0.0015 -0.0370 -0.0003 71  HIS   C CE1 
1595 N NE2 . HIS   B 65  ? 0.3115 0.2668 0.2760 0.0003  -0.0447 -0.0052 71  HIS   C NE2 
1596 N N   . TYR   B 66  ? 0.2354 0.2111 0.1730 0.0181  -0.0099 -0.0091 72  TYR   C N   
1597 C CA  . TYR   B 66  ? 0.2324 0.2121 0.1709 0.0222  -0.0042 -0.0112 72  TYR   C CA  
1598 C C   . TYR   B 66  ? 0.2223 0.2076 0.1733 0.0205  -0.0034 -0.0100 72  TYR   C C   
1599 O O   . TYR   B 66  ? 0.2100 0.2007 0.1687 0.0168  -0.0029 -0.0066 72  TYR   C O   
1600 C CB  . TYR   B 66  ? 0.2525 0.2397 0.1909 0.0234  0.0040  -0.0089 72  TYR   C CB  
1601 C CG  . TYR   B 66  ? 0.2828 0.2653 0.2060 0.0273  0.0058  -0.0095 72  TYR   C CG  
1602 C CD1 . TYR   B 66  ? 0.3007 0.2789 0.2131 0.0337  0.0075  -0.0140 72  TYR   C CD1 
1603 C CD2 . TYR   B 66  ? 0.2957 0.2780 0.2142 0.0255  0.0062  -0.0055 72  TYR   C CD2 
1604 C CE1 . TYR   B 66  ? 0.3331 0.3064 0.2282 0.0388  0.0095  -0.0147 72  TYR   C CE1 
1605 C CE2 . TYR   B 66  ? 0.3260 0.3030 0.2274 0.0303  0.0076  -0.0056 72  TYR   C CE2 
1606 C CZ  . TYR   B 66  ? 0.3590 0.3318 0.2481 0.0372  0.0096  -0.0101 72  TYR   C CZ  
1607 O OH  . TYR   B 66  ? 0.4115 0.3787 0.2806 0.0434  0.0114  -0.0103 72  TYR   C OH  
1608 N N   . PRO   B 67  ? 0.2181 0.2017 0.1699 0.0241  -0.0038 -0.0131 73  PRO   C N   
1609 C CA  . PRO   B 67  ? 0.2200 0.2085 0.1813 0.0242  -0.0036 -0.0123 73  PRO   C CA  
1610 C C   . PRO   B 67  ? 0.2351 0.2343 0.2044 0.0254  0.0024  -0.0127 73  PRO   C C   
1611 O O   . PRO   B 67  ? 0.2559 0.2572 0.2235 0.0285  0.0072  -0.0147 73  PRO   C O   
1612 C CB  . PRO   B 67  ? 0.2353 0.2169 0.1939 0.0284  -0.0067 -0.0157 73  PRO   C CB  
1613 C CG  . PRO   B 67  ? 0.2393 0.2168 0.1889 0.0321  -0.0053 -0.0198 73  PRO   C CG  
1614 C CD  . PRO   B 67  ? 0.2201 0.1968 0.1633 0.0293  -0.0049 -0.0180 73  PRO   C CD  
1615 N N   . VAL   B 68  ? 0.2083 0.2141 0.1868 0.0234  0.0024  -0.0110 74  VAL   C N   
1616 C CA  . VAL   B 68  ? 0.2139 0.2297 0.2038 0.0241  0.0067  -0.0120 74  VAL   C CA  
1617 C C   . VAL   B 68  ? 0.2000 0.2202 0.1982 0.0255  0.0033  -0.0135 74  VAL   C C   
1618 O O   . VAL   B 68  ? 0.2157 0.2325 0.2100 0.0249  -0.0008 -0.0120 74  VAL   C O   
1619 C CB  . VAL   B 68  ? 0.2449 0.2646 0.2382 0.0200  0.0098  -0.0088 74  VAL   C CB  
1620 C CG1 . VAL   B 68  ? 0.2846 0.3012 0.2694 0.0202  0.0142  -0.0071 74  VAL   C CG1 
1621 C CG2 . VAL   B 68  ? 0.2409 0.2586 0.2326 0.0164  0.0058  -0.0061 74  VAL   C CG2 
1622 N N   . SER   B 69  ? 0.1815 0.2097 0.1921 0.0277  0.0053  -0.0165 75  SER   C N   
1623 C CA  . SER   B 69  ? 0.1819 0.2157 0.2022 0.0291  0.0013  -0.0189 75  SER   C CA  
1624 C C   . SER   B 69  ? 0.1711 0.2106 0.2008 0.0250  0.0035  -0.0175 75  SER   C C   
1625 O O   . SER   B 69  ? 0.1955 0.2370 0.2290 0.0223  0.0094  -0.0153 75  SER   C O   
1626 C CB  . SER   B 69  ? 0.2180 0.2579 0.2506 0.0335  0.0012  -0.0235 75  SER   C CB  
1627 O OG  . SER   B 69  ? 0.3034 0.3378 0.3284 0.0378  -0.0009 -0.0250 75  SER   C OG  
1628 N N   . PHE   B 70  ? 0.1677 0.2091 0.2002 0.0249  -0.0010 -0.0187 76  PHE   C N   
1629 C CA  . PHE   B 70  ? 0.1612 0.2069 0.2032 0.0214  0.0000  -0.0181 76  PHE   C CA  
1630 C C   . PHE   B 70  ? 0.1670 0.2178 0.2198 0.0241  -0.0059 -0.0235 76  PHE   C C   
1631 O O   . PHE   B 70  ? 0.1813 0.2311 0.2291 0.0290  -0.0113 -0.0265 76  PHE   C O   
1632 C CB  . PHE   B 70  ? 0.1596 0.2003 0.1909 0.0178  0.0006  -0.0136 76  PHE   C CB  
1633 C CG  . PHE   B 70  ? 0.1588 0.1948 0.1780 0.0197  -0.0033 -0.0127 76  PHE   C CG  
1634 C CD1 . PHE   B 70  ? 0.1667 0.1961 0.1745 0.0197  -0.0029 -0.0099 76  PHE   C CD1 
1635 C CD2 . PHE   B 70  ? 0.1684 0.2063 0.1879 0.0213  -0.0067 -0.0141 76  PHE   C CD2 
1636 C CE1 . PHE   B 70  ? 0.1717 0.1966 0.1705 0.0209  -0.0053 -0.0075 76  PHE   C CE1 
1637 C CE2 . PHE   B 70  ? 0.1751 0.2090 0.1830 0.0235  -0.0083 -0.0119 76  PHE   C CE2 
1638 C CZ  . PHE   B 70  ? 0.1779 0.2055 0.1765 0.0228  -0.0072 -0.0079 76  PHE   C CZ  
1639 N N   . SER   B 71  ? 0.1484 0.2042 0.2162 0.0217  -0.0055 -0.0248 77  SER   C N   
1640 C CA  . SER   B 71  ? 0.1677 0.2282 0.2480 0.0246  -0.0124 -0.0314 77  SER   C CA  
1641 C C   . SER   B 71  ? 0.1752 0.2327 0.2446 0.0271  -0.0180 -0.0332 77  SER   C C   
1642 O O   . SER   B 71  ? 0.1904 0.2430 0.2448 0.0259  -0.0156 -0.0285 77  SER   C O   
1643 C CB  . SER   B 71  ? 0.1599 0.2262 0.2632 0.0209  -0.0102 -0.0323 77  SER   C CB  
1644 O OG  . SER   B 71  ? 0.1860 0.2500 0.2882 0.0164  -0.0069 -0.0280 77  SER   C OG  
1645 N N   . LYS   B 72  ? 0.1784 0.2390 0.2559 0.0313  -0.0255 -0.0403 78  LYS   C N   
1646 C CA  . LYS   B 72  ? 0.1953 0.2536 0.2624 0.0349  -0.0304 -0.0428 78  LYS   C CA  
1647 C C   . LYS   B 72  ? 0.1857 0.2446 0.2611 0.0303  -0.0283 -0.0418 78  LYS   C C   
1648 O O   . LYS   B 72  ? 0.2128 0.2750 0.3073 0.0259  -0.0265 -0.0421 78  LYS   C O   
1649 C CB  . LYS   B 72  ? 0.2271 0.2881 0.3000 0.0421  -0.0406 -0.0523 78  LYS   C CB  
1650 C CG  . LYS   B 72  ? 0.2716 0.3311 0.3345 0.0475  -0.0432 -0.0526 78  LYS   C CG  
1651 C CD  . LYS   B 72  ? 0.4072 0.4672 0.4676 0.0566  -0.0544 -0.0612 78  LYS   C CD  
1652 C CE  . LYS   B 72  ? 0.5186 0.5733 0.5572 0.0632  -0.0560 -0.0586 78  LYS   C CE  
1653 N NZ  . LYS   B 72  ? 0.5834 0.6322 0.5985 0.0649  -0.0520 -0.0526 78  LYS   C NZ  
1654 N N   . PRO   B 73  ? 0.1834 0.2394 0.2466 0.0316  -0.0284 -0.0406 79  PRO   C N   
1655 C CA  . PRO   B 73  ? 0.1841 0.2403 0.2555 0.0276  -0.0268 -0.0398 79  PRO   C CA  
1656 C C   . PRO   B 73  ? 0.2001 0.2596 0.2921 0.0285  -0.0331 -0.0477 79  PRO   C C   
1657 O O   . PRO   B 73  ? 0.2158 0.2764 0.3083 0.0350  -0.0415 -0.0561 79  PRO   C O   
1658 C CB  . PRO   B 73  ? 0.2114 0.2650 0.2661 0.0314  -0.0271 -0.0391 79  PRO   C CB  
1659 C CG  . PRO   B 73  ? 0.2310 0.2821 0.2678 0.0345  -0.0253 -0.0354 79  PRO   C CG  
1660 C CD  . PRO   B 73  ? 0.1861 0.2385 0.2277 0.0366  -0.0287 -0.0388 79  PRO   C CD  
1661 N N   . SER   B 74  ? 0.1947 0.2551 0.3040 0.0223  -0.0297 -0.0450 80  SER   C N   
1662 C CA  . SER   B 74  ? 0.2123 0.2755 0.3458 0.0220  -0.0355 -0.0518 80  SER   C CA  
1663 C C   . SER   B 74  ? 0.2047 0.2666 0.3527 0.0158  -0.0315 -0.0475 80  SER   C C   
1664 O O   . SER   B 74  ? 0.1960 0.2549 0.3334 0.0124  -0.0248 -0.0395 80  SER   C O   
1665 C CB  . SER   B 74  ? 0.2650 0.3330 0.4142 0.0216  -0.0366 -0.0541 80  SER   C CB  
1666 O OG  . SER   B 74  ? 0.3295 0.3986 0.4847 0.0154  -0.0266 -0.0453 80  SER   C OG  
1667 N N   . LEU   B 75  ? 0.1974 0.2608 0.3702 0.0149  -0.0371 -0.0534 81  LEU   C N   
1668 C CA  . LEU   B 75  ? 0.2072 0.2685 0.3969 0.0094  -0.0342 -0.0494 81  LEU   C CA  
1669 C C   . LEU   B 75  ? 0.2216 0.2858 0.4282 0.0032  -0.0259 -0.0417 81  LEU   C C   
