data_7I3B
# 
_entry.id   7I3B 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I3B         pdb_00007i3b 10.2210/pdb7i3b/pdb 
WWPDB D_1001408262 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I3B 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                            15892.732 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2S)-2-methoxy-2-(pyridin-3-yl)acetyl]piperidine-3-carboxamide' 277.319   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                               65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                     78.133    3   ?         ? ? ? 
5 water       nat water                                                                    18.015    354 ?         ? ? ? 
# 
_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 '(3S)-1-[(2S)-2-methoxy-2-(pyridin-3-yl)acetyl]piperidine-3-carboxamide' A1B1E 
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 
A1B1E non-polymer         . '(3S)-1-[(2S)-2-methoxy-2-(pyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C14 H19 N3 O3'  277.319 
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 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B1E 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B1E 
_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 A1B1E 1   201 201 A1B1E LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 1   DMS   DMS A . 
F 4 DMS   1   204 2   DMS   DMS A . 
G 3 ZN    1   201 1   ZN    ZN  C . 
H 4 DMS   1   202 1   DMS   DMS C . 
I 5 HOH   1   301 189 HOH   HOH A . 
I 5 HOH   2   302 88  HOH   HOH A . 
I 5 HOH   3   303 319 HOH   HOH A . 
I 5 HOH   4   304 86  HOH   HOH A . 
I 5 HOH   5   305 193 HOH   HOH A . 
I 5 HOH   6   306 267 HOH   HOH A . 
I 5 HOH   7   307 209 HOH   HOH A . 
I 5 HOH   8   308 314 HOH   HOH A . 
I 5 HOH   9   309 253 HOH   HOH A . 
I 5 HOH   10  310 122 HOH   HOH A . 
I 5 HOH   11  311 4   HOH   HOH A . 
I 5 HOH   12  312 116 HOH   HOH A . 
I 5 HOH   13  313 169 HOH   HOH A . 
I 5 HOH   14  314 316 HOH   HOH A . 
I 5 HOH   15  315 320 HOH   HOH A . 
I 5 HOH   16  316 180 HOH   HOH A . 
I 5 HOH   17  317 156 HOH   HOH A . 
I 5 HOH   18  318 354 HOH   HOH A . 
I 5 HOH   19  319 295 HOH   HOH A . 
I 5 HOH   20  320 95  HOH   HOH A . 
I 5 HOH   21  321 12  HOH   HOH A . 
I 5 HOH   22  322 128 HOH   HOH A . 
I 5 HOH   23  323 336 HOH   HOH A . 
I 5 HOH   24  324 195 HOH   HOH A . 
I 5 HOH   25  325 333 HOH   HOH A . 
I 5 HOH   26  326 163 HOH   HOH A . 
I 5 HOH   27  327 99  HOH   HOH A . 
I 5 HOH   28  328 131 HOH   HOH A . 
I 5 HOH   29  329 37  HOH   HOH A . 
I 5 HOH   30  330 308 HOH   HOH A . 
I 5 HOH   31  331 276 HOH   HOH A . 
I 5 HOH   32  332 312 HOH   HOH A . 
I 5 HOH   33  333 93  HOH   HOH A . 
I 5 HOH   34  334 35  HOH   HOH A . 
I 5 HOH   35  335 133 HOH   HOH A . 
I 5 HOH   36  336 10  HOH   HOH A . 
I 5 HOH   37  337 250 HOH   HOH A . 
I 5 HOH   38  338 77  HOH   HOH A . 
I 5 HOH   39  339 318 HOH   HOH A . 
I 5 HOH   40  340 52  HOH   HOH A . 
I 5 HOH   41  341 45  HOH   HOH A . 
I 5 HOH   42  342 259 HOH   HOH A . 
I 5 HOH   43  343 79  HOH   HOH A . 
I 5 HOH   44  344 7   HOH   HOH A . 
I 5 HOH   45  345 330 HOH   HOH A . 
I 5 HOH   46  346 118 HOH   HOH A . 
I 5 HOH   47  347 243 HOH   HOH A . 
I 5 HOH   48  348 141 HOH   HOH A . 
I 5 HOH   49  349 2   HOH   HOH A . 
I 5 HOH   50  350 59  HOH   HOH A . 
I 5 HOH   51  351 121 HOH   HOH A . 
I 5 HOH   52  352 326 HOH   HOH A . 
I 5 HOH   53  353 103 HOH   HOH A . 
I 5 HOH   54  354 240 HOH   HOH A . 
I 5 HOH   55  355 332 HOH   HOH A . 
I 5 HOH   56  356 154 HOH   HOH A . 
I 5 HOH   57  357 8   HOH   HOH A . 
I 5 HOH   58  358 204 HOH   HOH A . 
I 5 HOH   59  359 235 HOH   HOH A . 
I 5 HOH   60  360 33  HOH   HOH A . 
I 5 HOH   61  361 96  HOH   HOH A . 
I 5 HOH   62  362 41  HOH   HOH A . 
I 5 HOH   63  363 20  HOH   HOH A . 
I 5 HOH   64  364 140 HOH   HOH A . 
I 5 HOH   65  365 30  HOH   HOH A . 
I 5 HOH   66  366 149 HOH   HOH A . 
I 5 HOH   67  367 31  HOH   HOH A . 
I 5 HOH   68  368 65  HOH   HOH A . 
I 5 HOH   69  369 237 HOH   HOH A . 
I 5 HOH   70  370 231 HOH   HOH A . 
I 5 HOH   71  371 25  HOH   HOH A . 
I 5 HOH   72  372 210 HOH   HOH A . 
I 5 HOH   73  373 66  HOH   HOH A . 
I 5 HOH   74  374 58  HOH   HOH A . 
I 5 HOH   75  375 76  HOH   HOH A . 
I 5 HOH   76  376 170 HOH   HOH A . 
I 5 HOH   77  377 81  HOH   HOH A . 
I 5 HOH   78  378 1   HOH   HOH A . 
I 5 HOH   79  379 315 HOH   HOH A . 
I 5 HOH   80  380 217 HOH   HOH A . 
I 5 HOH   81  381 282 HOH   HOH A . 
I 5 HOH   82  382 100 HOH   HOH A . 
I 5 HOH   83  383 278 HOH   HOH A . 
I 5 HOH   84  384 57  HOH   HOH A . 
I 5 HOH   85  385 168 HOH   HOH A . 
I 5 HOH   86  386 36  HOH   HOH A . 
I 5 HOH   87  387 68  HOH   HOH A . 
I 5 HOH   88  388 60  HOH   HOH A . 
I 5 HOH   89  389 186 HOH   HOH A . 
I 5 HOH   90  390 82  HOH   HOH A . 
I 5 HOH   91  391 211 HOH   HOH A . 
I 5 HOH   92  392 152 HOH   HOH A . 
I 5 HOH   93  393 6   HOH   HOH A . 
I 5 HOH   94  394 256 HOH   HOH A . 
I 5 HOH   95  395 91  HOH   HOH A . 
I 5 HOH   96  396 183 HOH   HOH A . 
I 5 HOH   97  397 344 HOH   HOH A . 
I 5 HOH   98  398 287 HOH   HOH A . 
I 5 HOH   99  399 273 HOH   HOH A . 
I 5 HOH   100 400 23  HOH   HOH A . 
I 5 HOH   101 401 340 HOH   HOH A . 
I 5 HOH   102 402 234 HOH   HOH A . 
I 5 HOH   103 403 192 HOH   HOH A . 
I 5 HOH   104 404 264 HOH   HOH A . 
I 5 HOH   105 405 205 HOH   HOH A . 
I 5 HOH   106 406 42  HOH   HOH A . 
I 5 HOH   107 407 223 HOH   HOH A . 
I 5 HOH   108 408 94  HOH   HOH A . 
I 5 HOH   109 409 123 HOH   HOH A . 
I 5 HOH   110 410 177 HOH   HOH A . 
I 5 HOH   111 411 255 HOH   HOH A . 
I 5 HOH   112 412 160 HOH   HOH A . 
I 5 HOH   113 413 347 HOH   HOH A . 
I 5 HOH   114 414 260 HOH   HOH A . 
I 5 HOH   115 415 201 HOH   HOH A . 
I 5 HOH   116 416 87  HOH   HOH A . 
I 5 HOH   117 417 61  HOH   HOH A . 
I 5 HOH   118 418 46  HOH   HOH A . 
I 5 HOH   119 419 236 HOH   HOH A . 
I 5 HOH   120 420 85  HOH   HOH A . 
I 5 HOH   121 421 75  HOH   HOH A . 
I 5 HOH   122 422 233 HOH   HOH A . 
I 5 HOH   123 423 83  HOH   HOH A . 
I 5 HOH   124 424 67  HOH   HOH A . 
I 5 HOH   125 425 241 HOH   HOH A . 
I 5 HOH   126 426 26  HOH   HOH A . 
I 5 HOH   127 427 74  HOH   HOH A . 
I 5 HOH   128 428 73  HOH   HOH A . 
I 5 HOH   129 429 191 HOH   HOH A . 
I 5 HOH   130 430 40  HOH   HOH A . 
I 5 HOH   131 431 331 HOH   HOH A . 
I 5 HOH   132 432 323 HOH   HOH A . 
I 5 HOH   133 433 327 HOH   HOH A . 
I 5 HOH   134 434 227 HOH   HOH A . 
I 5 HOH   135 435 300 HOH   HOH A . 
I 5 HOH   136 436 248 HOH   HOH A . 
I 5 HOH   137 437 284 HOH   HOH A . 
I 5 HOH   138 438 307 HOH   HOH A . 
I 5 HOH   139 439 311 HOH   HOH A . 
I 5 HOH   140 440 135 HOH   HOH A . 
I 5 HOH   141 441 110 HOH   HOH A . 
I 5 HOH   142 442 279 HOH   HOH A . 
I 5 HOH   143 443 288 HOH   HOH A . 
I 5 HOH   144 444 178 HOH   HOH A . 
I 5 HOH   145 445 198 HOH   HOH A . 
I 5 HOH   146 446 309 HOH   HOH A . 
I 5 HOH   147 447 266 HOH   HOH A . 
I 5 HOH   148 448 306 HOH   HOH A . 
I 5 HOH   149 449 214 HOH   HOH A . 
I 5 HOH   150 450 167 HOH   HOH A . 
I 5 HOH   151 451 215 HOH   HOH A . 
I 5 HOH   152 452 358 HOH   HOH A . 
I 5 HOH   153 453 341 HOH   HOH A . 
I 5 HOH   154 454 194 HOH   HOH A . 
I 5 HOH   155 455 329 HOH   HOH A . 
I 5 HOH   156 456 290 HOH   HOH A . 
I 5 HOH   157 457 356 HOH   HOH A . 
I 5 HOH   158 458 254 HOH   HOH A . 
I 5 HOH   159 459 148 HOH   HOH A . 
I 5 HOH   160 460 283 HOH   HOH A . 
I 5 HOH   161 461 286 HOH   HOH A . 
I 5 HOH   162 462 324 HOH   HOH A . 
I 5 HOH   163 463 265 HOH   HOH A . 
I 5 HOH   164 464 232 HOH   HOH A . 
I 5 HOH   165 465 114 HOH   HOH A . 
I 5 HOH   166 466 230 HOH   HOH A . 
I 5 HOH   167 467 302 HOH   HOH A . 
I 5 HOH   168 468 305 HOH   HOH A . 
J 5 HOH   1   301 338 HOH   HOH C . 
J 5 HOH   2   302 159 HOH   HOH C . 
J 5 HOH   3   303 143 HOH   HOH C . 
J 5 HOH   4   304 285 HOH   HOH C . 
J 5 HOH   5   305 238 HOH   HOH C . 
J 5 HOH   6   306 136 HOH   HOH C . 
J 5 HOH   7   307 334 HOH   HOH C . 
J 5 HOH   8   308 109 HOH   HOH C . 
J 5 HOH   9   309 353 HOH   HOH C . 
J 5 HOH   10  310 296 HOH   HOH C . 
J 5 HOH   11  311 64  HOH   HOH C . 
J 5 HOH   12  312 80  HOH   HOH C . 
J 5 HOH   13  313 108 HOH   HOH C . 
J 5 HOH   14  314 44  HOH   HOH C . 
J 5 HOH   15  315 22  HOH   HOH C . 
J 5 HOH   16  316 343 HOH   HOH C . 
J 5 HOH   17  317 13  HOH   HOH C . 
J 5 HOH   18  318 72  HOH   HOH C . 
J 5 HOH   19  319 107 HOH   HOH C . 
J 5 HOH   20  320 147 HOH   HOH C . 
J 5 HOH   21  321 89  HOH   HOH C . 
J 5 HOH   22  322 69  HOH   HOH C . 
J 5 HOH   23  323 102 HOH   HOH C . 
J 5 HOH   24  324 153 HOH   HOH C . 
J 5 HOH   25  325 162 HOH   HOH C . 
J 5 HOH   26  326 164 HOH   HOH C . 
J 5 HOH   27  327 127 HOH   HOH C . 
J 5 HOH   28  328 219 HOH   HOH C . 
J 5 HOH   29  329 275 HOH   HOH C . 
J 5 HOH   30  330 200 HOH   HOH C . 
J 5 HOH   31  331 27  HOH   HOH C . 
J 5 HOH   32  332 289 HOH   HOH C . 
J 5 HOH   33  333 18  HOH   HOH C . 
J 5 HOH   34  334 251 HOH   HOH C . 
J 5 HOH   35  335 351 HOH   HOH C . 
J 5 HOH   36  336 101 HOH   HOH C . 
J 5 HOH   37  337 184 HOH   HOH C . 
J 5 HOH   38  338 43  HOH   HOH C . 
J 5 HOH   39  339 225 HOH   HOH C . 
J 5 HOH   40  340 84  HOH   HOH C . 
J 5 HOH   41  341 29  HOH   HOH C . 
J 5 HOH   42  342 321 HOH   HOH C . 
J 5 HOH   43  343 165 HOH   HOH C . 
J 5 HOH   44  344 151 HOH   HOH C . 
J 5 HOH   45  345 172 HOH   HOH C . 
J 5 HOH   46  346 53  HOH   HOH C . 
J 5 HOH   47  347 173 HOH   HOH C . 
J 5 HOH   48  348 113 HOH   HOH C . 
J 5 HOH   49  349 182 HOH   HOH C . 
J 5 HOH   50  350 120 HOH   HOH C . 
J 5 HOH   51  351 138 HOH   HOH C . 
J 5 HOH   52  352 70  HOH   HOH C . 
J 5 HOH   53  353 129 HOH   HOH C . 
J 5 HOH   54  354 229 HOH   HOH C . 
J 5 HOH   55  355 281 HOH   HOH C . 
J 5 HOH   56  356 106 HOH   HOH C . 
J 5 HOH   57  357 5   HOH   HOH C . 
J 5 HOH   58  358 62  HOH   HOH C . 
J 5 HOH   59  359 132 HOH   HOH C . 
J 5 HOH   60  360 272 HOH   HOH C . 
J 5 HOH   61  361 208 HOH   HOH C . 
J 5 HOH   62  362 50  HOH   HOH C . 
J 5 HOH   63  363 21  HOH   HOH C . 
J 5 HOH   64  364 337 HOH   HOH C . 
J 5 HOH   65  365 48  HOH   HOH C . 
J 5 HOH   66  366 90  HOH   HOH C . 
J 5 HOH   67  367 175 HOH   HOH C . 
J 5 HOH   68  368 139 HOH   HOH C . 
J 5 HOH   69  369 197 HOH   HOH C . 
J 5 HOH   70  370 166 HOH   HOH C . 
J 5 HOH   71  371 348 HOH   HOH C . 
J 5 HOH   72  372 144 HOH   HOH C . 
J 5 HOH   73  373 11  HOH   HOH C . 
J 5 HOH   74  374 28  HOH   HOH C . 
J 5 HOH   75  375 145 HOH   HOH C . 
J 5 HOH   76  376 313 HOH   HOH C . 
J 5 HOH   77  377 335 HOH   HOH C . 
J 5 HOH   78  378 34  HOH   HOH C . 
J 5 HOH   79  379 185 HOH   HOH C . 
J 5 HOH   80  380 14  HOH   HOH C . 
J 5 HOH   81  381 98  HOH   HOH C . 
J 5 HOH   82  382 3   HOH   HOH C . 
J 5 HOH   83  383 310 HOH   HOH C . 
J 5 HOH   84  384 19  HOH   HOH C . 
J 5 HOH   85  385 342 HOH   HOH C . 
J 5 HOH   86  386 32  HOH   HOH C . 
J 5 HOH   87  387 111 HOH   HOH C . 
J 5 HOH   88  388 137 HOH   HOH C . 
J 5 HOH   89  389 9   HOH   HOH C . 
J 5 HOH   90  390 339 HOH   HOH C . 
J 5 HOH   91  391 134 HOH   HOH C . 
J 5 HOH   92  392 158 HOH   HOH C . 
J 5 HOH   93  393 292 HOH   HOH C . 
J 5 HOH   94  394 216 HOH   HOH C . 
J 5 HOH   95  395 271 HOH   HOH C . 
J 5 HOH   96  396 161 HOH   HOH C . 
J 5 HOH   97  397 54  HOH   HOH C . 
J 5 HOH   98  398 130 HOH   HOH C . 
J 5 HOH   99  399 104 HOH   HOH C . 
J 5 HOH   100 400 242 HOH   HOH C . 
J 5 HOH   101 401 51  HOH   HOH C . 
J 5 HOH   102 402 202 HOH   HOH C . 
J 5 HOH   103 403 24  HOH   HOH C . 
J 5 HOH   104 404 119 HOH   HOH C . 
J 5 HOH   105 405 15  HOH   HOH C . 
J 5 HOH   106 406 16  HOH   HOH C . 
J 5 HOH   107 407 124 HOH   HOH C . 
J 5 HOH   108 408 71  HOH   HOH C . 
J 5 HOH   109 409 126 HOH   HOH C . 
J 5 HOH   110 410 220 HOH   HOH C . 
J 5 HOH   111 411 125 HOH   HOH C . 
J 5 HOH   112 412 207 HOH   HOH C . 
J 5 HOH   113 413 63  HOH   HOH C . 
J 5 HOH   114 414 355 HOH   HOH C . 
J 5 HOH   115 415 277 HOH   HOH C . 
J 5 HOH   116 416 199 HOH   HOH C . 
J 5 HOH   117 417 97  HOH   HOH C . 
J 5 HOH   118 418 299 HOH   HOH C . 
J 5 HOH   119 419 105 HOH   HOH C . 
J 5 HOH   120 420 212 HOH   HOH C . 
J 5 HOH   121 421 179 HOH   HOH C . 
J 5 HOH   122 422 78  HOH   HOH C . 
J 5 HOH   123 423 142 HOH   HOH C . 
J 5 HOH   124 424 56  HOH   HOH C . 
J 5 HOH   125 425 176 HOH   HOH C . 
J 5 HOH   126 426 221 HOH   HOH C . 
J 5 HOH   127 427 146 HOH   HOH C . 
J 5 HOH   128 428 352 HOH   HOH C . 
J 5 HOH   129 429 317 HOH   HOH C . 
J 5 HOH   130 430 38  HOH   HOH C . 
J 5 HOH   131 431 47  HOH   HOH C . 
J 5 HOH   132 432 17  HOH   HOH C . 
J 5 HOH   133 433 49  HOH   HOH C . 
J 5 HOH   134 434 228 HOH   HOH C . 
J 5 HOH   135 435 298 HOH   HOH C . 
J 5 HOH   136 436 249 HOH   HOH C . 
J 5 HOH   137 437 190 HOH   HOH C . 
J 5 HOH   138 438 218 HOH   HOH C . 
J 5 HOH   139 439 92  HOH   HOH C . 
J 5 HOH   140 440 112 HOH   HOH C . 
J 5 HOH   141 441 247 HOH   HOH C . 
J 5 HOH   142 442 115 HOH   HOH C . 
J 5 HOH   143 443 244 HOH   HOH C . 
J 5 HOH   144 444 239 HOH   HOH C . 
J 5 HOH   145 445 270 HOH   HOH C . 
J 5 HOH   146 446 222 HOH   HOH C . 
J 5 HOH   147 447 187 HOH   HOH C . 
J 5 HOH   148 448 325 HOH   HOH C . 
J 5 HOH   149 449 174 HOH   HOH C . 
J 5 HOH   150 450 291 HOH   HOH C . 
J 5 HOH   151 451 357 HOH   HOH C . 
J 5 HOH   152 452 359 HOH   HOH C . 
J 5 HOH   153 453 350 HOH   HOH C . 
J 5 HOH   154 454 303 HOH   HOH C . 
J 5 HOH   155 455 181 HOH   HOH C . 
J 5 HOH   156 456 322 HOH   HOH C . 
J 5 HOH   157 457 328 HOH   HOH C . 
J 5 HOH   158 458 280 HOH   HOH C . 
J 5 HOH   159 459 346 HOH   HOH C . 
J 5 HOH   160 460 117 HOH   HOH C . 
J 5 HOH   161 461 245 HOH   HOH C . 
J 5 HOH   162 462 226 HOH   HOH C . 
J 5 HOH   163 463 252 HOH   HOH C . 
J 5 HOH   164 464 196 HOH   HOH C . 
J 5 HOH   165 465 155 HOH   HOH C . 
J 5 HOH   166 466 349 HOH   HOH C . 
J 5 HOH   167 467 268 HOH   HOH C . 
J 5 HOH   168 468 293 HOH   HOH C . 
J 5 HOH   169 469 261 HOH   HOH C . 
J 5 HOH   170 470 257 HOH   HOH C . 
J 5 HOH   171 471 263 HOH   HOH C . 
J 5 HOH   172 472 269 HOH   HOH C . 
J 5 HOH   173 473 171 HOH   HOH C . 
J 5 HOH   174 474 297 HOH   HOH C . 
J 5 HOH   175 475 224 HOH   HOH C . 
J 5 HOH   176 476 304 HOH   HOH C . 
J 5 HOH   177 477 274 HOH   HOH C . 
J 5 HOH   178 478 258 HOH   HOH C . 
J 5 HOH   179 479 345 HOH   HOH C . 
J 5 HOH   180 480 188 HOH   HOH C . 
J 5 HOH   181 481 262 HOH   HOH C . 
J 5 HOH   182 482 150 HOH   HOH C . 
J 5 HOH   183 483 157 HOH   HOH C . 
J 5 HOH   184 484 301 HOH   HOH C . 
J 5 HOH   185 485 203 HOH   HOH C . 
J 5 HOH   186 486 294 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           7I3B 
_cell.length_a           86.490 
_cell.length_b           57.130 
_cell.length_c           64.740 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.70 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I3B 
_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          7I3B 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   50.95 
_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   2024-11-22 
_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                     7I3B 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             43.10 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   80682 
_reflns.percent_possible_obs         72.6 
_reflns.pdbx_Rmerge_I_obs            0.056 
_reflns.pdbx_netI_over_sigmaI        16.7 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.061 
_reflns.pdbx_Rpim_I_all              0.024 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     443477 
_reflns.pdbx_chi_squared             0.90 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.15 
_reflns_shell.d_res_low                   1.18 
_reflns_shell.number_measured_all         622 
_reflns_shell.number_unique_obs           604 
_reflns_shell.Rmerge_I_obs                0.638 
_reflns_shell.pdbx_chi_squared            0.00 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        7.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             0.938 
_reflns_shell.pdbx_Rpim_I_all             0.632 
_reflns_shell.pdbx_CC_half                0.657 
_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                                 7I3B 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     80642 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             16.50 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    72.4 
_refine.ls_R_factor_obs                          0.1848 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1841 
_refine.ls_R_factor_R_free                       0.1972 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.060 
_refine.ls_number_reflns_R_free                  4081 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.967 
_refine.B_iso_mean                               20.25 
_refine.aniso_B[1][1]                            -0.85060 
_refine.aniso_B[2][2]                            -0.67750 
_refine.aniso_B[3][3]                            1.52810 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.19460 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.045 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.045 
_refine.pdbx_overall_SU_R_Blow_DPI               0.048 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.047 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I3B 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2157 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             354 
_refine_hist.number_atoms_total               2545 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        16.50 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.014 ? 2.00  2278 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.16  ? 2.00  3108 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  768  '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  409  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2278 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.96  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.35 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  284  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  2056 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.15 
_refine_ls_shell.d_res_low                        1.20 
_refine_ls_shell.number_reflns_R_work             1519 
_refine_ls_shell.R_factor_R_work                  0.3378 
_refine_ls_shell.percent_reflns_obs               11.72 
_refine_ls_shell.R_factor_R_free                  0.3833 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.83 
_refine_ls_shell.number_reflns_R_free             94 
_refine_ls_shell.number_reflns_all                1613 
_refine_ls_shell.R_factor_all                     0.3404 
# 
_struct.entry_id                  7I3B 
_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-0034380-001 (A71EV2A-x3937)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I3B 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
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 7I3B A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I3B 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,F,I 
2 1 B,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 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P6  AA6 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P7  AA7 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P8  AA8 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P9  AA9 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P10 AB1 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P11 AB2 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 ? ? ? ? ? ? ? 2.358 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.309 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 G ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 G ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
# 
_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_555 104.8 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.9 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 104.6 ? 