1670 O O   . LEU   B 75  ? 0.2365 0.3056 0.4636 0.0030  -0.0284 -0.0459 81  LEU   C O   
1671 C CB  . LEU   B 75  ? 0.2298 0.2910 0.4409 0.0117  -0.0448 -0.0601 81  LEU   C CB  
1672 C CG  . LEU   B 75  ? 0.3025 0.3595 0.5057 0.0162  -0.0512 -0.0663 81  LEU   C CG  
1673 C CD1 . LEU   B 75  ? 0.3328 0.3899 0.5578 0.0197  -0.0636 -0.0791 81  LEU   C CD1 
1674 C CD2 . LEU   B 75  ? 0.3138 0.3663 0.5161 0.0115  -0.0449 -0.0580 81  LEU   C CD2 
1675 N N   . ILE   B 76  ? 0.2055 0.2667 0.4047 -0.0014 -0.0162 -0.0307 82  ILE   C N   
1676 C CA  . ILE   B 76  ? 0.2117 0.2748 0.4200 -0.0061 -0.0061 -0.0216 82  ILE   C CA  
1677 C C   . ILE   B 76  ? 0.2188 0.2776 0.4369 -0.0110 -0.0005 -0.0131 82  ILE   C C   
1678 O O   . ILE   B 76  ? 0.2023 0.2557 0.4065 -0.0109 -0.0011 -0.0105 82  ILE   C O   
1679 C CB  . ILE   B 76  ? 0.2501 0.3125 0.4324 -0.0049 0.0003  -0.0162 82  ILE   C CB  
1680 C CG1 . ILE   B 76  ? 0.2893 0.3555 0.4647 0.0001  -0.0051 -0.0239 82  ILE   C CG1 
1681 C CG2 . ILE   B 76  ? 0.2644 0.3272 0.4488 -0.0084 0.0118  -0.0059 82  ILE   C CG2 
1682 C CD1 . ILE   B 76  ? 0.3355 0.4002 0.4874 0.0018  -0.0012 -0.0204 82  ILE   C CD1 
1683 N N   . PHE   B 77  ? 0.2144 0.2756 0.4571 -0.0151 0.0051  -0.0083 83  PHE   C N   
1684 C CA  . PHE   B 77  ? 0.2356 0.2918 0.4882 -0.0196 0.0111  0.0012  83  PHE   C CA  
1685 C C   . PHE   B 77  ? 0.2660 0.3181 0.4933 -0.0201 0.0206  0.0124  83  PHE   C C   
1686 O O   . PHE   B 77  ? 0.2836 0.3385 0.5001 -0.0192 0.0277  0.0163  83  PHE   C O   
1687 C CB  . PHE   B 77  ? 0.2267 0.2870 0.5139 -0.0240 0.0162  0.0050  83  PHE   C CB  
1688 C CG  . PHE   B 77  ? 0.2411 0.2954 0.5401 -0.0285 0.0226  0.0158  83  PHE   C CG  
1689 C CD1 . PHE   B 77  ? 0.2665 0.3149 0.5768 -0.0294 0.0147  0.0123  83  PHE   C CD1 
1690 C CD2 . PHE   B 77  ? 0.2634 0.3168 0.5582 -0.0307 0.0365  0.0297  83  PHE   C CD2 
1691 C CE1 . PHE   B 77  ? 0.2911 0.3328 0.6121 -0.0333 0.0203  0.0230  83  PHE   C CE1 
1692 C CE2 . PHE   B 77  ? 0.2865 0.3333 0.5905 -0.0343 0.0427  0.0410  83  PHE   C CE2 
1693 C CZ  . PHE   B 77  ? 0.2947 0.3356 0.6124 -0.0358 0.0344  0.0378  83  PHE   C CZ  
1694 N N   . VAL   B 78  ? 0.2851 0.3301 0.5035 -0.0209 0.0202  0.0171  84  VAL   C N   
1695 C CA  . VAL   B 78  ? 0.3057 0.3455 0.5004 -0.0207 0.0272  0.0272  84  VAL   C CA  
1696 C C   . VAL   B 78  ? 0.3148 0.3486 0.5216 -0.0240 0.0319  0.0372  84  VAL   C C   
1697 O O   . VAL   B 78  ? 0.3219 0.3523 0.5424 -0.0251 0.0258  0.0346  84  VAL   C O   
1698 C CB  . VAL   B 78  ? 0.3056 0.3423 0.4752 -0.0176 0.0208  0.0232  84  VAL   C CB  
1699 C CG1 . VAL   B 78  ? 0.3261 0.3568 0.4736 -0.0173 0.0260  0.0328  84  VAL   C CG1 
1700 C CG2 . VAL   B 78  ? 0.2957 0.3373 0.4536 -0.0144 0.0170  0.0149  84  VAL   C CG2 
1701 N N   . GLU   B 79  ? 0.3254 0.3576 0.5269 -0.0249 0.0430  0.0487  85  GLU   C N   
1702 C CA  . GLU   B 79  ? 0.3450 0.3710 0.5560 -0.0275 0.0496  0.0607  85  GLU   C CA  
1703 C C   . GLU   B 79  ? 0.3497 0.3669 0.5445 -0.0262 0.0447  0.0636  85  GLU   C C   
1704 O O   . GLU   B 79  ? 0.3516 0.3681 0.5232 -0.0231 0.0390  0.0587  85  GLU   C O   
1705 C CB  . GLU   B 79  ? 0.4070 0.4332 0.6094 -0.0269 0.0638  0.0728  85  GLU   C CB  
1706 C CG  . GLU   B 79  ? 0.5013 0.5371 0.7109 -0.0264 0.0690  0.0693  85  GLU   C CG  
1707 C CD  . GLU   B 79  ? 0.6193 0.6570 0.7996 -0.0218 0.0679  0.0643  85  GLU   C CD  
1708 O OE1 . GLU   B 79  ? 0.6349 0.6735 0.8065 -0.0204 0.0573  0.0537  85  GLU   C OE1 
1709 O OE2 . GLU   B 79  ? 0.6544 0.6923 0.8202 -0.0193 0.0781  0.0713  85  GLU   C OE2 
1710 N N   . ALA   B 80  ? 0.3479 0.3584 0.5564 -0.0285 0.0466  0.0717  86  ALA   C N   
1711 C CA  . ALA   B 80  ? 0.3545 0.3565 0.5504 -0.0269 0.0416  0.0749  86  ALA   C CA  
1712 C C   . ALA   B 80  ? 0.3753 0.3734 0.5372 -0.0232 0.0450  0.0815  86  ALA   C C   
1713 O O   . ALA   B 80  ? 0.3897 0.3888 0.5398 -0.0220 0.0543  0.0883  86  ALA   C O   
1714 C CB  . ALA   B 80  ? 0.3562 0.3507 0.5729 -0.0298 0.0447  0.0847  86  ALA   C CB  
1715 N N   . SER   B 81  ? 0.3583 0.3524 0.5052 -0.0208 0.0368  0.0786  87  SER   C N   
1716 C CA  . SER   B 81  ? 0.3532 0.3426 0.4702 -0.0170 0.0371  0.0837  87  SER   C CA  
1717 C C   . SER   B 81  ? 0.3655 0.3470 0.4814 -0.0159 0.0305  0.0869  87  SER   C C   
1718 O O   . SER   B 81  ? 0.3648 0.3448 0.5029 -0.0180 0.0269  0.0851  87  SER   C O   
1719 C CB  . SER   B 81  ? 0.3533 0.3483 0.4537 -0.0150 0.0320  0.0738  87  SER   C CB  
1720 O OG  . SER   B 81  ? 0.3380 0.3353 0.4446 -0.0150 0.0223  0.0645  87  SER   C OG  
1721 N N   . GLU   B 82  ? 0.3632 0.3393 0.4549 -0.0121 0.0282  0.0913  88  GLU   C N   
1722 C CA  . GLU   B 82  ? 0.3648 0.3344 0.4557 -0.0104 0.0205  0.0931  88  GLU   C CA  
1723 C C   . GLU   B 82  ? 0.3538 0.3293 0.4555 -0.0110 0.0109  0.0803  88  GLU   C C   
1724 O O   . GLU   B 82  ? 0.3518 0.3240 0.4625 -0.0102 0.0048  0.0794  88  GLU   C O   
1725 C CB  . GLU   B 82  ? 0.4362 0.4008 0.4983 -0.0057 0.0174  0.0971  88  GLU   C CB  
1726 C CG  . GLU   B 82  ? 0.5473 0.5034 0.5921 -0.0026 0.0250  0.1106  88  GLU   C CG  
1727 C CD  . GLU   B 82  ? 0.6953 0.6465 0.7110 0.0030  0.0190  0.1115  88  GLU   C CD  
1728 O OE1 . GLU   B 82  ? 0.7264 0.6830 0.7324 0.0037  0.0145  0.1025  88  GLU   C OE1 
1729 O OE2 . GLU   B 82  ? 0.7462 0.6878 0.7498 0.0070  0.0178  0.1209  88  GLU   C OE2 
1730 N N   . TYR   B 83  ? 0.3420 0.3260 0.4414 -0.0115 0.0100  0.0709  89  TYR   C N   
1731 C CA  . TYR   B 83  ? 0.3520 0.3419 0.4570 -0.0110 0.0026  0.0598  89  TYR   C CA  
1732 C C   . TYR   B 83  ? 0.3390 0.3330 0.4670 -0.0127 0.0013  0.0522  89  TYR   C C   
1733 O O   . TYR   B 83  ? 0.3445 0.3409 0.4795 -0.0111 -0.0049 0.0446  89  TYR   C O   
1734 C CB  . TYR   B 83  ? 0.3621 0.3579 0.4515 -0.0101 0.0022  0.0544  89  TYR   C CB  
1735 C CG  . TYR   B 83  ? 0.3939 0.3857 0.4607 -0.0080 0.0020  0.0597  89  TYR   C CG  
1736 C CD1 . TYR   B 83  ? 0.4138 0.4031 0.4733 -0.0058 -0.0050 0.0599  89  TYR   C CD1 
1737 C CD2 . TYR   B 83  ? 0.4137 0.4042 0.4670 -0.0075 0.0081  0.0638  89  TYR   C CD2 
1738 C CE1 . TYR   B 83  ? 0.4395 0.4248 0.4788 -0.0034 -0.0072 0.0632  89  TYR   C CE1 
1739 C CE2 . TYR   B 83  ? 0.4416 0.4278 0.4727 -0.0046 0.0066  0.0669  89  TYR   C CE2 
1740 C CZ  . TYR   B 83  ? 0.4661 0.4493 0.4902 -0.0025 -0.0017 0.0664  89  TYR   C CZ  
1741 O OH  . TYR   B 83  ? 0.5216 0.5000 0.5244 0.0009  -0.0050 0.0683  89  TYR   C OH  
1742 N N   . TYR   B 84  ? 0.3113 0.3068 0.4510 -0.0153 0.0067  0.0532  90  TYR   C N   
1743 C CA  . TYR   B 84  ? 0.3050 0.3043 0.4669 -0.0164 0.0038  0.0445  90  TYR   C CA  
1744 C C   . TYR   B 84  ? 0.3223 0.3188 0.5055 -0.0199 0.0087  0.0500  90  TYR   C C   
1745 O O   . TYR   B 84  ? 0.3269 0.3223 0.5062 -0.0216 0.0171  0.0591  90  TYR   C O   
1746 C CB  . TYR   B 84  ? 0.2838 0.2917 0.4412 -0.0158 0.0037  0.0358  90  TYR   C CB  
1747 C CG  . TYR   B 84  ? 0.2720 0.2837 0.4128 -0.0128 -0.0007 0.0294  90  TYR   C CG  
1748 C CD1 . TYR   B 84  ? 0.2781 0.2914 0.3990 -0.0122 0.0019  0.0318  90  TYR   C CD1 
1749 C CD2 . TYR   B 84  ? 0.2639 0.2776 0.4099 -0.0101 -0.0072 0.0210  90  TYR   C CD2 
1750 C CE1 . TYR   B 84  ? 0.2727 0.2895 0.3815 -0.0100 -0.0016 0.0269  90  TYR   C CE1 
1751 C CE2 . TYR   B 84  ? 0.2559 0.2739 0.3885 -0.0073 -0.0096 0.0165  90  TYR   C CE2 
1752 C CZ  . TYR   B 84  ? 0.2664 0.2860 0.3816 -0.0077 -0.0067 0.0197  90  TYR   C CZ  
1753 O OH  . TYR   B 84  ? 0.2493 0.2724 0.3543 -0.0056 -0.0088 0.0165  90  TYR   C OH  
1754 N N   . PRO   B 85  ? 0.3129 0.3091 0.5202 -0.0208 0.0036  0.0433  91  PRO   C N   
1755 C CA  . PRO   B 85  ? 0.3082 0.3033 0.5408 -0.0248 0.0076  0.0469  91  PRO   C CA  
1756 C C   . PRO   B 85  ? 0.3127 0.3164 0.5473 -0.0259 0.0113  0.0428  91  PRO   C C   
1757 O O   . PRO   B 85  ? 0.3174 0.3271 0.5370 -0.0232 0.0083  0.0348  91  PRO   C O   
1758 C CB  . PRO   B 85  ? 0.3045 0.2978 0.5608 -0.0243 -0.0019 0.0367  91  PRO   C CB  
1759 C CG  . PRO   B 85  ? 0.3123 0.3104 0.5532 -0.0194 -0.0094 0.0245  91  PRO   C CG  
1760 C CD  . PRO   B 85  ? 0.3011 0.2985 0.5142 -0.0177 -0.0061 0.0313  91  PRO   C CD  
1761 N N   . ALA   B 86  ? 0.3055 0.3103 0.5619 -0.0297 0.0173  0.0476  92  ALA   C N   
1762 C CA  . ALA   B 86  ? 0.3019 0.3155 0.5670 -0.0306 0.0197  0.0426  92  ALA   C CA  
1763 C C   . ALA   B 86  ? 0.2919 0.3098 0.5662 -0.0282 0.0075  0.0259  92  ALA   C C   
1764 O O   . ALA   B 86  ? 0.2879 0.3017 0.5782 -0.0280 -0.0003 0.0204  92  ALA   C O   
1765 C CB  . ALA   B 86  ? 0.2986 0.3123 0.5937 -0.0355 0.0272  0.0505  92  ALA   C CB  
1766 N N   . ARG   B 87  ? 0.2872 0.3121 0.5470 -0.0252 0.0053  0.0181  93  ARG   C N   
1767 C CA  . ARG   B 87  ? 0.2790 0.3071 0.5412 -0.0213 -0.0060 0.0031  93  ARG   C CA  
1768 C C   . ARG   B 87  ? 0.2829 0.3187 0.5338 -0.0187 -0.0065 -0.0031 93  ARG   C C   
1769 O O   . ARG   B 87  ? 0.2891 0.3274 0.5279 -0.0197 0.0017  0.0038  93  ARG   C O   
1770 C CB  . ARG   B 87  ? 0.2819 0.3060 0.5245 -0.0174 -0.0112 -0.0001 93  ARG   C CB  
1771 C CG  . ARG   B 87  ? 0.2594 0.2858 0.4706 -0.0152 -0.0071 0.0034  93  ARG   C CG  
1772 C CD  . ARG   B 87  ? 0.2536 0.2756 0.4486 -0.0136 -0.0080 0.0067  93  ARG   C CD  
1773 N NE  . ARG   B 87  ? 0.2566 0.2820 0.4283 -0.0101 -0.0091 0.0034  93  ARG   C NE  
1774 C CZ  . ARG   B 87  ? 0.2984 0.3255 0.4524 -0.0106 -0.0041 0.0081  93  ARG   C CZ  
1775 N NH1 . ARG   B 87  ? 0.2726 0.3022 0.4090 -0.0078 -0.0057 0.0053  93  ARG   C NH1 
1776 N NH2 . ARG   B 87  ? 0.3003 0.3267 0.4550 -0.0136 0.0027  0.0158  93  ARG   C NH2 
1777 N N   . TYR   B 88  ? 0.2768 0.3154 0.5292 -0.0143 -0.0164 -0.0162 94  TYR   C N   
1778 C CA  . TYR   B 88  ? 0.2774 0.3220 0.5161 -0.0107 -0.0180 -0.0220 94  TYR   C CA  
1779 C C   . TYR   B 88  ? 0.2488 0.2920 0.4573 -0.0067 -0.0187 -0.0226 94  TYR   C C   
1780 O O   . TYR   B 88  ? 0.2607 0.3011 0.4653 -0.0035 -0.0243 -0.0276 94  TYR   C O   
1781 C CB  . TYR   B 88  ? 0.2962 0.3441 0.5509 -0.0071 -0.0288 -0.0356 94  TYR   C CB  
1782 C CG  . TYR   B 88  ? 0.3274 0.3788 0.6133 -0.0113 -0.0277 -0.0351 94  TYR   C CG  
1783 C CD1 . TYR   B 88  ? 0.3529 0.4107 0.6401 -0.0123 -0.0224 -0.0324 94  TYR   C CD1 
1784 C CD2 . TYR   B 88  ? 0.3486 0.3971 0.6649 -0.0146 -0.0314 -0.0365 94  TYR   C CD2 
1785 C CE1 . TYR   B 88  ? 0.3619 0.4243 0.6807 -0.0163 -0.0202 -0.0313 94  TYR   C CE1 
1786 C CE2 . TYR   B 88  ? 0.3592 0.4117 0.7084 -0.0191 -0.0298 -0.0353 94  TYR   C CE2 
1787 C CZ  . TYR   B 88  ? 0.3722 0.4321 0.7225 -0.0200 -0.0235 -0.0321 94  TYR   C CZ  
1788 O OH  . TYR   B 88  ? 0.3972 0.4624 0.7820 -0.0244 -0.0207 -0.0303 94  TYR   C OH  
1789 N N   . GLN   B 89  ? 0.2048 0.2496 0.3933 -0.0068 -0.0124 -0.0169 95  GLN   C N   
1790 C CA  . GLN   B 89  ? 0.1859 0.2300 0.3487 -0.0035 -0.0129 -0.0173 95  GLN   C CA  
1791 C C   . GLN   B 89  ? 0.1723 0.2206 0.3284 0.0016  -0.0183 -0.0263 95  GLN   C C   
1792 O O   . GLN   B 89  ? 0.1916 0.2435 0.3525 0.0016  -0.0177 -0.0278 95  GLN   C O   
1793 C CB  . GLN   B 89  ? 0.1853 0.2278 0.3312 -0.0059 -0.0050 -0.0073 95  GLN   C CB  
1794 C CG  . GLN   B 89  ? 0.1984 0.2406 0.3215 -0.0030 -0.0060 -0.0077 95  GLN   C CG  
1795 C CD  . GLN   B 89  ? 0.2119 0.2505 0.3209 -0.0054 -0.0009 0.0012  95  GLN   C CD  
1796 O OE1 . GLN   B 89  ? 0.2306 0.2655 0.3437 -0.0081 0.0021  0.0078  95  GLN   C OE1 
1797 N NE2 . GLN   B 89  ? 0.2043 0.2433 0.2963 -0.0039 -0.0003 0.0016  95  GLN   C NE2 
1798 N N   . SER   B 90  ? 0.1643 0.2122 0.3088 0.0067  -0.0231 -0.0320 96  SER   C N   
1799 C CA  . SER   B 90  ? 0.1673 0.2181 0.3022 0.0128  -0.0282 -0.0399 96  SER   C CA  
1800 C C   . SER   B 90  ? 0.1720 0.2230 0.2832 0.0140  -0.0235 -0.0349 96  SER   C C   
1801 O O   . SER   B 90  ? 0.1777 0.2266 0.2803 0.0107  -0.0180 -0.0271 96  SER   C O   
1802 C CB  . SER   B 90  ? 0.1940 0.2439 0.3284 0.0191  -0.0357 -0.0493 96  SER   C CB  
1803 O OG  . SER   B 90  ? 0.2225 0.2706 0.3453 0.0198  -0.0327 -0.0457 96  SER   C OG  
1804 N N   . HIS   B 91  ? 0.1674 0.2204 0.2692 0.0191  -0.0266 -0.0397 97  HIS   C N   
1805 C CA  . HIS   B 91  ? 0.1715 0.2241 0.2528 0.0209  -0.0232 -0.0357 97  HIS   C CA  
1806 C C   . HIS   B 91  ? 0.1842 0.2356 0.2631 0.0151  -0.0166 -0.0272 97  HIS   C C   
1807 O O   . HIS   B 91  ? 0.1987 0.2481 0.2637 0.0143  -0.0129 -0.0218 97  HIS   C O   
1808 C CB  . HIS   B 91  ? 0.1704 0.2219 0.2383 0.0239  -0.0220 -0.0343 97  HIS   C CB  
1809 C CG  . HIS   B 91  ? 0.1935 0.2458 0.2599 0.0312  -0.0278 -0.0430 97  HIS   C CG  
1810 N ND1 . HIS   B 91  ? 0.2388 0.2916 0.2899 0.0387  -0.0300 -0.0465 97  HIS   C ND1 
1811 C CD2 . HIS   B 91  ? 0.2194 0.2714 0.2974 0.0328  -0.0324 -0.0491 97  HIS   C CD2 
1812 C CE1 . HIS   B 91  ? 0.2434 0.2964 0.2949 0.0453  -0.0357 -0.0550 97  HIS   C CE1 
1813 N NE2 . HIS   B 91  ? 0.2478 0.3003 0.3162 0.0419  -0.0377 -0.0574 97  HIS   C NE2 
1814 N N   . LEU   B 92  ? 0.1758 0.2285 0.2688 0.0116  -0.0150 -0.0263 98  LEU   C N   
1815 C CA  . LEU   B 92  ? 0.1619 0.2133 0.2516 0.0073  -0.0083 -0.0188 98  LEU   C CA  
1816 C C   . LEU   B 92  ? 0.1660 0.2194 0.2539 0.0092  -0.0079 -0.0205 98  LEU   C C   
1817 O O   . LEU   B 92  ? 0.1663 0.2234 0.2659 0.0116  -0.0121 -0.0266 98  LEU   C O   
1818 C CB  . LEU   B 92  ? 0.1789 0.2301 0.2846 0.0026  -0.0046 -0.0149 98  LEU   C CB  
1819 C CG  . LEU   B 92  ? 0.2114 0.2606 0.3120 -0.0008 0.0030  -0.0067 98  LEU   C CG  
1820 C CD1 . LEU   B 92  ? 0.2143 0.2587 0.2969 -0.0016 0.0045  -0.0015 98  LEU   C CD1 
1821 C CD2 . LEU   B 92  ? 0.2228 0.2719 0.3408 -0.0047 0.0073  -0.0020 98  LEU   C CD2 