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_555 101.9 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 118.5 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.9 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.5 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.3 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.9 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? G ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I3B 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    390 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    450 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14 ? ? -106.96 41.53 
2 1 ASN C 14 ? ? -105.11 40.49 
# 
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 14.6357 8.1957   14.4603 -0.0140 -0.0200 0.0002 0.0213 0.0017 0.0047 1.4555 0.8183 0.8974 0.9526  
-0.6432 -0.4596 0.0062 0.0629  0.1286 0.0500 0.0485 0.0274 -0.0650 -0.1078 -0.0547 
'X-RAY DIFFRACTION' 2 ? refined 25.6986 -20.1989 17.7079 -0.0202 -0.0157 0.0138 0.0115 0.0011 0.0196 0.6166 0.8587 0.3180 -0.2231 
-0.1452 -0.0469 0.0080 -0.0008 0.1096 0.0173 0.0344 0.0131 0.0398  -0.0041 -0.0424 
# 
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 ALA 147 ? B ALA 141 
7 1 Y 1 C MET 148 ? B MET 142 
8 1 Y 1 C GLU 149 ? B GLU 143 
9 1 Y 1 C GLN 150 ? B GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B1E N1   N  N N 1   
A1B1E C4   C  N N 2   
A1B1E C5   C  N N 3   
A1B1E C6   C  N S 4   
A1B1E C7   C  N N 5   
A1B1E C8   C  N N 6   
A1B1E C10  C  Y N 7   
A1B1E C13  C  Y N 8   
A1B1E O2   O  N N 9   
A1B1E C3   C  N N 10  
A1B1E N    N  N N 11  
A1B1E C2   C  N N 12  
A1B1E O1   O  N N 13  
A1B1E C1   C  N R 14  
A1B1E O    O  N N 15  
A1B1E C    C  N N 16  
A1B1E C9   C  Y N 17  
A1B1E N2   N  Y N 18  
A1B1E C12  C  Y N 19  
A1B1E C11  C  Y N 20  
A1B1E H12  H  N N 21  
A1B1E H11  H  N N 22  
A1B1E H7   H  N N 23  
A1B1E H8   H  N N 24  
A1B1E H9   H  N N 25  
A1B1E H10  H  N N 26  
A1B1E H1   H  N N 27  
A1B1E H13  H  N N 28  
A1B1E H14  H  N N 29  
A1B1E H15  H  N N 30  
A1B1E H18  H  N N 31  
A1B1E H5   H  N N 32  
A1B1E H6   H  N N 33  
A1B1E H    H  N N 34  
A1B1E H3   H  N N 35  
A1B1E H4   H  N N 36  
A1B1E H2   H  N N 37  
A1B1E H17  H  N N 38  
A1B1E H16  H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1B1E C   O    sing N N 1   
A1B1E O   C1   sing N N 2   
A1B1E C1  C2   sing N N 3   
A1B1E O1  C2   doub N N 4   
A1B1E C2  N    sing N N 5   
A1B1E N   C3   sing N N 6   
A1B1E C3  C4   sing N N 7   
A1B1E C4  C5   sing N N 8   
A1B1E C5  C6   sing N N 9   
A1B1E C6  C7   sing N N 10  
A1B1E N1  C7   sing N N 11  
A1B1E C7  O2   doub N N 12  
A1B1E C8  C6   sing N N 13  
A1B1E N   C8   sing N N 14  
A1B1E C9  C1   sing N N 15  
A1B1E C9  C10  doub Y N 16  
A1B1E C10 C11  sing Y N 17  
A1B1E C11 C12  doub Y N 18  
A1B1E C12 N2   sing Y N 19  
A1B1E N2  C13  doub Y N 20  
A1B1E C13 C9   sing Y N 21  
A1B1E N1  H12  sing N N 22  
A1B1E N1  H11  sing N N 23  
A1B1E C4  H7   sing N N 24  
A1B1E C4  H8   sing N N 25  
A1B1E C5  H9   sing N N 26  
A1B1E C5  H10  sing N N 27  
A1B1E C6  H1   sing N N 28  
A1B1E C8  H13  sing N N 29  
A1B1E C8  H14  sing N N 30  
A1B1E C10 H15  sing N N 31  
A1B1E C13 H18  sing N N 32  
A1B1E C3  H5   sing N N 33  
A1B1E C3  H6   sing N N 34  
A1B1E C1  H    sing N N 35  
A1B1E C   H3   sing N N 36  
A1B1E C   H4   sing N N 37  
A1B1E C   H2   sing N N 38  
A1B1E C12 H17  sing N N 39  
A1B1E C11 H16  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I3B 
_atom_sites.fract_transf_matrix[1][1]   0.011562 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000951 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017504 
_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]   0.015499 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.608 8.104   24.794 1.00 16.78  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.861 8.190   24.028 1.00 16.43  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.000 6.972   23.110 1.00 15.91  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.286 5.978   23.277 1.00 16.26  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.061 8.279   24.983 1.00 19.74  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.153 7.078   25.719 1.00 22.40  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.894 7.055   22.139 1.00 14.60  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.165 5.944   21.226 1.00 13.55  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.576 6.412   19.845 1.00 13.08  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.278 7.546   19.469 1.00 14.15  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.269 5.576   19.114 1.00 12.15  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.747 5.918   17.786 1.00 12.65  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.724 4.703   16.895 1.00 12.37  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.664 3.547   17.362 1.00 13.43  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.191 6.456   17.926 1.00 14.43  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.801 4.938   15.590 1.00 11.65  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.039 3.882   14.585 1.00 11.86  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.500 3.977   14.197 1.00 12.96  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 23.999 5.087   13.898 1.00 12.72  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.180 4.094   13.325 1.00 11.88  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.705 4.265   13.679 1.00 13.38  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.377 2.905   12.340 1.00 13.63  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.908 4.815   12.440 1.00 13.54  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.210 2.843   14.182 1.00 12.25  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.621 2.823   13.775 1.00 13.43  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.722 1.998   12.504 1.00 13.22  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.707 0.759   12.557 1.00 13.62  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.494 2.230   14.902 1.00 14.70  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.534 3.129   16.110 1.00 13.44  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.420 4.211   16.174 1.00 14.61  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.712 2.900   17.201 1.00 14.91  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.418 5.090   17.266 1.00 14.65  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.727 3.756   18.314 1.00 15.87  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.550 4.870   18.313 1.00 15.50  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.566 5.738   19.400 1.00 18.80  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.789 2.656   11.353 1.00 13.72  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.890 2.016   10.053 1.00 13.98  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.125 2.517   9.338  1.00 15.18  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.343 3.739   9.260  1.00 14.02  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.592 2.247   9.186  1.00 15.25  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.222 3.730   9.064  1.00 16.52  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.763 1.630   7.803  1.00 17.08  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.994 1.608   8.874  1.00 16.21  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.223 2.040   8.210  1.00 16.05  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.079 2.908   9.128  1.00 15.92  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.169 2.623   10.332 1.00 16.27  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.508 4.072   8.622  1.00 15.36  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.197 5.048   9.455  1.00 15.12  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.293 6.231   9.744  1.00 14.20  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.771 7.374   9.875  1.00 14.06  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.540 5.497   8.879  1.00 16.66  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.607 4.430   8.989  1.00 21.39  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.357 4.349   9.975  1.00 23.70  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.665 3.577   8.007  1.00 19.58  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.029 5.949   10.022 1.00 12.69  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.044 6.969   10.378 1.00 13.15  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.383 6.664   11.707 1.00 12.33  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.087 5.498   12.011 1.00 13.24  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.943 7.041   9.285  1.00 13.73  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.438 7.461   7.915  1.00 14.09  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.111 8.670   7.729  1.00 14.97  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.293 6.616   6.815  1.00 16.47  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.601 9.037   6.478  1.00 16.40  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.686 7.024   5.548  1.00 17.32  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.323 8.240   5.382  1.00 17.95  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.798 8.631   4.135  1.00 22.19  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.041 7.706   12.444 1.00 11.74  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.225 7.668   13.667 1.00 11.31  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.001 8.514   13.409 1.00 11.75  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.153 9.729   13.130 1.00 12.20  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.031 8.199   14.885 1.00 12.17  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.252 8.517   16.122 1.00 13.67  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.194 8.907   17.287 1.00 14.83  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.633 9.973   18.137 1.00 15.44  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.956 9.776   19.273 1.00 16.52  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.666 8.531   19.680 1.00 17.32  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.505 10.818  19.975 1.00 16.27  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.802 7.898   13.468 1.00 11.34  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.526 8.646   13.237 1.00 11.29  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.832 8.856   14.560 1.00 11.73  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.545 7.864   15.268 1.00 12.07  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.615 7.829   12.302 1.00 12.01  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.385 8.663   11.936 1.00 13.10  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.321 7.343   11.035 1.00 13.16  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.619 10.113  14.918 1.00 11.31  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 20.998 10.457  16.207 0.50 11.51  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.037 10.426  16.219 0.50 13.52  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.889 11.430  16.024 1.00 12.00  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.746 12.064  14.943 1.00 13.08  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.005 11.064  17.233 0.50 10.83  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.194 11.010  17.113 0.50 17.13  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.925 9.984   17.776 0.50 11.87  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.742 11.382  18.508 0.50 18.05  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.736 12.321  16.654 0.50 8.45   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.341 10.039  17.219 0.50 19.72  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.043 11.615  17.058 1.00 12.04  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.022 12.673  17.007 1.00 12.43  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.815 14.005  17.019 1.00 12.97  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.743 14.175  17.833 1.00 13.37  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.159 12.662  18.272 1.00 12.39  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.312 11.417  18.375 1.00 13.48  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.734 10.404  18.996 1.00 13.64  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.151 11.443  17.716 1.00 13.21  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.478 14.927  16.113 1.00 12.30  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.183 16.232  16.082 1.00 13.42  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.147 16.912  17.440 1.00 14.71  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.155 17.464  17.873 1.00 15.23  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.557 17.126  15.004 1.00 14.20  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.386 18.401  14.724 1.00 14.61  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.638 19.284  13.739 1.00 16.28  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.392 20.480  13.314 1.00 16.79  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.355 21.656  13.934 1.00 18.37  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.785 21.769  15.128 1.00 18.55  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 19.954 22.723  13.392 1.00 19.71  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.003 16.807  18.141 1.00 14.01  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 17.870 17.519  19.410 1.00 16.13  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.736 16.925  20.539 1.00 16.62  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 18.867 17.566  21.590 1.00 17.92  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.373 17.685  19.822 1.00 17.23  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.713 16.441  20.340 1.00 16.84  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.088 15.542  19.490 1.00 16.40  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.491 16.043  21.619 1.00 17.39  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.570 14.590  20.265 1.00 16.75  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.780 14.850  21.551 1.00 17.69  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.260 15.706  20.364 1.00 16.62  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.139 15.030  21.325 1.00 15.87  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.602 14.988  20.894 1.00 17.44  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.425 14.368  21.551 1.00 17.98  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.618 13.624  21.646 1.00 15.54  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.217 13.628  22.241 1.00 16.58  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.784 12.181  22.549 1.00 17.26  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.137 14.463  23.572 1.00 18.33  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 21.939 15.614  19.730 1.00 16.06  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.323 15.579  19.246 1.00 16.05  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.294 16.227  20.227 1.00 17.60  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 23.973 17.256  20.844 1.00 17.71  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.420 16.277  17.875 1.00 15.89  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.471 15.614  20.351 1.00 16.32  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.510 16.138  21.266 1.00 16.50  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.445 17.134  20.562 1.00 17.71  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.400 17.287  19.318 1.00 15.48  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.377 14.948  21.787 1.00 18.50  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.145 14.424  20.686 1.00 18.29  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.545 13.825  22.442 1.00 19.62  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.355 17.799  21.323 1.00 18.15  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.346 18.644  20.695 1.00 18.19  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.227 17.838  19.722 1.00 16.85  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.481 18.314  18.619 1.00 16.74  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.256 19.331  21.763 1.00 18.96  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.514 19.979  21.152 1.00 27.43  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.452 21.180  20.456 1.00 31.53  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.767 19.462  20.985 1.00 31.50  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.681 21.448  20.047 1.00 31.88  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.513 20.422  20.295 1.00 33.95  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.593 16.581  20.087 1.00 16.55  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.414 15.794  19.180 1.00 16.92  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.645 15.492  17.876 1.00 15.22  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.245 15.531  16.799 1.00 15.66  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.870 14.474  19.822 1.00 19.22  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.852 13.741  18.940 1.00 27.05  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 33.998 14.194  18.734 1.00 31.06  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.405 12.630  18.324 1.00 28.96  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.297 15.244  17.967 1.00 14.73  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.520 15.058  16.739 1.00 14.65  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.579 16.304  15.823 1.00 13.36  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.822 16.202  14.628 1.00 13.53  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.051 14.772  17.053 1.00 14.62  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.798 13.420  17.661 1.00 15.59  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.459 12.443  17.234 1.00 14.94  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 25.981 13.345  18.588 1.00 15.01  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.382 17.487  16.390 1.00 13.58  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.424 18.749  15.610 1.00 13.60  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.832 19.032  15.059 1.00 14.52  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 29.936 19.577  13.969 1.00 14.58  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 27.951 19.922  16.510 1.00 14.67  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.454 19.997  16.620 1.00 14.75  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.699 19.718  17.725 1.00 16.01  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.538 20.442  15.608 1.00 15.63  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.354 19.927  17.457 1.00 16.00  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.230 20.367  16.148 1.00 15.16  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.703 20.886  14.283 1.00 16.95  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.100 20.765  15.412 1.00 16.83  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.596 21.219  13.545 1.00 17.58  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.331 21.217  14.110 1.00 17.86  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.901 18.615  15.782 1.00 14.29  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.255 18.828  15.324 1.00 15.02  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.704 17.826  14.271 1.00 15.89  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.720 17.999  13.622 1.00 17.07  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.188 18.809  16.530 1.00 16.45  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.896 16.749  14.056 1.00 14.83  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.178 15.711  13.042 1.00 15.24  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.934 15.520  12.167 1.00 14.14  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.563 14.393  11.824 1.00 14.44  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.572 14.379  13.749 1.00 16.64  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 33.917 14.559  14.428 1.00 19.11  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 34.946 14.505  13.749 1.00 21.50  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 33.932 14.876  15.746 1.00 19.09  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.288 16.608  11.822 1.00 14.23  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 28.994 16.572  11.167 1.00 12.98  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.059 16.123  9.713  1.00 14.13  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.914 16.576  8.927  1.00 15.78  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.421 18.009  11.213 1.00 13.62  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.003 18.145  10.611 1.00 14.42  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 25.961 17.351  11.430 1.00 14.44  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.581 19.615  10.537 1.00 16.36  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.136 15.242  9.319  1.00 13.03  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 27.989 14.824  7.921  1.00 13.37  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.741 15.529  7.361  1.00 13.90  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.797 16.066  6.246  1.00 15.76  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.852 13.293  7.822  1.00 12.53  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.498 12.887  6.357  1.00 15.42  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.153 12.631  8.312  1.00 14.29  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.577 15.486  8.069  1.00 13.68  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.323 16.014  7.532  1.00 13.99  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.357 16.238  8.677  1.00 14.68  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.390 15.459  9.660  1.00 13.38  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.719 14.987  6.516  1.00 14.41  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.310 15.251  6.058  1.00 15.86  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.913 16.101  5.061  1.00 18.27  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.108 14.679  6.592  1.00 15.61  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.541 16.041  4.912  1.00 20.12  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.028 15.151  5.816  1.00 17.76  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.849 13.755  7.603  1.00 15.94  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.701 14.710  6.027  1.00 18.60  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.558 13.283  7.765  1.00 16.94  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.494 13.810  7.039  1.00 18.28  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.527 17.288  8.615  1.00 14.87  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.511 17.478  9.637  1.00 14.89  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.273 18.095  9.004  1.00 16.41  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.384 18.883  8.046  1.00 16.78  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.004 18.307  10.824 1.00 16.47  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.609 19.657  10.413 1.00 17.30  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.647 20.827  10.201 1.00 19.47  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 21.990 21.785  9.455  1.00 18.95  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.545 20.834  10.792 1.00 17.63  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.096 17.816  9.553  1.00 14.75  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.837 18.370  9.056  1.00 14.46  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.884 18.549  10.225 1.00 14.87  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.365 17.550  10.775 1.00 15.43  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.270 17.427  7.958  1.00 16.38  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.010 17.925  7.294  1.00 19.96  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.187 18.512  7.981  1.00 23.09  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.834 17.668  6.093  1.00 24.03  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.675 19.809  10.623 