1822 N N   . MET   B 93  ? 0.1570 0.2078 0.2310 0.0084  -0.0038 -0.0156 99  MET   C N   
1823 C CA  . MET   B 93  ? 0.1579 0.2100 0.2294 0.0107  -0.0033 -0.0171 99  MET   C CA  
1824 C C   . MET   B 93  ? 0.1697 0.2211 0.2418 0.0077  0.0037  -0.0118 99  MET   C C   
1825 O O   . MET   B 93  ? 0.1783 0.2253 0.2405 0.0052  0.0069  -0.0064 99  MET   C O   
1826 C CB  . MET   B 93  ? 0.1594 0.2077 0.2123 0.0136  -0.0049 -0.0164 99  MET   C CB  
1827 C CG  . MET   B 93  ? 0.2082 0.2571 0.2575 0.0177  -0.0103 -0.0206 99  MET   C CG  
1828 S SD  . MET   B 93  ? 0.2279 0.2722 0.2572 0.0206  -0.0102 -0.0173 99  MET   C SD  
1829 C CE  . MET   B 93  ? 0.2165 0.2575 0.2415 0.0145  -0.0054 -0.0099 99  MET   C CE  
1830 N N   . LEU   B 94  ? 0.1501 0.2055 0.2329 0.0085  0.0060  -0.0134 100 LEU   C N   
1831 C CA  . LEU   B 94  ? 0.1611 0.2161 0.2428 0.0069  0.0139  -0.0082 100 LEU   C CA  
1832 C C   . LEU   B 94  ? 0.1626 0.2162 0.2334 0.0102  0.0149  -0.0092 100 LEU   C C   
1833 O O   . LEU   B 94  ? 0.1608 0.2162 0.2330 0.0136  0.0102  -0.0142 100 LEU   C O   
1834 C CB  . LEU   B 94  ? 0.1638 0.2253 0.2689 0.0053  0.0185  -0.0077 100 LEU   C CB  
1835 C CG  . LEU   B 94  ? 0.1817 0.2440 0.3020 0.0017  0.0181  -0.0062 100 LEU   C CG  
1836 C CD1 . LEU   B 94  ? 0.1929 0.2614 0.3386 -0.0004 0.0238  -0.0043 100 LEU   C CD1 
1837 C CD2 . LEU   B 94  ? 0.2059 0.2618 0.3129 -0.0009 0.0211  0.0007  100 LEU   C CD2 
1838 N N   . ALA   B 95  ? 0.1728 0.2227 0.2324 0.0098  0.0207  -0.0047 101 ALA   C N   
1839 C CA  . ALA   B 95  ? 0.1781 0.2261 0.2282 0.0133  0.0224  -0.0060 101 ALA   C CA  
1840 C C   . ALA   B 95  ? 0.1818 0.2306 0.2312 0.0137  0.0318  -0.0017 101 ALA   C C   
1841 O O   . ALA   B 95  ? 0.1926 0.2405 0.2423 0.0110  0.0361  0.0036  101 ALA   C O   
1842 C CB  . ALA   B 95  ? 0.1929 0.2324 0.2228 0.0139  0.0182  -0.0055 101 ALA   C CB  
1843 N N   . VAL   B 96  ? 0.1817 0.2315 0.2286 0.0177  0.0352  -0.0037 102 VAL   C N   
1844 C CA  . VAL   B 96  ? 0.1966 0.2462 0.2381 0.0197  0.0445  0.0002  102 VAL   C CA  
1845 C C   . VAL   B 96  ? 0.2404 0.2795 0.2562 0.0212  0.0423  0.0011  102 VAL   C C   
1846 O O   . VAL   B 96  ? 0.2667 0.3008 0.2725 0.0235  0.0367  -0.0030 102 VAL   C O   
1847 C CB  . VAL   B 96  ? 0.2142 0.2699 0.2648 0.0242  0.0487  -0.0034 102 VAL   C CB  
1848 C CG1 . VAL   B 96  ? 0.2218 0.2770 0.2634 0.0278  0.0596  0.0005  102 VAL   C CG1 
1849 C CG2 . VAL   B 96  ? 0.2077 0.2740 0.2869 0.0224  0.0491  -0.0050 102 VAL   C CG2 
1850 N N   . GLY   B 97  ? 0.2681 0.3036 0.2748 0.0200  0.0460  0.0065  103 GLY   C N   
1851 C CA  . GLY   B 97  ? 0.2977 0.3232 0.2814 0.0216  0.0423  0.0068  103 GLY   C CA  
1852 C C   . GLY   B 97  ? 0.3196 0.3419 0.2951 0.0205  0.0458  0.0132  103 GLY   C C   
1853 O O   . GLY   B 97  ? 0.3174 0.3444 0.3058 0.0175  0.0506  0.0182  103 GLY   C O   
1854 N N   . HIS   B 98  ? 0.3215 0.3347 0.2756 0.0232  0.0424  0.0130  104 HIS   C N   
1855 C CA  . HIS   B 98  ? 0.3393 0.3478 0.2815 0.0237  0.0444  0.0188  104 HIS   C CA  
1856 C C   . HIS   B 98  ? 0.3410 0.3474 0.2871 0.0186  0.0369  0.0205  104 HIS   C C   
1857 O O   . HIS   B 98  ? 0.3313 0.3352 0.2774 0.0165  0.0281  0.0163  104 HIS   C O   
1858 C CB  . HIS   B 98  ? 0.3456 0.3447 0.2624 0.0299  0.0421  0.0164  104 HIS   C CB  
1859 C CG  . HIS   B 98  ? 0.3683 0.3619 0.2699 0.0320  0.0438  0.0224  104 HIS   C CG  
1860 N ND1 . HIS   B 98  ? 0.3835 0.3804 0.2851 0.0341  0.0558  0.0302  104 HIS   C ND1 
1861 C CD2 . HIS   B 98  ? 0.3842 0.3697 0.2729 0.0319  0.0348  0.0224  104 HIS   C CD2 
1862 C CE1 . HIS   B 98  ? 0.4061 0.3959 0.2922 0.0357  0.0537  0.0349  104 HIS   C CE1 
1863 N NE2 . HIS   B 98  ? 0.4157 0.3986 0.2935 0.0347  0.0405  0.0299  104 HIS   C NE2 
1864 N N   . SER   B 99  ? 0.3474 0.3547 0.2973 0.0167  0.0409  0.0273  105 SER   C N   
1865 C CA  . SER   B 99  ? 0.3618 0.3671 0.3155 0.0127  0.0348  0.0297  105 SER   C CA  
1866 C C   . SER   B 99  ? 0.3909 0.3924 0.3364 0.0143  0.0400  0.0380  105 SER   C C   
1867 O O   . SER   B 99  ? 0.4187 0.4229 0.3669 0.0160  0.0504  0.0431  105 SER   C O   
1868 C CB  . SER   B 99  ? 0.3864 0.3994 0.3637 0.0077  0.0343  0.0287  105 SER   C CB  
1869 O OG  . SER   B 99  ? 0.4857 0.4971 0.4661 0.0045  0.0268  0.0284  105 SER   C OG  
1870 N N   . GLU   B 100 ? 0.3698 0.3647 0.3046 0.0144  0.0328  0.0395  106 GLU   C N   
1871 C CA  . GLU   B 100 ? 0.3815 0.3711 0.3076 0.0159  0.0344  0.0474  106 GLU   C CA  
1872 C C   . GLU   B 100 ? 0.3830 0.3727 0.3207 0.0113  0.0264  0.0476  106 GLU   C C   
1873 O O   . GLU   B 100 ? 0.3652 0.3576 0.3112 0.0083  0.0195  0.0414  106 GLU   C O   
1874 C CB  . GLU   B 100 ? 0.4188 0.3992 0.3173 0.0225  0.0310  0.0472  106 GLU   C CB  
1875 C CG  . GLU   B 100 ? 0.5227 0.5030 0.4089 0.0282  0.0405  0.0477  106 GLU   C CG  
1876 C CD  . GLU   B 100 ? 0.6019 0.5722 0.4577 0.0365  0.0371  0.0466  106 GLU   C CD  
1877 O OE1 . GLU   B 100 ? 0.6603 0.6237 0.5032 0.0388  0.0326  0.0508  106 GLU   C OE1 
1878 O OE2 . GLU   B 100 ? 0.6006 0.5697 0.4453 0.0412  0.0382  0.0409  106 GLU   C OE2 
1879 N N   . PRO   B 101 ? 0.3958 0.3827 0.3351 0.0109  0.0277  0.0548  107 PRO   C N   
1880 C CA  . PRO   B 101 ? 0.3890 0.3769 0.3421 0.0068  0.0206  0.0543  107 PRO   C CA  
1881 C C   . PRO   B 101 ? 0.3591 0.3456 0.3086 0.0063  0.0090  0.0481  107 PRO   C C   
1882 O O   . PRO   B 101 ? 0.3649 0.3565 0.3301 0.0025  0.0050  0.0441  107 PRO   C O   
1883 C CB  . PRO   B 101 ? 0.4132 0.3955 0.3622 0.0083  0.0231  0.0637  107 PRO   C CB  
1884 C CG  . PRO   B 101 ? 0.4269 0.4093 0.3718 0.0107  0.0357  0.0702  107 PRO   C CG  
1885 C CD  . PRO   B 101 ? 0.4096 0.3927 0.3406 0.0141  0.0370  0.0645  107 PRO   C CD  
1886 N N   . GLY   B 102 ? 0.3324 0.3119 0.2617 0.0106  0.0039  0.0472  108 GLY   C N   
1887 C CA  . GLY   B 102 ? 0.3242 0.3015 0.2505 0.0104  -0.0073 0.0415  108 GLY   C CA  
1888 C C   . GLY   B 102 ? 0.2981 0.2802 0.2331 0.0076  -0.0091 0.0344  108 GLY   C C   
1889 O O   . GLY   B 102 ? 0.2971 0.2789 0.2358 0.0062  -0.0173 0.0304  108 GLY   C O   
1890 N N   . ASP   B 103 ? 0.2719 0.2586 0.2118 0.0070  -0.0012 0.0334  109 ASP   C N   
1891 C CA  . ASP   B 103 ? 0.2562 0.2467 0.2033 0.0050  -0.0026 0.0275  109 ASP   C CA  
1892 C C   . ASP   B 103 ? 0.2390 0.2366 0.2052 0.0006  -0.0034 0.0264  109 ASP   C C   
1893 O O   . ASP   B 103 ? 0.2328 0.2329 0.2041 -0.0008 -0.0054 0.0224  109 ASP   C O   
1894 C CB  . ASP   B 103 ? 0.2495 0.2421 0.1941 0.0069  0.0050  0.0261  109 ASP   C CB  
1895 C CG  . ASP   B 103 ? 0.2967 0.2823 0.2207 0.0124  0.0049  0.0248  109 ASP   C CG  
1896 O OD1 . ASP   B 103 ? 0.3085 0.2878 0.2226 0.0139  -0.0037 0.0218  109 ASP   C OD1 
1897 O OD2 . ASP   B 103 ? 0.3078 0.2943 0.2264 0.0156  0.0135  0.0266  109 ASP   C OD2 
1898 N N   . CYS   B 104 ? 0.2218 0.2221 0.1980 -0.0011 -0.0017 0.0299  110 CYS   C N   
1899 C CA  . CYS   B 104 ? 0.2166 0.2232 0.2092 -0.0039 -0.0028 0.0279  110 CYS   C CA  
1900 C C   . CYS   B 104 ? 0.2198 0.2266 0.2143 -0.0050 -0.0093 0.0255  110 CYS   C C   
1901 O O   . CYS   B 104 ? 0.2242 0.2264 0.2122 -0.0044 -0.0148 0.0266  110 CYS   C O   
1902 C CB  . CYS   B 104 ? 0.2313 0.2391 0.2339 -0.0049 -0.0013 0.0315  110 CYS   C CB  
1903 S SG  . CYS   B 104 ? 0.2726 0.2825 0.2827 -0.0051 0.0073  0.0340  110 CYS   C SG  
1904 N N   . GLY   B 105 ? 0.1943 0.2062 0.1969 -0.0062 -0.0088 0.0224  111 GLY   C N   
1905 C CA  . GLY   B 105 ? 0.1999 0.2130 0.2067 -0.0074 -0.0131 0.0213  111 GLY   C CA  
1906 C C   . GLY   B 105 ? 0.2086 0.2191 0.2097 -0.0073 -0.0143 0.0191  111 GLY   C C   
1907 O O   . GLY   B 105 ? 0.2203 0.2323 0.2273 -0.0086 -0.0161 0.0187  111 GLY   C O   
1908 N N   . GLY   B 106 ? 0.1968 0.2032 0.1873 -0.0055 -0.0126 0.0180  112 GLY   C N   
1909 C CA  . GLY   B 106 ? 0.1889 0.1922 0.1744 -0.0048 -0.0137 0.0154  112 GLY   C CA  
1910 C C   . GLY   B 106 ? 0.1801 0.1883 0.1729 -0.0052 -0.0107 0.0144  112 GLY   C C   
1911 O O   . GLY   B 106 ? 0.1835 0.1968 0.1806 -0.0045 -0.0066 0.0140  112 GLY   C O   
1912 N N   . ILE   B 107 ? 0.1819 0.1884 0.1766 -0.0061 -0.0130 0.0141  113 ILE   C N   
1913 C CA  . ILE   B 107 ? 0.1838 0.1942 0.1832 -0.0056 -0.0099 0.0143  113 ILE   C CA  
1914 C C   . ILE   B 107 ? 0.1832 0.1917 0.1767 -0.0030 -0.0082 0.0119  113 ILE   C C   
1915 O O   . ILE   B 107 ? 0.1951 0.1974 0.1820 -0.0023 -0.0104 0.0104  113 ILE   C O   
1916 C CB  . ILE   B 107 ? 0.2132 0.2231 0.2195 -0.0077 -0.0118 0.0170  113 ILE   C CB  
1917 C CG1 . ILE   B 107 ? 0.2451 0.2601 0.2608 -0.0095 -0.0121 0.0192  113 ILE   C CG1 
1918 C CG2 . ILE   B 107 ? 0.2386 0.2501 0.2458 -0.0062 -0.0083 0.0183  113 ILE   C CG2 
1919 C CD1 . ILE   B 107 ? 0.2828 0.2983 0.3089 -0.0120 -0.0132 0.0226  113 ILE   C CD1 
1920 N N   . LEU   B 108 ? 0.1588 0.1722 0.1548 -0.0010 -0.0050 0.0110  114 LEU   C N   
1921 C CA  . LEU   B 108 ? 0.1592 0.1717 0.1516 0.0020  -0.0041 0.0087  114 LEU   C CA  
1922 C C   . LEU   B 108 ? 0.1757 0.1877 0.1686 0.0030  -0.0041 0.0110  114 LEU   C C   
1923 O O   . LEU   B 108 ? 0.1772 0.1937 0.1737 0.0032  -0.0026 0.0127  114 LEU   C O   
1924 C CB  . LEU   B 108 ? 0.1626 0.1812 0.1589 0.0041  -0.0017 0.0060  114 LEU   C CB  
1925 C CG  . LEU   B 108 ? 0.1783 0.1978 0.1736 0.0080  -0.0016 0.0030  114 LEU   C CG  
1926 C CD1 . LEU   B 108 ? 0.1985 0.2136 0.1890 0.0091  -0.0014 0.0014  114 LEU   C CD1 
1927 C CD2 . LEU   B 108 ? 0.1823 0.2086 0.1855 0.0097  -0.0009 -0.0004 114 LEU   C CD2 
1928 N N   . ARG   B 109 ? 0.1733 0.1795 0.1623 0.0039  -0.0055 0.0113  115 ARG   C N   
1929 C CA  . ARG   B 109 ? 0.1790 0.1831 0.1678 0.0049  -0.0049 0.0149  115 ARG   C CA  
1930 C C   . ARG   B 109 ? 0.2004 0.2018 0.1838 0.0093  -0.0053 0.0130  115 ARG   C C   
1931 O O   . ARG   B 109 ? 0.2217 0.2199 0.2026 0.0103  -0.0070 0.0095  115 ARG   C O   
1932 C CB  . ARG   B 109 ? 0.2150 0.2121 0.2069 0.0014  -0.0073 0.0182  115 ARG   C CB  
1933 C CG  . ARG   B 109 ? 0.2968 0.2960 0.2956 -0.0027 -0.0083 0.0199  115 ARG   C CG  
1934 C CD  . ARG   B 109 ? 0.3648 0.3566 0.3688 -0.0060 -0.0125 0.0216  115 ARG   C CD  
1935 N NE  . ARG   B 109 ? 0.4944 0.4891 0.5088 -0.0085 -0.0099 0.0277  115 ARG   C NE  
1936 C CZ  . ARG   B 109 ? 0.5475 0.5470 0.5709 -0.0113 -0.0100 0.0292  115 ARG   C CZ  
1937 N NH1 . ARG   B 109 ? 0.5509 0.5514 0.5728 -0.0121 -0.0137 0.0253  115 ARG   C NH1 
1938 N NH2 . ARG   B 109 ? 0.5764 0.5796 0.6107 -0.0130 -0.0063 0.0352  115 ARG   C NH2 
1939 N N   . CYS   B 110 ? 0.1915 0.1935 0.1727 0.0123  -0.0039 0.0159  116 CYS   C N   
1940 C CA  . CYS   B 110 ? 0.2163 0.2142 0.1919 0.0170  -0.0051 0.0154  116 CYS   C CA  
1941 C C   . CYS   B 110 ? 0.2495 0.2405 0.2242 0.0164  -0.0041 0.0225  116 CYS   C C   
1942 O O   . CYS   B 110 ? 0.2471 0.2374 0.2274 0.0121  -0.0025 0.0270  116 CYS   C O   
1943 C CB  . CYS   B 110 ? 0.2189 0.2225 0.1910 0.0225  -0.0051 0.0126  116 CYS   C CB  
1944 S SG  . CYS   B 110 ? 0.2081 0.2154 0.1764 0.0250  -0.0016 0.0176  116 CYS   C SG  
1945 N N   . GLN   B 111 ? 0.2898 0.2757 0.2586 0.0210  -0.0050 0.0240  117 GLN   C N   
1946 C CA  . GLN   B 111 ? 0.3183 0.2969 0.2869 0.0207  -0.0034 0.0320  117 GLN   C CA  
1947 C C   . GLN   B 111 ? 0.3218 0.3047 0.2902 0.0209  0.0024  0.0391  117 GLN   C C   
1948 O O   . GLN   B 111 ? 0.3542 0.3325 0.3264 0.0189  0.0056  0.0473  117 GLN   C O   
1949 C CB  . GLN   B 111 ? 0.3624 0.3345 0.3234 0.0268  -0.0056 0.0325  117 GLN   C CB  
1950 C CG  . GLN   B 111 ? 0.4122 0.3893 0.3635 0.0341  -0.0050 0.0317  117 GLN   C CG  
1951 C CD  . GLN   B 111 ? 0.5280 0.4990 0.4721 0.0407  -0.0085 0.0314  117 GLN   C CD  
1952 O OE1 . GLN   B 111 ? 0.5724 0.5458 0.5164 0.0440  -0.0129 0.0238  117 GLN   C OE1 
1953 N NE2 . GLN   B 111 ? 0.5340 0.4969 0.4730 0.0430  -0.0065 0.0402  117 GLN   C NE2 
1954 N N   . HIS   B 112 ? 0.2857 0.2775 0.2507 0.0235  0.0041  0.0361  118 HIS   C N   
1955 C CA  . HIS   B 112 ? 0.2772 0.2736 0.2402 0.0254  0.0100  0.0418  118 HIS   C CA  
1956 C C   . HIS   B 112 ? 0.2793 0.2815 0.2534 0.0196  0.0126  0.0427  118 HIS   C C   
1957 O O   . HIS   B 112 ? 0.3097 0.3159 0.2847 0.0206  0.0185  0.0483  118 HIS   C O   
1958 C CB  . HIS   B 112 ? 0.2726 0.2743 0.2244 0.0333  0.0095  0.0374  118 HIS   C CB  
1959 C CG  . HIS   B 112 ? 0.2721 0.2687 0.2132 0.0400  0.0057  0.0358  118 HIS   C CG  
1960 N ND1 . HIS   B 112 ? 0.2707 0.2695 0.2116 0.0425  -0.0006 0.0267  118 HIS   C ND1 
1961 C CD2 . HIS   B 112 ? 0.2951 0.2852 0.2262 0.0453  0.0074  0.0427  118 HIS   C CD2 
1962 C CE1 . HIS   B 112 ? 0.3089 0.3025 0.2407 0.0488  -0.0033 0.0274  118 HIS   C CE1 
1963 N NE2 . HIS   B 112 ? 0.3225 0.3102 0.2468 0.0510  0.0011  0.0371  118 HIS   C NE2 
1964 N N   . GLY   B 113 ? 0.2468 0.2495 0.2286 0.0143  0.0085  0.0375  119 GLY   C N   
1965 C CA  . GLY   B 113 ? 0.2364 0.2440 0.2285 0.0093  0.0097  0.0380  119 GLY   C CA  
1966 C C   . GLY   B 113 ? 0.2114 0.2233 0.2046 0.0082  0.0061  0.0304  119 GLY   C C   
1967 O O   . GLY   B 113 ? 0.2178 0.2277 0.2067 0.0093  0.0027  0.0251  119 GLY   C O   
1968 N N   . VAL   B 114 ? 0.1999 0.2176 0.1996 0.0061  0.0075  0.0304  120 VAL   C N   
1969 C CA  . VAL   B 114 ? 0.1849 0.2060 0.1866 0.0049  0.0047  0.0247  120 VAL   C CA  
1970 C C   . VAL   B 114 ? 0.1740 0.1992 0.1703 0.0098  0.0046  0.0196  120 VAL   C C   
1971 O O   . VAL   B 114 ? 0.1903 0.2194 0.1836 0.0142  0.0072  0.0199  120 VAL   C O   
1972 C CB  . VAL   B 114 ? 0.1969 0.2225 0.2082 0.0017  0.0055  0.0264  120 VAL   C CB  