1.00 15.80  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.804 20.128  11.732 0.50 16.94  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.812 20.071  11.757 0.50 17.73  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.349 19.687  11.486 1.00 17.53  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.689 19.173  12.415 1.00 18.17  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 15.885 21.629  12.014 0.50 17.74  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 15.951 21.525  12.204 0.50 21.03  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 14.868 22.033  12.908 0.50 18.38  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.625 22.373  11.121 0.50 26.45  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 13.852 19.826  10.241 1.00 17.60  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.469 19.428  9.945  1.00 17.84  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.231 17.930  10.135 1.00 17.43  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.098 17.540  10.396 1.00 19.22  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.055 19.819  8.528  1.00 20.44  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.626 19.004  7.517  1.00 25.79  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.284 17.093  10.115 1.00 15.44  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.197 15.634  10.314 1.00 14.98  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.659 15.191  11.705 1.00 14.79  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.571 13.990  12.005 1.00 14.19  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.077 14.928  9.258  1.00 16.01  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.527 15.080  7.829  1.00 17.57  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.400 14.402  6.777  1.00 16.72  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.307 12.943  6.908  1.00 14.52  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.483 12.087  5.908  1.00 16.81  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.717 12.529  4.675  1.00 17.70  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.347 10.775  6.110  1.00 16.31  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.216 16.097  12.519 1.00 14.69  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 14.847 15.768  13.787 1.00 13.51  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.011 14.767  13.640 1.00 13.00  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.208 13.909  14.495 1.00 13.41  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 13.854 15.255  14.848 1.00 14.96  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.445 15.043  16.234 1.00 15.12  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.271 15.879  16.688 1.00 15.94  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.072 14.042  16.895 1.00 15.06  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.813 14.878  12.568 1.00 12.80  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 17.912 13.935  12.346 1.00 11.55  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.255 14.650  12.221 1.00 12.58  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.343 15.771  11.638 1.00 13.49  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.672 13.143  11.054 1.00 12.65  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.584 12.012  11.107 1.00 14.04  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.518 11.283  9.772  1.00 15.39  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 16.877 11.005  12.241 1.00 14.61  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.304 13.998  12.681 1.00 11.90  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.678 14.471  12.486 1.00 11.97  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.541 13.249  12.362 1.00 11.97  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.338 12.209  13.050 1.00 12.30  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.139 15.321  13.708 1.00 12.19  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.573 15.900  13.615 1.00 12.96  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.679 17.269  14.302 1.00 14.01  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.602 14.951  14.240 1.00 12.91  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.505 13.309  11.446 1.00 11.56  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.449 12.228  11.172 1.00 10.92  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.872 12.740  11.350 1.00 11.66  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.200 13.788  10.768 1.00 12.12  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.235 11.620  9.757  1.00 11.56  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.269 10.534  9.475  1.00 13.44  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.811 11.059  9.624  1.00 12.84  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.663 12.044  12.135 1.00 11.84  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.079 12.382  12.326 1.00 11.97  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 28.960 11.208  11.894 1.00 13.15  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.493 10.073  11.652 1.00 13.38  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.354 12.754  13.783 1.00 13.63  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.045 11.675  14.653 1.00 14.31  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.248 11.505  11.692 1.00 14.24  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.186 10.472  11.249 1.00 15.24  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.825 9.740   12.437 1.00 17.00  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 31.997 10.343  13.518 1.00 18.57  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.253 11.085  10.346 1.00 17.60  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 32.958 12.061  11.102 1.00 20.93  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.139 8.425   12.264 1.00 17.25  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.715 7.628   13.346 1.00 18.83  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.063 7.046   12.901 1.00 20.86  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.290 6.814   11.699 1.00 20.03  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.781 6.450   13.723 1.00 19.28  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.668 5.557   12.619 1.00 19.40  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.378 6.908   14.090 1.00 19.99  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 34.929 6.753   13.879 1.00 22.09  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.206 6.123   13.556 1.00 23.69  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 35.987 4.617   13.357 1.00 23.91  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.502 4.051   12.380 1.00 25.94  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.256 6.458   14.634 1.00 27.06  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.734 6.073   15.893 1.00 31.63  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.556 7.928   14.684 1.00 27.40  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.187 3.989   14.232 1.00 23.61  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.915 2.546   14.081 1.00 24.63  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.678 2.245   13.191 1.00 23.04  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.741 3.041   13.149 1.00 21.95  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.699 1.910   15.444 1.00 27.73  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.665 1.108   12.495 1.00 21.89  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.542 0.693   11.653 1.00 22.39  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.443 0.101   12.493 1.00 21.96  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.720 -0.663  13.423 1.00 23.31  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 32.977 -0.316  10.588 1.00 24.22  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.898 0.309   9.514  1.00 30.48  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.234 -0.723  8.475  1.00 37.30  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.056 -1.626  8.704  1.00 37.70  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.556 -0.643  7.333  1.00 39.48  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.202 0.471   12.173 1.00 18.36  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.027 -0.027  12.869 1.00 18.28  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.434 -1.295  12.293 1.00 16.61  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.735 -1.678  11.156 1.00 18.25  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.494 -1.893  13.077 1.00 16.04  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.883 -3.175  12.718 1.00 17.21  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.432 -3.136  12.272 1.00 16.54  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.885 -4.182  11.865 1.00 16.71  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.041 -4.192  13.848 1.00 17.93  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.743 -4.622  14.210 1.00 21.59  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.784 -1.995  12.393 1.00 15.11  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.391 -1.899  11.964 1.00 14.07  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.321 -1.817  10.438 1.00 15.14  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.213 -1.248  9.787  1.00 17.00  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.767 -0.639  12.572 1.00 13.28  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.649 -0.688  14.085 1.00 14.54  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.288 -1.796  14.628 1.00 15.05  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.845 0.368   14.731 1.00 15.18  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.285 -2.387  9.869  1.00 15.72  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 22.018 -2.285  8.415  1.00 17.12  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.680 -1.577  8.245  1.00 16.17  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.764 -1.750  9.060  1.00 17.21  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 22.010 -3.628  7.740  1.00 21.60  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 20.967 -4.376  8.294  1.00 26.25  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 23.358 -4.363  7.933  1.00 22.86  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.578 -0.741  7.221  1.00 15.80  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.355 0.006   6.986  1.00 14.42  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.389 -0.767  6.098  1.00 14.93  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.782 -1.302  5.032  1.00 15.51  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.671 1.398   6.368  1.00 14.06  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.767 2.167   7.133  1.00 15.23  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.398 2.262   6.211  1.00 14.20  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.399 2.461   8.659  1.00 16.02  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.121 -0.790  6.480  1.00 13.19  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 16.043 -1.404  5.690  1.00 13.65  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.799 -0.548  4.423  1.00 14.69  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.791 0.697   4.458  1.00 14.79  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.762 -1.444  6.494  1.00 13.60  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.580 -1.240  3.286  1.00 16.64  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.259 -0.559  2.031  1.00 18.02  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.976 -1.267  1.546  1.00 20.08  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 14.020 -2.219  0.756  1.00 21.12  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.449 -0.665  1.026  1.00 18.87  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.776 -0.098  1.547  1.00 18.44  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.751 1.412   1.817  1.00 16.64  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.068 1.881   2.304  1.00 16.39  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.261 3.039   2.920  1.00 17.44  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.261 3.894   3.067  1.00 16.23  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.464 3.350   3.414  1.00 19.08  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.849 -0.748  1.990  1.00 19.10  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.546 -1.413  1.860  1.00 19.86  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.392 -0.428  2.137  1.00 20.75  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.545 0.713   2.534  1.00 22.81  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.517 -2.552  2.876  1.00 18.73  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.410 -1.964  4.601  1.00 18.64  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 9.123  -0.982  2.041  1.00 24.07  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.906  -0.241  2.332  1.00 27.06  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.147  -0.921  3.508  1.00 25.87  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.918  -0.809  3.599  1.00 26.07  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 7.010  -0.249  1.061  1.00 34.30  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 5.844  0.713   1.044  1.00 45.61  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 5.072  0.692   0.051  1.00 47.74  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.679  1.472   2.036  1.00 51.21  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.855  -1.622  4.429  1.00 22.41  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.174  -2.234  5.598  1.00 19.92  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.426  -1.189  6.403  1.00 20.33  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.871  -0.039  6.569  1.00 20.68  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.183  -2.957  6.490  1.00 19.71  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.883  -4.502  5.822  1.00 20.69  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.260  -1.597  6.927  1.00 17.49  ? 59  GLN   A N   1 
ATOM   411  C  CA  A GLN   A 1 53  ? 4.425  -0.803  7.855  0.50 16.96  ? 59  GLN   A CA  1 
ATOM   412  C  CA  B GLN   A 1 53  ? 4.537  -0.753  7.813  0.50 17.41  ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.215  -1.548  9.145  1.00 15.50  ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.376  -1.163  9.940  1.00 15.89  ? 59  GLN   A O   1 
ATOM   415  C  CB  A GLN   A 1 53  ? 3.044  -0.329  7.315  0.50 17.49  ? 59  GLN   A CB  1 
ATOM   416  C  CB  B GLN   A 1 53  ? 3.393  -0.094  7.026  0.50 19.16  ? 59  GLN   A CB  1 
ATOM   417  C  CG  A GLN   A 1 53  ? 3.084  0.921   6.379  0.50 16.79  ? 59  GLN   A CG  1 
ATOM   418  C  CG  B GLN   A 1 53  ? 3.936  0.727   5.769  0.50 18.18  ? 59  GLN   A CG  1 
ATOM   419  C  CD  A GLN   A 1 53  ? 1.709  1.476   6.028  0.50 18.91  ? 59  GLN   A CD  1 
ATOM   420  C  CD  B GLN   A 1 53  ? 4.952  1.820   6.169  0.50 19.45  ? 59  GLN   A CD  1 
ATOM   421  O  OE1 A GLN   A 1 53  ? 1.202  1.278   4.918  0.50 21.65  ? 59  GLN   A OE1 1 
ATOM   422  O  OE1 B GLN   A 1 53  ? 5.967  2.179   5.476  0.50 17.17  ? 59  GLN   A OE1 1 
ATOM   423  N  NE2 A GLN   A 1 53  ? 1.067  2.172   6.959  0.50 17.44  ? 59  GLN   A NE2 1 
ATOM   424  N  NE2 B GLN   A 1 53  ? 4.721  2.386   7.339  0.50 20.00  ? 59  GLN   A NE2 1 
ATOM   425  N  N   . THR   A 1 54  ? 4.958  -2.657  9.383  1.00 14.09  ? 60  THR   A N   1 
ATOM   426  C  CA  . THR   A 1 54  ? 4.953  -3.380  10.643 1.00 14.84  ? 60  THR   A CA  1 
ATOM   427  C  C   . THR   A 1 54  ? 6.417  -3.640  11.048 1.00 14.18  ? 60  THR   A C   1 
ATOM   428  O  O   . THR   A 1 54  ? 7.288  -3.841  10.199 1.00 16.00  ? 60  THR   A O   1 
ATOM   429  C  CB  . THR   A 1 54  ? 4.172  -4.653  10.642 1.00 17.08  ? 60  THR   A CB  1 
ATOM   430  O  OG1 . THR   A 1 54  ? 4.785  -5.588  9.795  1.00 23.58  ? 60  THR   A OG1 1 
ATOM   431  C  CG2 . THR   A 1 54  ? 2.749  -4.479  10.227 1.00 17.65  ? 60  THR   A CG2 1 
ATOM   432  N  N   . GLY   A 1 55  ? 6.675  -3.556  12.326 1.00 12.66  ? 61  GLY   A N   1 
ATOM   433  C  CA  . GLY   A 1 55  ? 8.040  -3.755  12.819 1.00 12.43  ? 61  GLY   A CA  1 
ATOM   434  C  C   . GLY   A 1 55  ? 8.046  -3.788  14.326 1.00 11.86  ? 61  GLY   A C   1 
ATOM   435  O  O   . GLY   A 1 55  ? 7.022  -4.024  14.962 1.00 12.29  ? 61  GLY   A O   1 
ATOM   436  N  N   . VAL   A 1 56  ? 9.243  -3.590  14.931 1.00 10.66  ? 62  VAL   A N   1 
ATOM   437  C  CA  . VAL   A 1 56  ? 9.395  -3.672  16.388 1.00 10.98  ? 62  VAL   A CA  1 
ATOM   438  C  C   . VAL   A 1 56  ? 10.260 -2.512  16.813 1.00 10.61  ? 62  VAL   A C   1 
ATOM   439  O  O   . VAL   A 1 56  ? 11.257 -2.214  16.145 1.00 11.80  ? 62  VAL   A O   1 
ATOM   440  C  CB  . VAL   A 1 56  ? 10.089 -5.023  16.726 1.00 12.58  ? 62  VAL   A CB  1 
ATOM   441  C  CG1 . VAL   A 1 56  ? 10.469 -5.107  18.192 1.00 14.79  ? 62  VAL   A CG1 1 
ATOM   442  C  CG2 . VAL   A 1 56  ? 9.184  -6.223  16.367 1.00 12.58  ? 62  VAL   A CG2 1 
ATOM   443  N  N   . TYR   A 1 57  ? 9.890  -1.849  17.914 1.00 10.95  ? 63  TYR   A N   1 
ATOM   444  C  CA  . TYR   A 1 57  ? 10.748 -0.758  18.395 1.00 10.50  ? 63  TYR   A CA  1 
ATOM   445  C  C   . TYR   A 1 57  ? 11.197 -0.964  19.841 1.00 10.49  ? 63  TYR   A C   1 
ATOM   446  O  O   . TYR   A 1 57  ? 10.490 -1.572  20.641 1.00 11.79  ? 63  TYR   A O   1 
ATOM   447  C  CB  . TYR   A 1 57  ? 10.086 0.649   18.267 1.00 10.95  ? 63  TYR   A CB  1 
ATOM   448  C  CG  . TYR   A 1 57  ? 9.101  1.059   19.347 1.00 10.72  ? 63  TYR   A CG  1 
ATOM   449  C  CD1 . TYR   A 1 57  ? 7.813  0.536   19.371 1.00 11.49  ? 63  TYR   A CD1 1 
ATOM   450  C  CD2 . TYR   A 1 57  ? 9.458  1.960   20.337 1.00 11.67  ? 63  TYR   A CD2 1 
ATOM   451  C  CE1 . TYR   A 1 57  ? 6.904  0.884   20.374 1.00 13.20  ? 63  TYR   A CE1 1 
ATOM   452  C  CE2 . TYR   A 1 57  ? 8.553  2.319   21.349 1.00 12.25  ? 63  TYR   A CE2 1 
ATOM   453  C  CZ  . TYR   A 1 57  ? 7.281  1.784   21.337 1.00 13.72  ? 63  TYR   A CZ  1 
ATOM   454  O  OH  . TYR   A 1 57  ? 6.364  2.118   22.319 1.00 15.69  ? 63  TYR   A OH  1 
ATOM   455  N  N   . TYR   A 1 58  ? 12.320 -0.351  20.214 1.00 10.35  ? 64  TYR   A N   1 
ATOM   456  C  CA  . TYR   A 1 58  ? 12.791 -0.376  21.604 1.00 11.50  ? 64  TYR   A CA  1 
ATOM   457  C  C   . TYR   A 1 58  ? 12.330 0.838   22.404 1.00 10.78  ? 64  TYR   A C   1 
ATOM   458  O  O   . TYR   A 1 58  ? 12.552 1.990   22.022 1.00 10.90  ? 64  TYR   A O   1 
ATOM   459  C  CB  . TYR   A 1 58  ? 14.350 -0.462  21.658 1.00 12.52  ? 64  TYR   A CB  1 
ATOM   460  C  CG  . TYR   A 1 58  ? 14.817 -0.593  23.080 1.00 12.84  ? 64  TYR   A CG  1 
ATOM   461  C  CD1 . TYR   A 1 58  ? 14.504 -1.710  23.823 1.00 13.15  ? 64  TYR   A CD1 1 
ATOM   462  C  CD2 . TYR   A 1 58  ? 15.551 0.425   23.693 1.00 13.04  ? 64  TYR   A CD2 1 
ATOM   463  C  CE1 . TYR   A 1 58  ? 14.887 -1.815  25.154 1.00 14.71  ? 64  TYR   A CE1 1 
ATOM   464  C  CE2 . TYR   A 1 58  ? 15.928 0.336   25.030 1.00 14.31  ? 64  TYR   A CE2 1 
ATOM   465  C  CZ  . TYR   A 1 58  ? 15.632 -0.810  25.730 1.00 14.57  ? 64  TYR   A CZ  1 
ATOM   466  O  OH  . TYR   A 1 58  ? 15.995 -0.927  27.073 1.00 16.42  ? 64  TYR   A OH  1 
ATOM   467  N  N   . CYS   A 1 59  ? 11.676 0.544   23.525 1.00 10.48  ? 65  CYS   A N   1 
ATOM   468  C  CA  . CYS   A 1 59  ? 11.157 1.551   24.464 1.00 12.17  ? 65  CYS   A CA  1 
ATOM   469  C  C   . CYS   A 1 59  ? 12.005 1.521   25.768 1.00 12.59  ? 65  CYS   A C   1 
ATOM   470  O  O   . CYS   A 1 59  ? 11.806 0.614   26.622 1.00 12.49  ? 65  CYS   A O   1 
ATOM   471  C  CB  . CYS   A 1 59  ? 9.703  1.232   24.753 1.00 13.03  ? 65  CYS   A CB  1 
ATOM   472  S  SG  . CYS   A 1 59  ? 8.974  2.353   26.010 1.00 13.12  ? 65  CYS   A SG  1 
ATOM   473  N  N   . SER   A 1 60  ? 12.922 2.486   25.954 1.00 12.37  ? 66  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 60  ? 13.804 2.482   27.128 1.00 13.36  ? 66  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 60  ? 13.096 2.666   28.458 1.00 13.33  ? 66  SER   A C   1 
ATOM   476  O  O   . SER   A 1 60  ? 13.507 2.041   29.433 1.00 14.58  ? 66  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 60  ? 14.912 3.514   26.959 1.00 15.87  ? 66  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 60  ? 14.464 4.847   27.062 1.00 18.27  ? 66  SER   A OG  1 
ATOM   479  N  N   . SER   A 1 61  ? 11.937 3.409   28.453 1.00 12.12  ? 67  SER   A N   1 
ATOM   480  C  CA  . SER   A 1 61  ? 11.164 3.619   29.675 1.00 13.29  ? 67  SER   A CA  1 
ATOM   481  C  C   . SER   A 1 61  ? 10.352 2.382   30.107 1.00 12.82  ? 67  SER   A C   1 
ATOM   482  O  O   . SER   A 1 61  ? 9.728  2.407   31.139 1.00 12.95  ? 67  SER   A O   1 
ATOM   483  C  CB  . SER   A 1 61  ? 10.274 4.839   29.510 1.00 14.04  ? 67  SER   A CB  1 
ATOM   484  O  OG  . SER   A 1 61  ? 9.254  4.590   28.570 1.00 13.31  ? 67  SER   A OG  1 
ATOM   485  N  N   . ARG   A 1 62  ? 10.419 1.286   29.323 1.00 12.39  ? 68  ARG   A N   1 
ATOM   486  C  CA  . ARG   A 1 62  ? 9.840  -0.007  29.688 1.00 13.15  ? 68  ARG   A CA  1 
ATOM   487  C  C   . ARG   A 1 62  ? 10.869 -1.128  29.652 1.00 14.75  ? 68  ARG   A C   1 
ATOM   488  O  O   . ARG   A 1 62  ? 10.526 -2.291  29.923 1.00 14.51  ? 68  ARG   A O   1 
ATOM   489  C  CB  . ARG   A 1 62  ? 8.652  -0.336  28.765 1.00 13.29  ? 68  ARG   A CB  1 
ATOM   490  C  CG  . ARG   A 1 62  ? 7.505  0.649   28.892 1.00 13.92  ? 68  ARG   A CG  1 
ATOM   491  C  CD  . ARG   A 1 62  ? 6.744  0.366   30.167 1.00 14.34  ? 68  ARG   A CD  1 
ATOM   492  N  NE  . ARG   A 1 62  ? 5.604  1.281   30.315 1.00 15.60  ? 68  ARG   A NE  1 
ATOM   493  C  CZ  . ARG   A 1 62  ? 5.642  2.443   30.964 1.00 14.50  ? 68  ARG   A CZ  1 
ATOM   494  N  NH1 . ARG   A 1 62  ? 6.782  2.868   31.540 1.00 15.98  ? 68  ARG   A NH1 1 
ATOM   495  N  NH2 . ARG   A 1 62  ? 4.532  3.189   31.080 1.00 16.42  ? 68  ARG   A NH2 1 
ATOM   496  N  N   . ARG   A 1 63  ? 12.098 -0.872  29.194 1.00 14.86  ? 69  ARG   A N   1 
ATOM   497  C  CA  . ARG   A 1 63  ? 13.073 -1.955  28.900 1.00 15.53  ? 69  ARG   A CA  1 
ATOM   498  C  C   . ARG   A 1 63  ? 12.438 -3.082  28.051 1.00 16.77  ? 69  ARG   A C   1 
ATOM   499  O  O   . ARG   A 1 63  ? 12.613 -4.291  28.314 1.00 18.25  ? 69  ARG   A O   1 
ATOM   500  C  CB  . ARG   A 1 63  ? 13.717 -2.561  30.154 1.00 18.26  ? 69  ARG   A CB  1 
ATOM   501  C  CG  . ARG   A 1 63  ? 14.684 -1.609  30.756 1.00 18.59  ? 69  ARG   A CG  1 
ATOM   502  C  CD  . ARG   A 1 63  ? 15.538 -2.422  31.747 1.00 19.43  ? 69  ARG   A CD  1 
ATOM   503  N  NE  . ARG   A 1 63  ? 16.300 -1.477  32.537 1.00 21.89  ? 69  ARG   A NE  1 
ATOM   504  C  CZ  . ARG   A 1 63  ? 15.982 -1.090  33.771 1.00 18.86  ? 69  ARG   A CZ  1 
ATOM   505  N  NH1 . ARG   A 1 63  ? 14.905 -1.590  34.385 1.00 20.10  ? 69  ARG   A NH1 1 
ATOM   506  N  NH2 . ARG   A 1 63  ? 16.743 -0.218  34.409 1.00 20.55  ? 69  ARG   A NH2 1 
ATOM   507  N  N   . LYS   A 1 64  ? 11.730 -2.683  27.021 1.00 14.41  ? 70  LYS   A N   1 
ATOM   508  C  CA  . LYS   A 1 64  ? 11.006 -3.664  26.218 1.00 15.10  ? 70  LYS   A CA  1 
ATOM   509  C  C   . LYS   A 1 64  ? 10.992 -3.277  24.778 1.00 14.35  ? 70  LYS   A C   1 
ATOM   510  O  O   . LYS   A 1 64  ? 10.913 -2.090  24.431 1.00 13.99  ? 70  LYS   A O   1 
ATOM   511  C  CB  . LYS   A 1 64  ? 9.544  -3.739  26.733 1.00 19.03  ? 70  LYS   A CB  1 
ATOM   512  C  CG  . LYS   A 1 64  ? 8.770  -5.004  26.285 1.00 29.66  ? 70  LYS   A CG  1 
ATOM   513  C  CD  . LYS   A 1 64  ? 7.750  -5.380  27.345 1.00 38.06  ? 70  LYS   A CD  1 
ATOM   514  C  CE  . LYS   A 1 64  ? 6.963  -6.625  26.959 1.00 43.36  ? 70  LYS   A CE  1 
ATOM   515  N  NZ  . LYS   A 1 64  ? 7.830  -7.725  26.435 1.00 44.46  ? 70  LYS   A NZ  1 
ATOM   516  N  N   . HIS   A 1 65  ? 10.970 -4.307  23.916 1.00 12.86  ? 71  HIS   A N   1 
ATOM   517  C  CA  . HIS   A 1 65  ? 10.743 -4.165  22.481 1.00 12.66  ? 71  HIS   A CA  1 
ATOM   518  C  C   . HIS   A 1 65  ? 9.282  -4.500  22.184 1.00 14.10  ? 71  HIS   A C   1 
ATOM   519  O  O   . HIS   A 1 65  ? 8.779  -5.554  22.594 1.00 17.36  ? 71  HIS   A O   1 
ATOM   520  C  CB  . HIS   A 1 65  ? 11.664 -5.120  21.678 1.00 11.79  ? 71  HIS   A CB  1 
ATOM   521  C  CG  . HIS   A 1 65  ? 13.121 -4.771  21.800 1.00 13.55  ? 71  HIS   A CG  1 
ATOM   522  N  ND1 . HIS   A 1 65  ? 13.840 -4.096  20.806 1.00 16.87  ? 71  HIS   A ND1 1 
ATOM   523  C  CD2 . HIS   A 1 65  ? 13.968 -5.093  22.796 1.00 12.03  ? 71  HIS   A CD2 1 
ATOM   524  C  CE1 . HIS   A 1 65  ? 15.111 -4.061  21.230 1.00 13.68  ? 71  HIS   A CE1 1 
ATOM   525  N  NE2 . HIS   A 1 65  ? 15.211 -4.612  22.421 1.00 16.14  ? 71  HIS   A NE2 1 
ATOM   526  N  N   . TYR   A 1 66  ? 8.587  -3.623  21.478 1.00 11.85  ? 72  TYR   A N   1 
ATOM   527  C  CA  . TYR   A 1 66  ? 7.166  -3.817  21.167 1.00 13.37  ? 72  TYR   A CA  1 
ATOM   528  C  C   . TYR   A 1 66  ? 6.918  -3.925  19.688 1.00 12.26  ? 72  TYR   A C   1 
ATOM   529  O  O   . TYR   A 1 66  ? 7.411  -3.098  18.932 1.00 12.18  ? 72  TYR   A O   1 
ATOM   530  C  CB  . TYR   A 1 66  ? 6.354  -2.556  21.665 1.00 13.45  ? 72  TYR   A CB  1 
ATOM   531  C  CG  . TYR   A 1 66  ? 6.286  -2.392  23.177 1.00 14.20  ? 72  TYR   A CG  1 
ATOM   532  C  CD1 . TYR   A 1 66  ? 5.461  -3.208  23.955 1.00 15.89  ? 72  TYR   A CD1 1 
ATOM   533  C  CD2 . TYR   A 1 66  ? 7.032  -1.421  23.817 1.00 14.54  ? 72  TYR   A CD2 1 
ATOM   534  C  CE1 . TYR   A 1 66  ? 5.339  -3.015  25.327 1.00 16.29  ? 72  TYR   A CE1 1 
ATOM   535  C  CE2 . TYR   A 1 66  ? 6.923  -1.214  25.196 1.00 15.35  ? 72  TYR   A CE2 1 
ATOM   536  C  CZ  . TYR   A 1 66  ? 6.081  -2.022  25.940 1.00 16.48  ? 72  TYR   A CZ  1 
ATOM   537  O  OH  . TYR   A 1 66  ? 5.999  -1.852  27.306 1.00 18.39  ? 72  TYR   A OH  1 
ATOM   538  N  N   . PRO   A 1 67  ? 6.098  -4.887  19.274 1.00 12.27  ? 73  PRO   A N   1 
ATOM   539  C  CA  . PRO   A 1 67  ? 5.664  -4.930  17.868 1.00 11.76  ? 73  PRO   A CA  1 
ATOM   540  C  C   . PRO   A 1 67  ? 4.621  -3.849  17.579 1.00 13.53  ? 73  PRO   A C   1 
ATOM   541  O  O   . PRO   A 1 67  ? 3.702  -3.662  18.402 1.00 15.63  ? 73  PRO   A O   1 
ATOM   542  C  CB  . PRO   A 1 67  ? 5.028  -6.327  17.699 1.00 13.87  ? 73  PRO   A CB  1 
ATOM   543  C  CG  . PRO   A 1 67  ? 4.641  -6.747  19.104 1.00 15.49  ? 73  PRO   A CG  1 
ATOM   544  C  CD  . PRO   A 1 67  ? 5.528  -5.995  20.092 1.00 13.00  ? 73  PRO   A CD  1 
ATOM   545  N  N   . VAL   A 1 68  ? 4.770  -3.190  16.469 1.00 12.64  ? 74  VAL   A N   1 
ATOM   546  C  CA  . VAL   A 1 68  ? 3.832  -2.110  16.086 1.00 14.01  ? 74  VAL   A CA  1 
ATOM   547  C  C   . VAL   A 1 68  ? 3.522  -2.095  14.633 1.00 12.59  ? 74  VAL   A C   1 
ATOM   548  O  O   . VAL   A 1 68  ? 4.316  -2.459  13.786 1.00 13.84  ? 74  VAL   A O   1 
ATOM   549  C  CB  . VAL   A 1 68  ? 4.406  -0.715  16.472 1.00 15.67  ? 74  VAL   A CB  1 
ATOM   550  C  CG1 . VAL   A 1 68  ? 4.368  -0.506  17.989 1.00 17.45  ? 74  VAL   A CG1 1 
ATOM   551  C  CG2 . VAL   A 1 68  ? 5.824  -0.507  15.933 1.00 16.21  ? 74  VAL   A CG2 1 
ATOM   552  N  N   . SER   A 1 69  ? 2.328  -1.541  14.314 1.00 13.67  ? 75  SER   A N   1 
ATOM   553  C  CA  A SER   A 1 69  ? 1.964  -1.134  12.950 0.50 14.15  ? 75  SER   A CA  1 
ATOM   554  C  CA  B SER   A 1 69  ? 1.888  -1.141  12.984 0.50 14.41  ? 75  SER   A CA  1 
ATOM   555  C  C   . SER   A 1 69  ? 2.170  0.372   12.912 1.00 13.94  ? 75  SER   A C   1 
ATOM   556  O  O   . SER   A 1 69  ? 1.793  1.068   13.868 1.00 14.87  ? 75  SER   A O   1 
ATOM   557  C  CB  A SER   A 1 69  ? 0.495  -1.411  12.658 0.50 16.12  ? 75  SER   A CB  1 
ATOM   558  C  CB  B SER   A 1 69  ? 0.377  -1.350  12.882 0.50 16.69  ? 75  SER   A CB  1 
ATOM   559  O  OG  A SER   A 1 69  ? 0.234  -2.787  12.814 0.50 19.26  ? 75  SER   A OG  1 
ATOM   560  O  OG  B SER   A 1 69  ? -0.102 -0.870  11.637 0.50 20.47  ? 75  SER   A OG  1 
ATOM   561  N  N   . PHE   A 1 70  ? 2.756  0.896   11.838 1.00 14.21  ? 76  PHE   A N   1 
ATOM   562  C  CA  . PHE   A 1 70  ? 3.059  2.318   11.775 1.00 14.80  ? 76  PHE   A CA  1 
ATOM   563  C  C   . PHE   A 1 70  ? 2.677  2.898   10.443 1.00 14.80  ? 76  PHE   A C   1 
ATOM   564  O  O   . PHE   A 1 70  ? 2.615  2.191   9.432  1.00 16.26  ? 76  PHE   A O   1 
ATOM   565  C  CB  . PHE   A 1 70  ? 4.574  2.572   12.152 1.00 14.74  ? 76  PHE   A CB  1 
ATOM   566  C  CG  . PHE   A 1 70  ? 5.601  1.772   11.343 1.00 14.26  ? 76  PHE   A CG  1 
ATOM   567  C  CD1 . PHE   A 1 70  ? 6.023  0.520   11.764 1.00 13.72  ? 76  PHE   A CD1 1 
ATOM   568  C  CD2 . PHE   A 1 70  ? 6.163  2.293   10.187 1.00 14.04  ? 76  PHE   A CD2 1 
ATOM   569  C  CE1 . PHE   A 1 70  ? 6.976  -0.198  11.031 1.00 14.03  ? 76  PHE   A CE1 1 
ATOM   570  C  CE2 . PHE   A 1 70  ? 7.129  1.570   9.465  1.00 14.29  ? 76  PHE   A CE2 1 
ATOM   571  C  CZ  . PHE   A 1 70  ? 7.488  0.308   9.874  1.00 13.96  ? 76  PHE   A CZ  1 
ATOM   572  N  N   . SER   A 1 71  ? 2.377  4.204   10.416 1.00 15.13  ? 77  SER   A N   1 
ATOM   573  C  CA  . SER   A 1 71  ? 1.984  4.906   9.203  1.00 15.76  ? 77  SER   A CA  1 
ATOM   574  C  C   . SER   A 1 71  ? 3.157  5.158   8.249  1.00 16.11  ? 77  SER   A C   1 
ATOM   575  O  O   . SER   A 1 71  ? 4.317  5.042   8.654  1.00 15.75  ? 77  SER   A O   1 
ATOM   576  C  CB  . SER   A 1 71  ? 1.280  6.214   9.584  1.00 18.21  ? 77  SER   A CB  1 
ATOM   577  O  OG  . SER   A 1 71  ? 2.137  7.133   10.240 1.00 19.45  ? 77  SER   A OG  1 
ATOM   578  N  N   . LYS   A 1 72  ? 2.870  5.482   7.003  1.00 16.12  ? 78  LYS   A N   1 
ATOM   579  C  CA  . LYS   A 1 72  ? 3.925  5.788   6.054  1.00 16.71  ? 78  LYS   A CA  1 
ATOM   580  C  C   . LYS   A 1 72  ? 4.543  7.144   6.389  1.00 17.87  ? 78  LYS   A C   1 
ATOM   581  O  O   . LYS   A 1 72  ? 3.850  8.009   6.948  1.00 18.34  ? 78  LYS   A O   1 
ATOM   582  C  CB  . LYS   A 1 72  ? 3.334  5.776   4.635  1.00 19.15  ? 78  LYS   A CB  1 
ATOM   583  C  CG  . LYS   A 1 72  ? 2.879  4.378   4.239  1.00 22.43  ? 78  LYS   A CG  1 
ATOM   584  C  CD  . LYS   A 1 72  ? 2.542  4.309   2.756  1.00 29.98  ? 78  LYS   A CD  1 
ATOM   585  C  CE  . LYS   A 1 72  ? 2.217  2.887   2.364  1.00 36.26  ? 78  LYS   A CE  1 
ATOM   586  N  NZ  . LYS   A 1 72  ? 2.526  2.635   0.930  1.00 40.99  ? 78  LYS   A NZ  1 
ATOM   587  N  N   . PRO   A 1 73  ? 5.809  7.380   6.065  1.00 17.68  ? 79  PRO   A N   1 
ATOM   588  C  CA  . PRO   A 1 73  ? 6.434  8.670   6.381  1.00 17.23  ? 79  PRO   A CA  1 
ATOM   589  C  C   . PRO   A 1 73  ? 5.656  9.858   5.824  1.00 18.63  ? 79  PRO   A C   1 
ATOM   590  O  O   . PRO   A 1 73  ? 5.287  9.862   4.645  1.00 21.71  ? 79  PRO   A O   1 
ATOM   591  C  CB  . PRO   A 1 73  ? 7.829  8.555   5.741  1.00 20.02  ? 79  PRO   A CB  1 
ATOM   592  C  CG  . PRO   A 1 73  ? 8.079  7.110   5.536  1.00 23.64  ? 79  PRO   A CG  1 
ATOM   593  C  CD  . PRO   A 1 73  ? 6.750  6.443   5.395  1.00 19.08  ? 79  PRO   A CD  1 
ATOM   594  N  N   . SER   A 1 74  ? 5.370  10.832  6.681  1.00 18.17  ? 80  SER   A N   1 
ATOM   595  C  CA  . SER   A 1 74  ? 4.487  11.939  6.311  1.00 19.42  ? 80  SER   A CA  1 
ATOM   596  C  C   . SER   A 1 74  ? 4.881  13.200  7.069  1.00 18.63  ? 80  SER   A C   1 
ATOM   597  O  O   . SER   A 1 74  ? 5.696  13.187  7.986  1.00 18.27  ? 80  SER   A O   1 
ATOM   598  C  CB  . SER   A 1 74  ? 3.010  11.614  6.651  1.00 25.17  ? 80  SER   A CB  1 
ATOM   599  O  OG  . SER   A 1 74  ? 2.665  10.242  6.650  1.00 35.13  ? 80  SER   A OG  1 
ATOM   600  N  N   . LEU   A 1 75  ? 4.177  14.315  6.733  1.00 21.11  ? 81  LEU   A N   1 
ATOM   601  C  CA  . LEU   A 1 75  ? 4.347  15.611  7.377  1.00 23.14  ? 81  LEU   A CA  1 
ATOM   602  C  C   . LEU   A 1 75  ? 3.260  15.682  8.456  1.00 24.49  ? 81  LEU   A C   1 
ATOM   603  O  O   . LEU   A 1 75  ? 2.061  15.763  8.134  1.00 26.59  ? 81  LEU   A O   1 
ATOM   604  C  CB  . LEU   A 1 75  ? 4.154  16.710  6.305  1.00 24.34  ? 81  LEU   A CB  1 
ATOM   605  C  CG  . LEU   A 1 75  ? 4.477  18.125  6.682  1.00 28.12  ? 81  LEU   A CG  1 
ATOM   606  C  CD1 . LEU   A 1 75  ? 5.956  18.294  6.942  1.00 28.64  ? 81  LEU   A CD1 1 
ATOM   607  C  CD2 . LEU   A 1 75  ? 4.103  19.082  5.526  1.00 29.55  ? 81  LEU   A CD2 1 
ATOM   608  N  N   . ILE   A 1 76  ? 3.656  15.624  9.714  1.00 23.65  ? 82  ILE   A N   1 
ATOM   609  C  CA  A ILE   A 1 76  ? 2.792  15.547  10.891 0.50 25.50  ? 82  ILE   A CA  1 
ATOM   610  C  CA  B ILE   A 1 76  ? 2.744  15.623  10.845 0.50 25.33  ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.002  16.761  11.807 1.00 26.39  ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.156  17.115  12.082 1.00 25.85  ? 82  ILE   A O   1 
ATOM   613  C  CB  A ILE   A 1 76  ? 3.172  14.244  11.662 0.50 26.00  ? 82  ILE   A CB  1 
ATOM   614  C  CB  B ILE   A 1 76  ? 2.840  14.291  11.603 0.50 25.32  ? 82  ILE   A CB  1 
ATOM   615  C  CG1 A ILE   A 1 76  ? 2.930  12.940  10.833 0.50 26.78  ? 82  ILE   A CG1 1 
ATOM   616  C  CG1 B ILE   A 1 76  ? 2.755  13.071  10.647 0.50 26.29  ? 82  ILE   A CG1 1 
ATOM   617  C  CG2 A ILE   A 1 76  ? 2.523  14.152  13.050 0.50 26.59  ? 82  ILE   A CG2 1 
ATOM   618  C  CG2 B ILE   A 1 76  ? 1.809  14.232  12.750 0.50 26.00  ? 82  ILE   A CG2 1 
ATOM   619  C  CD1 A ILE   A 1 76  ? 1.435  12.409  10.785 0.50 27.45  ? 82  ILE   A CD1 1 
ATOM   620  C  CD1 B ILE   A 1 76  ? 2.811  11.817  11.260 0.50 25.83  ? 82  ILE   A CD1 1 
ATOM   621  N  N   . PHE   A 1 77  ? 1.929  17.325  12.360 1.00 27.18  ? 83  PHE   A N   1 
ATOM   622  C  CA  . PHE   A 1 77  ? 2.032  18.406  13.332 1.00 27.26  ? 83  PHE   A CA  1 
ATOM   623  C  C   . PHE   A 1 77  ? 2.426  17.803  14.697 1.00 28.38  ? 83  PHE   A C   1 
ATOM   624  O  O   . PHE   A 1 77  ? 1.846  16.815  15.153 1.00 31.57  ? 83  PHE   A O   1 
ATOM   625  C  CB  . PHE   A 1 77  ? 0.690  19.168  13.481 1.00 28.58  ? 83  PHE   A CB  1 
ATOM   626  C  CG  . PHE   A 1 77  ? 0.909  20.497  14.145 1.00 31.19  ? 83  PHE   A CG  1 
ATOM   627  C  CD1 . PHE   A 1 77  ? 1.571  21.515  13.481 1.00 33.54  ? 83  PHE   A CD1 1 
ATOM   628  C  CD2 . PHE   A 1 77  ? 0.522  20.705  15.458 1.00 33.60  ? 83  PHE   A CD2 1 
ATOM   629  C  CE1 . PHE   A 1 77  ? 1.778  22.740  14.090 1.00 35.97  ? 83  PHE   A CE1 1 
ATOM   630  C  CE2 . PHE   A 1 77  ? 0.717  21.940  16.062 1.00 34.27  ? 83  PHE   A CE2 1 
ATOM   631  C  CZ  . PHE   A 1 77  ? 1.316  22.956  15.368 1.00 35.82  ? 83  PHE   A CZ  1 
ATOM   632  N  N   . VAL   A 1 78  ? 3.506  18.328  15.291 1.00 25.04  ? 84  VAL   A N   1 
ATOM   633  C  CA  . VAL   A 1 78  ? 3.981  17.872  16.589 1.00 23.34  ? 84  VAL   A CA  1 
ATOM   634  C  C   . VAL   A 1 78  ? 3.884  19.046  17.582 1.00 24.03  ? 84  VAL   A C   1 
ATOM   635  O  O   . VAL   A 1 78  ? 4.402  20.117  17.266 1.00 24.24  ? 84  VAL   A O   1 
ATOM   636  C  CB  . VAL   A 1 78  ? 5.458  17.373  16.454 1.00 21.87  ? 84  VAL   A CB  1 
ATOM   637  C  CG1 . VAL   A 1 78  ? 5.994  16.910  17.819 1.00 22.97  ? 84  VAL   A CG1 1 
ATOM   638  C  CG2 . VAL   A 1 78  ? 5.544  16.237  15.408 1.00 22.38  ? 84  VAL   A CG2 1 
ATOM   639  N  N   . GLU   A 1 79  ? 3.338  18.780  18.795 1.00 23.69  ? 85  GLU   A N   1 
ATOM   640  C  CA  . GLU   A 1 79  ? 3.183  19.789  19.858 1.00 27.25  ? 85  GLU   A CA  1 
ATOM   641  C  C   . GLU   A 1 79  ? 4.537  20.295  20.356 1.00 28.74  ? 85  GLU   A C   1 
ATOM   642  O  O   . GLU   A 1 79  ? 5.531  19.554  20.328 1.00 27.86  ? 85  GLU   A O   1 
ATOM   643  C  CB  . GLU   A 1 79  ? 2.320  19.264  21.033 1.00 31.88  ? 85  GLU   A CB  1 
ATOM   644  C  CG  . GLU   A 1 79  ? 2.971  18.239  21.941 1.00 42.62  ? 85  GLU   A CG  1 
ATOM   645  C  CD  . GLU   A 1 79  ? 2.094  17.489  22.933 1.00 57.09  ? 85  GLU   A CD  1 
ATOM   646  O  OE1 . GLU   A 1 79  ? 1.158  18.102  23.502 1.00 60.49  ? 85  GLU   A OE1 1 
ATOM   647  O  OE2 . GLU   A 1 79  ? 2.360  16.283  23.156 1.00 60.97  ? 85  GLU   A OE2 1 
ATOM   648  N  N   . ALA   A 1 80  ? 4.555  21.571  20.841 1.00 29.96  ? 86  ALA   A N   1 
ATOM   649  C  CA  . ALA   A 1 80  ? 5.754  22.219  21.396 1.00 33.51  ? 86  ALA   A CA  1 
ATOM   650  C  C   . ALA   A 1 80  ? 6.354  21.398  22.498 1.00 36.69  ? 86  ALA   A C   1 
ATOM   651  O  O   . ALA   A 1 80  ? 5.634  20.759  23.276 1.00 38.75  ? 86  ALA   A O   1 
ATOM   652  C  CB  . ALA   A 1 80  ? 5.428  23.597  21.946 1.00 34.89  ? 86  ALA   A CB  1 
ATOM   653  N  N   . SER   A 1 81  ? 7.679  21.332  22.519 1.00 36.29  ? 87  SER   A N   1 
ATOM   654  C  CA  . SER   A 1 81  ? 8.418  20.614  23.556 1.00 35.48  ? 87  SER   A CA  1 
ATOM   655  C  C   . SER   A 1 81  ? 9.552  21.560  24.044 1.00 35.15  ? 87  SER   A C   1 
ATOM   656  O  O   . SER   A 1 81  ? 9.653  22.694  23.590 1.00 36.23  ? 87  SER   A O   1 
ATOM   657  C  CB  . SER   A 1 81  ? 9.021  19.341  22.971 1.00 36.52  ? 87  SER   A CB  1 
ATOM   658  O  OG  . SER   A 1 81  ? 10.013 19.673  22.008 1.00 36.03  ? 87  SER   A OG  1 
ATOM   659  N  N   . GLU   A 1 82  ? 10.445 21.068  24.912 1.00 35.30  ? 88  GLU   A N   1 
ATOM   660  C  CA  . GLU   A 1 82  ? 11.627 21.843  25.319 1.00 34.39  ? 88  GLU   A CA  1 
ATOM   661  C  C   . GLU   A 1 82  ? 12.612 21.974  24.127 1.00 29.63  ? 88  GLU   A C   1 
ATOM   662  O  O   . GLU   A 1 82  ? 13.457 22.850  24.160 1.00 29.40  ? 88  GLU   A O   1 
ATOM   663  C  CB  . GLU   A 1 82  ? 12.353 21.109  26.466 1.00 39.39  ? 88  GLU   A CB  1 
ATOM   664  C  CG  . GLU   A 1 82  ? 11.517 21.033  27.730 1.00 48.57  ? 88  GLU   A CG  1 
ATOM   665  C  CD  . GLU   A 1 82  ? 11.792 19.799  28.568 1.00 59.14  ? 88  GLU   A CD  1 
ATOM   666  O  OE1 . GLU   A 1 82  ? 10.875 19.361  29.302 1.00 62.63  ? 88  GLU   A OE1 1 
ATOM   667  O  OE2 . GLU   A 1 82  ? 12.921 19.263  28.481 1.00 60.57  ? 88  GLU   A OE2 1 
ATOM   668  N  N   . TYR   A 1 83  ? 12.481 21.137  23.067 1.00 27.45  ? 89  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 83  ? 13.454 21.173  21.952 1.00 24.63  ? 89  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 83  ? 12.996 21.844  20.693 1.00 22.90  ? 89  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 83  ? 13.830 22.283  19.890 1.00 22.44  ? 89  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 83  ? 13.824 19.739  21.610 1.00 23.59  ? 89  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 83  ? 14.465 19.053  22.788 1.00 22.96  ? 89  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 83  ? 13.723 18.240  23.634 1.00 26.30  ? 89  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 83  ? 15.786 19.302  23.122 1.00 23.70  ? 89  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 83  ? 14.313 17.608  24.723 1.00 27.80  ? 89  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 83  ? 16.397 18.646  24.180 1.00 25.99  ? 89  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 83  ? 15.637 17.860  25.028 1.00 28.90  ? 89  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 83  ? 16.250 17.199  26.073 1.00 32.29  ? 89  TYR   A OH  1 
ATOM   680  N  N   . TYR   A 1 84  ? 11.674 21.853  20.442 1.00 23.74  ? 90  TYR   A N   1 
ATOM   681  C  CA  . TYR   A 1 84  ? 11.153 22.492  19.227 1.00 22.66  ? 90  TYR   A CA  1 
ATOM   682  C  C   . TYR   A 1 84  ? 9.832  23.203  19.563 1.00 25.75  ? 90  TYR   A C   1 
ATOM   683  O  O   . TYR   A 1 84  ? 9.064  22.651  20.371 1.00 27.28  ? 90  TYR   A O   1 
ATOM   684  C  CB  . TYR   A 1 84  ? 10.817 21.414  18.132 1.00 21.71  ? 90  TYR   A CB  1 
ATOM   685  C  CG  . TYR   A 1 84  ? 11.998 20.619  17.583 1.00 18.92  ? 90  TYR   A CG  1 
ATOM   686  C  CD1 . TYR   A 1 84  ? 12.916 21.202  16.723 1.00 18.81  ? 90  TYR   A CD1 1 
ATOM   687  C  CD2 . TYR   A 1 84  ? 12.172 19.284  17.912 1.00 18.04  ? 90  TYR   A CD2 1 
ATOM   688  C  CE1 . TYR   A 1 84  ? 14.000 20.477  16.220 1.00 18.32  ? 90  TYR   A CE1 1 
ATOM   689  C  CE2 . TYR   A 1 84  ? 13.240 18.551  17.424 1.00 17.59  ? 90  TYR   A CE2 1 
ATOM   690  C  CZ  . TYR   A 1 84  ? 14.173 19.165  16.614 1.00 16.97  ? 90  TYR   A CZ  1 
ATOM   691  O  OH  . TYR   A 1 84  ? 15.240 18.454  16.123 1.00 16.50  ? 90  TYR   A OH  1 
ATOM   692  N  N   . PRO   A 1 85  ? 9.491  24.254  18.825 1.00 27.32  ? 91  PRO   A N   1 
ATOM   693  C  CA  . PRO   A 1 85  ? 8.138  24.828  18.967 1.00 28.29  ? 91  PRO   A CA  1 
ATOM   694  C  C   . PRO   A 1 85  ? 7.137  23.869  18.310 1.00 29.76  ? 91  PRO   A C   1 
ATOM   695  O  O   . PRO   A 1 85  ? 7.537  22.901  17.607 1.00 29.14  ? 91  PRO   A O   1 
ATOM   696  C  CB  . PRO   A 1 85  ? 8.240  26.138  18.165 1.00 30.09  ? 91  PRO   A CB  1 
ATOM   697  C  CG  . PRO   A 1 85  ? 9.246  25.857  17.118 1.00 30.25  ? 91  PRO   A CG  1 
ATOM   698  C  CD  . PRO   A 1 85  ? 10.274 24.959  17.788 1.00 27.29  ? 91  PRO   A CD  1 
ATOM   699  N  N   . ALA   A 1 86  ? 5.829  24.154  18.425 1.00 31.02  ? 92  ALA   A N   1 
ATOM   700  C  CA  . ALA   A 1 86  ? 4.817  23.331  17.742 1.00 30.71  ? 92  ALA   A CA  1 
ATOM   701  C  C   . ALA   A 1 86  ? 5.047  23.577  16.233 1.00 29.85  ? 92  ALA   A C   1 
ATOM   702  O  O   . ALA   A 1 86  ? 5.327  24.699  15.839 1.00 31.16  ? 92  ALA   A O   1 
ATOM   703  C  CB  . ALA   A 1 86  ? 3.419  23.787  18.152 1.00 30.81  ? 92  ALA   A CB  1 
ATOM   704  N  N   . ARG   A 1 87  ? 5.129  22.506  15.439 1.00 27.63  ? 93  ARG   A N   1 
ATOM   705  C  CA  . ARG   A 1 87  ? 5.528  22.650  14.041 1.00 26.77  ? 93  ARG   A CA  1 
ATOM   706  C  C   . ARG   A 1 87  ? 5.201  21.373  13.265 1.00 26.53  ? 93  ARG   A C   1 
ATOM   707  O  O   . ARG   A 1 87  ? 4.768  20.384  13.867 1.00 27.59  ? 93  ARG   A O   1 
ATOM   708  C  CB  . ARG   A 1 87  ? 7.060  22.868  13.991 1.00 27.27  ? 93  ARG   A CB  1 
ATOM   709  C  CG  . ARG   A 1 87  ? 7.883  21.516  14.143 1.00 27.41  ? 93  ARG   A CG  1 
ATOM   710  C  CD  . ARG   A 1 87  ? 9.298  21.752  14.556 1.00 26.35  ? 93  ARG   A CD  1 
ATOM   711  N  NE  . ARG   A 1 87  ? 10.232 20.672  14.180 1.00 26.12  ? 93  ARG   A NE  1 
ATOM   712  C  CZ  . ARG   A 1 87  ? 10.321 19.455  14.695 1.00 28.27  ? 93  ARG   A CZ  1 
ATOM   713  N  NH1 . ARG   A 1 87  ? 9.412  19.025  15.593 1.00 27.35  ? 93  ARG   A NH1 1 
ATOM   714  N  NH2 . ARG   A 1 87  ? 11.282 18.631  14.286 1.00 21.65  ? 93  ARG   A NH2 1 
ATOM   715  N  N   . TYR   A 1 88  ? 5.467  21.387  11.949 1.00 26.94  ? 94  TYR   A N   1 
ATOM   716  C  CA  . TYR   A 1 88  ? 5.312  20.202  11.134 1.00 27.43  ? 94  TYR   A CA  1 
ATOM   717  C  C   . TYR   A 1 88  ? 6.644  19.513  11.011 1.00 23.97  ? 94  TYR   A C   1 
ATOM   718  O  O   . TYR   A 1 88  ? 7.623  20.119  10.546 1.00 24.74  ? 94  TYR   A O   1 
ATOM   719  C  CB  . TYR   A 1 88  ? 4.809  20.543  9.741  1.00 28.59  ? 94  TYR   A CB  1 
ATOM   720  C  CG  . TYR   A 1 88  ? 3.336  20.863  9.766  1.00 29.34  ? 94  TYR   A CG  1 
ATOM   721  C  CD1 . TYR   A 1 88  ? 2.386  19.852  9.793  1.00 30.42  ? 94  TYR   A CD1 1 
ATOM   722  C  CD2 . TYR   A 1 88  ? 2.890  22.175  9.883  1.00 30.75  ? 94  TYR   A CD2 1 
ATOM   723  C  CE1 . TYR   A 1 88  ? 1.032  20.137  9.852  1.00 32.29  ? 94  TYR   A CE1 1 
ATOM   724  C  CE2 . TYR   A 1 88  ? 1.536  22.468  9.956  1.00 32.64  ? 94  TYR   A CE2 1 
ATOM   725  C  CZ  . TYR   A 1 88  ? 0.612  21.442  9.974  1.00 34.11  ? 94  TYR   A CZ  1 
ATOM   726  O  OH  . TYR   A 1 88  ? -0.729 21.715  10.063 1.00 37.47  ? 94  TYR   A OH  1 
ATOM   727  N  N   . GLN   A 1 89  ? 6.691  18.235  11.446 1.00 20.82  ? 95  GLN   A N   1 
ATOM   728  C  CA  . GLN   A 1 89  ? 7.910  17.421  11.299 1.00 19.40  ? 95  GLN   A CA  1 
ATOM   729  C  C   . GLN   A 1 89  ? 7.703  16.538  10.057 1.00 18.78  ? 95  GLN   A C   1 
ATOM   730  O  O   . GLN   A 1 89  ? 6.630  15.925  9.883  1.00 19.84  ? 95  GLN   A O   1 
ATOM   731  C  CB  . GLN   A 1 89  ? 8.158  16.578  12.566 1.00 19.00  ? 95  GLN   A CB  1 
ATOM   732  C  CG  . GLN   A 1 89  ? 9.409  15.756  12.451 1.00 17.84  ? 95  GLN   A CG  1 
ATOM   733  C  CD  . GLN   A 1 89  ? 9.968  15.307  13.795 1.00 16.59  ? 95  GLN   A CD  1 
ATOM   734  O  OE1 . GLN   A 1 89  ? 9.987  16.024  14.807 1.00 18.21  ? 95  GLN   A OE1 1 
ATOM   735  N  NE2 . GLN   A 1 89  ? 10.449 14.083  13.806 1.00 17.46  ? 95  GLN   A NE2 1 
ATOM   736  N  N   . SER   A 1 90  ? 8.714  16.468  9.174  1.00 17.11  ? 96  SER   A N   1 
ATOM   737  C  CA  . SER   A 1 90  ? 8.605  15.677  7.973  1.00 16.41  ? 96  SER   A CA  1 
ATOM   738  C  C   . SER   A 1 90  ? 9.205  14.268  8.162  1.00 16.89  ? 96  SER   A C   1 
ATOM   739  O  O   . SER   A 1 90  ? 9.975  14.023  9.104  1.00 17.15  ? 96  SER   A O   1 
ATOM   740  C  CB  . SER   A 1 90  ? 9.290  16.397  6.813  1.00 19.46  ? 96  SER   A CB  1 
ATOM   741  O  OG  . SER   A 1 90  ? 10.670 16.526  7.125  1.00 23.12  ? 96  SER   A OG  1 
ATOM   742  N  N   . HIS   A 1 91  ? 8.813  13.353  7.251  1.00 17.57  ? 97  HIS   A N   1 
ATOM   743  C  CA  . HIS   A 1 91  ? 9.314  11.987  7.204  1.00 16.63  ? 97  HIS   A CA  1 
ATOM   744  C  C   . HIS   A 1 91  ? 9.032  11.284  8.552  1.00 15.13  ? 97  HIS   A C   1 
ATOM   745  O  O   . HIS   A 1 91  ? 9.844  10.420  8.975  1.00 15.24  ? 97  HIS   A O   1 
ATOM   746  C  CB  . HIS   A 1 91  ? 10.837 11.926  6.823  1.00 17.37  ? 97  HIS   A CB  1 
ATOM   747  C  CG  . HIS   A 1 91  ? 11.133 12.508  5.464  1.00 19.59  ? 97  HIS   A CG  1 
ATOM   748  N  ND1 . HIS   A 1 91  ? 11.226 11.706  4.357  1.00 21.62  ? 97  HIS   A ND1 1 
ATOM   749  C  CD2 . HIS   A 1 91  ? 11.265 13.803  5.082  1.00 21.26  ? 97  HIS   A CD2 1 
ATOM   750  C  CE1 . HIS   A 1 91  ? 11.466 12.520  3.328  1.00 22.15  ? 97  HIS   A CE1 1 
ATOM   751  N  NE2 . HIS   A 1 91  ? 11.496 13.792  3.712  1.00 22.67  ? 97  HIS   A NE2 1 
ATOM   752  N  N   . LEU   A 1 92  ? 7.919  11.568  9.182  1.00 14.90  ? 98  LEU   A N   1 
ATOM   753  C  CA  . LEU   A 1 92  ? 7.576  11.001  10.492 1.00 15.28  ? 98  LEU   A CA  1 
ATOM   754  C  C   . LEU   A 1 92  ? 6.509  9.911   10.322 1.00 14.67  ? 98  LEU   A C   1 
ATOM   755  O  O   . LEU   A 1 92  ? 5.583  10.075  9.535  1.00 15.52  ? 98  LEU   A O   1 
ATOM   756  C  CB  . LEU   A 1 92  ? 7.032  12.131  11.398 1.00 16.79  ? 98  LEU   A CB  1 
ATOM   757  C  CG  . LEU   A 1 92  ? 6.726  11.720  12.890 1.00 18.38  ? 98  LEU   A CG  1 
ATOM   758  C  CD1 . LEU   A 1 92  ? 8.008  11.427  13.633 1.00 18.01  ? 98  LEU   A CD1 1 
ATOM   759  C  CD2 . LEU   A 1 92  ? 6.019  12.864  13.661 1.00 20.72  ? 98  LEU   A CD2 1 
ATOM   760  N  N   . MET   A 1 93  ? 6.656  8.815   11.068 1.00 15.08  ? 99  MET   A N   1 
ATOM   761  C  CA  . MET   A 1 93  ? 5.710  7.682   11.048 1.00 14.58  ? 99  MET   A CA  1 
ATOM   762  C  C   . MET   A 1 93  ? 5.117  7.535   12.440 1.00 15.51  ? 99  MET   A C   1 
ATOM   763  O  O   . MET   A 1 93  ? 5.875  7.577   13.413 1.00 16.39  ? 99  MET   A O   1 
ATOM   764  C  CB  . MET   A 1 93  ? 6.476  6.410   10.683 1.00 14.97  ? 99  MET   A CB  1 
ATOM   765  C  CG  . MET   A 1 93  ? 7.100  6.529   9.287  1.00 14.97  ? 99  MET   A CG  1 
ATOM   766  S  SD  . MET   A 1 93  ? 8.187  5.157   8.808  1.00 18.40  ? 99  MET   A SD  1 
ATOM   767  C  CE  . MET   A 1 93  ? 9.529  5.367   10.045 1.00 21.81  ? 99  MET   A CE  1 
ATOM   768  N  N   . LEU   A 1 94  ? 3.792  7.352   12.587 1.00 14.47  ? 100 LEU   A N   1 
ATOM   769  C  CA  . LEU   A 1 94  ? 3.199  7.211   13.907 1.00 15.37  ? 100 LEU   A CA  1 
ATOM   770  C  C   . LEU   A 1 94  ? 2.699  5.795   14.156 1.00 14.05  ? 100 LEU   A C   1 
ATOM   771  O  O   . LEU   A 1 94  ? 2.270  5.094   13.225 1.00 15.30  ? 100 LEU   A O   1 
ATOM   772  C  CB  . LEU   A 1 94  ? 1.971  8.150   14.084 1.00 17.88  ? 100 LEU   A CB  1 
ATOM   773  C  CG  . LEU   A 1 94  ? 2.218  9.629   14.043 1.00 22.54  ? 100 LEU   A CG  1 
ATOM   774  C  CD1 . LEU   A 1 94  ? 0.918  10.402  14.395 1.00 25.46  ? 100 LEU   A CD1 1 
ATOM   775  C  CD2 . LEU   A 1 94  ? 3.289  10.062  15.070 1.00 24.26  ? 100 LEU   A CD2 1 
ATOM   776  N  N   . ALA   A 1 95  ? 2.730  5.392   15.429 1.00 14.50  ? 101 ALA   A N   1 
ATOM   777  C  CA  . ALA   A 1 95  ? 2.172  4.108   15.862 1.00 14.30  ? 101 ALA   A CA  1 
ATOM   778  C  C   . ALA   A 1 95  ? 1.562  4.315   17.256 1.00 13.45  ? 101 ALA   A C   1 
ATOM   779  O  O   . ALA   A 1 95  ? 1.860  5.312   17.937 1.00 14.04  ? 101 ALA   A O   1 
ATOM   780  C  CB  . ALA   A 1 95  ? 3.299  3.034   15.995 1.00 14.33  ? 101 ALA   A CB  1 
ATOM   781  N  N   . VAL   A 1 96  ? 0.757  3.334   17.698 1.00 13.53  ? 102 VAL   A N   1 
ATOM   782  C  CA  . VAL   A 1 96  ? 0.258  3.324   19.036 1.00 14.13  ? 102 VAL   A CA  1 
ATOM   783  C  C   . VAL   A 1 96  ? 1.298  2.577   19.925 1.00 15.27  ? 102 VAL   A C   1 
ATOM   784  O  O   . VAL   A 1 96  ? 1.628  1.428   19.681 1.00 16.54  ? 102 VAL   A O   1 
ATOM   785  C  CB  . VAL   A 1 96  ? -1.088 2.602   19.080 1.00 14.25  ? 102 VAL   A CB  1 
ATOM   786  C  CG1 . VAL   A 1 96  ? -1.573 2.433   20.529 1.00 15.26  ? 102 VAL   A CG1 1 
ATOM   787  C  CG2 . VAL   A 1 96  ? -2.110 3.376   18.224 1.00 14.27  ? 102 VAL   A CG2 1 