1973 C CG1 . VAL   B 114 ? 0.1930 0.2212 0.2057 0.0010  0.0030  0.0215  120 VAL   C CG1 
1974 C CG2 . VAL   B 114 ? 0.2051 0.2264 0.2243 -0.0036 0.0032  0.0299  120 VAL   C CG2 
1975 N N   . VAL   B 115 ? 0.1700 0.1944 0.1656 0.0096  0.0016  0.0146  121 VAL   C N   
1976 C CA  . VAL   B 115 ? 0.1696 0.1979 0.1644 0.0135  0.0005  0.0091  121 VAL   C CA  
1977 C C   . VAL   B 115 ? 0.1777 0.2102 0.1801 0.0115  0.0001  0.0066  121 VAL   C C   
1978 O O   . VAL   B 115 ? 0.1684 0.2050 0.1729 0.0147  -0.0006 0.0028  121 VAL   C O   
1979 C CB  . VAL   B 115 ? 0.1680 0.1937 0.1609 0.0145  -0.0017 0.0058  121 VAL   C CB  
1980 C CG1 . VAL   B 115 ? 0.1802 0.2107 0.1773 0.0175  -0.0036 -0.0002 121 VAL   C CG1 
1981 C CG2 . VAL   B 115 ? 0.1777 0.1987 0.1633 0.0174  -0.0020 0.0080  121 VAL   C CG2 
1982 N N   . GLY   B 116 ? 0.1666 0.1972 0.1727 0.0068  -0.0002 0.0081  122 GLY   C N   
1983 C CA  . GLY   B 116 ? 0.1776 0.2109 0.1905 0.0051  -0.0006 0.0067  122 GLY   C CA  
1984 C C   . GLY   B 116 ? 0.1595 0.1893 0.1728 0.0010  -0.0012 0.0093  122 GLY   C C   
1985 O O   . GLY   B 116 ? 0.1688 0.1944 0.1779 -0.0005 -0.0022 0.0115  122 GLY   C O   
1986 N N   . ILE   B 117 ? 0.1548 0.1857 0.1731 -0.0003 -0.0013 0.0090  123 ILE   C N   
1987 C CA  . ILE   B 117 ? 0.1679 0.1949 0.1841 -0.0031 -0.0023 0.0118  123 ILE   C CA  
1988 C C   . ILE   B 117 ? 0.1626 0.1890 0.1798 -0.0032 -0.0004 0.0116  123 ILE   C C   
1989 O O   . ILE   B 117 ? 0.1615 0.1916 0.1867 -0.0024 0.0009  0.0097  123 ILE   C O   
1990 C CB  . ILE   B 117 ? 0.1889 0.2168 0.2103 -0.0046 -0.0040 0.0141  123 ILE   C CB  
1991 C CG1 . ILE   B 117 ? 0.1904 0.2229 0.2205 -0.0034 -0.0032 0.0124  123 ILE   C CG1 
1992 C CG2 . ILE   B 117 ? 0.2156 0.2435 0.2376 -0.0054 -0.0053 0.0159  123 ILE   C CG2 
1993 C CD1 . ILE   B 117 ? 0.2195 0.2524 0.2555 -0.0047 -0.0053 0.0150  123 ILE   C CD1 
1994 N N   . VAL   B 118 ? 0.1515 0.1732 0.1610 -0.0037 0.0000  0.0137  124 VAL   C N   
1995 C CA  . VAL   B 118 ? 0.1598 0.1810 0.1698 -0.0034 0.0037  0.0152  124 VAL   C CA  
1996 C C   . VAL   B 118 ? 0.1609 0.1835 0.1797 -0.0048 0.0040  0.0176  124 VAL   C C   
1997 O O   . VAL   B 118 ? 0.1714 0.1923 0.1897 -0.0057 0.0007  0.0194  124 VAL   C O   
1998 C CB  . VAL   B 118 ? 0.1790 0.1941 0.1759 -0.0025 0.0039  0.0175  124 VAL   C CB  
1999 C CG1 . VAL   B 118 ? 0.1889 0.2034 0.1852 -0.0017 0.0095  0.0210  124 VAL   C CG1 
2000 C CG2 . VAL   B 118 ? 0.1997 0.2124 0.1885 -0.0007 0.0033  0.0144  124 VAL   C CG2 
2001 N N   . SER   B 119 ? 0.1692 0.1948 0.1981 -0.0049 0.0073  0.0173  125 SER   C N   
2002 C CA  . SER   B 119 ? 0.1731 0.1993 0.2130 -0.0062 0.0074  0.0192  125 SER   C CA  
2003 C C   . SER   B 119 ? 0.2031 0.2283 0.2483 -0.0070 0.0129  0.0236  125 SER   C C   
2004 O O   . SER   B 119 ? 0.2035 0.2260 0.2535 -0.0081 0.0135  0.0281  125 SER   C O   
2005 C CB  . SER   B 119 ? 0.1942 0.2253 0.2462 -0.0056 0.0048  0.0137  125 SER   C CB  
2006 O OG  . SER   B 119 ? 0.1962 0.2273 0.2605 -0.0065 0.0041  0.0144  125 SER   C OG  
2007 N N   . THR   B 120 ? 0.2037 0.2311 0.2500 -0.0063 0.0173  0.0229  126 THR   C N   
2008 C CA  . THR   B 120 ? 0.2220 0.2498 0.2761 -0.0070 0.0244  0.0278  126 THR   C CA  
2009 C C   . THR   B 120 ? 0.2329 0.2600 0.2750 -0.0046 0.0299  0.0294  126 THR   C C   
2010 O O   . THR   B 120 ? 0.2171 0.2440 0.2488 -0.0028 0.0272  0.0251  126 THR   C O   
2011 C CB  . THR   B 120 ? 0.2408 0.2746 0.3182 -0.0084 0.0248  0.0242  126 THR   C CB  
2012 O OG1 . THR   B 120 ? 0.2631 0.3018 0.3427 -0.0067 0.0244  0.0184  126 THR   C OG1 
2013 C CG2 . THR   B 120 ? 0.2574 0.2918 0.3459 -0.0094 0.0185  0.0203  126 THR   C CG2 
2014 N N   . GLY   B 121 ? 0.2584 0.2848 0.3018 -0.0043 0.0380  0.0358  127 GLY   C N   
2015 C CA  . GLY   B 121 ? 0.2953 0.3218 0.3277 -0.0010 0.0445  0.0372  127 GLY   C CA  
2016 C C   . GLY   B 121 ? 0.3216 0.3498 0.3625 -0.0009 0.0555  0.0448  127 GLY   C C   
2017 O O   . GLY   B 121 ? 0.3174 0.3447 0.3699 -0.0036 0.0576  0.0504  127 GLY   C O   
2018 N N   . GLY   B 122 ? 0.3552 0.3857 0.3909 0.0024  0.0629  0.0455  128 GLY   C N   
2019 C CA  . GLY   B 122 ? 0.3655 0.3986 0.4091 0.0031  0.0756  0.0539  128 GLY   C CA  
2020 C C   . GLY   B 122 ? 0.3694 0.4114 0.4284 0.0041  0.0818  0.0508  128 GLY   C C   
2021 O O   . GLY   B 122 ? 0.3567 0.4034 0.4262 0.0031  0.0750  0.0422  128 GLY   C O   
2022 N N   . ASN   B 123 ? 0.3744 0.4192 0.4351 0.0067  0.0951  0.0582  129 ASN   C N   
2023 C CA  . ASN   B 123 ? 0.3762 0.4307 0.4534 0.0082  0.1021  0.0556  129 ASN   C CA  
2024 C C   . ASN   B 123 ? 0.3581 0.4135 0.4239 0.0120  0.0958  0.0454  129 ASN   C C   
2025 O O   . ASN   B 123 ? 0.3699 0.4336 0.4547 0.0120  0.0955  0.0398  129 ASN   C O   
2026 C CB  . ASN   B 123 ? 0.3935 0.4567 0.5084 0.0026  0.1015  0.0543  129 ASN   C CB  
2027 C CG  . ASN   B 123 ? 0.4558 0.5198 0.5873 -0.0005 0.1121  0.0658  129 ASN   C CG  
2028 O OD1 . ASN   B 123 ? 0.4779 0.5403 0.5982 0.0029  0.1249  0.0755  129 ASN   C OD1 
2029 N ND2 . ASN   B 123 ? 0.4833 0.5492 0.6413 -0.0063 0.1070  0.0651  129 ASN   C ND2 
2030 N N   . GLY   B 124 ? 0.3295 0.3759 0.3660 0.0154  0.0898  0.0428  130 GLY   C N   
2031 C CA  . GLY   B 124 ? 0.2980 0.3436 0.3237 0.0188  0.0834  0.0338  130 GLY   C CA  
2032 C C   . GLY   B 124 ? 0.2598 0.3071 0.2968 0.0153  0.0713  0.0258  130 GLY   C C   
2033 O O   . GLY   B 124 ? 0.2699 0.3183 0.3050 0.0178  0.0670  0.0189  130 GLY   C O   
2034 N N   . LEU   B 125 ? 0.2413 0.2884 0.2887 0.0102  0.0658  0.0268  131 LEU   C N   
2035 C CA  . LEU   B 125 ? 0.2248 0.2730 0.2798 0.0078  0.0550  0.0199  131 LEU   C CA  
2036 C C   . LEU   B 125 ? 0.2269 0.2671 0.2662 0.0061  0.0476  0.0207  131 LEU   C C   
2037 O O   . LEU   B 125 ? 0.2604 0.2962 0.2927 0.0051  0.0502  0.0268  131 LEU   C O   
2038 C CB  . LEU   B 125 ? 0.2394 0.2946 0.3226 0.0040  0.0544  0.0193  131 LEU   C CB  
2039 C CG  . LEU   B 125 ? 0.2688 0.3334 0.3746 0.0047  0.0613  0.0189  131 LEU   C CG  
2040 C CD1 . LEU   B 125 ? 0.2820 0.3520 0.4172 0.0002  0.0610  0.0198  131 LEU   C CD1 
2041 C CD2 . LEU   B 125 ? 0.2780 0.3463 0.3852 0.0082  0.0562  0.0105  131 LEU   C CD2 
2042 N N   . VAL   B 126 ? 0.1848 0.2237 0.2206 0.0059  0.0388  0.0148  132 VAL   C N   
2043 C CA  . VAL   B 126 ? 0.1923 0.2258 0.2189 0.0040  0.0320  0.0152  132 VAL   C CA  
2044 C C   . VAL   B 126 ? 0.1831 0.2207 0.2236 0.0021  0.0260  0.0108  132 VAL   C C   
2045 O O   . VAL   B 126 ? 0.1818 0.2233 0.2285 0.0038  0.0236  0.0056  132 VAL   C O   
2046 C CB  . VAL   B 126 ? 0.2138 0.2405 0.2204 0.0062  0.0277  0.0133  132 VAL   C CB  
2047 C CG1 . VAL   B 126 ? 0.2428 0.2708 0.2491 0.0086  0.0252  0.0077  132 VAL   C CG1 
2048 C CG2 . VAL   B 126 ? 0.2219 0.2444 0.2231 0.0038  0.0209  0.0139  132 VAL   C CG2 