ATOM   788  N  N   . GLY   A 1 97  ? 1.791  3.278   20.934 1.00 14.64  ? 103 GLY   A N   1 
ATOM   789  C  CA  . GLY   A 1 97  ? 2.786  2.685   21.838 1.00 15.07  ? 103 GLY   A CA  1 
ATOM   790  C  C   . GLY   A 1 97  ? 3.248  3.710   22.827 1.00 16.45  ? 103 GLY   A C   1 
ATOM   791  O  O   . GLY   A 1 97  ? 2.964  4.899   22.722 1.00 18.32  ? 103 GLY   A O   1 
ATOM   792  N  N   . HIS   A 1 98  ? 3.961  3.223   23.874 1.00 17.17  ? 104 HIS   A N   1 
ATOM   793  C  CA  . HIS   A 1 98  ? 4.471  4.092   24.880 1.00 18.12  ? 104 HIS   A CA  1 
ATOM   794  C  C   . HIS   A 1 98  ? 5.760  4.831   24.485 1.00 17.21  ? 104 HIS   A C   1 
ATOM   795  O  O   . HIS   A 1 98  ? 6.690  4.174   23.977 1.00 17.32  ? 104 HIS   A O   1 
ATOM   796  C  CB  . HIS   A 1 98  ? 4.671  3.266   26.190 1.00 18.07  ? 104 HIS   A CB  1 
ATOM   797  C  CG  . HIS   A 1 98  ? 5.027  4.132   27.326 1.00 18.31  ? 104 HIS   A CG  1 
ATOM   798  N  ND1 . HIS   A 1 98  ? 4.116  4.988   27.876 1.00 18.94  ? 104 HIS   A ND1 1 
ATOM   799  C  CD2 . HIS   A 1 98  ? 6.219  4.312   27.937 1.00 19.30  ? 104 HIS   A CD2 1 
ATOM   800  C  CE1 . HIS   A 1 98  ? 4.778  5.671   28.806 1.00 19.58  ? 104 HIS   A CE1 1 
ATOM   801  N  NE2 . HIS   A 1 98  ? 6.056  5.282   28.861 1.00 18.91  ? 104 HIS   A NE2 1 
ATOM   802  N  N   . SER   A 1 99  ? 5.869  6.126   24.728 1.00 17.18  ? 105 SER   A N   1 
ATOM   803  C  CA  . SER   A 1 99  ? 7.037  6.917   24.410 1.00 17.62  ? 105 SER   A CA  1 
ATOM   804  C  C   . SER   A 1 99  ? 6.976  8.100   25.310 1.00 21.17  ? 105 SER   A C   1 
ATOM   805  O  O   . SER   A 1 99  ? 6.033  8.920   25.202 1.00 23.87  ? 105 SER   A O   1 
ATOM   806  C  CB  . SER   A 1 99  ? 7.067  7.328   22.912 1.00 18.00  ? 105 SER   A CB  1 
ATOM   807  O  OG  . SER   A 1 99  ? 8.111  8.232   22.570 1.00 19.48  ? 105 SER   A OG  1 
ATOM   808  N  N   . GLU   A 1 100 ? 7.944  8.217   26.170 1.00 17.97  ? 106 GLU   A N   1 
ATOM   809  C  CA  . GLU   A 1 100 ? 7.975  9.348   27.056 1.00 20.80  ? 106 GLU   A CA  1 
ATOM   810  C  C   . GLU   A 1 100 ? 9.358  9.980   26.825 1.00 22.97  ? 106 GLU   A C   1 
ATOM   811  O  O   . GLU   A 1 100 ? 10.251 9.547   26.007 1.00 23.64  ? 106 GLU   A O   1 
ATOM   812  C  CB  . GLU   A 1 100 ? 7.512  8.927   28.530 1.00 22.75  ? 106 GLU   A CB  1 
ATOM   813  C  CG  . GLU   A 1 100 ? 8.399  7.902   29.142 1.00 20.23  ? 106 GLU   A CG  1 
ATOM   814  C  CD  . GLU   A 1 100 ? 8.103  7.539   30.578 1.00 19.67  ? 106 GLU   A CD  1 
ATOM   815  O  OE1 . GLU   A 1 100 ? 8.670  8.183   31.488 1.00 24.61  ? 106 GLU   A OE1 1 
ATOM   816  O  OE2 . GLU   A 1 100 ? 7.350  6.562   30.777 1.00 19.43  ? 106 GLU   A OE2 1 
ATOM   817  N  N   . PRO   A 1 101 ? 9.508  11.195  27.369 1.00 27.50  ? 107 PRO   A N   1 
ATOM   818  C  CA  . PRO   A 1 101 ? 10.774 11.875  27.257 1.00 27.83  ? 107 PRO   A CA  1 
ATOM   819  C  C   . PRO   A 1 101 ? 11.890 10.979  27.827 1.00 25.77  ? 107 PRO   A C   1 
ATOM   820  O  O   . PRO   A 1 101 ? 11.708 10.378  28.923 1.00 27.99  ? 107 PRO   A O   1 
ATOM   821  C  CB  . PRO   A 1 101 ? 10.529 13.141  28.096 1.00 29.79  ? 107 PRO   A CB  1 
ATOM   822  C  CG  . PRO   A 1 101 ? 9.086  13.380  27.967 1.00 31.07  ? 107 PRO   A CG  1 
ATOM   823  C  CD  . PRO   A 1 101 ? 8.560  11.992  28.170 1.00 28.49  ? 107 PRO   A CD  1 
ATOM   824  N  N   . GLY   A 1 102 ? 12.937 10.806  27.011 1.00 19.62  ? 108 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 102 ? 14.086 9.918   27.187 1.00 19.38  ? 108 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 102 ? 14.062 8.720   26.237 1.00 16.36  ? 108 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 102 ? 15.084 8.103   26.059 1.00 16.31  ? 108 GLY   A O   1 
ATOM   828  N  N   . ASP   A 1 103 ? 12.892 8.354   25.657 1.00 15.10  ? 109 ASP   A N   1 
ATOM   829  C  CA  . ASP   A 1 103 ? 12.813 7.236   24.725 1.00 14.49  ? 109 ASP   A CA  1 
ATOM   830  C  C   . ASP   A 1 103 ? 13.316 7.558   23.320 1.00 13.71  ? 109 ASP   A C   1 
ATOM   831  O  O   . ASP   A 1 103 ? 13.526 6.643   22.518 1.00 13.14  ? 109 ASP   A O   1 
ATOM   832  C  CB  . ASP   A 1 103 ? 11.364 6.692   24.631 1.00 14.07  ? 109 ASP   A CB  1 
ATOM   833  C  CG  . ASP   A 1 103 ? 10.991 5.935   25.896 1.00 14.63  ? 109 ASP   A CG  1 
ATOM   834  O  OD1 . ASP   A 1 103 ? 11.859 5.258   26.431 1.00 13.96  ? 109 ASP   A OD1 1 
ATOM   835  O  OD2 . ASP   A 1 103 ? 9.804  6.016   26.328 1.00 14.09  ? 109 ASP   A OD2 1 
ATOM   836  N  N   . CYS   A 1 104 ? 13.533 8.836   22.997 1.00 12.31  ? 110 CYS   A N   1 
ATOM   837  C  CA  . CYS   A 1 104 ? 14.100 9.177   21.668 1.00 12.97  ? 110 CYS   A CA  1 
ATOM   838  C  C   . CYS   A 1 104 ? 15.397 8.467   21.455 1.00 12.87  ? 110 CYS   A C   1 
ATOM   839  O  O   . CYS   A 1 104 ? 16.237 8.359   22.328 1.00 12.97  ? 110 CYS   A O   1 
ATOM   840  C  CB  . CYS   A 1 104 ? 14.279 10.685  21.565 1.00 12.50  ? 110 CYS   A CB  1 
ATOM   841  S  SG  . CYS   A 1 104 ? 12.709 11.599  21.318 1.00 16.19  ? 110 CYS   A SG  1 
ATOM   842  N  N   . GLY   A 1 105 ? 15.578 7.964   20.227 1.00 12.29  ? 111 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 105 ? 16.795 7.253   19.873 1.00 12.09  ? 111 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 105 ? 16.621 5.754   19.785 1.00 11.70  ? 111 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 105 ? 17.473 5.053   19.232 1.00 11.96  ? 111 GLY   A O   1 
ATOM   846  N  N   . GLY   A 1 106 ? 15.538 5.231   20.378 1.00 11.70  ? 112 GLY   A N   1 
ATOM   847  C  CA  . GLY   A 1 106 ? 15.271 3.804   20.281 1.00 12.09  ? 112 GLY   A CA  1 
ATOM   848  C  C   . GLY   A 1 106 ? 15.044 3.380   18.836 1.00 10.68  ? 112 GLY   A C   1 
ATOM   849  O  O   . GLY   A 1 106 ? 14.347 4.078   18.099 1.00 10.66  ? 112 GLY   A O   1 
ATOM   850  N  N   . ILE   A 1 107 ? 15.578 2.226   18.449 1.00 10.67  ? 113 ILE   A N   1 
ATOM   851  C  CA  . ILE   A 1 107 ? 15.411 1.798   17.034 1.00 10.63  ? 113 ILE   A CA  1 
ATOM   852  C  C   . ILE   A 1 107 ? 14.087 1.120   16.731 1.00 10.36  ? 113 ILE   A C   1 
ATOM   853  O  O   . ILE   A 1 107 ? 13.607 0.301   17.536 1.00 10.70  ? 113 ILE   A O   1 
ATOM   854  C  CB  . ILE   A 1 107 ? 16.588 0.841   16.705 1.00 10.70  ? 113 ILE   A CB  1 
ATOM   855  C  CG1 . ILE   A 1 107 ? 17.871 1.707   16.434 1.00 12.85  ? 113 ILE   A CG1 1 
ATOM   856  C  CG2 . ILE   A 1 107 ? 16.323 -0.046  15.448 1.00 12.31  ? 113 ILE   A CG2 1 
ATOM   857  C  CD1 . ILE   A 1 107 ? 19.176 0.852   16.302 1.00 16.12  ? 113 ILE   A CD1 1 
ATOM   858  N  N   . LEU   A 1 108 ? 13.496 1.476   15.612 1.00 9.59   ? 114 LEU   A N   1 
ATOM   859  C  CA  . LEU   A 1 108 ? 12.390 0.751   14.990 1.00 10.31  ? 114 LEU   A CA  1 
ATOM   860  C  C   . LEU   A 1 108 ? 13.024 -0.081  13.856 1.00 9.68   ? 114 LEU   A C   1 
ATOM   861  O  O   . LEU   A 1 108 ? 13.800 0.447   13.016 1.00 10.56  ? 114 LEU   A O   1 
ATOM   862  C  CB  . LEU   A 1 108 ? 11.396 1.761   14.375 1.00 10.58  ? 114 LEU   A CB  1 
ATOM   863  C  CG  . LEU   A 1 108 ? 10.282 1.135   13.473 1.00 11.02  ? 114 LEU   A CG  1 
ATOM   864  C  CD1 . LEU   A 1 108 ? 9.301  0.283   14.304 1.00 12.78  ? 114 LEU   A CD1 1 
ATOM   865  C  CD2 . LEU   A 1 108 ? 9.475  2.243   12.686 1.00 12.58  ? 114 LEU   A CD2 1 
ATOM   866  N  N   . ARG   A 1 109 ? 12.711 -1.373  13.814 1.00 10.45  ? 115 ARG   A N   1 
ATOM   867  C  CA  . ARG   A 1 109 ? 13.284 -2.286  12.776 1.00 11.78  ? 115 ARG   A CA  1 
ATOM   868  C  C   . ARG   A 1 109 ? 12.211 -3.188  12.232 1.00 12.00  ? 115 ARG   A C   1 
ATOM   869  O  O   . ARG   A 1 109 ? 11.210 -3.482  12.871 1.00 11.82  ? 115 ARG   A O   1 
ATOM   870  C  CB  . ARG   A 1 109 ? 14.443 -3.104  13.382 1.00 12.95  ? 115 ARG   A CB  1 
ATOM   871  C  CG  . ARG   A 1 109 ? 13.965 -4.101  14.473 1.00 12.90  ? 115 ARG   A CG  1 
ATOM   872  C  CD  . ARG   A 1 109 ? 15.211 -4.843  15.012 1.00 14.03  ? 115 ARG   A CD  1 
ATOM   873  N  NE  . ARG   A 1 109 ? 15.994 -3.972  15.877 1.00 14.85  ? 115 ARG   A NE  1 
ATOM   874  C  CZ  . ARG   A 1 109 ? 17.301 -3.749  15.773 1.00 15.16  ? 115 ARG   A CZ  1 
ATOM   875  N  NH1 . ARG   A 1 109 ? 17.975 -4.145  14.688 1.00 15.86  ? 115 ARG   A NH1 1 
ATOM   876  N  NH2 . ARG   A 1 109 ? 17.929 -3.018  16.688 1.00 15.65  ? 115 ARG   A NH2 1 
ATOM   877  N  N   . CYS   A 1 110 ? 12.461 -3.684  11.011 1.00 14.00  ? 116 CYS   A N   1 
ATOM   878  C  CA  . CYS   A 1 110 ? 11.557 -4.637  10.334 1.00 17.28  ? 116 CYS   A CA  1 
ATOM   879  C  C   . CYS   A 1 110 ? 12.421 -5.822  9.942  1.00 19.66  ? 116 CYS   A C   1 
ATOM   880  O  O   . CYS   A 1 110 ? 13.610 -5.929  10.288 1.00 18.61  ? 116 CYS   A O   1 
ATOM   881  C  CB  . CYS   A 1 110 ? 10.881 -3.990  9.123  1.00 16.19  ? 116 CYS   A CB  1 
ATOM   882  S  SG  . CYS   A 1 110 ? 12.048 -3.596  7.765  1.00 16.00  ? 116 CYS   A SG  1 
ATOM   883  N  N   . GLN   A 1 111 ? 11.790 -6.761  9.163  1.00 22.17  ? 117 GLN   A N   1 
ATOM   884  C  CA  . GLN   A 1 111 ? 12.546 -7.906  8.689  1.00 24.42  ? 117 GLN   A CA  1 
ATOM   885  C  C   . GLN   A 1 111 ? 13.790 -7.550  7.821  1.00 24.94  ? 117 GLN   A C   1 
ATOM   886  O  O   . GLN   A 1 111 ? 14.736 -8.328  7.757  1.00 28.35  ? 117 GLN   A O   1 
ATOM   887  C  CB  . GLN   A 1 111 ? 11.631 -8.909  7.926  1.00 28.81  ? 117 GLN   A CB  1 
ATOM   888  C  CG  . GLN   A 1 111 ? 11.142 -8.362  6.595  1.00 33.40  ? 117 GLN   A CG  1 
ATOM   889  C  CD  . GLN   A 1 111 ? 10.211 -9.296  5.848  1.00 40.62  ? 117 GLN   A CD  1 
ATOM   890  O  OE1 . GLN   A 1 111 ? 8.981  -9.158  5.913  1.00 42.56  ? 117 GLN   A OE1 1 
ATOM   891  N  NE2 . GLN   A 1 111 ? 10.774 -10.235 5.094  1.00 40.28  ? 117 GLN   A NE2 1 
ATOM   892  N  N   . HIS   A 1 112 ? 13.821 -6.365  7.218  1.00 20.45  ? 118 HIS   A N   1 
ATOM   893  C  CA  . HIS   A 1 112 ? 14.920 -5.942  6.314  1.00 19.52  ? 118 HIS   A CA  1 
ATOM   894  C  C   . HIS   A 1 112 ? 16.059 -5.172  6.996  1.00 20.08  ? 118 HIS   A C   1 
ATOM   895  O  O   . HIS   A 1 112 ? 17.097 -4.907  6.390  1.00 22.50  ? 118 HIS   A O   1 
ATOM   896  C  CB  . HIS   A 1 112 ? 14.321 -5.093  5.199  1.00 18.59  ? 118 HIS   A CB  1 
ATOM   897  C  CG  . HIS   A 1 112 ? 13.202 -5.816  4.485  1.00 22.40  ? 118 HIS   A CG  1 
ATOM   898  N  ND1 . HIS   A 1 112 ? 11.881 -5.423  4.604  1.00 22.33  ? 118 HIS   A ND1 1 
ATOM   899  C  CD2 . HIS   A 1 112 ? 13.276 -6.813  3.559  1.00 25.68  ? 118 HIS   A CD2 1 
ATOM   900  C  CE1 . HIS   A 1 112 ? 11.174 -6.277  3.864  1.00 26.21  ? 118 HIS   A CE1 1 
ATOM   901  N  NE2 . HIS   A 1 112 ? 11.981 -7.109  3.198  1.00 27.59  ? 118 HIS   A NE2 1 
ATOM   902  N  N   . GLY   A 1 113 ? 15.827 -4.711  8.245  1.00 17.91  ? 119 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 113 ? 16.847 -3.920  8.926  1.00 16.19  ? 119 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 113 ? 16.250 -2.749  9.688  1.00 14.10  ? 119 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 113 ? 15.063 -2.748  10.025 1.00 13.45  ? 119 GLY   A O   1 
ATOM   906  N  N   . VAL   A 1 114 ? 17.097 -1.733  9.965  1.00 12.94  ? 120 VAL   A N   1 
ATOM   907  C  CA  . VAL   A 1 114 ? 16.633 -0.541  10.737 1.00 12.80  ? 120 VAL   A CA  1 
ATOM   908  C  C   . VAL   A 1 114 ? 15.791 0.392   9.868  1.00 11.90  ? 120 VAL   A C   1 
ATOM   909  O  O   . VAL   A 1 114 ? 16.213 0.732   8.747  1.00 11.85  ? 120 VAL   A O   1 
ATOM   910  C  CB  . VAL   A 1 114 ? 17.856 0.227   11.295 1.00 12.33  ? 120 VAL   A CB  1 
ATOM   911  C  CG1 . VAL   A 1 114 ? 17.428 1.538   11.989 1.00 13.52  ? 120 VAL   A CG1 1 
ATOM   912  C  CG2 . VAL   A 1 114 ? 18.643 -0.658  12.265 1.00 13.50  ? 120 VAL   A CG2 1 
ATOM   913  N  N   . VAL   A 1 115 ? 14.634 0.784   10.360 1.00 11.23  ? 121 VAL   A N   1 
ATOM   914  C  CA  . VAL   A 1 115 ? 13.685 1.613   9.677  1.00 12.12  ? 121 VAL   A CA  1 
ATOM   915  C  C   . VAL   A 1 115 ? 13.841 3.067   10.082 1.00 12.31  ? 121 VAL   A C   1 
ATOM   916  O  O   . VAL   A 1 115 ? 13.708 3.992   9.284  1.00 13.04  ? 121 VAL   A O   1 
ATOM   917  C  CB  . VAL   A 1 115 ? 12.240 1.111   9.947  1.00 12.96  ? 121 VAL   A CB  1 
ATOM   918  C  CG1 . VAL   A 1 115 ? 11.157 2.089   9.418  1.00 15.45  ? 121 VAL   A CG1 1 
ATOM   919  C  CG2 . VAL   A 1 115 ? 12.016 -0.302  9.398  1.00 14.73  ? 121 VAL   A CG2 1 
ATOM   920  N  N   . GLY   A 1 116 ? 14.041 3.301   11.381 1.00 11.60  ? 122 GLY   A N   1 
ATOM   921  C  CA  . GLY   A 1 116 ? 14.135 4.658   11.910 1.00 11.90  ? 122 GLY   A CA  1 
ATOM   922  C  C   . GLY   A 1 116 ? 14.348 4.680   13.408 1.00 10.67  ? 122 GLY   A C   1 
ATOM   923  O  O   . GLY   A 1 116 ? 14.686 3.628   13.989 1.00 10.99  ? 122 GLY   A O   1 
ATOM   924  N  N   . ILE   A 1 117 ? 14.228 5.870   14.020 1.00 10.54  ? 123 ILE   A N   1 
ATOM   925  C  CA  . ILE   A 1 117 ? 14.436 5.985   15.474 1.00 10.25  ? 123 ILE   A CA  1 
ATOM   926  C  C   . ILE   A 1 117 ? 13.289 6.736   16.088 1.00 11.13  ? 123 ILE   A C   1 
ATOM   927  O  O   . ILE   A 1 117 ? 12.699 7.620   15.447 1.00 12.03  ? 123 ILE   A O   1 
ATOM   928  C  CB  . ILE   A 1 117 ? 15.775 6.698   15.849 1.00 11.37  ? 123 ILE   A CB  1 
ATOM   929  C  CG1 . ILE   A 1 117 ? 15.933 8.032   15.123 1.00 12.81  ? 123 ILE   A CG1 1 
ATOM   930  C  CG2 . ILE   A 1 117 ? 16.945 5.742   15.645 1.00 12.50  ? 123 ILE   A CG2 1 
ATOM   931  C  CD1 . ILE   A 1 117 ? 17.214 8.855   15.598 1.00 14.54  ? 123 ILE   A CD1 1 
ATOM   932  N  N   . VAL   A 1 118 ? 13.027 6.496   17.371 1.00 11.18  ? 124 VAL   A N   1 
ATOM   933  C  CA  . VAL   A 1 118 ? 11.966 7.212   18.089 1.00 11.56  ? 124 VAL   A CA  1 
ATOM   934  C  C   . VAL   A 1 118 ? 12.326 8.705   18.088 1.00 11.79  ? 124 VAL   A C   1 
ATOM   935  O  O   . VAL   A 1 118 ? 13.478 9.081   18.408 1.00 12.09  ? 124 VAL   A O   1 
ATOM   936  C  CB  . VAL   A 1 118 ? 11.833 6.730   19.561 1.00 12.37  ? 124 VAL   A CB  1 
ATOM   937  C  CG1 . VAL   A 1 118 ? 10.829 7.589   20.353 1.00 12.38  ? 124 VAL   A CG1 1 
ATOM   938  C  CG2 . VAL   A 1 118 ? 11.377 5.265   19.624 1.00 12.96  ? 124 VAL   A CG2 1 
ATOM   939  N  N   . SER   A 1 119 ? 11.336 9.578   17.785 1.00 11.95  ? 125 SER   A N   1 
ATOM   940  C  CA  . SER   A 1 119 ? 11.512 11.033  17.736 1.00 13.23  ? 125 SER   A CA  1 
ATOM   941  C  C   . SER   A 1 119 ? 10.395 11.770  18.492 1.00 15.56  ? 125 SER   A C   1 
ATOM   942  O  O   . SER   A 1 119 ? 10.662 12.887  18.967 1.00 17.37  ? 125 SER   A O   1 
ATOM   943  C  CB  . SER   A 1 119 ? 11.639 11.477  16.282 1.00 14.01  ? 125 SER   A CB  1 
ATOM   944  O  OG  . SER   A 1 119 ? 11.717 12.885  16.116 1.00 15.69  ? 125 SER   A OG  1 
ATOM   945  N  N   . THR   A 1 120 ? 9.192  11.182  18.636 1.00 15.19  ? 126 THR   A N   1 
ATOM   946  C  CA  . THR   A 1 120 ? 8.083  11.911  19.316 1.00 16.67  ? 126 THR   A CA  1 
ATOM   947  C  C   . THR   A 1 120 ? 7.321  10.942  20.236 1.00 17.47  ? 126 THR   A C   1 
ATOM   948  O  O   . THR   A 1 120 ? 7.441  9.743   20.100 1.00 17.08  ? 126 THR   A O   1 
ATOM   949  C  CB  . THR   A 1 120 ? 7.112  12.594  18.284 1.00 19.18  ? 126 THR   A CB  1 
ATOM   950  O  OG1 . THR   A 1 120 ? 6.320  11.598  17.637 1.00 20.17  ? 126 THR   A OG1 1 
ATOM   951  C  CG2 . THR   A 1 120 ? 7.815  13.483  17.269 1.00 19.27  ? 126 THR   A CG2 1 
ATOM   952  N  N   . GLY   A 1 121 ? 6.490  11.468  21.175 1.00 18.87  ? 127 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 121 ? 5.724  10.617  22.071 1.00 21.59  ? 127 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 121 ? 4.548  11.330  22.725 1.00 24.01  ? 127 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 121 ? 4.222  12.417  22.339 1.00 26.89  ? 127 GLY   A O   1 
ATOM   956  N  N   . GLY   A 1 122 ? 3.920  10.620  23.679 1.00 22.93  ? 128 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 122 ? 2.789  11.116  24.469 1.00 22.83  ? 128 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 122 ? 1.449  10.560  24.031 1.00 24.12  ? 128 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 122 ? 1.281  10.172  22.860 1.00 24.32  ? 128 GLY   A O   1 
ATOM   960  N  N   . ASN   A 1 123 ? 0.479  10.584  24.937 1.00 23.94  ? 129 ASN   A N   1 
ATOM   961  C  CA  . ASN   A 1 123 ? -0.907 10.254  24.567 1.00 25.55  ? 129 ASN   A CA  1 
ATOM   962  C  C   . ASN   A 1 123 ? -1.092 8.859   24.019 1.00 22.65  ? 129 ASN   A C   1 
ATOM   963  O  O   . ASN   A 1 123 ? -2.115 8.589   23.352 1.00 21.45  ? 129 ASN   A O   1 
ATOM   964  C  CB  . ASN   A 1 123 ? -1.438 11.331  23.548 1.00 28.86  ? 129 ASN   A CB  1 
ATOM   965  C  CG  . ASN   A 1 123 ? -1.512 12.721  24.140 1.00 34.81  ? 129 ASN   A CG  1 
ATOM   966  O  OD1 . ASN   A 1 123 ? -1.594 12.870  25.365 1.00 37.54  ? 129 ASN   A OD1 1 
ATOM   967  N  ND2 . ASN   A 1 123 ? -1.569 13.762  23.303 1.00 34.11  ? 129 ASN   A ND2 1 
ATOM   968  N  N   . GLY   A 1 124 ? -0.194 7.946   24.363 1.00 20.42  ? 130 GLY   A N   1 
ATOM   969  C  CA  . GLY   A 1 124 ? -0.273 6.600   23.860 1.00 19.29  ? 130 GLY   A CA  1 
ATOM   970  C  C   . GLY   A 1 124 ? 0.151  6.484   22.406 1.00 15.86  ? 130 GLY   A C   1 
ATOM   971  O  O   . GLY   A 1 124 ? -0.047 5.416   21.869 1.00 18.37  ? 130 GLY   A O   1 
ATOM   972  N  N   . LEU   A 1 125 ? 0.864  7.488   21.848 1.00 15.20  ? 131 LEU   A N   1 
ATOM   973  C  CA  . LEU   A 1 125 ? 1.428  7.436   20.475 1.00 15.46  ? 131 LEU   A CA  1 
ATOM   974  C  C   . LEU   A 1 125 ? 2.944  7.517   20.540 1.00 16.79  ? 131 LEU   A C   1 
ATOM   975  O  O   . LEU   A 1 125 ? 3.523  8.093   21.496 1.00 18.66  ? 131 LEU   A O   1 
ATOM   976  C  CB  . LEU   A 1 125 ? 0.913  8.618   19.655 1.00 16.26  ? 131 LEU   A CB  1 
ATOM   977  C  CG  . LEU   A 1 125 ? -0.617 8.608   19.443 1.00 17.09  ? 131 LEU   A CG  1 
ATOM   978  C  CD1 . LEU   A 1 125 ? -1.102 10.013  19.065 1.00 19.02  ? 131 LEU   A CD1 1 
ATOM   979  C  CD2 . LEU   A 1 125 ? -1.012 7.500   18.396 1.00 17.40  ? 131 LEU   A CD2 1 
ATOM   980  N  N   . VAL   A 1 126 ? 3.596  6.908   19.555 1.00 14.43  ? 132 VAL   A N   1 
ATOM   981  C  CA  . VAL   A 1 126 ? 5.053  7.013   19.422 1.00 14.78  ? 132 VAL   A CA  1 
ATOM   982  C  C   . VAL   A 1 126 ? 5.304  7.399   17.932 1.00 14.41  ? 132 VAL   A C   1 
ATOM   983  O  O   . VAL   A 1 126 ? 4.704  6.819   17.026 1.00 14.47  ? 132 VAL   A O   1 
ATOM   984  C  CB  . VAL   A 1 126 ? 5.753  5.702   19.860 1.00 14.15  ? 132 VAL   A CB  1 
ATOM   985  C  CG1 . VAL   A 1 126 ? 5.158  4.478   19.161 1.00 14.78  ? 132 VAL   A CG1 1 
ATOM   986  C  CG2 . VAL   A 1 126 ? 7.280  5.807   19.665 1.00 14.04  ? 132 VAL   A CG2 1 
ATOM   987  N  N   . GLY   A 1 127 ? 6.211  8.342   17.694 1.00 13.76  ? 133 GLY   A N   1 
ATOM   988  C  CA  . GLY   A 1 127 ? 6.560  8.736   16.321 1.00 13.76  ? 133 GLY   A CA  1 
ATOM   989  C  C   . GLY   A 1 127 ? 8.014  8.406   16.047 1.00 13.59  ? 133 GLY   A C   1 
ATOM   990  O  O   . GLY   A 1 127 ? 8.887  8.549   16.924 1.00 15.16  ? 133 GLY   A O   1 
ATOM   991  N  N   . PHE   A 1 128 ? 8.244  7.968   14.840 1.00 12.60  ? 134 PHE   A N   1 
ATOM   992  C  CA  . PHE   A 1 128 ? 9.608  7.549   14.390 1.00 12.74  ? 134 PHE   A CA  1 
ATOM   993  C  C   . PHE   A 1 128 ? 10.074 8.350   13.204 1.00 13.26  ? 134 PHE   A C   1 
ATOM   994  O  O   . PHE   A 1 128 ? 9.314  8.523   12.251 1.00 13.81  ? 134 PHE   A O   1 
ATOM   995  C  CB  . PHE   A 1 128 ? 9.572  6.059   13.958 1.00 13.19  ? 134 PHE   A CB  1 
ATOM   996  C  CG  . PHE   A 1 128 ? 8.953  5.131   14.995 1.00 12.73  ? 134 PHE   A CG  1 
ATOM   997  C  CD1 . PHE   A 1 128 ? 9.694  4.671   16.075 1.00 12.31  ? 134 PHE   A CD1 1 
ATOM   998  C  CD2 . PHE   A 1 128 ? 7.633  4.705   14.858 1.00 13.68  ? 134 PHE   A CD2 1 
ATOM   999  C  CE1 . PHE   A 1 128 ? 9.115  3.793   16.997 1.00 12.83  ? 134 PHE   A CE1 1 
ATOM   1000 C  CE2 . PHE   A 1 128 ? 7.067  3.859   15.796 1.00 13.99  ? 134 PHE   A CE2 1 
ATOM   1001 C  CZ  . PHE   A 1 128 ? 7.822  3.375   16.835 1.00 13.25  ? 134 PHE   A CZ  1 
ATOM   1002 N  N   . ALA   A 1 129 ? 11.311 8.857   13.286 1.00 12.55  ? 135 ALA   A N   1 
ATOM   1003 C  CA  . ALA   A 1 129 ? 11.964 9.518   12.130 1.00 13.05  ? 135 ALA   A CA  1 
ATOM   1004 C  C   . ALA   A 1 129 ? 12.453 8.440   11.169 1.00 12.62  ? 135 ALA   A C   1 
ATOM   1005 O  O   . ALA   A 1 129 ? 13.339 7.648   11.537 1.00 12.36  ? 135 ALA   A O   1 
ATOM   1006 C  CB  . ALA   A 1 129 ? 13.111 10.375  12.630 1.00 12.66  ? 135 ALA   A CB  1 
ATOM   1007 N  N   . ASP   A 1 130 ? 11.903 8.386   9.949  1.00 12.33  ? 136 ASP   A N   1 
ATOM   1008 C  CA  . ASP   A 1 130 ? 12.324 7.384   8.974  1.00 13.64  ? 136 ASP   A CA  1 
ATOM   1009 C  C   . ASP   A 1 130 ? 13.717 7.685   8.450  1.00 13.28  ? 136 ASP   A C   1 
ATOM   1010 O  O   . ASP   A 1 130 ? 14.108 8.851   8.322  1.00 14.39  ? 136 ASP   A O   1 
ATOM   1011 C  CB  . ASP   A 1 130 ? 11.333 7.456   7.775  1.00 15.78  ? 136 ASP   A CB  1 
ATOM   1012 C  CG  . ASP   A 1 130 ? 11.608 6.467   6.696  1.00 20.38  ? 136 ASP   A CG  1 
ATOM   1013 O  OD1 . ASP   A 1 130 ? 11.718 5.249   7.006  1.00 17.70  ? 136 ASP   A OD1 1 
ATOM   1014 O  OD2 . ASP   A 1 130 ? 11.849 6.917   5.533  1.00 24.88  ? 136 ASP   A OD2 1 
ATOM   1015 N  N   . VAL   A 1 131 ? 14.478 6.632   8.183  1.00 12.52  ? 137 VAL   A N   1 
ATOM   1016 C  CA  . VAL   A 1 131 ? 15.804 6.769   7.530  1.00 13.15  ? 137 VAL   A CA  1 
ATOM   1017 C  C   . VAL   A 1 131 ? 15.937 5.965   6.237  1.00 13.22  ? 137 VAL   A C   1 
ATOM   1018 O  O   . VAL   A 1 131 ? 17.005 6.003   5.605  1.00 12.58  ? 137 VAL   A O   1 
ATOM   1019 C  CB  . VAL   A 1 131 ? 16.976 6.428   8.479  1.00 12.13  ? 137 VAL   A CB  1 
ATOM   1020 C  CG1 . VAL   A 1 131 ? 17.019 7.376   9.707  1.00 12.92  ? 137 VAL   A CG1 1 
ATOM   1021 C  CG2 . VAL   A 1 131 ? 16.984 4.955   8.905  1.00 13.18  ? 137 VAL   A CG2 1 
ATOM   1022 N  N   . ARG   A 1 132 ? 14.865 5.288   5.805  1.00 13.48  ? 138 ARG   A N   1 
ATOM   1023 C  CA  . ARG   A 1 132 ? 14.942 4.369   4.658  1.00 13.49  ? 138 ARG   A CA  1 
ATOM   1024 C  C   . ARG   A 1 132 ? 15.201 5.044   3.336  1.00 15.11  ? 138 ARG   A C   1 
ATOM   1025 O  O   . ARG   A 1 132 ? 15.669 4.387   2.389  1.00 15.63  ? 138 ARG   A O   1 
ATOM   1026 C  CB  . ARG   A 1 132 ? 13.670 3.487   4.573  1.00 14.42  ? 138 ARG   A CB  1 
ATOM   1027 C  CG  . ARG   A 1 132 ? 13.564 2.529   5.799  1.00 13.77  ? 138 ARG   A CG  1 
ATOM   1028 C  CD  . ARG   A 1 132 ? 12.275 1.734   5.631  1.00 14.31  ? 138 ARG   A CD  1 
ATOM   1029 N  NE  . ARG   A 1 132 ? 11.115 2.620   5.848  1.00 14.99  ? 138 ARG   A NE  1 
ATOM   1030 C  CZ  . ARG   A 1 132 ? 9.850  2.226   5.938  1.00 16.44  ? 138 ARG   A CZ  1 
ATOM   1031 N  NH1 . ARG   A 1 132 ? 9.519  0.973   5.652  1.00 16.90  ? 138 ARG   A NH1 1 
ATOM   1032 N  NH2 . ARG   A 1 132 ? 8.899  3.112   6.230  1.00 17.99  ? 138 ARG   A NH2 1 
ATOM   1033 N  N   . ASP   A 1 133 ? 14.912 6.359   3.226  1.00 14.44  ? 139 ASP   A N   1 
ATOM   1034 C  CA  . ASP   A 1 133 ? 15.163 7.063   1.969  1.00 15.55  ? 139 ASP   A CA  1 
ATOM   1035 C  C   . ASP   A 1 133 ? 16.595 7.598   1.901  1.00 15.82  ? 139 ASP   A C   1 
ATOM   1036 O  O   . ASP   A 1 133 ? 16.989 8.089   0.846  1.00 16.93  ? 139 ASP   A O   1 
ATOM   1037 C  CB  . ASP   A 1 133 ? 14.155 8.239   1.846  1.00 17.09  ? 139 ASP   A CB  1 
ATOM   1038 C  CG  . ASP   A 1 133 ? 14.362 9.301   2.928  1.00 19.85  ? 139 ASP   A CG  1 
ATOM   1039 O  OD1 . ASP   A 1 133 ? 14.493 8.937   4.128  1.00 19.20  ? 139 ASP   A OD1 1 
ATOM   1040 O  OD2 . ASP   A 1 133 ? 14.381 10.494  2.606  1.00 21.99  ? 139 ASP   A OD2 1 
ATOM   1041 N  N   . LEU   A 1 134 ? 17.400 7.521   2.974  1.00 13.93  ? 140 LEU   A N   1 
ATOM   1042 C  CA  . LEU   A 1 134 ? 18.757 8.078   3.016  1.00 13.61  ? 140 LEU   A CA  1 
ATOM   1043 C  C   . LEU   A 1 134 ? 19.722 7.033   2.480  1.00 13.74  ? 140 LEU   A C   1 
ATOM   1044 O  O   . LEU   A 1 134 ? 20.419 6.331   3.220  1.00 13.64  ? 140 LEU   A O   1 
ATOM   1045 C  CB  . LEU   A 1 134 ? 19.100 8.491   4.461  1.00 13.55  ? 140 LEU   A CB  1 
ATOM   1046 C  CG  . LEU   A 1 134 ? 18.117 9.500   5.123  1.00 14.67  ? 140 LEU   A CG  1 
ATOM   1047 C  CD1 . LEU   A 1 134 ? 18.532 9.741   6.585  1.00 15.21  ? 140 LEU   A CD1 1 
ATOM   1048 C  CD2 . LEU   A 1 134 ? 18.096 10.813  4.370  1.00 17.05  ? 140 LEU   A CD2 1 
ATOM   1049 N  N   . LEU   A 1 135 ? 19.741 6.901   1.150  1.00 13.78  ? 141 LEU   A N   1 
ATOM   1050 C  CA  . LEU   A 1 135 ? 20.507 5.809   0.509  1.00 14.55  ? 141 LEU   A CA  1 
ATOM   1051 C  C   . LEU   A 1 135 ? 21.999 5.921   0.692  1.00 15.43  ? 141 LEU   A C   1 
ATOM   1052 O  O   . LEU   A 1 135 ? 22.721 4.898   0.765  1.00 16.18  ? 141 LEU   A O   1 
ATOM   1053 C  CB  . LEU   A 1 135 ? 20.170 5.691   -1.012 1.00 16.27  ? 141 LEU   A CB  1 
ATOM   1054 C  CG  . LEU   A 1 135 ? 18.650 5.686   -1.330 1.00 17.55  ? 141 LEU   A CG  1 
ATOM   1055 C  CD1 . LEU   A 1 135 ? 18.418 5.338   -2.837 1.00 19.48  ? 141 LEU   A CD1 1 
ATOM   1056 C  CD2 . LEU   A 1 135 ? 17.848 4.660   -0.503 1.00 19.21  ? 141 LEU   A CD2 1 
ATOM   1057 N  N   . TRP   A 1 136 ? 22.468 7.162   0.865  1.00 14.36  ? 142 TRP   A N   1 
ATOM   1058 C  CA  . TRP   A 1 136 ? 23.873 7.419   1.062  1.00 14.58  ? 142 TRP   A CA  1 
ATOM   1059 C  C   . TRP   A 1 136 ? 24.415 6.817   2.348  1.00 14.71  ? 142 TRP   A C   1 
ATOM   1060 O  O   . TRP   A 1 136 ? 25.639 6.689   2.475  1.00 15.83  ? 142 TRP   A O   1 
ATOM   1061 C  CB  . TRP   A 1 136 ? 24.170 8.929   0.938  1.00 14.83  ? 142 TRP   A CB  1 
ATOM   1062 C  CG  . TRP   A 1 136 ? 23.357 9.757   1.878  1.00 13.86  ? 142 TRP   A CG  1 
ATOM   1063 C  CD1 . TRP   A 1 136 ? 22.223 10.446  1.578  1.00 15.05  ? 142 TRP   A CD1 1 
ATOM   1064 C  CD2 . TRP   A 1 136 ? 23.690 10.091  3.242  1.00 14.63  ? 142 TRP   A CD2 1 
ATOM   1065 N  NE1 . TRP   A 1 136 ? 21.753 11.103  2.719  1.00 16.52  ? 142 TRP   A NE1 1 
ATOM   1066 C  CE2 . TRP   A 1 136 ? 22.666 10.925  3.731  1.00 14.88  ? 142 TRP   A CE2 1 
ATOM   1067 C  CE3 . TRP   A 1 136 ? 24.755 9.769   4.085  1.00 15.34  ? 142 TRP   A CE3 1 
ATOM   1068 C  CZ2 . TRP   A 1 136 ? 22.680 11.416  5.051  1.00 16.18  ? 142 TRP   A CZ2 1 
ATOM   1069 C  CZ3 . TRP   A 1 136 ? 24.791 10.289  5.371  1.00 17.53  ? 142 TRP   A CZ3 1 
ATOM   1070 C  CH2 . TRP   A 1 136 ? 23.770 11.113  5.827  1.00 16.76  ? 142 TRP   A CH2 1 
ATOM   1071 N  N   . LEU   A 1 137 ? 23.554 6.490   3.352  1.00 13.89  ? 143 LEU   A N   1 
ATOM   1072 C  CA  . LEU   A 1 137 ? 24.063 5.835   4.565  1.00 15.55  ? 143 LEU   A CA  1 
ATOM   1073 C  C   . LEU   A 1 137 ? 24.756 4.506   4.247  1.00 18.15  ? 143 LEU   A C   1 
ATOM   1074 O  O   . LEU   A 1 137 ? 25.578 4.048   5.052  1.00 19.24  ? 143 LEU   A O   1 
ATOM   1075 C  CB  . LEU   A 1 137 ? 22.915 5.574   5.536  1.00 15.04  ? 143 LEU   A CB  1 
ATOM   1076 C  CG  . LEU   A 1 137 ? 22.356 6.813   6.223  1.00 15.10  ? 143 LEU   A CG  1 
ATOM   1077 C  CD1 . LEU   A 1 137 ? 21.115 6.448   6.987  1.00 16.62  ? 143 LEU   A CD1 1 
ATOM   1078 C  CD2 . LEU   A 1 137 ? 23.438 7.447   7.201  1.00 16.23  ? 143 LEU   A CD2 1 
ATOM   1079 N  N   . ASP   A 1 138 ? 24.446 3.886   3.070  1.00 20.00  ? 144 ASP   A N   1 
ATOM   1080 C  CA  . ASP   A 1 138 ? 25.026 2.573   2.705  1.00 22.30  ? 144 ASP   A CA  1 
ATOM   1081 C  C   . ASP   A 1 138 ? 26.353 2.653   1.977  1.00 26.20  ? 144 ASP   A C   1 
ATOM   1082 O  O   . ASP   A 1 138 ? 26.910 1.604   1.622  1.00 28.44  ? 144 ASP   A O   1 
ATOM   1083 C  CB  . ASP   A 1 138 ? 24.056 1.821   1.746  1.00 23.01  ? 144 ASP   A CB  1 
ATOM   1084 C  CG  . ASP   A 1 138 ? 22.700 1.480   2.310  1.00 26.66  ? 144 ASP   A CG  1 
ATOM   1085 O  OD1 . ASP   A 1 138 ? 22.532 1.561   3.549  1.00 27.70  ? 144 ASP   A OD1 1 
ATOM   1086 O  OD2 . ASP   A 1 138 ? 21.782 1.145   1.518  1.00 33.61  ? 144 ASP   A OD2 1 
ATOM   1087 N  N   . GLU   A 1 139 ? 26.878 3.858   1.722  1.00 26.80  ? 145 GLU   A N   1 
ATOM   1088 C  CA  . GLU   A 1 139 ? 28.132 3.994   0.964  1.00 29.60  ? 145 GLU   A CA  1 
ATOM   1089 C  C   . GLU   A 1 139 ? 29.135 4.918   1.637  1.00 30.04  ? 145 GLU   A C   1 
ATOM   1090 O  O   . GLU   A 1 139 ? 28.771 5.623   2.585  1.00 30.64  ? 145 GLU   A O   1 
ATOM   1091 C  CB  . GLU   A 1 139 ? 27.808 4.471   -0.452 1.00 34.10  ? 145 GLU   A CB  1 
ATOM   1092 C  CG  . GLU   A 1 139 ? 27.075 5.796   -0.480 1.00 42.27  ? 145 GLU   A CG  1 
ATOM   1093 C  CD  . GLU   A 1 139 ? 26.218 6.056   -1.706 1.00 49.87  ? 145 GLU   A CD  1 
ATOM   1094 O  OE1 . GLU   A 1 139 ? 25.978 7.248   -2.017 1.00 48.72  ? 145 GLU   A OE1 1 
ATOM   1095 O  OE2 . GLU   A 1 139 ? 25.789 5.072   -2.355 1.00 53.64  ? 145 GLU   A OE2 1 
ATOM   1096 N  N   . SER   B 1 1   ? 21.813 -21.293 7.587  1.00 17.82  ? 7   SER   C N   1 
ATOM   1097 C  CA  . SER   B 1 1   ? 20.661 -21.102 8.503  1.00 17.36  ? 7   SER   C CA  1 
ATOM   1098 C  C   . SER   B 1 1   ? 20.638 -22.205 9.570  1.00 16.90  ? 7   SER   C C   1 
ATOM   1099 O  O   . SER   B 1 1   ? 21.311 -23.239 9.419  1.00 18.17  ? 7   SER   C O   1 
ATOM   1100 C  CB  . SER   B 1 1   ? 19.354 -21.133 7.704  1.00 20.85  ? 7   SER   C CB  1 
ATOM   1101 O  OG  . SER   B 1 1   ? 19.203 -22.416 7.124  1.00 24.64  ? 7   SER   C OG  1 
ATOM   1102 N  N   . GLY   B 1 2   ? 19.897 -21.969 10.649 1.00 17.04  ? 8   GLY   C N   1 
ATOM   1103 C  CA  . GLY   B 1 2   ? 19.720 -22.971 11.697 1.00 15.82  ? 8   GLY   C CA  1 
ATOM   1104 C  C   . GLY   B 1 2   ? 19.438 -22.353 13.059 1.00 14.90  ? 8   GLY   C C   1 
ATOM   1105 O  O   . GLY   B 1 2   ? 19.796 -21.215 13.313 1.00 16.01  ? 8   GLY   C O   1 
ATOM   1106 N  N   . ALA   B 1 3   ? 18.760 -23.094 13.930 1.00 13.97  ? 9   ALA   C N   1 
ATOM   1107 C  CA  . ALA   B 1 3   ? 18.434 -22.611 15.273 1.00 14.15  ? 9   ALA   C CA  1 
ATOM   1108 C  C   . ALA   B 1 3   ? 18.555 -23.731 16.295 1.00 13.26  ? 9   ALA   C C   1 
ATOM   1109 O  O   . ALA   B 1 3   ? 18.607 -24.920 15.917 1.00 14.71  ? 9   ALA   C O   1 
ATOM   1110 C  CB  . ALA   B 1 3   ? 16.994 -22.059 15.267 1.00 17.30  ? 9   ALA   C CB  1 
ATOM   1111 N  N   . ILE   B 1 4   ? 18.566 -23.350 17.576 1.00 12.95  ? 10  ILE   C N   1 
ATOM   1112 C  CA  . ILE   B 1 4   ? 18.474 -24.291 18.692 1.00 14.28  ? 10  ILE   C CA  1 
ATOM   1113 C  C   . ILE   B 1 4   ? 17.081 -24.116 19.304 1.00 13.81  ? 10  ILE   C C   1 
ATOM   1114 O  O   . ILE   B 1 4   ? 16.640 -22.962 19.503 1.00 14.37  ? 10  ILE   C O   1 
ATOM   1115 C  CB  . ILE   B 1 4   ? 19.516 -23.981 19.778 1.00 13.28  ? 10  ILE   C CB  1 
ATOM   1116 C  CG1 . ILE   B 1 4   ? 20.940 -23.816 19.189 1.00 14.46  ? 10  ILE   C CG1 1 
ATOM   1117 C  CG2 . ILE   B 1 4   ? 19.460 -25.060 20.883 1.00 14.79  ? 10  ILE   C CG2 1 
ATOM   1118 C  CD1 . ILE   B 1 4   ? 21.890 -23.214 20.216 1.00 14.42  ? 10  ILE   C CD1 1 
ATOM   1119 N  N   . TYR   B 1 5   ? 16.376 -25.209 19.602 1.00 13.79  ? 11  TYR   C N   1 
ATOM   1120 C  CA  . TYR   B 1 5   ? 15.051 -25.150 20.184 1.00 14.82  ? 11  TYR   C CA  1 
ATOM   1121 C  C   . TYR   B 1 5   ? 15.100 -25.817 21.548 1.00 14.53  ? 11  TYR   C C   1 
ATOM   1122 O  O   . TYR   B 1 5   ? 15.185 -27.051 21.625 1.00 16.25  ? 11  TYR   C O   1 
ATOM   1123 C  CB  . TYR   B 1 5   ? 14.016 -25.849 19.272 1.00 15.76  ? 11  TYR   C CB  1 
ATOM   1124 C  CG  . TYR   B 1 5   ? 13.811 -25.086 17.967 1.00 15.70  ? 11  TYR   C CG  1 
ATOM   1125 C  CD1 . TYR   B 1 5   ? 12.984 -23.964 17.910 1.00 15.48  ? 11  TYR   C CD1 1 
ATOM   1126 C  CD2 . TYR   B 1 5   ? 14.504 -25.438 16.815 1.00 16.57  ? 11  TYR   C CD2 1 
ATOM   1127 C  CE1 . TYR   B 1 5   ? 12.843 -23.232 16.732 1.00 17.12  ? 11  TYR   C CE1 1 
ATOM   1128 C  CE2 . TYR   B 1 5   ? 14.379 -24.712 15.638 1.00 18.15  ? 11  TYR   C CE2 1 
ATOM   1129 C  CZ  . TYR   B 1 5   ? 13.550 -23.612 15.604 1.00 18.00  ? 11  TYR   C CZ  1 
ATOM   1130 O  OH  . TYR   B 1 5   ? 13.475 -22.888 14.434 1.00 19.80  ? 11  TYR   C OH  1 
ATOM   1131 N  N   . VAL   B 1 6   ? 15.135 -25.053 22.637 1.00 15.47  ? 12  VAL   C N   1 
ATOM   1132 C  CA  . VAL   B 1 6   ? 15.212 -25.596 24.011 1.00 16.29  ? 12  VAL   C CA  1 
ATOM   1133 C  C   . VAL   B 1 6   ? 14.077 -24.988 24.850 1.00 16.38  ? 12  VAL   C C   1 
ATOM   1134 O  O   . VAL   B 1 6   ? 13.905 -23.769 24.855 1.00 15.53  ? 12  VAL   C O   1 
ATOM   1135 C  CB  . VAL   B 1 6   ? 16.620 -25.338 24.627 1.00 17.36  ? 12  VAL   C CB  1 
ATOM   1136 C  CG1 . VAL   B 1 6   ? 17.016 -23.848 24.561 1.00 17.95  ? 12  VAL   C CG1 1 
ATOM   1137 C  CG2 . VAL   B 1 6   ? 16.659 -25.845 26.056 1.00 18.91  ? 12  VAL   C CG2 1 
ATOM   1138 N  N   . GLY   B 1 7   ? 13.258 -25.823 25.523 1.00 17.75  ? 13  GLY   C N   1 
ATOM   1139 C  CA  . GLY   B 1 7   ? 12.141 -25.268 26.296 1.00 18.25  ? 13  GLY   C CA  1 
ATOM   1140 C  C   . GLY   B 1 7   ? 11.193 -24.441 25.429 1.00 18.31  ? 13  GLY   C C   1 
ATOM   1141 O  O   . GLY   B 1 7   ? 10.924 -24.816 24.281 1.00 19.62  ? 13  GLY   C O   1 
ATOM   1142 N  N   . ASN   B 1 8   ? 10.867 -23.238 25.870 1.00 18.33  ? 14  ASN   C N   1 
ATOM   1143 C  CA  . ASN   B 1 8   ? 10.086 -22.328 25.032 1.00 18.69  ? 14  ASN   C CA  1 
ATOM   1144 C  C   . ASN   B 1 8   ? 10.967 -21.226 24.460 1.00 17.85  ? 14  ASN   C C   1 
ATOM   1145 O  O   . ASN   B 1 8   ? 10.511 -20.095 24.305 1.00 18.14  ? 14  ASN   C O   1 
ATOM   1146 C  CB  . ASN   B 1 8   ? 8.841  -21.765 25.753 1.00 21.19  ? 14  ASN   C CB  1 
ATOM   1147 C  CG  . ASN   B 1 8   ? 7.758  -22.821 25.911 1.00 28.00  ? 14  ASN   C CG  1 
ATOM   1148 O  OD1 . ASN   B 1 8   ? 6.886  -22.979 25.054 1.00 30.84  ? 14  ASN   C OD1 1 
ATOM   1149 N  ND2 . ASN   B 1 8   ? 7.841  -23.594 26.977 1.00 29.60  ? 14  ASN   C ND2 1 
ATOM   1150 N  N   . TYR   B 1 9   ? 12.172 -21.600 24.049 1.00 15.14  ? 15  TYR   C N   1 
ATOM   1151 C  CA  . TYR   B 1 9   ? 13.138 -20.644 23.473 1.00 14.95  ? 15  TYR   C CA  1 
ATOM   1152 C  C   . TYR   B 1 9   ? 13.620 -21.105 22.102 1.00 14.61  ? 15  TYR   C C   1 
ATOM   1153 O  O   . TYR   B 1 9   ? 13.804 -22.314 21.889 1.00 15.32  ? 15  TYR   C O   1 
ATOM   1154 C  CB  . TYR   B 1 9   ? 14.374 -20.516 24.398 1.00 15.25  ? 15  TYR   C CB  1 
ATOM   1155 C  CG  . TYR   B 1 9   ? 14.066 -19.971 25.788 1.00 16.36  ? 15  TYR   C CG  1 
ATOM   1156 C  CD1 . TYR   B 1 9   ? 13.485 -18.715 25.955 1.00 18.45  ? 15  TYR   C CD1 1 
ATOM   1157 C  CD2 . TYR   B 1 9   ? 14.333 -20.724 26.930 1.00 18.76  ? 15  TYR   C CD2 1 
ATOM   1158 C  CE1 . TYR   B 1 9   ? 13.176 -18.227 27.226 1.00 21.29  ? 15  TYR   C CE1 1 
ATOM   1159 C  CE2 . TYR   B 1 9   ? 14.085 -20.212 28.209 1.00 21.37  ? 15  TYR   C CE2 1 
ATOM   1160 C  CZ  . TYR   B 1 9   ? 13.538 -18.953 28.343 1.00 24.10  ? 15  TYR   C CZ  1 
ATOM   1161 O  OH  . TYR   B 1 9   ? 13.247 -18.419 29.589 1.00 29.60  ? 15  TYR   C OH  1 
ATOM   1162 N  N   . ARG   B 1 10  ? 13.875 -20.156 21.202 1.00 13.47  ? 16  ARG   C N   1 
ATOM   1163 C  CA  . ARG   B 1 10  ? 14.491 -20.382 19.888 1.00 13.03  ? 16  ARG   C CA  1 
ATOM   1164 C  C   . ARG   B 1 10  ? 15.753 -19.511 19.891 1.00 12.96  ? 16  ARG   C C   1 
ATOM   1165 O  O   . ARG   B 1 10  ? 15.675 -18.285 20.095 1.00 13.67  ? 16  ARG   C O   1 
ATOM   1166 C  CB  . ARG   B 1 10  ? 13.546 -19.945 18.746 1.00 14.30  ? 16  ARG   C CB  1 
ATOM   1167 C  CG  . ARG   B 1 10  ? 14.180 -19.782 17.365 1.00 15.18  ? 16  ARG   C CG  1 
ATOM   1168 C  CD  . ARG   B 1 10  ? 13.095 -19.490 16.328 1.00 15.66  ? 16  ARG   C CD  1 
ATOM   1169 N  NE  . ARG   B 1 10  ? 13.527 -18.544 15.286 1.00 16.09  ? 16  ARG   C NE  1 
ATOM   1170 C  CZ  . ARG   B 1 10  ? 14.034 -18.850 14.083 1.00 17.94  ? 16  ARG   C CZ  1 
ATOM   1171 N  NH1 . ARG   B 1 10  ? 14.295 -20.120 13.759 1.00 19.45  ? 16  ARG   C NH1 1 
ATOM   1172 N  NH2 . ARG   B 1 10  ? 14.373 -17.884 13.233 1.00 18.10  ? 16  ARG   C NH2 1 
ATOM   1173 N  N   . VAL   B 1 11  ? 16.934 -20.131 19.668 1.00 12.49  ? 17  VAL   C N   1 
ATOM   1174 C  CA  . VAL   B 1 11  ? 18.232 -19.401 19.631 1.00 11.91  ? 17  VAL   C CA  1 
ATOM   1175 C  C   . VAL   B 1 11  ? 18.715 -19.333 18.208 1.00 12.90  ? 17  VAL   C C   1 
ATOM   1176 O  O   . VAL   B 1 11  ? 18.873 -20.413 17.568 1.00 13.04  ? 17  VAL   C O   1 
ATOM   1177 C  CB  . VAL   B 1 11  ? 19.281 -20.147 20.497 1.00 12.84  ? 17  VAL   C CB  1 
ATOM   1178 C  CG1 . VAL   B 1 11  ? 20.537 -19.301 20.588 1.00 14.65  ? 17  VAL   C CG1 1 
ATOM   1179 C  CG2 . VAL   B 1 11  ? 18.740 -20.501 21.896 1.00 14.84  ? 17  VAL   C CG2 1 
ATOM   1180 N  N   . VAL   B 1 12  ? 18.941 -18.135 17.683 1.00 12.04  ? 18  VAL   C N   1 
ATOM   1181 C  CA  A VAL   B 1 12  ? 19.395 -17.959 16.298 0.50 12.34  ? 18  VAL   C CA  1 
ATOM   1182 C  CA  B VAL   B 1 12  ? 19.352 -17.989 16.295 0.50 13.75  ? 18  VAL   C CA  1 
ATOM   1183 C  C   . VAL   B 1 12  ? 20.523 -16.965 16.220 1.00 12.77  ? 18  VAL   C C   1 
ATOM   1184 O  O   . VAL   B 1 12  ? 20.767 -16.193 17.173 1.00 13.08  ? 18  VAL   C O   1 
ATOM   1185 C  CB  A VAL   B 1 12  ? 18.244 -17.432 15.377 0.50 12.05  ? 18  VAL   C CB  1 
ATOM   1186 C  CB  B VAL   B 1 12  ? 18.073 -17.472 15.529 0.50 16.76  ? 18  VAL   C CB  1 
ATOM   1187 C  CG1 A VAL   B 1 12  ? 17.263 -18.558 15.087 0.50 13.31  ? 18  VAL   C CG1 1 
ATOM   1188 C  CG1 B VAL   B 1 12  ? 18.330 -17.248 14.061 0.50 17.25  ? 18  VAL   C CG1 1 
ATOM   1189 C  CG2 A VAL   B 1 12  ? 17.602 -16.118 15.912 0.50 9.44   ? 18  VAL   C CG2 1 
ATOM   1190 C  CG2 B VAL   B 1 12  ? 16.926 -18.457 15.679 0.50 19.52  ? 18  VAL   C CG2 1 
ATOM   1191 N  N   . ASN   B 1 13  ? 21.226 -16.909 15.059 1.00 11.95  ? 19  ASN   C N   1 
ATOM   1192 C  CA  . ASN   B 1 13  ? 22.224 -15.862 14.864 1.00 11.53  ? 19  ASN   C CA  1 
ATOM   1193 C  C   . ASN   B 1 13  ? 21.419 -14.523 14.809 1.00 13.11  ? 19  ASN   C C   1 
ATOM   1194 O  O   . ASN   B 1 13  ? 20.408 -14.420 14.116 1.00 12.80  ? 19  ASN   C O   1 
ATOM   1195 C  CB  . ASN   B 1 13  ? 22.924 -16.010 13.494 1.00 11.97  ? 19  ASN   C CB  1 
ATOM   1196 C  CG  . ASN   B 1 13  ? 23.777 -17.268 13.420 1.00 12.62  ? 19  ASN   C CG  1 
ATOM   1197 O  OD1 . ASN   B 1 13  ? 23.325 -18.346 12.999 1.00 13.22  ? 19  ASN   C OD1 1 
ATOM   1198 N  ND2 . ASN   B 1 13  ? 25.003 -17.154 13.913 1.00 12.51  ? 19  ASN   C ND2 1 
ATOM   1199 N  N   . ARG   B 1 14  ? 21.910 -13.492 15.518 1.00 12.57  ? 20  ARG   C N   1 
ATOM   1200 C  CA  . ARG   B 1 14  ? 21.191 -12.186 15.539 1.00 12.76  ? 20  ARG   C CA  1 
ATOM   1201 C  C   . ARG   B 1 14  ? 21.028 -11.667 14.101 1.00 13.83  ? 20  ARG   C C   1 
ATOM   1202 O  O   . ARG   B 1 14  ? 19.972 -11.118 13.748 1.00 13.41  ? 20  ARG   C O   1 
ATOM   1203 C  CB  . ARG   B 1 14  ? 21.980 -11.180 16.393 1.00 12.40  ? 20  ARG   C CB  1 
ATOM   1204 C  CG  . ARG   B 1 14  ? 21.143 -9.873  16.652 1.00 12.91  ? 20  ARG   C CG  1 
ATOM   1205 C  CD  . ARG   B 1 14  ? 22.006 -8.913  17.440 1.00 13.90  ? 20  ARG   C CD  1 
ATOM   1206 N  NE  . ARG   B 1 14  ? 21.326 -7.650  17.854 1.00 14.24  ? 20  ARG   C NE  1 
ATOM   1207 C  CZ  . ARG   B 1 14  ? 21.255 -6.549  17.107 1.00 14.01  ? 20  ARG   C CZ  1 
ATOM   1208 N  NH1 . ARG   B 1 14  ? 21.641 -6.575  15.840 1.00 15.33  ? 20  ARG   C NH1 1 
ATOM   1209 N  NH2 . ARG   B 1 14  ? 20.760 -5.425  17.615 1.00 14.35  ? 20  ARG   C NH2 1 
ATOM   1210 N  N   . HIS   B 1 15  ? 22.045 -11.861 13.245 1.00 13.18  ? 21  HIS   C N   1 
ATOM   1211 C  CA  . HIS   B 1 15  ? 21.984 -11.311 11.878 1.00 13.64  ? 21  HIS   C CA  1 
ATOM   1212 C  C   . HIS   B 1 15  ? 20.963 -12.042 10.979 1.00 14.80  ? 21  HIS   C C   1 
ATOM   1213 O  O   . HIS   B 1 15  ? 20.652 -11.541 9.907  1.00 15.99  ? 21  HIS   C O   1 
ATOM   1214 C  CB  . HIS   B 1 15  ? 23.387 -11.196 11.213 1.00 13.67  ? 21  HIS   C CB  1 
ATOM   1215 C  CG  . HIS   B 1 15  ? 23.977 -12.517 10.772 1.00 13.37  ? 21  HIS   C CG  1 
ATOM   1216 N  ND1 . HIS   B 1 15  ? 24.718 -13.332 11.637 1.00 14.23  ? 21  HIS   C ND1 1 
ATOM   1217 C  CD2 . HIS   B 1 15  ? 23.977 -13.084 9.539  1.00 14.14  ? 21  HIS   C CD2 1 
ATOM   1218 C  CE1 . HIS   B 1 15  ? 25.104 -14.390 10.909 1.00 14.50  ? 21  HIS   C CE1 1 
ATOM   1219 N  NE2 . HIS   B 1 15  ? 24.673 -14.289 9.645  1.00 14.51  ? 21  HIS   C NE2 1 
ATOM   1220 N  N   . LEU   B 1 16  ? 20.453 -13.202 11.403 1.00 13.89  ? 22  LEU   C N   1 
ATOM   1221 C  CA  . LEU   B 1 16  ? 19.429 -13.954 10.659 1.00 14.89  ? 22  LEU   C CA  1 
ATOM   1222 C  C   . LEU   B 1 16  ? 18.050 -13.894 11.336 1.00 15.48  ? 22  LEU   C C   1 
ATOM   1223 O  O   . LEU   B 1 16  ? 17.132 -14.626 10.909 1.00 15.92  ? 22  LEU   C O   1 
ATOM   1224 C  CB  . LEU   B 1 16  ? 19.901 -15.406 10.472 1.00 14.98  ? 22  LEU   C CB  1 
ATOM   1225 C  CG  . LEU   B 1 16  ? 21.202 -15.540 9.672  1.00 15.21  ? 22  LEU   C CG  1 
ATOM   1226 C  CD1 . LEU   B 1 16  ? 21.624 -17.029 9.584  1.00 15.93  ? 22  LEU   C CD1 1 
ATOM   1227 C  CD2 . LEU   B 1 16  ? 21.090 -14.909 8.265  1.00 15.22  ? 22  LEU   C CD2 1 
ATOM   1228 N  N   . ALA   B 1 17  ? 17.901 -13.135 12.440 1.00 15.23  ? 23  ALA   C N   1 
ATOM   1229 C  CA  . ALA   B 1 17  ? 16.613 -13.079 13.154 1.00 15.49  ? 23  ALA   C CA  1 
ATOM   1230 C  C   . ALA   B 1 17  ? 15.502 -12.519 12.268 1.00 16.59  ? 23  ALA   C C   1 
ATOM   1231 O  O   . ALA   B 1 17  ? 15.739 -11.592 11.467 1.00 16.89  ? 23  ALA   C O   1 
ATOM   1232 C  CB  . ALA   B 1 17  ? 16.734 -12.236 14.435 1.00 16.62  ? 23  ALA   C CB  1 
ATOM   1233 N  N   . THR   B 1 18  ? 14.321 -13.087 12.422 1.00 16.09  ? 24  THR   C N   1 
ATOM   1234 C  CA  . THR   B 1 18  ? 13.156 -12.676 11.634 1.00 17.54  ? 24  THR   C CA  1 
ATOM   1235 C  C   . THR   B 1 18  ? 12.335 -11.605 12.386 1.00 16.32  ? 24  THR   C C   1 
ATOM   1236 O  O   . THR   B 1 18  ? 12.571 -11.300 13.568 1.00 17.63  ? 24  THR   C O   1 
ATOM   1237 C  CB  . THR   B 1 18  ? 12.243 -13.917 11.371 1.00 18.59  ? 24  THR   C CB  1 
ATOM   1238 O  OG1 . THR   B 1 18  ? 11.701 -14.323 12.611 1.00 19.08  ? 24  THR   C OG1 1 
ATOM   1239 C  CG2 . THR   B 1 18  ? 12.974 -15.104 10.693 1.00 19.51  ? 24  THR   C CG2 1 
ATOM   1240 N  N   . HIS   B 1 19  ? 11.300 -11.027 11.693 1.00 17.83  ? 25  HIS   C N   1 
ATOM   1241 C  CA  . HIS   B 1 19  ? 10.387 -10.095 12.388 1.00 18.90  ? 25  HIS   C CA  1 
ATOM   1242 C  C   . HIS   B 1 19  ? 9.679  -10.833 13.527 1.00 16.38  ? 25  HIS   C C   1 
ATOM   1243 O  O   . HIS   B 1 19  ? 9.613  -10.276 14.626 1.00 17.54  ? 25  HIS   C O   1 
ATOM   1244 C  CB  . HIS   B 1 19  ? 9.293  -9.560  11.431 1.00 20.34  ? 25  HIS   C CB  1 
ATOM   1245 C  CG  . HIS   B 1 19  ? 8.148  -8.858  12.143 1.00 21.74  ? 25  HIS   C CG  1 
ATOM   1246 N  ND1 . HIS   B 1 19  ? 8.294  -7.594  12.676 1.00 24.10  ? 25  HIS   C ND1 1 
ATOM   1247 C  CD2 . HIS   B 1 19  ? 6.954  -9.351  12.538 1.00 23.37  ? 25  HIS   C CD2 1 
ATOM   1248 C  CE1 . HIS   B 1 19  ? 7.114  -7.272  13.197 1.00 24.31  ? 25  HIS   C CE1 1 
ATOM   1249 N  NE2 . HIS   B 1 19  ? 6.282  -8.316  13.184 1.00 24.29  ? 25  HIS   C NE2 1 
ATOM   1250 N  N   . ASN   B 1 20  ? 9.282  -12.091 13.326 1.00 17.36  ? 26  ASN   C N   1 
ATOM   1251 C  CA  . ASN   B 1 20  ? 8.628  -12.834 14.415 1.00 18.55  ? 26  ASN   C CA  1 
ATOM   1252 C  C   . ASN   B 1 20  ? 9.557  -13.011 15.616 1.00 17.43  ? 26  ASN   C C   1 
ATOM   1253 O  O   . ASN   B 1 20  ? 9.131  -12.899 16.765 1.00 16.41  ? 26  ASN   C O   1 
ATOM   1254 C  CB  . ASN   B 1 20  ? 8.091  -14.196 13.955 1.00 19.64  ? 26  ASN   C CB  1 
ATOM   1255 C  CG  . ASN   B 1 20  ? 7.266  -14.882 15.047 1.00 25.59  ? 26  ASN   C CG  1 
ATOM   1256 O  OD1 . ASN   B 1 20  ? 6.151  -14.438 15.388 1.00 29.35  ? 26  ASN   C OD1 1 
ATOM   1257 N  ND2 . ASN   B 1 20  ? 7.811  -15.919 15.677 1.00 27.61  ? 26  ASN   C ND2 1 
ATOM   1258 N  N   . ASP   B 1 21  ? 10.890 -13.234 15.348 1.00 16.40  ? 27  ASP   C N   1 
ATOM   1259 C  CA  . ASP   B 1 21  ? 11.828 -13.317 16.457 1.00 15.72  ? 27  ASP   C CA  1 
ATOM   1260 C  C   . ASP   B 1 21  ? 11.874 -12.009 17.271 1.00 15.04  ? 27  ASP   C C   1 
ATOM   1261 O  O   . ASP   B 1 21  ? 11.802 -12.012 18.488 1.00 16.28  ? 27  ASP   C O   1 
ATOM   1262 C  CB  . ASP   B 1 21  ? 13.257 -13.626 15.964 1.00 15.08  ? 27  ASP   C CB  1 
ATOM   1263 C  CG  . ASP   B 1 21  ? 13.460 -15.041 15.483 1.00 15.97  ? 27  ASP   C CG  1 
ATOM   1264 O  OD1 . ASP   B 1 21  ? 12.855 -15.966 16.089 1.00 17.05  ? 27  ASP   C OD1 1 
ATOM   1265 O  OD2 . ASP   B 1 21  ? 14.158 -15.220 14.440 1.00 15.70  ? 27  ASP   C OD2 1 
ATOM   1266 N  N   . TRP   B 1 22  ? 11.981 -10.858 16.574 1.00 15.33  ? 28  TRP   C N   1 
ATOM   1267 C  CA  . TRP   B 1 22  ? 12.026 -9.558  17.249 1.00 16.33  ? 28  TRP   C CA  1 
ATOM   1268 C  C   . TRP   B 1 22  ? 10.681 -9.219  17.954 1.00 16.25  ? 28  TRP   C C   1 
ATOM   1269 O  O   . TRP   B 1 22  ? 10.702 -8.601  19.027 1.00 16.83  ? 28  TRP   C O   1 
ATOM   1270 C  CB  . TRP   B 1 22  ? 12.384 -8.469  16.258 1.00 16.61  ? 28  TRP   C CB  1 
ATOM   1271 C  CG  . TRP   B 1 22  ? 13.878 -8.429  16.008 1.00 16.14  ? 28  TRP   C CG  1 
ATOM   1272 C  CD1 . TRP   B 1 22  ? 14.540 -8.913  14.919 1.00 17.12  ? 28  TRP   C CD1 1 
ATOM   1273 C  CD2 . TRP   B 1 22  ? 14.883 -7.828  16.857 1.00 15.36  ? 28  TRP   C CD2 1 
ATOM   1274 N  NE1 . TRP   B 1 22  ? 15.896 -8.640  15.023 1.00 17.24  ? 28  TRP   C NE1 1 
ATOM   1275 C  CE2 . TRP   B 1 22  ? 16.129 -7.992  16.215 1.00 17.00  ? 28  TRP   C CE2 1 
ATOM   1276 C  CE3 . TRP   B 1 22  ? 14.841 -7.131  18.069 1.00 17.73  ? 28  TRP   C CE3 1 
ATOM   1277 C  CZ2 . TRP   B 1 22  ? 17.291 -7.432  16.702 1.00 15.88  ? 28  TRP   C CZ2 1 
ATOM   1278 C  CZ3 . TRP   B 1 22  ? 16.030 -6.640  18.587 1.00 18.15  ? 28  TRP   C CZ3 1 
ATOM   1279 C  CH2 . TRP   B 1 22  ? 17.233 -6.783  17.885 1.00 17.14  ? 28  TRP   C CH2 1 
ATOM   1280 N  N   . ALA   B 1 23  ? 9.557  -9.692  17.401 1.00 16.89  ? 29  ALA   C N   1 
ATOM   1281 C  CA  . ALA   B 1 23  ? 8.237  -9.452  18.009 1.00 17.62  ? 29  ALA   C CA  1 
ATOM   1282 C  C   . ALA   B 1 23  ? 7.978  -10.351 19.231 1.00 19.22  ? 29  ALA   C C   1 
ATOM   1283 O  O   . ALA   B 1 23  ? 7.032  -10.142 19.990 1.00 19.70  ? 29  ALA   C O   1 
ATOM   1284 C  CB  . ALA   B 1 23  ? 7.149  -9.691  16.975 1.00 18.30  ? 29  ALA   C CB  1 
ATOM   1285 N  N   . ASN   B 1 24  ? 8.827  -11.379 19.443 1.00 18.40  ? 30  ASN   C N   1 
ATOM   1286 C  CA  . ASN   B 1 24  ? 8.720  -12.291 20.594 1.00 17.49  ? 30  ASN   C CA  1 
ATOM   1287 C  C   . ASN   B 1 24  ? 10.081 -12.356 21.303 1.00 16.95  ? 30  ASN   C C   1 
ATOM   1288 O  O   . ASN   B 1 24  ? 10.500 -13.430 21.751 1.00 15.99  ? 30  ASN   C O   1 
ATOM   1289 C  CB  . ASN   B 1 24  ? 8.262  -13.671 20.082 1.00 18.42  ? 30  ASN   C CB  1 
ATOM   1290 C  CG  . ASN   B 1 24  ? 6.844  -13.614 19.588 1.00 20.01  ? 30  ASN   C CG  1 
ATOM   1291 O  OD1 . ASN   B 1 24  ? 5.893  -13.629 20.419 1.00 21.92  ? 30  ASN   C OD1 1 
ATOM   1292 N  ND2 . ASN   B 1 24  ? 6.657  -13.490 18.269 1.00 19.99  ? 30  ASN   C ND2 1 
ATOM   1293 N  N   . LEU   B 1 25  ? 10.785 -11.241 21.372 1.00 17.07  ? 31  LEU   C N   1 
ATOM   1294 C  CA  . LEU   B 1 25  ? 12.163 -11.218 21.874 1.00 16.54  ? 31  LEU   C CA  1 
ATOM   1295 C  C   . LEU   B 1 25  ? 12.306 -11.528 23.349 1.00 17.85  ? 31  LEU   C C   1 
ATOM   1296 O  O   . LEU   B 1 25  ? 11.541 -11.025 24.186 1.00 18.32  ? 31  LEU   C O   1 
ATOM   1297 C  CB  . LEU   B 1 25  ? 12.724 -9.822  21.603 1.00 17.31  ? 31  LEU   C CB  1 
ATOM   1298 C  CG  . LEU   B 1 25  ? 14.201 -9.645  21.979 1.00 16.43  ? 31  LEU   C CG  1 
ATOM   1299 C  CD1 . LEU   B 1 25  ? 15.139 -10.515 21.103 1.00 16.89  ? 31  LEU   C CD1 1 
ATOM   1300 C  CD2 . LEU   B 1 25  ? 14.609 -8.186  21.860 1.00 18.62  ? 31  LEU   C CD2 1 
ATOM   1301 N  N   . VAL   B 1 26  ? 13.289 -12.357 23.682 1.00 16.78  ? 32  VAL   C N   1 
ATOM   1302 C  CA  . VAL   B 1 26  ? 13.623 -12.622 25.086 1.00 17.41  ? 32  VAL   C CA  1 
ATOM   1303 C  C   . VAL   B 1 26  ? 14.961 -11.906 25.394 1.00 18.07  ? 32  VAL   C C   1 
ATOM   1304 O  O   . VAL   B 1 26  ? 15.082 -11.252 26.435 1.00 19.49  ? 32  VAL   C O   1 
ATOM   1305 C  CB  . VAL   B 1 26  ? 13.781 -14.138 25.325 1.00 17.59  ? 32  VAL   C CB  1 
ATOM   1306 C  CG1 . VAL   B 1 26  ? 14.326 -14.432 26.727 1.00 19.45  ? 32  VAL   C CG1 1 
ATOM   1307 C  CG2 . VAL   B 1 26  ? 12.445 -14.849 25.106 1.00 17.03  ? 32  VAL   C CG2 1 
ATOM   1308 N  N   . TRP   B 1 27  ? 15.998 -12.064 24.523 1.00 15.77  ? 33  TRP   C N   1 
ATOM   1309 C  CA  . TRP   B 1 27  ? 17.313 -11.488 24.826 1.00 16.18  ? 33  TRP   C CA  1 
ATOM   1310 C  C   . TRP   B 1 27  ? 18.101 -11.420 23.512 1.00 15.60  ? 33  TRP   C C   1 
ATOM   1311 O  O   . TRP   B 1 27  ? 17.920 -12.303 22.652 1.00 15.18  ? 33  TRP   C O   1 
ATOM   1312 C  CB  . TRP   B 1 27  ? 18.034 -12.405 25.867 1.00 17.16  ? 33  TRP   C CB  1 
ATOM   1313 C  CG  . TRP   B 1 27  ? 19.508 -12.139 26.066 1.00 17.79  ? 33  TRP   C CG  1 
ATOM   1314 C  CD1 . TRP   B 1 27  ? 20.080 -11.193 26.872 1.00 19.91  ? 33  TRP   C CD1 1 
ATOM   1315 C  CD2 . TRP   B 1 27  ? 20.591 -12.809 25.405 1.00 16.50  ? 33  TRP   C CD2 1 
ATOM   1316 N  NE1 . TRP   B 1 27  ? 21.466 -11.280 26.800 1.00 20.91  ? 33  TRP   C NE1 1 
ATOM   1317 C  CE2 . TRP   B 1 27  ? 21.797 -12.282 25.922 1.00 18.13  ? 33  TRP   C CE2 1 
ATOM   1318 C  CE3 . TRP   B 1 27  ? 20.659 -13.833 24.441 1.00 16.32  ? 33  TRP   C CE3 1 
ATOM   1319 C  CZ2 . TRP   B 1 27  ? 23.054 -12.758 25.523 1.00 17.91  ? 33  TRP   C CZ2 1 