2049 N N   . GLY   B 127 ? 0.1706 0.2070 0.2147 -0.0004 0.0232  0.0125  133 GLY   C N   
2050 C CA  . GLY   B 127 ? 0.1696 0.2093 0.2246 -0.0010 0.0176  0.0079  133 GLY   C CA  
2051 C C   . GLY   B 127 ? 0.1708 0.2071 0.2150 -0.0010 0.0122  0.0073  133 GLY   C C   
2052 O O   . GLY   B 127 ? 0.1814 0.2134 0.2176 -0.0023 0.0122  0.0113  133 GLY   C O   
2053 N N   . PHE   B 128 ? 0.1565 0.1948 0.2009 0.0009  0.0079  0.0025  134 PHE   C N   
2054 C CA  . PHE   B 128 ? 0.1604 0.1966 0.1962 0.0012  0.0043  0.0025  134 PHE   C CA  
2055 C C   . PHE   B 128 ? 0.1665 0.2060 0.2102 0.0025  0.0011  -0.0011 134 PHE   C C   
2056 O O   . PHE   B 128 ? 0.1696 0.2126 0.2199 0.0050  -0.0009 -0.0060 134 PHE   C O   
2057 C CB  . PHE   B 128 ? 0.1573 0.1920 0.1835 0.0035  0.0029  0.0009  134 PHE   C CB  
2058 C CG  . PHE   B 128 ? 0.1616 0.1926 0.1799 0.0036  0.0052  0.0024  134 PHE   C CG  
2059 C CD1 . PHE   B 128 ? 0.1592 0.1846 0.1674 0.0023  0.0046  0.0055  134 PHE   C CD1 
2060 C CD2 . PHE   B 128 ? 0.1838 0.2170 0.2054 0.0057  0.0070  -0.0001 134 PHE   C CD2 
2061 C CE1 . PHE   B 128 ? 0.1726 0.1940 0.1724 0.0034  0.0060  0.0057  134 PHE   C CE1 
2062 C CE2 . PHE   B 128 ? 0.1939 0.2236 0.2074 0.0068  0.0093  0.0006  134 PHE   C CE2 
2063 C CZ  . PHE   B 128 ? 0.1952 0.2185 0.1968 0.0059  0.0087  0.0033  134 PHE   C CZ  
2064 N N   . ALA   B 129 ? 0.1522 0.1907 0.1947 0.0015  0.0001  0.0009  135 ALA   C N   
2065 C CA  . ALA   B 129 ? 0.1419 0.1832 0.1893 0.0038  -0.0026 -0.0028 135 ALA   C CA  
2066 C C   . ALA   B 129 ? 0.1513 0.1934 0.1890 0.0073  -0.0035 -0.0042 135 ALA   C C   
2067 O O   . ALA   B 129 ? 0.1433 0.1834 0.1735 0.0062  -0.0022 -0.0002 135 ALA   C O   
2068 C CB  . ALA   B 129 ? 0.1430 0.1832 0.1932 0.0020  -0.0028 0.0002  135 ALA   C CB  
2069 N N   . ASP   B 130 ? 0.1512 0.1958 0.1893 0.0118  -0.0060 -0.0096 136 ASP   C N   
2070 C CA  . ASP   B 130 ? 0.1492 0.1937 0.1761 0.0161  -0.0062 -0.0099 136 ASP   C CA  
2071 C C   . ASP   B 130 ? 0.1709 0.2167 0.1947 0.0178  -0.0048 -0.0083 136 ASP   C C   
2072 O O   . ASP   B 130 ? 0.1729 0.2207 0.2035 0.0186  -0.0060 -0.0111 136 ASP   C O   
2073 C CB  . ASP   B 130 ? 0.1692 0.2158 0.1968 0.0218  -0.0104 -0.0169 136 ASP   C CB  
2074 C CG  . ASP   B 130 ? 0.2601 0.3057 0.2740 0.0275  -0.0107 -0.0168 136 ASP   C CG  
2075 O OD1 . ASP   B 130 ? 0.2533 0.2961 0.2601 0.0261  -0.0082 -0.0118 136 ASP   C OD1 
2076 O OD2 . ASP   B 130 ? 0.3024 0.3495 0.3118 0.0338  -0.0134 -0.0213 136 ASP   C OD2 
2077 N N   . VAL   B 131 ? 0.1612 0.2060 0.1757 0.0190  -0.0020 -0.0040 137 VAL   C N   
2078 C CA  . VAL   B 131 ? 0.1624 0.2098 0.1747 0.0217  0.0008  -0.0021 137 VAL   C CA  
2079 C C   . VAL   B 131 ? 0.1859 0.2335 0.1860 0.0283  0.0026  -0.0016 137 VAL   C C   
2080 O O   . VAL   B 131 ? 0.2002 0.2502 0.1967 0.0317  0.0065  0.0008  137 VAL   C O   
2081 C CB  . VAL   B 131 ? 0.1759 0.2230 0.1920 0.0165  0.0040  0.0048  137 VAL   C CB  
2082 C CG1 . VAL   B 131 ? 0.1800 0.2262 0.2055 0.0113  0.0018  0.0048  137 VAL   C CG1 
2083 C CG2 . VAL   B 131 ? 0.1958 0.2388 0.2068 0.0140  0.0053  0.0098  137 VAL   C CG2 
2084 N N   . ARG   B 132 ? 0.1746 0.2197 0.1681 0.0310  0.0000  -0.0037 138 ARG   C N   
2085 C CA  . ARG   B 132 ? 0.1801 0.2239 0.1602 0.0376  0.0014  -0.0021 138 ARG   C CA  
2086 C C   . ARG   B 132 ? 0.2175 0.2641 0.1901 0.0463  0.0004  -0.0071 138 ARG   C C   
2087 O O   . ARG   B 132 ? 0.2418 0.2876 0.2010 0.0526  0.0038  -0.0037 138 ARG   C O   
2088 C CB  . ARG   B 132 ? 0.1870 0.2271 0.1625 0.0389  -0.0022 -0.0035 138 ARG   C CB  
2089 C CG  . ARG   B 132 ? 0.1918 0.2281 0.1713 0.0320  -0.0006 0.0016  138 ARG   C CG  
2090 C CD  . ARG   B 132 ? 0.1954 0.2288 0.1720 0.0341  -0.0045 -0.0011 138 ARG   C CD  
2091 N NE  . ARG   B 132 ? 0.1870 0.2236 0.1730 0.0337  -0.0089 -0.0085 138 ARG   C NE  
2092 C CZ  . ARG   B 132 ? 0.1945 0.2305 0.1833 0.0347  -0.0122 -0.0119 138 ARG   C CZ  
2093 N NH1 . ARG   B 132 ? 0.2026 0.2345 0.1831 0.0376  -0.0128 -0.0097 138 ARG   C NH1 
2094 N NH2 . ARG   B 132 ? 0.2031 0.2429 0.2042 0.0333  -0.0149 -0.0175 138 ARG   C NH2 
2095 N N   . ASP   B 133 ? 0.2093 0.2583 0.1894 0.0475  -0.0044 -0.0151 139 ASP   C N   
2096 C CA  . ASP   B 133 ? 0.2319 0.2828 0.2048 0.0566  -0.0067 -0.0218 139 ASP   C CA  
2097 C C   . ASP   B 133 ? 0.2400 0.2943 0.2127 0.0581  -0.0009 -0.0191 139 ASP   C C   
2098 O O   . ASP   B 133 ? 0.2583 0.3139 0.2218 0.0671  -0.0015 -0.0242 139 ASP   C O   
2099 C CB  . ASP   B 133 ? 0.2510 0.3026 0.2344 0.0576  -0.0154 -0.0324 139 ASP   C CB  
2100 C CG  . ASP   B 133 ? 0.2955 0.3484 0.2968 0.0499  -0.0152 -0.0324 139 ASP   C CG  
2101 O OD1 . ASP   B 133 ? 0.2780 0.3302 0.2853 0.0417  -0.0112 -0.0253 139 ASP   C OD1 
2102 O OD2 . ASP   B 133 ? 0.2984 0.3524 0.3071 0.0525  -0.0195 -0.0398 139 ASP   C OD2 
2103 N N   . LEU   B 134 ? 0.2277 0.2832 0.2102 0.0503  0.0043  -0.0121 140 LEU   C N   
2104 C CA  . LEU   B 134 ? 0.2322 0.2919 0.2184 0.0512  0.0097  -0.0097 140 LEU   C CA  
2105 C C   . LEU   B 134 ? 0.2465 0.3077 0.2223 0.0548  0.0183  -0.0014 140 LEU   C C   
2106 O O   . LEU   B 134 ? 0.2455 0.3076 0.2281 0.0488  0.0238  0.0072  140 LEU   C O   
2107 C CB  . LEU   B 134 ? 0.2264 0.2867 0.2292 0.0414  0.0099  -0.0061 140 LEU   C CB  
2108 C CG  . LEU   B 134 ? 0.2447 0.3029 0.2581 0.0375  0.0029  -0.0121 140 LEU   C CG  
2109 C CD1 . LEU   B 134 ? 0.2539 0.3115 0.2796 0.0289  0.0034  -0.0071 140 LEU   C CD1 
2110 C CD2 . LEU   B 134 ? 0.2535 0.3131 0.2696 0.0436  -0.0014 -0.0213 140 LEU   C CD2 
2111 N N   . LEU   B 135 ? 0.2425 0.3037 0.2017 0.0653  0.0194  -0.0040 141 LEU   C N   
2112 C CA  . LEU   B 135 ? 0.2684 0.3300 0.2154 0.0697  0.0286  0.0052  141 LEU   C CA  
2113 C C   . LEU   B 135 ? 0.2851 0.3527 0.2396 0.0690  0.0382  0.0118  141 LEU   C C   
2114 O O   . LEU   B 135 ? 0.3107 0.3791 0.2645 0.0677  0.0469  0.0224  141 LEU   C O   
2115 C CB  . LEU   B 135 ? 0.2713 0.3308 0.1956 0.0826  0.0277  0.0014  141 LEU   C CB  
2116 C CG  . LEU   B 135 ? 0.2865 0.3411 0.2047 0.0851  0.0166  -0.0071 141 LEU   C CG  
2117 C CD1 . LEU   B 135 ? 0.3245 0.3766 0.2185 0.0991  0.0150  -0.0106 141 LEU   C CD1 
2118 C CD2 . LEU   B 135 ? 0.2803 0.3306 0.2049 0.0763  0.0145  -0.0021 141 LEU   C CD2 
2119 N N   . TRP   B 136 ? 0.2756 0.3476 0.2390 0.0701  0.0368  0.0056  142 TRP   C N   
2120 C CA  . TRP   B 136 ? 0.2761 0.3551 0.2486 0.0704  0.0457  0.0106  142 TRP   C CA  
2121 C C   . TRP   B 136 ? 0.2814 0.3618 0.2735 0.0585  0.0482  0.0193  142 TRP   C C   
2122 O O   . TRP   B 136 ? 0.2938 0.3805 0.2961 0.0579  0.0561  0.0254  142 TRP   C O   
2123 C CB  . TRP   B 136 ? 0.2682 0.3504 0.2463 0.0745  0.0418  0.0008  142 TRP   C CB  