ATOM   1320 C  CZ3 . TRP   B 1 27  ? 21.907 -14.340 24.101 1.00 17.47  ? 33  TRP   C CZ3 1 
ATOM   1321 C  CH2 . TRP   B 1 27  ? 23.077 -13.750 24.577 1.00 17.63  ? 33  TRP   C CH2 1 
ATOM   1322 N  N   . GLU   B 1 28  ? 18.956 -10.418 23.355 1.00 15.19  ? 34  GLU   C N   1 
ATOM   1323 C  CA  . GLU   B 1 28  ? 19.808 -10.338 22.172 1.00 15.93  ? 34  GLU   C CA  1 
ATOM   1324 C  C   . GLU   B 1 28  ? 21.113 -9.661  22.530 1.00 16.26  ? 34  GLU   C C   1 
ATOM   1325 O  O   . GLU   B 1 28  ? 21.131 -8.765  23.427 1.00 15.90  ? 34  GLU   C O   1 
ATOM   1326 C  CB  . GLU   B 1 28  ? 19.130 -9.658  20.974 1.00 16.11  ? 34  GLU   C CB  1 
ATOM   1327 C  CG  . GLU   B 1 28  ? 18.571 -8.282  21.260 1.00 17.11  ? 34  GLU   C CG  1 
ATOM   1328 C  CD  . GLU   B 1 28  ? 19.551 -7.122  21.211 1.00 19.30  ? 34  GLU   C CD  1 
ATOM   1329 O  OE1 . GLU   B 1 28  ? 19.258 -6.102  21.872 1.00 21.06  ? 34  GLU   C OE1 1 
ATOM   1330 O  OE2 . GLU   B 1 28  ? 20.567 -7.179  20.476 1.00 18.05  ? 34  GLU   C OE2 1 
ATOM   1331 N  N   . ASP   B 1 29  ? 22.194 -10.016 21.822 1.00 14.78  ? 35  ASP   C N   1 
ATOM   1332 C  CA  . ASP   B 1 29  ? 23.484 -9.387  22.059 1.00 14.65  ? 35  ASP   C CA  1 
ATOM   1333 C  C   . ASP   B 1 29  ? 24.255 -9.339  20.740 1.00 15.37  ? 35  ASP   C C   1 
ATOM   1334 O  O   . ASP   B 1 29  ? 24.688 -10.394 20.257 1.00 14.67  ? 35  ASP   C O   1 
ATOM   1335 C  CB  . ASP   B 1 29  ? 24.217 -10.171 23.163 1.00 15.43  ? 35  ASP   C CB  1 
ATOM   1336 C  CG  . ASP   B 1 29  ? 25.543 -9.601  23.572 1.00 19.99  ? 35  ASP   C CG  1 
ATOM   1337 O  OD1 . ASP   B 1 29  ? 26.274 -9.129  22.701 1.00 19.79  ? 35  ASP   C OD1 1 
ATOM   1338 O  OD2 . ASP   B 1 29  ? 25.904 -9.747  24.748 1.00 23.41  ? 35  ASP   C OD2 1 
ATOM   1339 N  N   . SER   B 1 30  ? 24.404 -8.127  20.161 1.00 14.42  ? 36  SER   C N   1 
ATOM   1340 C  CA  A SER   B 1 30  ? 25.125 -7.967  18.904 0.50 14.70  ? 36  SER   C CA  1 
ATOM   1341 C  CA  B SER   B 1 30  ? 25.109 -8.023  18.893 0.50 15.07  ? 36  SER   C CA  1 
ATOM   1342 C  C   . SER   B 1 30  ? 26.593 -8.411  18.991 1.00 15.36  ? 36  SER   C C   1 
ATOM   1343 O  O   . SER   B 1 30  ? 27.109 -9.016  18.036 1.00 15.05  ? 36  SER   C O   1 
ATOM   1344 C  CB  A SER   B 1 30  ? 25.031 -6.525  18.415 0.50 16.11  ? 36  SER   C CB  1 
ATOM   1345 C  CB  B SER   B 1 30  ? 24.924 -6.643  18.280 0.50 17.46  ? 36  SER   C CB  1 
ATOM   1346 O  OG  A SER   B 1 30  ? 25.971 -6.261  17.384 0.50 16.18  ? 36  SER   C OG  1 
ATOM   1347 O  OG  B SER   B 1 30  ? 25.402 -5.670  19.189 0.50 19.24  ? 36  SER   C OG  1 
ATOM   1348 N  N   . SER   B 1 31  ? 27.266 -8.135  20.141 1.00 15.32  ? 37  SER   C N   1 
ATOM   1349 C  CA  . SER   B 1 31  ? 28.679 -8.528  20.244 1.00 16.36  ? 37  SER   C CA  1 
ATOM   1350 C  C   . SER   B 1 31  ? 28.862 -10.041 20.208 1.00 15.10  ? 37  SER   C C   1 
ATOM   1351 O  O   . SER   B 1 31  ? 29.943 -10.501 19.831 1.00 16.03  ? 37  SER   C O   1 
ATOM   1352 C  CB  . SER   B 1 31  ? 29.300 -7.987  21.520 1.00 19.15  ? 37  SER   C CB  1 
ATOM   1353 O  OG  . SER   B 1 31  ? 28.910 -8.687  22.678 1.00 23.59  ? 37  SER   C OG  1 
ATOM   1354 N  N   . ARG   B 1 32  ? 27.805 -10.847 20.507 1.00 13.96  ? 38  ARG   C N   1 
ATOM   1355 C  CA  . ARG   B 1 32  ? 27.875 -12.308 20.445 1.00 13.82  ? 38  ARG   C CA  1 
ATOM   1356 C  C   . ARG   B 1 32  ? 27.248 -12.871 19.163 1.00 13.09  ? 38  ARG   C C   1 
ATOM   1357 O  O   . ARG   B 1 32  ? 27.280 -14.093 18.966 1.00 12.43  ? 38  ARG   C O   1 
ATOM   1358 C  CB  . ARG   B 1 32  ? 27.120 -12.900 21.657 1.00 15.82  ? 38  ARG   C CB  1 
ATOM   1359 C  CG  . ARG   B 1 32  ? 27.799 -12.558 22.994 1.00 16.32  ? 38  ARG   C CG  1 
ATOM   1360 C  CD  . ARG   B 1 32  ? 27.027 -13.111 24.202 1.00 13.96  ? 38  ARG   C CD  1 
ATOM   1361 N  NE  . ARG   B 1 32  ? 27.113 -14.597 24.252 1.00 14.01  ? 38  ARG   C NE  1 
ATOM   1362 C  CZ  . ARG   B 1 32  ? 27.074 -15.340 25.352 1.00 14.30  ? 38  ARG   C CZ  1 
ATOM   1363 N  NH1 . ARG   B 1 32  ? 26.956 -14.771 26.546 1.00 14.85  ? 38  ARG   C NH1 1 
ATOM   1364 N  NH2 . ARG   B 1 32  ? 27.231 -16.662 25.272 1.00 14.06  ? 38  ARG   C NH2 1 
ATOM   1365 N  N   . ASP   B 1 33  ? 26.566 -12.036 18.351 1.00 12.68  ? 39  ASP   C N   1 
ATOM   1366 C  CA  . ASP   B 1 33  ? 25.790 -12.493 17.209 1.00 12.65  ? 39  ASP   C CA  1 
ATOM   1367 C  C   . ASP   B 1 33  ? 24.658 -13.448 17.629 1.00 11.88  ? 39  ASP   C C   1 
ATOM   1368 O  O   . ASP   B 1 33  ? 24.384 -14.400 16.900 1.00 11.90  ? 39  ASP   C O   1 
ATOM   1369 C  CB  . ASP   B 1 33  ? 26.636 -13.101 16.095 1.00 11.70  ? 39  ASP   C CB  1 
ATOM   1370 C  CG  . ASP   B 1 33  ? 25.852 -13.432 14.816 1.00 13.37  ? 39  ASP   C CG  1 
ATOM   1371 O  OD1 . ASP   B 1 33  ? 24.951 -12.635 14.424 1.00 13.92  ? 39  ASP   C OD1 1 
ATOM   1372 O  OD2 . ASP   B 1 33  ? 26.162 -14.455 14.184 1.00 12.74  ? 39  ASP   C OD2 1 
ATOM   1373 N  N   . LEU   B 1 34  ? 24.018 -13.245 18.789 1.00 11.53  ? 40  LEU   C N   1 
ATOM   1374 C  CA  . LEU   B 1 34  ? 22.923 -14.137 19.249 1.00 12.07  ? 40  LEU   C CA  1 
ATOM   1375 C  C   . LEU   B 1 34  ? 21.629 -13.379 19.506 1.00 12.26  ? 40  LEU   C C   1 
ATOM   1376 O  O   . LEU   B 1 34  ? 21.644 -12.214 19.991 1.00 13.13  ? 40  LEU   C O   1 
ATOM   1377 C  CB  . LEU   B 1 34  ? 23.341 -14.824 20.572 1.00 12.75  ? 40  LEU   C CB  1 
ATOM   1378 C  CG  . LEU   B 1 34  ? 24.424 -15.948 20.449 1.00 13.07  ? 40  LEU   C CG  1 
ATOM   1379 C  CD1 . LEU   B 1 34  ? 24.668 -16.560 21.868 1.00 14.34  ? 40  LEU   C CD1 1 
ATOM   1380 C  CD2 . LEU   B 1 34  ? 23.973 -17.053 19.468 1.00 13.68  ? 40  LEU   C CD2 1 
ATOM   1381 N  N   . LEU   B 1 35  ? 20.534 -14.084 19.290 1.00 11.89  ? 41  LEU   C N   1 
ATOM   1382 C  CA  . LEU   B 1 35  ? 19.212 -13.541 19.654 1.00 13.23  ? 41  LEU   C CA  1 
ATOM   1383 C  C   . LEU   B 1 35  ? 18.364 -14.762 20.035 1.00 12.59  ? 41  LEU   C C   1 
ATOM   1384 O  O   . LEU   B 1 35  ? 18.479 -15.854 19.440 1.00 13.61  ? 41  LEU   C O   1 
ATOM   1385 C  CB  . LEU   B 1 35  ? 18.565 -12.831 18.421 1.00 12.73  ? 41  LEU   C CB  1 
ATOM   1386 C  CG  . LEU   B 1 35  ? 17.162 -12.227 18.685 1.00 13.25  ? 41  LEU   C CG  1 
ATOM   1387 C  CD1 . LEU   B 1 35  ? 16.960 -10.920 17.928 1.00 14.86  ? 41  LEU   C CD1 1 
ATOM   1388 C  CD2 . LEU   B 1 35  ? 16.076 -13.253 18.342 1.00 14.48  ? 41  LEU   C CD2 1 
ATOM   1389 N  N   . VAL   B 1 36  ? 17.578 -14.601 21.093 1.00 13.42  ? 42  VAL   C N   1 
ATOM   1390 C  CA  . VAL   B 1 36  ? 16.651 -15.617 21.605 1.00 13.10  ? 42  VAL   C CA  1 
ATOM   1391 C  C   . VAL   B 1 36  ? 15.230 -15.084 21.597 1.00 13.11  ? 42  VAL   C C   1 
ATOM   1392 O  O   . VAL   B 1 36  ? 15.007 -13.949 22.089 1.00 15.01  ? 42  VAL   C O   1 
ATOM   1393 C  CB  . VAL   B 1 36  ? 17.056 -16.060 23.027 1.00 13.52  ? 42  VAL   C CB  1 
ATOM   1394 C  CG1 . VAL   B 1 36  ? 16.074 -17.101 23.593 1.00 15.63  ? 42  VAL   C CG1 1 
ATOM   1395 C  CG2 . VAL   B 1 36  ? 18.490 -16.646 23.016 1.00 14.30  ? 42  VAL   C CG2 1 
ATOM   1396 N  N   . SER   B 1 37  ? 14.322 -15.848 21.040 1.00 13.59  ? 43  SER   C N   1 
ATOM   1397 C  CA  . SER   B 1 37  ? 12.911 -15.502 21.007 1.00 13.82  ? 43  SER   C CA  1 
ATOM   1398 C  C   . SER   B 1 37  ? 12.096 -16.593 21.689 1.00 15.24  ? 43  SER   C C   1 
ATOM   1399 O  O   . SER   B 1 37  ? 12.576 -17.707 21.951 1.00 15.68  ? 43  SER   C O   1 
ATOM   1400 C  CB  . SER   B 1 37  ? 12.431 -15.268 19.578 1.00 14.76  ? 43  SER   C CB  1 
ATOM   1401 O  OG  . SER   B 1 37  ? 12.597 -16.442 18.790 1.00 15.91  ? 43  SER   C OG  1 
ATOM   1402 N  N   . SER   B 1 38  ? 10.858 -16.253 22.074 1.00 16.02  ? 44  SER   C N   1 
ATOM   1403 C  CA  . SER   B 1 38  ? 9.980  -17.213 22.726 1.00 17.09  ? 44  SER   C CA  1 
ATOM   1404 C  C   . SER   B 1 38  ? 9.153  -18.021 21.702 1.00 18.86  ? 44  SER   C C   1 
ATOM   1405 O  O   . SER   B 1 38  ? 8.832  -17.520 20.629 1.00 20.28  ? 44  SER   C O   1 
ATOM   1406 C  CB  . SER   B 1 38  ? 9.081  -16.506 23.739 1.00 20.33  ? 44  SER   C CB  1 
ATOM   1407 O  OG  . SER   B 1 38  ? 8.227  -15.614 23.051 1.00 24.04  ? 44  SER   C OG  1 
ATOM   1408 N  N   . THR   B 1 39  ? 8.823  -19.279 22.021 1.00 18.68  ? 45  THR   C N   1 
ATOM   1409 C  CA  . THR   B 1 39  ? 8.074  -20.153 21.126 1.00 19.53  ? 45  THR   C CA  1 
ATOM   1410 C  C   . THR   B 1 39  ? 6.775  -20.612 21.821 1.00 22.36  ? 45  THR   C C   1 
ATOM   1411 O  O   . THR   B 1 39  ? 6.716  -20.696 23.043 1.00 21.69  ? 45  THR   C O   1 
ATOM   1412 C  CB  . THR   B 1 39  ? 8.920  -21.407 20.764 1.00 20.27  ? 45  THR   C CB  1 
ATOM   1413 O  OG1 . THR   B 1 39  ? 9.169  -22.167 21.944 1.00 21.52  ? 45  THR   C OG1 1 
ATOM   1414 C  CG2 . THR   B 1 39  ? 10.302 -21.048 20.160 1.00 20.88  ? 45  THR   C CG2 1 
ATOM   1415 N  N   . THR   B 1 40  ? 5.773  -20.988 21.019 1.00 24.93  ? 46  THR   C N   1 
ATOM   1416 C  CA  . THR   B 1 40  ? 4.531  -21.542 21.595 1.00 26.62  ? 46  THR   C CA  1 
ATOM   1417 C  C   . THR   B 1 40  ? 4.748  -23.020 21.934 1.00 26.86  ? 46  THR   C C   1 
ATOM   1418 O  O   . THR   B 1 40  ? 4.362  -23.481 23.020 1.00 28.49  ? 46  THR   C O   1 
ATOM   1419 C  CB  . THR   B 1 40  ? 3.347  -21.278 20.670 1.00 30.81  ? 46  THR   C CB  1 
ATOM   1420 O  OG1 . THR   B 1 40  ? 3.673  -21.819 19.397 1.00 35.03  ? 46  THR   C OG1 1 
ATOM   1421 C  CG2 . THR   B 1 40  ? 3.106  -19.802 20.481 1.00 30.10  ? 46  THR   C CG2 1 
ATOM   1422 N  N   . ALA   B 1 41  ? 5.406  -23.765 21.030 1.00 25.22  ? 47  ALA   C N   1 
ATOM   1423 C  CA  . ALA   B 1 41  ? 5.667  -25.181 21.284 1.00 24.99  ? 47  ALA   C CA  1 
ATOM   1424 C  C   . ALA   B 1 41  ? 7.001  -25.423 22.030 1.00 22.98  ? 47  ALA   C C   1 
ATOM   1425 O  O   . ALA   B 1 41  ? 7.942  -24.650 21.867 1.00 22.54  ? 47  ALA   C O   1 
ATOM   1426 C  CB  . ALA   B 1 41  ? 5.683  -25.942 19.961 1.00 26.75  ? 47  ALA   C CB  1 
ATOM   1427 N  N   . GLN   B 1 42  ? 7.113  -26.487 22.811 1.00 23.14  ? 48  GLN   C N   1 
ATOM   1428 C  CA  . GLN   B 1 42  ? 8.344  -26.839 23.502 1.00 24.06  ? 48  GLN   C CA  1 
ATOM   1429 C  C   . GLN   B 1 42  ? 9.326  -27.486 22.532 1.00 23.53  ? 48  GLN   C C   1 
ATOM   1430 O  O   . GLN   B 1 42  ? 8.933  -28.260 21.654 1.00 25.05  ? 48  GLN   C O   1 
ATOM   1431 C  CB  . GLN   B 1 42  ? 8.055  -27.767 24.687 1.00 29.67  ? 48  GLN   C CB  1 
ATOM   1432 C  CG  . GLN   B 1 42  ? 7.379  -27.023 25.840 1.00 39.46  ? 48  GLN   C CG  1 
ATOM   1433 C  CD  . GLN   B 1 42  ? 7.254  -27.955 27.008 1.00 50.81  ? 48  GLN   C CD  1 
ATOM   1434 O  OE1 . GLN   B 1 42  ? 6.373  -28.827 27.043 1.00 54.51  ? 48  GLN   C OE1 1 
ATOM   1435 N  NE2 . GLN   B 1 42  ? 8.141  -27.813 27.984 1.00 53.64  ? 48  GLN   C NE2 1 
ATOM   1436 N  N   . GLY   B 1 43  ? 10.596 -27.111 22.667 1.00 20.17  ? 49  GLY   C N   1 
ATOM   1437 C  CA  . GLY   B 1 43  ? 11.706 -27.656 21.884 1.00 19.86  ? 49  GLY   C CA  1 
ATOM   1438 C  C   . GLY   B 1 43  ? 12.344 -28.833 22.602 1.00 19.99  ? 49  GLY   C C   1 
ATOM   1439 O  O   . GLY   B 1 43  ? 12.126 -29.025 23.809 1.00 22.48  ? 49  GLY   C O   1 
ATOM   1440 N  N   . CYS   B 1 44  ? 13.171 -29.554 21.898 1.00 18.99  ? 50  CYS   C N   1 
ATOM   1441 C  CA  . CYS   B 1 44  ? 13.748 -30.775 22.447 1.00 19.92  ? 50  CYS   C CA  1 
ATOM   1442 C  C   . CYS   B 1 44  ? 15.253 -30.816 22.512 1.00 19.48  ? 50  CYS   C C   1 
ATOM   1443 O  O   . CYS   B 1 44  ? 15.796 -31.865 22.915 1.00 21.99  ? 50  CYS   C O   1 
ATOM   1444 C  CB  . CYS   B 1 44  ? 13.212 -31.966 21.658 1.00 21.06  ? 50  CYS   C CB  1 
ATOM   1445 S  SG  . CYS   B 1 44  ? 11.399 -32.059 21.679 1.00 29.38  ? 50  CYS   C SG  1 
ATOM   1446 N  N   . ASP   B 1 45  ? 15.951 -29.748 22.150 1.00 16.59  ? 51  ASP   C N   1 
ATOM   1447 C  CA  . ASP   B 1 45  ? 17.407 -29.755 22.191 1.00 16.60  ? 51  ASP   C CA  1 
ATOM   1448 C  C   . ASP   B 1 45  ? 17.815 -29.540 23.642 1.00 16.65  ? 51  ASP   C C   1 
ATOM   1449 O  O   . ASP   B 1 45  ? 17.100 -28.877 24.434 1.00 18.53  ? 51  ASP   C O   1 
ATOM   1450 C  CB  . ASP   B 1 45  ? 17.976 -28.601 21.333 1.00 16.20  ? 51  ASP   C CB  1 
ATOM   1451 C  CG  . ASP   B 1 45  ? 17.801 -28.777 19.840 1.00 19.62  ? 51  ASP   C CG  1 
ATOM   1452 O  OD1 . ASP   B 1 45  ? 17.825 -29.924 19.373 1.00 20.75  ? 51  ASP   C OD1 1 
ATOM   1453 O  OD2 . ASP   B 1 45  ? 17.636 -27.745 19.120 1.00 17.81  ? 51  ASP   C OD2 1 
ATOM   1454 N  N   . THR   B 1 46  ? 18.929 -30.166 24.019 1.00 14.50  ? 52  THR   C N   1 
ATOM   1455 C  CA  . THR   B 1 46  ? 19.529 -29.996 25.339 1.00 15.13  ? 52  THR   C CA  1 
ATOM   1456 C  C   . THR   B 1 46  ? 20.798 -29.163 25.158 1.00 14.60  ? 52  THR   C C   1 
ATOM   1457 O  O   . THR   B 1 46  ? 21.617 -29.458 24.272 1.00 15.31  ? 52  THR   C O   1 
ATOM   1458 C  CB  . THR   B 1 46  ? 19.932 -31.368 25.910 1.00 17.88  ? 52  THR   C CB  1 
ATOM   1459 O  OG1 . THR   B 1 46  ? 18.746 -32.183 26.105 1.00 20.36  ? 52  THR   C OG1 1 
ATOM   1460 C  CG2 . THR   B 1 46  ? 20.748 -31.233 27.242 1.00 19.32  ? 52  THR   C CG2 1 
ATOM   1461 N  N   . ILE   B 1 47  ? 20.972 -28.133 25.988 1.00 14.77  ? 53  ILE   C N   1 
ATOM   1462 C  CA  . ILE   B 1 47  ? 22.173 -27.311 25.953 1.00 13.86  ? 53  ILE   C CA  1 
ATOM   1463 C  C   . ILE   B 1 47  ? 23.271 -27.977 26.787 1.00 13.54  ? 53  ILE   C C   1 
ATOM   1464 O  O   . ILE   B 1 47  ? 23.012 -28.411 27.917 1.00 15.01  ? 53  ILE   C O   1 
ATOM   1465 C  CB  . ILE   B 1 47  ? 21.909 -25.904 26.514 1.00 14.58  ? 53  ILE   C CB  1 
ATOM   1466 C  CG1 . ILE   B 1 47  ? 20.713 -25.212 25.864 1.00 15.52  ? 53  ILE   C CG1 1 
ATOM   1467 C  CG2 . ILE   B 1 47  ? 23.163 -25.044 26.441 1.00 15.58  ? 53  ILE   C CG2 1 
ATOM   1468 C  CD1 . ILE   B 1 47  ? 20.883 -25.090 24.303 1.00 18.21  ? 53  ILE   C CD1 1 
ATOM   1469 N  N   . ALA   B 1 48  ? 24.480 -28.057 26.255 1.00 12.53  ? 54  ALA   C N   1 
ATOM   1470 C  CA  . ALA   B 1 48  ? 25.605 -28.622 27.003 1.00 12.38  ? 54  ALA   C CA  1 
ATOM   1471 C  C   . ALA   B 1 48  ? 25.968 -27.675 28.160 1.00 12.65  ? 54  ALA   C C   1 
ATOM   1472 O  O   . ALA   B 1 48  ? 25.938 -26.446 28.019 1.00 12.94  ? 54  ALA   C O   1 
ATOM   1473 C  CB  . ALA   B 1 48  ? 26.793 -28.712 26.080 1.00 12.23  ? 54  ALA   C CB  1 
ATOM   1474 N  N   . ARG   B 1 49  ? 26.303 -28.252 29.318 1.00 13.22  ? 55  ARG   C N   1 
ATOM   1475 C  CA  . ARG   B 1 49  ? 26.766 -27.508 30.505 1.00 12.94  ? 55  ARG   C CA  1 
ATOM   1476 C  C   . ARG   B 1 49  ? 28.100 -28.167 30.876 1.00 13.67  ? 55  ARG   C C   1 
ATOM   1477 O  O   . ARG   B 1 49  ? 28.131 -29.225 31.536 1.00 14.51  ? 55  ARG   C O   1 
ATOM   1478 C  CB  . ARG   B 1 49  ? 25.729 -27.544 31.632 1.00 13.89  ? 55  ARG   C CB  1 
ATOM   1479 C  CG  . ARG   B 1 49  ? 24.372 -26.989 31.188 1.00 12.75  ? 55  ARG   C CG  1 
ATOM   1480 C  CD  . ARG   B 1 49  ? 24.382 -25.516 30.821 1.00 14.32  ? 55  ARG   C CD  1 
ATOM   1481 N  NE  . ARG   B 1 49  ? 23.040 -25.086 30.430 1.00 14.32  ? 55  ARG   C NE  1 
ATOM   1482 C  CZ  . ARG   B 1 49  ? 22.797 -23.989 29.724 1.00 14.50  ? 55  ARG   C CZ  1 
ATOM   1483 N  NH1 . ARG   B 1 49  ? 23.785 -23.164 29.406 1.00 13.96  ? 55  ARG   C NH1 1 
ATOM   1484 N  NH2 . ARG   B 1 49  ? 21.547 -23.695 29.341 1.00 14.88  ? 55  ARG   C NH2 1 
ATOM   1485 N  N   . CYS   B 1 50  ? 29.194 -27.607 30.352 1.00 12.73  ? 56  CYS   C N   1 
ATOM   1486 C  CA  . CYS   B 1 50  ? 30.520 -28.258 30.383 1.00 13.20  ? 56  CYS   C CA  1 
ATOM   1487 C  C   . CYS   B 1 50  ? 31.582 -27.312 29.860 1.00 12.54  ? 56  CYS   C C   1 
ATOM   1488 O  O   . CYS   B 1 50  ? 31.277 -26.193 29.428 1.00 13.50  ? 56  CYS   C O   1 
ATOM   1489 C  CB  . CYS   B 1 50  ? 30.458 -29.488 29.455 1.00 12.73  ? 56  CYS   C CB  1 
ATOM   1490 S  SG  . CYS   B 1 50  ? 30.334 -29.055 27.660 1.00 12.69  ? 56  CYS   C SG  1 
ATOM   1491 N  N   . ASP   B 1 51  ? 32.863 -27.770 29.900 1.00 13.83  ? 57  ASP   C N   1 
ATOM   1492 C  CA  . ASP   B 1 51  ? 34.011 -27.052 29.317 1.00 15.02  ? 57  ASP   C CA  1 
ATOM   1493 C  C   . ASP   B 1 51  ? 34.675 -27.905 28.208 1.00 15.58  ? 57  ASP   C C   1 
ATOM   1494 O  O   . ASP   B 1 51  ? 35.881 -27.775 27.981 1.00 15.83  ? 57  ASP   C O   1 
ATOM   1495 C  CB  . ASP   B 1 51  ? 35.012 -26.622 30.400 1.00 18.27  ? 57  ASP   C CB  1 
ATOM   1496 C  CG  . ASP   B 1 51  ? 35.706 -27.746 31.096 1.00 21.65  ? 57  ASP   C CG  1 
ATOM   1497 O  OD1 . ASP   B 1 51  ? 35.365 -28.911 30.835 1.00 20.34  ? 57  ASP   C OD1 1 
ATOM   1498 O  OD2 . ASP   B 1 51  ? 36.655 -27.460 31.880 1.00 27.63  ? 57  ASP   C OD2 1 
ATOM   1499 N  N   . CYS   B 1 52  ? 33.891 -28.757 27.522 1.00 13.97  ? 58  CYS   C N   1 
ATOM   1500 C  CA  . CYS   B 1 52  ? 34.457 -29.535 26.370 1.00 13.83  ? 58  CYS   C CA  1 
ATOM   1501 C  C   . CYS   B 1 52  ? 35.134 -28.628 25.350 1.00 12.87  ? 58  CYS   C C   1 
ATOM   1502 O  O   . CYS   B 1 52  ? 34.694 -27.486 25.124 1.00 12.88  ? 58  CYS   C O   1 
ATOM   1503 C  CB  . CYS   B 1 52  ? 33.355 -30.339 25.665 1.00 14.18  ? 58  CYS   C CB  1 
ATOM   1504 S  SG  . CYS   B 1 52  ? 32.741 -31.774 26.594 1.00 13.88  ? 58  CYS   C SG  1 
ATOM   1505 N  N   . GLN   B 1 53  ? 36.184 -29.143 24.744 1.00 12.81  ? 59  GLN   C N   1 
ATOM   1506 C  CA  . GLN   B 1 53  ? 36.873 -28.547 23.596 1.00 13.83  ? 59  GLN   C CA  1 
ATOM   1507 C  C   . GLN   B 1 53  ? 36.941 -29.480 22.425 1.00 13.01  ? 59  GLN   C C   1 
ATOM   1508 O  O   . GLN   B 1 53  ? 37.700 -29.246 21.468 1.00 13.26  ? 59  GLN   C O   1 
ATOM   1509 C  CB  . GLN   B 1 53  ? 38.279 -28.075 23.979 1.00 14.05  ? 59  GLN   C CB  1 
ATOM   1510 C  CG  . GLN   B 1 53  ? 38.239 -26.848 24.863 1.00 17.82  ? 59  GLN   C CG  1 
ATOM   1511 C  CD  . GLN   B 1 53  ? 39.611 -26.286 25.116 1.00 19.03  ? 59  GLN   C CD  1 
ATOM   1512 O  OE1 . GLN   B 1 53  ? 40.105 -26.316 26.274 1.00 21.60  ? 59  GLN   C OE1 1 
ATOM   1513 N  NE2 . GLN   B 1 53  ? 40.268 -25.761 24.049 1.00 16.86  ? 59  GLN   C NE2 1 
ATOM   1514 N  N   . THR   B 1 54  ? 36.158 -30.572 22.446 1.00 12.44  ? 60  THR   C N   1 
ATOM   1515 C  CA  . THR   B 1 54  ? 36.036 -31.438 21.262 1.00 12.95  ? 60  THR   C CA  1 
ATOM   1516 C  C   . THR   B 1 54  ? 34.547 -31.708 21.016 1.00 12.96  ? 60  THR   C C   1 
ATOM   1517 O  O   . THR   B 1 54  ? 33.752 -31.812 21.965 1.00 13.40  ? 60  THR   C O   1 
ATOM   1518 C  CB  . THR   B 1 54  ? 36.773 -32.721 21.343 1.00 16.15  ? 60  THR   C CB  1 
ATOM   1519 O  OG1 . THR   B 1 54  ? 36.234 -33.509 22.331 1.00 19.88  ? 60  THR   C OG1 1 
ATOM   1520 C  CG2 . THR   B 1 54  ? 38.253 -32.511 21.611 1.00 16.60  ? 60  THR   C CG2 1 
ATOM   1521 N  N   . GLY   B 1 55  ? 34.168 -31.759 19.748 1.00 11.88  ? 61  GLY   C N   1 
ATOM   1522 C  CA  . GLY   B 1 55  ? 32.767 -31.972 19.407 1.00 12.46  ? 61  GLY   C CA  1 
ATOM   1523 C  C   . GLY   B 1 55  ? 32.618 -32.175 17.920 1.00 10.99  ? 61  GLY   C C   1 
ATOM   1524 O  O   . GLY   B 1 55  ? 33.600 -32.486 17.226 1.00 12.51  ? 61  GLY   C O   1 
ATOM   1525 N  N   . VAL   B 1 56  ? 31.381 -32.058 17.427 1.00 10.71  ? 62  VAL   C N   1 
ATOM   1526 C  CA  . VAL   B 1 56  ? 31.104 -32.264 15.988 1.00 11.02  ? 62  VAL   C CA  1 
ATOM   1527 C  C   . VAL   B 1 56  ? 30.195 -31.131 15.565 1.00 10.81  ? 62  VAL   C C   1 
ATOM   1528 O  O   . VAL   B 1 56  ? 29.249 -30.822 16.280 1.00 11.61  ? 62  VAL   C O   1 
ATOM   1529 C  CB  . VAL   B 1 56  ? 30.368 -33.620 15.834 1.00 11.44  ? 62  VAL   C CB  1 
ATOM   1530 C  CG1 . VAL   B 1 56  ? 29.871 -33.817 14.391 1.00 13.52  ? 62  VAL   C CG1 1 
ATOM   1531 C  CG2 . VAL   B 1 56  ? 31.279 -34.818 16.216 1.00 12.35  ? 62  VAL   C CG2 1 
ATOM   1532 N  N   . TYR   B 1 57  ? 30.455 -30.559 14.377 1.00 11.33  ? 63  TYR   C N   1 
ATOM   1533 C  CA  . TYR   B 1 57  ? 29.558 -29.490 13.896 1.00 9.97   ? 63  TYR   C CA  1 
ATOM   1534 C  C   . TYR   B 1 57  ? 28.991 -29.842 12.532 1.00 10.64  ? 63  TYR   C C   1 
ATOM   1535 O  O   . TYR   B 1 57  ? 29.661 -30.497 11.729 1.00 11.89  ? 63  TYR   C O   1 
ATOM   1536 C  CB  . TYR   B 1 57  ? 30.225 -28.067 13.860 1.00 11.06  ? 63  TYR   C CB  1 
ATOM   1537 C  CG  . TYR   B 1 57  ? 31.106 -27.741 12.654 1.00 11.45  ? 63  TYR   C CG  1 
ATOM   1538 C  CD1 . TYR   B 1 57  ? 32.391 -28.245 12.551 1.00 11.80  ? 63  TYR   C CD1 1 
ATOM   1539 C  CD2 . TYR   B 1 57  ? 30.647 -26.904 11.643 1.00 11.17  ? 63  TYR   C CD2 1 
ATOM   1540 C  CE1 . TYR   B 1 57  ? 33.211 -27.938 11.450 1.00 12.32  ? 63  TYR   C CE1 1 
ATOM   1541 C  CE2 . TYR   B 1 57  ? 31.458 -26.584 10.548 1.00 12.04  ? 63  TYR   C CE2 1 
ATOM   1542 C  CZ  . TYR   B 1 57  ? 32.736 -27.100 10.459 1.00 12.75  ? 63  TYR   C CZ  1 
ATOM   1543 O  OH  . TYR   B 1 57  ? 33.615 -26.803 9.401  1.00 14.74  ? 63  TYR   C OH  1 
ATOM   1544 N  N   . TYR   B 1 58  ? 27.853 -29.258 12.209 1.00 10.87  ? 64  TYR   C N   1 
ATOM   1545 C  CA  . TYR   B 1 58  ? 27.232 -29.417 10.883 1.00 11.40  ? 64  TYR   C CA  1 
ATOM   1546 C  C   . TYR   B 1 58  ? 27.606 -28.266 9.971  1.00 11.38  ? 64  TYR   C C   1 
ATOM   1547 O  O   . TYR   B 1 58  ? 27.368 -27.079 10.262 1.00 11.42  ? 64  TYR   C O   1 
ATOM   1548 C  CB  . TYR   B 1 58  ? 25.707 -29.545 10.973 1.00 12.77  ? 64  TYR   C CB  1 
ATOM   1549 C  CG  . TYR   B 1 58  ? 25.107 -29.809 9.604  1.00 13.78  ? 64  TYR   C CG  1 
ATOM   1550 C  CD1 . TYR   B 1 58  ? 25.411 -30.970 8.908  1.00 13.80  ? 64  TYR   C CD1 1 
ATOM   1551 C  CD2 . TYR   B 1 58  ? 24.243 -28.909 9.023  1.00 14.24  ? 64  TYR   C CD2 1 
ATOM   1552 C  CE1 . TYR   B 1 58  ? 24.929 -31.189 7.610  1.00 15.29  ? 64  TYR   C CE1 1 
ATOM   1553 C  CE2 . TYR   B 1 58  ? 23.725 -29.141 7.735  1.00 14.68  ? 64  TYR   C CE2 1 
ATOM   1554 C  CZ  . TYR   B 1 58  ? 24.049 -30.301 7.072  1.00 15.24  ? 64  TYR   C CZ  1 
ATOM   1555 O  OH  . TYR   B 1 58  ? 23.594 -30.514 5.765  1.00 17.91  ? 64  TYR   C OH  1 
ATOM   1556 N  N   . CYS   B 1 59  ? 28.156 -28.632 8.841  1.00 10.82  ? 65  CYS   C N   1 
ATOM   1557 C  CA  . CYS   B 1 59  ? 28.555 -27.699 7.757  1.00 12.46  ? 65  CYS   C CA  1 
ATOM   1558 C  C   . CYS   B 1 59  ? 27.609 -27.899 6.535  1.00 12.97  ? 65  CYS   C C   1 
ATOM   1559 O  O   . CYS   B 1 59  ? 27.784 -28.841 5.744  1.00 13.35  ? 65  CYS   C O   1 
ATOM   1560 C  CB  . CYS   B 1 59  ? 29.998 -27.969 7.383  1.00 12.07  ? 65  CYS   C CB  1 
ATOM   1561 S  SG  . CYS   B 1 59  ? 30.579 -26.919 6.001  1.00 14.15  ? 65  CYS   C SG  1 
ATOM   1562 N  N   . SER   B 1 60  ? 26.626 -27.020 6.380  1.00 14.15  ? 66  SER   C N   1 
ATOM   1563 C  CA  A SER   B 1 60  ? 25.640 -27.194 5.315  0.50 15.41  ? 66  SER   C CA  1 
ATOM   1564 C  CA  B SER   B 1 60  ? 25.639 -27.160 5.314  0.50 14.91  ? 66  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 60  ? 26.242 -27.075 3.914  1.00 15.28  ? 66  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 60  ? 25.814 -27.828 3.041  1.00 16.48  ? 66  SER   C O   1 
ATOM   1567 C  CB  A SER   B 1 60  ? 24.457 -26.259 5.499  0.50 17.54  ? 66  SER   C CB  1 
ATOM   1568 C  CB  B SER   B 1 60  ? 24.534 -26.126 5.456  0.50 15.32  ? 66  SER   C CB  1 
ATOM   1569 O  OG  A SER   B 1 60  ? 24.877 -24.911 5.452  0.50 20.08  ? 66  SER   C OG  1 
ATOM   1570 O  OG  B SER   B 1 60  ? 23.595 -26.367 4.422  0.50 15.27  ? 66  SER   C OG  1 
ATOM   1571 N  N   . SER   B 1 61  ? 27.274 -26.224 3.734  1.00 13.60  ? 67  SER   C N   1 
ATOM   1572 C  CA  . SER   B 1 61  ? 27.912 -26.075 2.410  1.00 14.30  ? 67  SER   C CA  1 
ATOM   1573 C  C   . SER   B 1 61  ? 28.751 -27.288 2.012  1.00 16.33  ? 67  SER   C C   1 
ATOM   1574 O  O   . SER   B 1 61  ? 29.207 -27.348 0.870  1.00 17.61  ? 67  SER   C O   1 
ATOM   1575 C  CB  . SER   B 1 61  ? 28.751 -24.813 2.393  1.00 14.79  ? 67  SER   C CB  1 
ATOM   1576 O  OG  . SER   B 1 61  ? 29.869 -24.935 3.255  1.00 15.55  ? 67  SER   C OG  1 
ATOM   1577 N  N   . ARG   B 1 62  ? 28.906 -28.307 2.883  1.00 14.91  ? 68  ARG   C N   1 
ATOM   1578 C  CA  . ARG   B 1 62  ? 29.540 -29.568 2.519  1.00 15.10  ? 68  ARG   C CA  1 
ATOM   1579 C  C   . ARG   B 1 62  ? 28.606 -30.774 2.729  1.00 15.50  ? 68  ARG   C C   1 
ATOM   1580 O  O   . ARG   B 1 62  ? 29.015 -31.922 2.545  1.00 16.56  ? 68  ARG   C O   1 
ATOM   1581 C  CB  . ARG   B 1 62  ? 30.815 -29.774 3.338  1.00 14.96  ? 68  ARG   C CB  1 
ATOM   1582 C  CG  . ARG   B 1 62  ? 31.857 -28.680 3.129  1.00 18.93  ? 68  ARG   C CG  1 
ATOM   1583 C  CD  . ARG   B 1 62  ? 32.529 -28.916 1.808  1.00 18.23  ? 68  ARG   C CD  1 
ATOM   1584 N  NE  . ARG   B 1 62  ? 33.561 -27.885 1.501  1.00 21.91  ? 68  ARG   C NE  1 
ATOM   1585 C  CZ  . ARG   B 1 62  ? 33.339 -26.736 0.873  1.00 25.53  ? 68  ARG   C CZ  1 
ATOM   1586 N  NH1 . ARG   B 1 62  ? 32.134 -26.460 0.383  1.00 26.47  ? 68  ARG   C NH1 1 