2124 C CG  . TRP   B 136 ? 0.2644 0.3429 0.2553 0.0673  0.0309  -0.0061 142 TRP   C CG  
2125 C CD1 . TRP   B 136 ? 0.2747 0.3484 0.2616 0.0692  0.0213  -0.0156 142 TRP   C CD1 
2126 C CD2 . TRP   B 136 ? 0.2475 0.3270 0.2581 0.0573  0.0291  -0.0034 142 TRP   C CD2 
2127 N NE1 . TRP   B 136 ? 0.2742 0.3461 0.2775 0.0607  0.0150  -0.0179 142 TRP   C NE1 
2128 C CE2 . TRP   B 136 ? 0.2582 0.3330 0.2742 0.0540  0.0195  -0.0106 142 TRP   C CE2 
2129 C CE3 . TRP   B 136 ? 0.2467 0.3304 0.2713 0.0513  0.0343  0.0045  142 TRP   C CE3 
2130 C CZ2 . TRP   B 136 ? 0.2648 0.3384 0.2966 0.0455  0.0158  -0.0092 142 TRP   C CZ2 
2131 C CZ3 . TRP   B 136 ? 0.2625 0.3451 0.3029 0.0434  0.0289  0.0043  142 TRP   C CZ3 
2132 C CH2 . TRP   B 136 ? 0.2624 0.3398 0.3048 0.0409  0.0202  -0.0022 142 TRP   C CH2 
2133 N N   . LEU   B 137 ? 0.2759 0.3509 0.2739 0.0497  0.0414  0.0196  143 LEU   C N   
2134 C CA  . LEU   B 137 ? 0.2768 0.3522 0.2915 0.0396  0.0424  0.0267  143 LEU   C CA  
2135 C C   . LEU   B 137 ? 0.3356 0.4121 0.3505 0.0392  0.0516  0.0378  143 LEU   C C   
2136 O O   . LEU   B 137 ? 0.3549 0.4342 0.3866 0.0327  0.0542  0.0439  143 LEU   C O   
2137 C CB  . LEU   B 137 ? 0.2528 0.3211 0.2692 0.0322  0.0339  0.0247  143 LEU   C CB  
2138 C CG  . LEU   B 137 ? 0.2475 0.3146 0.2698 0.0296  0.0259  0.0170  143 LEU   C CG  
2139 C CD1 . LEU   B 137 ? 0.2390 0.2996 0.2601 0.0240  0.0199  0.0160  143 LEU   C CD1 
2140 C CD2 . LEU   B 137 ? 0.2505 0.3215 0.2892 0.0253  0.0256  0.0182  143 LEU   C CD2 
2141 N N   . ASP   B 138 ? 0.3744 0.4481 0.3717 0.0458  0.0556  0.0403  144 ASP   C N   
2142 C CA  . ASP   B 138 ? 0.4248 0.4976 0.4189 0.0466  0.0646  0.0516  144 ASP   C CA  
2143 C C   . ASP   B 138 ? 0.4696 0.5501 0.4643 0.0528  0.0771  0.0582  144 ASP   C C   
2144 O O   . ASP   B 138 ? 0.4826 0.5627 0.4764 0.0534  0.0862  0.0691  144 ASP   C O   
2145 C CB  . ASP   B 138 ? 0.4584 0.5245 0.4295 0.0537  0.0634  0.0510  144 ASP   C CB  
2146 C CG  . ASP   B 138 ? 0.5098 0.5676 0.4787 0.0486  0.0542  0.0483  144 ASP   C CG  
2147 O OD1 . ASP   B 138 ? 0.5195 0.5758 0.5038 0.0391  0.0496  0.0481  144 ASP   C OD1 
2148 O OD2 . ASP   B 138 ? 0.5494 0.6023 0.5006 0.0551  0.0513  0.0457  144 ASP   C OD2 
2149 N N   . GLU   B 139 ? 0.4892 0.5760 0.4824 0.0592  0.0783  0.0517  145 GLU   C N   
2150 C CA  . GLU   B 139 ? 0.5226 0.6174 0.5139 0.0671  0.0913  0.0572  145 GLU   C CA  
2151 C C   . GLU   B 139 ? 0.5378 0.6418 0.5524 0.0635  0.0941  0.0570  145 GLU   C C   
2152 O O   . GLU   B 139 ? 0.5575 0.6697 0.5748 0.0695  0.1060  0.0622  145 GLU   C O   
2153 C CB  . GLU   B 139 ? 0.5785 0.6727 0.5436 0.0814  0.0919  0.0499  145 GLU   C CB  
2154 C CG  . GLU   B 139 ? 0.6635 0.7576 0.6280 0.0838  0.0810  0.0352  145 GLU   C CG  
2155 C CD  . GLU   B 139 ? 0.7866 0.8773 0.7254 0.0970  0.0770  0.0256  145 GLU   C CD  
2156 O OE1 . GLU   B 139 ? 0.8026 0.8954 0.7413 0.1023  0.0722  0.0147  145 GLU   C OE1 
2157 O OE2 . GLU   B 139 ? 0.8228 0.9082 0.7420 0.1023  0.0778  0.0285  145 GLU   C OE2 
2158 N N1  . A1BSJ C .   ? 0.2874 0.3069 0.3918 0.0140  0.0242  -0.0059 201 A1BSJ A N1  
2159 C C4  . A1BSJ C .   ? 0.4364 0.4313 0.4640 0.0023  0.0756  -0.0467 201 A1BSJ A C4  
2160 C C5  . A1BSJ C .   ? 0.4389 0.4331 0.4824 0.0058  0.0732  -0.0455 201 A1BSJ A C5  
2161 C C6  . A1BSJ C .   ? 0.4369 0.4371 0.4818 0.0066  0.0596  -0.0390 201 A1BSJ A C6  
2162 C C7  . A1BSJ C .   ? 0.4407 0.4413 0.5042 0.0102  0.0573  -0.0358 201 A1BSJ A C7  
2163 C C8  . A1BSJ C .   ? 0.4548 0.4462 0.5055 0.0062  0.0540  -0.0436 201 A1BSJ A C8  
2164 C C10 . A1BSJ C .   ? 0.3923 0.3823 0.4543 0.0053  0.0375  -0.0406 201 A1BSJ A C10 
2165 C C13 . A1BSJ C .   ? 0.3140 0.3264 0.4264 0.0161  0.0331  -0.0112 201 A1BSJ A C13 
2166 C C15 . A1BSJ C .   ? 0.3981 0.3903 0.4915 0.0144  0.0592  -0.0358 201 A1BSJ A C15 
2167 O O2  . A1BSJ C .   ? 0.3064 0.3172 0.4387 0.0191  0.0377  -0.0074 201 A1BSJ A O2  
2168 C C12 . A1BSJ C .   ? 0.3506 0.3559 0.4459 0.0140  0.0381  -0.0222 201 A1BSJ A C12 
2169 C C11 . A1BSJ C .   ? 0.3677 0.3621 0.4539 0.0105  0.0391  -0.0321 201 A1BSJ A C11 
2170 C C9  . A1BSJ C .   ? 0.4110 0.3936 0.4657 0.0039  0.0483  -0.0484 201 A1BSJ A C9  
2171 C C14 . A1BSJ C .   ? 0.3720 0.3763 0.4776 0.0169  0.0489  -0.0229 201 A1BSJ A C14 
2172 N N   . A1BSJ C .   ? 0.4205 0.4096 0.4859 0.0084  0.0537  -0.0426 201 A1BSJ A N   
2173 O O1  . A1BSJ C .   ? 0.4906 0.4769 0.5187 0.0006  0.0516  -0.0499 201 A1BSJ A O1  
2174 C C1  . A1BSJ C .   ? 0.4243 0.4300 0.4547 0.0042  0.0492  -0.0348 201 A1BSJ A C1  
2175 O O   . A1BSJ C .   ? 0.4103 0.4198 0.4423 0.0048  0.0385  -0.0301 201 A1BSJ A O   
2176 C C   . A1BSJ C .   ? 0.4053 0.4165 0.4216 0.0020  0.0292  -0.0284 201 A1BSJ A C   
2177 C C3  . A1BSJ C .   ? 0.4216 0.4228 0.4360 0.0001  0.0640  -0.0411 201 A1BSJ A C3  
2178 C C2  . A1BSJ C .   ? 0.4247 0.4308 0.4410 0.0013  0.0512  -0.0354 201 A1BSJ A C2  
2184 N N1  . A1BSJ F .   ? 0.2328 0.2582 0.3201 -0.0105 0.0096  0.0247  201 A1BSJ C N1  
2185 C C4  . A1BSJ F .   ? 0.4847 0.4906 0.4773 0.0051  0.0604  0.0664  201 A1BSJ C C4  
2186 C C5  . A1BSJ F .   ? 0.4754 0.4825 0.4865 0.0003  0.0550  0.0659  201 A1BSJ C C5  
2187 C C6  . A1BSJ F .   ? 0.4703 0.4794 0.4862 -0.0019 0.0446  0.0572  201 A1BSJ C C6  
2188 C C7  . A1BSJ F .   ? 0.4558 0.4674 0.4930 -0.0061 0.0398  0.0551  201 A1BSJ C C7  
2189 C C8  . A1BSJ F .   ? 0.4450 0.4504 0.4748 -0.0059 0.0332  0.0575  201 A1BSJ C C8  
2190 C C10 . A1BSJ F .   ? 0.3357 0.3410 0.3851 -0.0090 0.0151  0.0499  201 A1BSJ C C10 
2191 C C13 . A1BSJ F .   ? 0.2608 0.2824 0.3549 -0.0121 0.0133  0.0315  201 A1BSJ C C13 
2192 C C15 . A1BSJ F .   ? 0.3573 0.3676 0.4297 -0.0117 0.0332  0.0567  201 A1BSJ C C15 
2193 O O2  . A1BSJ F .   ? 0.2406 0.2621 0.3530 -0.0135 0.0128  0.0312  201 A1BSJ C O2  
2194 C C12 . A1BSJ F .   ? 0.2981 0.3146 0.3756 -0.0116 0.0181  0.0400  201 A1BSJ C C12 
2195 C C11 . A1BSJ F .   ? 0.3088 0.3192 0.3805 -0.0111 0.0146  0.0448  201 A1BSJ C C11 
2196 C C9  . A1BSJ F .   ? 0.3681 0.3690 0.4106 -0.0081 0.0231  0.0587  201 A1BSJ C C9  
2197 C C14 . A1BSJ F .   ? 0.3189 0.3356 0.4043 -0.0128 0.0267  0.0459  201 A1BSJ C C14 
2198 N N   . A1BSJ F .   ? 0.3887 0.3945 0.4359 -0.0086 0.0301  0.0576  201 A1BSJ C N   
2199 O O1  . A1BSJ F .   ? 0.4795 0.4793 0.4888 -0.0029 0.0305  0.0593  201 A1BSJ C O1  
2200 C C1  . A1BSJ F .   ? 0.4737 0.4828 0.4761 0.0001  0.0395  0.0502  201 A1BSJ C C1  
2201 O O   . A1BSJ F .   ? 0.4621 0.4724 0.4686 -0.0018 0.0304  0.0439  201 A1BSJ C O   
2202 C C   . A1BSJ F .   ? 0.4546 0.4640 0.4492 -0.0003 0.0250  0.0380  201 A1BSJ C C   
2203 C C3  . A1BSJ F .   ? 0.4844 0.4903 0.4647 0.0072  0.0544  0.0581  201 A1BSJ C C3  
2204 C C2  . A1BSJ F .   ? 0.4842 0.4916 0.4701 0.0043  0.0439  0.0503  201 A1BSJ C C2  
# 