ATOM   1587 N  NH2 . ARG   B 1 62  ? 34.349 -25.903 0.616  1.00 27.36  ? 68  ARG   C NH2 1 
ATOM   1588 N  N   . ARG   B 1 63  ? 27.397 -30.532 3.274  1.00 15.58  ? 69  ARG   C N   1 
ATOM   1589 C  CA  . ARG   B 1 63  ? 26.435 -31.601 3.699  1.00 16.44  ? 69  ARG   C CA  1 
ATOM   1590 C  C   . ARG   B 1 63  ? 27.140 -32.612 4.575  1.00 17.51  ? 69  ARG   C C   1 
ATOM   1591 O  O   . ARG   B 1 63  ? 27.001 -33.828 4.395  1.00 19.31  ? 69  ARG   C O   1 
ATOM   1592 C  CB  . ARG   B 1 63  ? 25.775 -32.298 2.489  1.00 17.39  ? 69  ARG   C CB  1 
ATOM   1593 C  CG  . ARG   B 1 63  ? 24.928 -31.415 1.618  1.00 20.99  ? 69  ARG   C CG  1 
ATOM   1594 C  CD  . ARG   B 1 63  ? 23.694 -30.975 2.304  1.00 25.36  ? 69  ARG   C CD  1 
ATOM   1595 N  NE  . ARG   B 1 63  ? 22.709 -30.521 1.331  1.00 27.74  ? 69  ARG   C NE  1 
ATOM   1596 C  CZ  . ARG   B 1 63  ? 22.488 -29.248 1.028  1.00 30.06  ? 69  ARG   C CZ  1 
ATOM   1597 N  NH1 . ARG   B 1 63  ? 23.245 -28.287 1.555  1.00 28.65  ? 69  ARG   C NH1 1 
ATOM   1598 N  NH2 . ARG   B 1 63  ? 21.526 -28.924 0.175  1.00 29.64  ? 69  ARG   C NH2 1 
ATOM   1599 N  N   . LYS   B 1 64  ? 27.948 -32.103 5.538  1.00 15.14  ? 70  LYS   C N   1 
ATOM   1600 C  CA  . LYS   B 1 64  ? 28.751 -32.999 6.343  1.00 16.19  ? 70  LYS   C CA  1 
ATOM   1601 C  C   . LYS   B 1 64  ? 28.839 -32.524 7.766  1.00 15.08  ? 70  LYS   C C   1 
ATOM   1602 O  O   . LYS   B 1 64  ? 28.867 -31.320 8.034  1.00 14.91  ? 70  LYS   C O   1 
ATOM   1603 C  CB  . LYS   B 1 64  ? 30.182 -32.992 5.779  1.00 20.36  ? 70  LYS   C CB  1 
ATOM   1604 C  CG  . LYS   B 1 64  ? 30.547 -34.093 4.792  1.00 31.52  ? 70  LYS   C CG  1 
ATOM   1605 C  CD  . LYS   B 1 64  ? 32.006 -34.560 5.038  1.00 37.71  ? 70  LYS   C CD  1 
ATOM   1606 C  CE  . LYS   B 1 64  ? 32.550 -35.325 3.860  1.00 44.87  ? 70  LYS   C CE  1 
ATOM   1607 N  NZ  . LYS   B 1 64  ? 32.132 -34.731 2.558  1.00 49.61  ? 70  LYS   C NZ  1 
ATOM   1608 N  N   . HIS   B 1 65  ? 28.945 -33.492 8.670  1.00 14.09  ? 71  HIS   C N   1 
ATOM   1609 C  CA  . HIS   B 1 65  ? 29.266 -33.235 10.085 1.00 13.94  ? 71  HIS   C CA  1 
ATOM   1610 C  C   . HIS   B 1 65  ? 30.726 -33.509 10.289 1.00 15.57  ? 71  HIS   C C   1 
ATOM   1611 O  O   . HIS   B 1 65  ? 31.210 -34.611 9.992  1.00 18.05  ? 71  HIS   C O   1 
ATOM   1612 C  CB  . HIS   B 1 65  ? 28.431 -34.120 11.026 1.00 14.52  ? 71  HIS   C CB  1 
ATOM   1613 C  CG  . HIS   B 1 65  ? 26.959 -33.844 10.974 1.00 13.22  ? 71  HIS   C CG  1 
ATOM   1614 N  ND1 . HIS   B 1 65  ? 26.292 -33.059 11.919 1.00 16.35  ? 71  HIS   C ND1 1 
ATOM   1615 C  CD2 . HIS   B 1 65  ? 26.056 -34.283 10.070 1.00 13.37  ? 71  HIS   C CD2 1 
ATOM   1616 C  CE1 . HIS   B 1 65  ? 24.999 -33.090 11.569 1.00 14.04  ? 71  HIS   C CE1 1 
ATOM   1617 N  NE2 . HIS   B 1 65  ? 24.810 -33.805 10.471 1.00 16.21  ? 71  HIS   C NE2 1 
ATOM   1618 N  N   . TYR   B 1 66  ? 31.473 -32.541 10.843 1.00 12.84  ? 72  TYR   C N   1 
ATOM   1619 C  CA  . TYR   B 1 66  ? 32.912 -32.715 11.020 1.00 12.49  ? 72  TYR   C CA  1 
ATOM   1620 C  C   . TYR   B 1 66  ? 33.279 -32.766 12.492 1.00 12.31  ? 72  TYR   C C   1 
ATOM   1621 O  O   . TYR   B 1 66  ? 32.870 -31.892 13.250 1.00 12.34  ? 72  TYR   C O   1 
ATOM   1622 C  CB  . TYR   B 1 66  ? 33.659 -31.480 10.436 1.00 13.61  ? 72  TYR   C CB  1 
ATOM   1623 C  CG  . TYR   B 1 66  ? 33.613 -31.390 8.909  1.00 13.93  ? 72  TYR   C CG  1 
ATOM   1624 C  CD1 . TYR   B 1 66  ? 34.475 -32.141 8.128  1.00 16.17  ? 72  TYR   C CD1 1 
ATOM   1625 C  CD2 . TYR   B 1 66  ? 32.809 -30.459 8.264  1.00 14.91  ? 72  TYR   C CD2 1 
ATOM   1626 C  CE1 . TYR   B 1 66  ? 34.498 -32.013 6.739  1.00 17.58  ? 72  TYR   C CE1 1 
ATOM   1627 C  CE2 . TYR   B 1 66  ? 32.823 -30.326 6.877  1.00 15.82  ? 72  TYR   C CE2 1 
ATOM   1628 C  CZ  . TYR   B 1 66  ? 33.678 -31.101 6.130  1.00 17.38  ? 72  TYR   C CZ  1 
ATOM   1629 O  OH  . TYR   B 1 66  ? 33.653 -30.948 4.767  1.00 18.28  ? 72  TYR   C OH  1 
ATOM   1630 N  N   . PRO   B 1 67  ? 34.092 -33.740 12.901 1.00 12.76  ? 73  PRO   C N   1 
ATOM   1631 C  CA  . PRO   B 1 67  ? 34.625 -33.728 14.285 1.00 12.11  ? 73  PRO   C CA  1 
ATOM   1632 C  C   . PRO   B 1 67  ? 35.742 -32.667 14.395 1.00 13.35  ? 73  PRO   C C   1 
ATOM   1633 O  O   . PRO   B 1 67  ? 36.600 -32.578 13.484 1.00 15.59  ? 73  PRO   C O   1 
ATOM   1634 C  CB  . PRO   B 1 67  ? 35.216 -35.139 14.465 1.00 14.85  ? 73  PRO   C CB  1 
ATOM   1635 C  CG  . PRO   B 1 67  ? 35.458 -35.644 13.083 1.00 17.56  ? 73  PRO   C CG  1 
ATOM   1636 C  CD  . PRO   B 1 67  ? 34.569 -34.916 12.113 1.00 14.00  ? 73  PRO   C CD  1 
ATOM   1637 N  N   . VAL   B 1 68  ? 35.698 -31.850 15.429 1.00 11.65  ? 74  VAL   C N   1 
ATOM   1638 C  CA  . VAL   B 1 68  ? 36.683 -30.762 15.568 1.00 12.53  ? 74  VAL   C CA  1 
ATOM   1639 C  C   . VAL   B 1 68  ? 37.079 -30.577 17.011 1.00 12.31  ? 74  VAL   C C   1 
ATOM   1640 O  O   . VAL   B 1 68  ? 36.331 -30.856 17.944 1.00 12.47  ? 74  VAL   C O   1 
ATOM   1641 C  CB  . VAL   B 1 68  ? 36.100 -29.397 15.075 1.00 13.76  ? 74  VAL   C CB  1 
ATOM   1642 C  CG1 . VAL   B 1 68  ? 36.022 -29.323 13.536 1.00 16.10  ? 74  VAL   C CG1 1 
ATOM   1643 C  CG2 . VAL   B 1 68  ? 34.734 -29.089 15.731 1.00 14.36  ? 74  VAL   C CG2 1 
ATOM   1644 N  N   . SER   B 1 69  ? 38.297 -30.039 17.177 1.00 12.79  ? 75  SER   C N   1 
ATOM   1645 C  CA  . SER   B 1 69  ? 38.733 -29.400 18.413 1.00 12.67  ? 75  SER   C CA  1 
ATOM   1646 C  C   . SER   B 1 69  ? 38.451 -27.911 18.320 1.00 12.57  ? 75  SER   C C   1 
ATOM   1647 O  O   . SER   B 1 69  ? 38.587 -27.323 17.237 1.00 12.83  ? 75  SER   C O   1 
ATOM   1648 C  CB  . SER   B 1 69  ? 40.240 -29.592 18.624 1.00 14.59  ? 75  SER   C CB  1 
ATOM   1649 O  OG  . SER   B 1 69  ? 40.521 -30.970 18.719 1.00 19.77  ? 75  SER   C OG  1 
ATOM   1650 N  N   . PHE   B 1 70  ? 38.004 -27.293 19.395 1.00 12.22  ? 76  PHE   C N   1 
ATOM   1651 C  CA  . PHE   B 1 70  ? 37.643 -25.875 19.363 1.00 12.23  ? 76  PHE   C CA  1 
ATOM   1652 C  C   . PHE   B 1 70  ? 38.132 -25.148 20.612 1.00 12.29  ? 76  PHE   C C   1 
ATOM   1653 O  O   . PHE   B 1 70  ? 38.300 -25.763 21.666 1.00 12.47  ? 76  PHE   C O   1 
ATOM   1654 C  CB  . PHE   B 1 70  ? 36.104 -25.662 19.089 1.00 12.68  ? 76  PHE   C CB  1 
ATOM   1655 C  CG  . PHE   B 1 70  ? 35.205 -26.368 20.100 1.00 11.24  ? 76  PHE   C CG  1 
ATOM   1656 C  CD1 . PHE   B 1 70  ? 34.789 -27.680 19.895 1.00 12.25  ? 76  PHE   C CD1 1 
ATOM   1657 C  CD2 . PHE   B 1 70  ? 34.774 -25.710 21.236 1.00 12.24  ? 76  PHE   C CD2 1 
ATOM   1658 C  CE1 . PHE   B 1 70  ? 33.949 -28.305 20.818 1.00 12.27  ? 76  PHE   C CE1 1 
ATOM   1659 C  CE2 . PHE   B 1 70  ? 33.918 -26.342 22.136 1.00 11.60  ? 76  PHE   C CE2 1 
ATOM   1660 C  CZ  . PHE   B 1 70  ? 33.565 -27.648 21.965 1.00 12.22  ? 76  PHE   C CZ  1 
ATOM   1661 N  N   . SER   B 1 71  ? 38.383 -23.868 20.477 1.00 11.65  ? 77  SER   C N   1 
ATOM   1662 C  CA  . SER   B 1 71  ? 38.989 -23.075 21.544 1.00 12.40  ? 77  SER   C CA  1 
ATOM   1663 C  C   . SER   B 1 71  ? 37.994 -22.665 22.624 1.00 13.69  ? 77  SER   C C   1 
ATOM   1664 O  O   . SER   B 1 71  ? 36.807 -22.955 22.544 1.00 14.76  ? 77  SER   C O   1 
ATOM   1665 C  CB  . SER   B 1 71  ? 39.685 -21.868 20.924 1.00 13.45  ? 77  SER   C CB  1 
ATOM   1666 O  OG  . SER   B 1 71  ? 38.789 -20.941 20.312 1.00 15.83  ? 77  SER   C OG  1 
ATOM   1667 N  N   . LYS   B 1 72  ? 38.471 -22.030 23.682 1.00 15.05  ? 78  LYS   C N   1 
ATOM   1668 C  CA  . LYS   B 1 72  ? 37.615 -21.618 24.805 1.00 14.75  ? 78  LYS   C CA  1 
ATOM   1669 C  C   . LYS   B 1 72  ? 36.895 -20.334 24.399 1.00 14.82  ? 78  LYS   C C   1 
ATOM   1670 O  O   . LYS   B 1 72  ? 37.480 -19.517 23.657 1.00 16.68  ? 78  LYS   C O   1 
ATOM   1671 C  CB  . LYS   B 1 72  ? 38.538 -21.280 26.003 1.00 19.20  ? 78  LYS   C CB  1 
ATOM   1672 C  CG  . LYS   B 1 72  ? 39.301 -22.492 26.486 1.00 21.96  ? 78  LYS   C CG  1 
ATOM   1673 C  CD  . LYS   B 1 72  ? 40.371 -22.082 27.535 1.00 31.72  ? 78  LYS   C CD  1 
ATOM   1674 C  CE  . LYS   B 1 72  ? 41.000 -23.319 28.134 1.00 41.13  ? 78  LYS   C CE  1 
ATOM   1675 N  NZ  . LYS   B 1 72  ? 39.936 -24.258 28.597 1.00 46.56  ? 78  LYS   C NZ  1 
ATOM   1676 N  N   . PRO   B 1 73  ? 35.652 -20.096 24.854 1.00 14.32  ? 79  PRO   C N   1 
ATOM   1677 C  CA  . PRO   B 1 73  ? 34.935 -18.850 24.459 1.00 15.07  ? 79  PRO   C CA  1 
ATOM   1678 C  C   . PRO   B 1 73  ? 35.687 -17.593 24.827 1.00 15.46  ? 79  PRO   C C   1 
ATOM   1679 O  O   . PRO   B 1 73  ? 36.116 -17.450 25.986 1.00 17.56  ? 79  PRO   C O   1 
ATOM   1680 C  CB  . PRO   B 1 73  ? 33.634 -18.892 25.263 1.00 17.31  ? 79  PRO   C CB  1 
ATOM   1681 C  CG  . PRO   B 1 73  ? 33.459 -20.316 25.655 1.00 18.91  ? 79  PRO   C CG  1 
ATOM   1682 C  CD  . PRO   B 1 73  ? 34.847 -20.951 25.759 1.00 15.58  ? 79  PRO   C CD  1 
ATOM   1683 N  N   . SER   B 1 74  ? 35.928 -16.708 23.838 1.00 14.40  ? 80  SER   C N   1 
ATOM   1684 C  CA  . SER   B 1 74  ? 36.807 -15.551 24.073 1.00 15.53  ? 80  SER   C CA  1 
ATOM   1685 C  C   . SER   B 1 74  ? 36.394 -14.400 23.168 1.00 15.72  ? 80  SER   C C   1 
ATOM   1686 O  O   . SER   B 1 74  ? 35.530 -14.541 22.312 1.00 14.54  ? 80  SER   C O   1 
ATOM   1687 C  CB  . SER   B 1 74  ? 38.256 -15.919 23.723 1.00 18.73  ? 80  SER   C CB  1 
ATOM   1688 O  OG  . SER   B 1 74  ? 38.678 -17.103 24.394 1.00 24.07  ? 80  SER   C OG  1 
ATOM   1689 N  N   . LEU   B 1 75  ? 37.075 -13.253 23.362 1.00 16.46  ? 81  LEU   C N   1 
ATOM   1690 C  CA  . LEU   B 1 75  ? 36.892 -12.040 22.584 1.00 17.55  ? 81  LEU   C CA  1 
ATOM   1691 C  C   . LEU   B 1 75  ? 37.913 -12.105 21.433 1.00 18.77  ? 81  LEU   C C   1 
ATOM   1692 O  O   . LEU   B 1 75  ? 39.138 -12.031 21.672 1.00 21.05  ? 81  LEU   C O   1 
ATOM   1693 C  CB  . LEU   B 1 75  ? 37.125 -10.806 23.496 1.00 19.59  ? 81  LEU   C CB  1 
ATOM   1694 C  CG  . LEU   B 1 75  ? 36.855 -9.453  22.887 1.00 22.51  ? 81  LEU   C CG  1 
ATOM   1695 C  CD1 . LEU   B 1 75  ? 35.365 -9.256  22.662 1.00 21.61  ? 81  LEU   C CD1 1 
ATOM   1696 C  CD2 . LEU   B 1 75  ? 37.373 -8.314  23.827 1.00 24.88  ? 81  LEU   C CD2 1 
ATOM   1697 N  N   . ILE   B 1 76  ? 37.436 -12.350 20.206 1.00 18.78  ? 82  ILE   C N   1 
ATOM   1698 C  CA  . ILE   B 1 76  ? 38.244 -12.614 19.014 1.00 20.10  ? 82  ILE   C CA  1 
ATOM   1699 C  C   . ILE   B 1 76  ? 38.006 -11.512 17.974 1.00 20.27  ? 82  ILE   C C   1 
ATOM   1700 O  O   . ILE   B 1 76  ? 36.828 -11.188 17.722 1.00 18.64  ? 82  ILE   C O   1 
ATOM   1701 C  CB  . ILE   B 1 76  ? 37.836 -13.999 18.418 1.00 22.54  ? 82  ILE   C CB  1 
ATOM   1702 C  CG1 . ILE   B 1 76  ? 38.094 -15.178 19.401 1.00 24.67  ? 82  ILE   C CG1 1 
ATOM   1703 C  CG2 . ILE   B 1 76  ? 38.472 -14.273 17.022 1.00 24.37  ? 82  ILE   C CG2 1 
ATOM   1704 C  CD1 . ILE   B 1 76  ? 39.580 -15.529 19.568 1.00 26.34  ? 82  ILE   C CD1 1 
ATOM   1705 N  N   . PHE   B 1 77  ? 39.066 -11.004 17.300 1.00 20.73  ? 83  PHE   C N   1 
ATOM   1706 C  CA  . PHE   B 1 77  ? 38.865 -10.042 16.206 1.00 20.76  ? 83  PHE   C CA  1 
ATOM   1707 C  C   . PHE   B 1 77  ? 38.491 -10.892 14.972 1.00 20.91  ? 83  PHE   C C   1 
ATOM   1708 O  O   . PHE   B 1 77  ? 39.192 -11.844 14.597 1.00 23.52  ? 83  PHE   C O   1 
ATOM   1709 C  CB  . PHE   B 1 77  ? 40.158 -9.233  15.907 1.00 21.64  ? 83  PHE   C CB  1 
ATOM   1710 C  CG  . PHE   B 1 77  ? 39.878 -8.038  15.002 1.00 22.46  ? 83  PHE   C CG  1 
ATOM   1711 C  CD1 . PHE   B 1 77  ? 39.141 -6.961  15.456 1.00 23.15  ? 83  PHE   C CD1 1 
ATOM   1712 C  CD2 . PHE   B 1 77  ? 40.228 -8.069  13.652 1.00 23.77  ? 83  PHE   C CD2 1 
ATOM   1713 C  CE1 . PHE   B 1 77  ? 38.837 -5.883  14.605 1.00 24.82  ? 83  PHE   C CE1 1 
ATOM   1714 C  CE2 . PHE   B 1 77  ? 39.929 -6.995  12.808 1.00 24.33  ? 83  PHE   C CE2 1 
ATOM   1715 C  CZ  . PHE   B 1 77  ? 39.255 -5.902  13.295 1.00 24.78  ? 83  PHE   C CZ  1 
ATOM   1716 N  N   . VAL   B 1 78  ? 37.379 -10.525 14.323 1.00 17.35  ? 84  VAL   C N   1 
ATOM   1717 C  CA  . VAL   B 1 78  ? 36.851 -11.257 13.173 1.00 17.53  ? 84  VAL   C CA  1 
ATOM   1718 C  C   . VAL   B 1 78  ? 36.945 -10.333 11.947 1.00 17.59  ? 84  VAL   C C   1 
ATOM   1719 O  O   . VAL   B 1 78  ? 36.462 -9.201  12.021 1.00 17.76  ? 84  VAL   C O   1 
ATOM   1720 C  CB  . VAL   B 1 78  ? 35.367 -11.658 13.465 1.00 17.90  ? 84  VAL   C CB  1 
ATOM   1721 C  CG1 . VAL   B 1 78  ? 34.791 -12.428 12.300 1.00 18.59  ? 84  VAL   C CG1 1 
ATOM   1722 C  CG2 . VAL   B 1 78  ? 35.250 -12.462 14.771 1.00 19.14  ? 84  VAL   C CG2 1 
ATOM   1723 N  N   . GLU   B 1 79  ? 37.474 -10.794 10.800 1.00 16.59  ? 85  GLU   C N   1 
ATOM   1724 C  CA  . GLU   B 1 79  ? 37.499 -9.986  9.580  1.00 17.64  ? 85  GLU   C CA  1 
ATOM   1725 C  C   . GLU   B 1 79  ? 36.091 -9.756  9.039  1.00 16.88  ? 85  GLU   C C   1 
ATOM   1726 O  O   . GLU   B 1 79  ? 35.125 -10.424 9.442  1.00 16.29  ? 85  GLU   C O   1 
ATOM   1727 C  CB  . GLU   B 1 79  ? 38.364 -10.667 8.493  1.00 21.11  ? 85  GLU   C CB  1 
ATOM   1728 C  CG  . GLU   B 1 79  ? 39.848 -10.697 8.845  1.00 27.49  ? 85  GLU   C CG  1 
ATOM   1729 C  CD  . GLU   B 1 79  ? 40.453 -9.320  9.086  1.00 36.23  ? 85  GLU   C CD  1 
ATOM   1730 O  OE1 . GLU   B 1 79  ? 40.124 -8.371  8.333  1.00 40.08  ? 85  GLU   C OE1 1 
ATOM   1731 O  OE2 . GLU   B 1 79  ? 41.225 -9.172  10.062 1.00 38.58  ? 85  GLU   C OE2 1 
ATOM   1732 N  N   . ALA   B 1 80  ? 35.945 -8.739  8.191  1.00 17.13  ? 86  ALA   C N   1 
ATOM   1733 C  CA  . ALA   B 1 80  ? 34.666 -8.396  7.624  1.00 17.99  ? 86  ALA   C CA  1 
ATOM   1734 C  C   . ALA   B 1 80  ? 34.049 -9.581  6.895  1.00 19.19  ? 86  ALA   C C   1 
ATOM   1735 O  O   . ALA   B 1 80  ? 34.773 -10.389 6.314  1.00 21.55  ? 86  ALA   C O   1 
ATOM   1736 C  CB  . ALA   B 1 80  ? 34.845 -7.235  6.641  1.00 19.43  ? 86  ALA   C CB  1 
ATOM   1737 N  N   . SER   B 1 81  ? 32.745 -9.727  7.045  1.00 17.68  ? 87  SER   C N   1 
ATOM   1738 C  CA  . SER   B 1 81  ? 32.038 -10.773 6.344  1.00 18.98  ? 87  SER   C CA  1 
ATOM   1739 C  C   . SER   B 1 81  ? 30.915 -10.107 5.543  1.00 20.12  ? 87  SER   C C   1 
ATOM   1740 O  O   . SER   B 1 81  ? 30.749 -8.848  5.563  1.00 20.06  ? 87  SER   C O   1 
ATOM   1741 C  CB  . SER   B 1 81  ? 31.464 -11.766 7.355  1.00 18.33  ? 87  SER   C CB  1 
ATOM   1742 O  OG  . SER   B 1 81  ? 30.416 -11.102 8.065  1.00 18.27  ? 87  SER   C OG  1 
ATOM   1743 N  N   . GLU   B 1 82  ? 30.104 -10.918 4.870  1.00 21.54  ? 88  GLU   C N   1 
ATOM   1744 C  CA  . GLU   B 1 82  ? 28.988 -10.308 4.139  1.00 22.51  ? 88  GLU   C CA  1 
ATOM   1745 C  C   . GLU   B 1 82  ? 27.932 -9.682  5.077  1.00 22.18  ? 88  GLU   C C   1 
ATOM   1746 O  O   . GLU   B 1 82  ? 27.200 -8.795  4.642  1.00 23.89  ? 88  GLU   C O   1 
ATOM   1747 C  CB  . GLU   B 1 82  ? 28.386 -11.298 3.135  1.00 27.59  ? 88  GLU   C CB  1 
ATOM   1748 C  CG  . GLU   B 1 82  ? 27.583 -12.431 3.718  1.00 36.10  ? 88  GLU   C CG  1 
ATOM   1749 C  CD  . GLU   B 1 82  ? 26.875 -13.209 2.623  1.00 42.44  ? 88  GLU   C CD  1 
ATOM   1750 O  OE1 . GLU   B 1 82  ? 27.494 -13.412 1.551  1.00 43.36  ? 88  GLU   C OE1 1 
ATOM   1751 O  OE2 . GLU   B 1 82  ? 25.704 -13.606 2.834  1.00 43.50  ? 88  GLU   C OE2 1 
ATOM   1752 N  N   . TYR   B 1 83  ? 27.968 -10.001 6.378  1.00 19.50  ? 89  TYR   C N   1 
ATOM   1753 C  CA  . TYR   B 1 83  ? 26.944 -9.508  7.287  1.00 19.10  ? 89  TYR   C CA  1 
ATOM   1754 C  C   . TYR   B 1 83  ? 27.437 -8.667  8.483  1.00 19.93  ? 89  TYR   C C   1 
ATOM   1755 O  O   . TYR   B 1 83  ? 26.591 -8.068  9.147  1.00 21.05  ? 89  TYR   C O   1 
ATOM   1756 C  CB  . TYR   B 1 83  ? 26.080 -10.709 7.781  1.00 18.08  ? 89  TYR   C CB  1 
ATOM   1757 C  CG  . TYR   B 1 83  ? 26.908 -11.912 8.249  1.00 17.60  ? 89  TYR   C CG  1 
ATOM   1758 C  CD1 . TYR   B 1 83  ? 27.309 -12.916 7.351  1.00 17.37  ? 89  TYR   C CD1 1 
ATOM   1759 C  CD2 . TYR   B 1 83  ? 27.305 -12.038 9.576  1.00 16.69  ? 89  TYR   C CD2 1 
ATOM   1760 C  CE1 . TYR   B 1 83  ? 28.077 -14.007 7.770  1.00 16.30  ? 89  TYR   C CE1 1 
ATOM   1761 C  CE2 . TYR   B 1 83  ? 28.058 -13.125 10.009 1.00 16.74  ? 89  TYR   C CE2 1 
ATOM   1762 C  CZ  . TYR   B 1 83  ? 28.454 -14.106 9.103  1.00 15.56  ? 89  TYR   C CZ  1 
ATOM   1763 O  OH  . TYR   B 1 83  ? 29.255 -15.149 9.500  1.00 16.63  ? 89  TYR   C OH  1 
ATOM   1764 N  N   . TYR   B 1 84  ? 28.757 -8.540  8.748  1.00 17.46  ? 90  TYR   C N   1 
ATOM   1765 C  CA  . TYR   B 1 84  ? 29.284 -7.606  9.772  1.00 16.87  ? 90  TYR   C CA  1 
ATOM   1766 C  C   . TYR   B 1 84  ? 30.614 -7.000  9.256  1.00 16.78  ? 90  TYR   C C   1 
ATOM   1767 O  O   . TYR   B 1 84  ? 31.327 -7.642  8.500  1.00 16.68  ? 90  TYR   C O   1 
ATOM   1768 C  CB  . TYR   B 1 84  ? 29.637 -8.343  11.106 1.00 16.19  ? 90  TYR   C CB  1 
ATOM   1769 C  CG  . TYR   B 1 84  ? 28.451 -8.786  11.936 1.00 15.18  ? 90  TYR   C CG  1 
ATOM   1770 C  CD1 . TYR   B 1 84  ? 27.531 -7.863  12.449 1.00 15.23  ? 90  TYR   C CD1 1 
ATOM   1771 C  CD2 . TYR   B 1 84  ? 28.273 -10.104 12.244 1.00 14.57  ? 90  TYR   C CD2 1 
ATOM   1772 C  CE1 . TYR   B 1 84  ? 26.457 -8.270  13.255 1.00 15.21  ? 90  TYR   C CE1 1 
ATOM   1773 C  CE2 . TYR   B 1 84  ? 27.196 -10.526 13.034 1.00 14.23  ? 90  TYR   C CE2 1 
ATOM   1774 C  CZ  . TYR   B 1 84  ? 26.301 -9.606  13.565 1.00 14.76  ? 90  TYR   C CZ  1 
ATOM   1775 O  OH  . TYR   B 1 84  ? 25.229 -10.022 14.360 1.00 14.60  ? 90  TYR   C OH  1 
ATOM   1776 N  N   . PRO   B 1 85  ? 30.992 -5.797  9.720  1.00 17.41  ? 91  PRO   C N   1 
ATOM   1777 C  CA  . PRO   B 1 85  ? 32.339 -5.295  9.425  1.00 17.08  ? 91  PRO   C CA  1 
ATOM   1778 C  C   . PRO   B 1 85  ? 33.365 -6.084  10.242 1.00 17.54  ? 91  PRO   C C   1 
ATOM   1779 O  O   . PRO   B 1 85  ? 33.015 -6.863  11.164 1.00 17.07  ? 91  PRO   C O   1 
ATOM   1780 C  CB  . PRO   B 1 85  ? 32.237 -3.825  9.890  1.00 17.86  ? 91  PRO   C CB  1 
ATOM   1781 C  CG  . PRO   B 1 85  ? 31.333 -3.907  11.071 1.00 18.46  ? 91  PRO   C CG  1 
ATOM   1782 C  CD  . PRO   B 1 85  ? 30.261 -4.928  10.685 1.00 17.67  ? 91  PRO   C CD  1 
ATOM   1783 N  N   . ALA   B 1 86  ? 34.657 -5.791  10.023 1.00 16.61  ? 92  ALA   C N   1 
ATOM   1784 C  CA  . ALA   B 1 86  ? 35.718 -6.367  10.857 1.00 18.24  ? 92  ALA   C CA  1 
ATOM   1785 C  C   . ALA   B 1 86  ? 35.513 -5.782  12.278 1.00 19.05  ? 92  ALA   C C   1 
ATOM   1786 O  O   . ALA   B 1 86  ? 35.211 -4.570  12.417 1.00 20.65  ? 92  ALA   C O   1 
ATOM   1787 C  CB  . ALA   B 1 86  ? 37.089 -5.948  10.309 1.00 18.49  ? 92  ALA   C CB  1 
ATOM   1788 N  N   . ARG   B 1 87  ? 35.533 -6.655  13.292 1.00 18.63  ? 93  ARG   C N   1 
ATOM   1789 C  CA  . ARG   B 1 87  ? 35.222 -6.234  14.647 1.00 18.92  ? 93  ARG   C CA  1 
ATOM   1790 C  C   . ARG   B 1 87  ? 35.596 -7.324  15.632 1.00 18.08  ? 93  ARG   C C   1 
ATOM   1791 O  O   . ARG   B 1 87  ? 35.803 -8.468  15.270 1.00 17.51  ? 93  ARG   C O   1 
ATOM   1792 C  CB  . ARG   B 1 87  ? 33.700 -5.939  14.802 1.00 18.93  ? 93  ARG   C CB  1 
ATOM   1793 C  CG  . ARG   B 1 87  ? 32.852 -7.226  14.656 1.00 17.40  ? 93  ARG   C CG  1 
ATOM   1794 C  CD  . ARG   B 1 87  ? 31.374 -6.943  14.815 1.00 18.02  ? 93  ARG   C CD  1 
ATOM   1795 N  NE  . ARG   B 1 87  ? 30.670 -8.219  15.030 1.00 17.37  ? 93  ARG   C NE  1 
ATOM   1796 C  CZ  . ARG   B 1 87  ? 29.595 -8.392  15.778 1.00 18.08  ? 93  ARG   C CZ  1 
ATOM   1797 N  NH1 . ARG   B 1 87  ? 28.986 -7.344  16.341 1.00 17.91  ? 93  ARG   C NH1 1 
ATOM   1798 N  NH2 . ARG   B 1 87  ? 29.095 -9.607  15.947 1.00 18.56  ? 93  ARG   C NH2 1 
ATOM   1799 N  N   . TYR   B 1 88  ? 35.558 -6.970  16.921 1.00 19.52  ? 94  TYR   C N   1 
ATOM   1800 C  CA  . TYR   B 1 88  ? 35.694 -7.952  17.982 1.00 20.84  ? 94  TYR   C CA  1 
ATOM   1801 C  C   . TYR   B 1 88  ? 34.319 -8.625  18.215 1.00 19.08  ? 94  TYR   C C   1 
ATOM   1802 O  O   . TYR   B 1 88  ? 33.313 -7.932  18.300 1.00 19.78  ? 94  TYR   C O   1 
ATOM   1803 C  CB  . TYR   B 1 88  ? 36.070 -7.202  19.281 1.00 23.24  ? 94  TYR   C CB  1 
ATOM   1804 C  CG  . TYR   B 1 88  ? 37.542 -6.864  19.301 1.00 25.60  ? 94  TYR   C CG  1 
ATOM   1805 C  CD1 . TYR   B 1 88  ? 38.491 -7.838  19.556 1.00 26.31  ? 94  TYR   C CD1 1 
ATOM   1806 C  CD2 . TYR   B 1 88  ? 37.988 -5.586  18.967 1.00 26.94  ? 94  TYR   C CD2 1 
ATOM   1807 C  CE1 . TYR   B 1 88  ? 39.856 -7.542  19.528 1.00 27.80  ? 94  TYR   C CE1 1 
ATOM   1808 C  CE2 . TYR   B 1 88  ? 39.335 -5.275  18.954 1.00 28.25  ? 94  TYR   C CE2 1 
ATOM   1809 C  CZ  . TYR   B 1 88  ? 40.268 -6.258  19.223 1.00 29.34  ? 94  TYR   C CZ  1 
ATOM   1810 O  OH  . TYR   B 1 88  ? 41.604 -5.916  19.211 1.00 32.33  ? 94  TYR   C OH  1 
ATOM   1811 N  N   . GLN   B 1 89  ? 34.287 -9.946  18.329 1.00 17.08  ? 95  GLN   C N   1 
ATOM   1812 C  CA  . GLN   B 1 89  ? 33.073 -10.690 18.688 1.00 15.78  ? 95  GLN   C CA  1 
ATOM   1813 C  C   . GLN   B 1 89  ? 33.390 -11.407 20.003 1.00 14.24  ? 95  GLN   C C   1 
ATOM   1814 O  O   . GLN   B 1 89  ? 34.488 -11.992 20.155 1.00 15.23  ? 95  GLN   C O   1 
ATOM   1815 C  CB  . GLN   B 1 89  ? 32.700 -11.646 17.552 1.00 16.16  ? 95  GLN   C CB  1 
ATOM   1816 C  CG  . GLN   B 1 89  ? 31.442 -12.438 17.854 1.00 17.06  ? 95  GLN   C CG  1 
ATOM   1817 C  CD  . GLN   B 1 89  ? 30.726 -12.987 16.632 1.00 16.04  ? 95  GLN   C CD  1 
ATOM   1818 O  OE1 . GLN   B 1 89  ? 30.701 -12.383 15.540 1.00 16.57  ? 95  GLN   C OE1 1 
ATOM   1819 N  NE2 . GLN   B 1 89  ? 30.161 -14.150 16.796 1.00 14.85  ? 95  GLN   C NE2 1 
ATOM   1820 N  N   . SER   B 1 90  ? 32.463 -11.396 20.944 1.00 13.57  ? 96  SER   C N   1 
ATOM   1821 C  CA  . SER   B 1 90  ? 32.637 -12.016 22.238 1.00 14.15  ? 96  SER   C CA  1 
ATOM   1822 C  C   . SER   B 1 90  ? 32.041 -13.422 22.272 1.00 13.07  ? 96  SER   C C   1 
ATOM   1823 O  O   . SER   B 1 90  ? 31.196 -13.789 21.444 1.00 13.53  ? 96  SER   C O   1 
ATOM   1824 C  CB  . SER   B 1 90  ? 32.087 -11.131 23.374 1.00 16.05  ? 96  SER   C CB  1 
ATOM   1825 O  OG  . SER   B 1 90  ? 30.689 -11.086 23.208 1.00 16.31  ? 96  SER   C OG  1 
ATOM   1826 N  N   . HIS   B 1 91  ? 32.484 -14.202 23.277 1.00 13.54  ? 97  HIS   C N   1 
ATOM   1827 C  CA  . HIS   B 1 91  ? 32.013 -15.562 23.538 1.00 13.45  ? 97  HIS   C CA  1 
ATOM   1828 C  C   . HIS   B 1 91  ? 32.133 -16.430 22.273 1.00 12.96  ? 97  HIS   C C   1 
ATOM   1829 O  O   . HIS   B 1 91  ? 31.238 -17.254 22.014 1.00 13.81  ? 97  HIS   C O   1 
ATOM   1830 C  CB  . HIS   B 1 91  ? 30.553 -15.551 24.105 1.00 14.56  ? 97  HIS   C CB  1 
ATOM   1831 C  CG  . HIS   B 1 91  ? 30.404 -14.788 25.396 1.00 15.54  ? 97  HIS   C CG  1 
ATOM   1832 N  ND1 . HIS   B 1 91  ? 30.416 -15.428 26.606 1.00 17.42  ? 97  HIS   C ND1 1 
ATOM   1833 C  CD2 . HIS   B 1 91  ? 30.313 -13.441 25.615 1.00 16.03  ? 97  HIS   C CD2 1 
ATOM   1834 C  CE1 . HIS   B 1 91  ? 30.296 -14.480 27.538 1.00 18.03  ? 97  HIS   C CE1 1 
ATOM   1835 N  NE2 . HIS   B 1 91  ? 30.219 -13.266 26.993 1.00 18.24  ? 97  HIS   C NE2 1 
ATOM   1836 N  N   . LEU   B 1 92  ? 33.198 -16.279 21.527 1.00 12.63  ? 98  LEU   C N   1 
ATOM   1837 C  CA  . LEU   B 1 92  ? 33.399 -16.984 20.275 1.00 12.72  ? 98  LEU   C CA  1 
ATOM   1838 C  C   . LEU   B 1 92  ? 34.497 -18.051 20.448 1.00 12.45  ? 98  LEU   C C   1 
ATOM   1839 O  O   . LEU   B 1 92  ? 35.475 -17.838 21.168 1.00 13.00  ? 98  LEU   C O   1 
ATOM   1840 C  CB  . LEU   B 1 92  ? 33.874 -15.970 19.180 1.00 14.17  ? 98  LEU   C CB  1 
ATOM   1841 C  CG  . LEU   B 1 92  ? 33.972 -16.548 17.761 1.00 14.95  ? 98  LEU   C CG  1 
ATOM   1842 C  CD1 . LEU   B 1 92  ? 32.596 -16.865 17.181 1.00 15.39  ? 98  LEU   C CD1 1 
ATOM   1843 C  CD2 . LEU   B 1 92  ? 34.657 -15.532 16.812 1.00 16.21  ? 98  LEU   C CD2 1 
ATOM   1844 N  N   . MET   B 1 93  ? 34.291 -19.218 19.802 1.00 12.29  ? 99  MET   C N   1 
ATOM   1845 C  CA  . MET   B 1 93  ? 35.225 -20.348 19.862 1.00 11.68  ? 99  MET   C CA  1 
ATOM   1846 C  C   . MET   B 1 93  ? 35.644 -20.641 18.426 1.00 12.55  ? 99  MET   C C   1 
ATOM   1847 O  O   . MET   B 1 93  ? 34.763 -20.679 17.560 1.00 13.13  ? 99  MET   C O   1 
ATOM   1848 C  CB  . MET   B 1 93  ? 34.500 -21.559 20.436 1.00 13.34  ? 99  MET   C CB  1 
ATOM   1849 C  CG  . MET   B 1 93  ? 34.044 -21.294 21.857 1.00 14.86  ? 99  MET   C CG  1 
ATOM   1850 S  SD  . MET   B 1 93  ? 33.017 -22.620 22.485 1.00 14.87  ? 99  MET   C SD  1 
ATOM   1851 C  CE  . MET   B 1 93  ? 31.525 -22.456 21.436 1.00 15.15  ? 99  MET   C CE  1 
ATOM   1852 N  N   . LEU   B 1 94  ? 36.931 -20.917 18.144 1.00 11.81  ? 100 LEU   C N   1 
ATOM   1853 C  CA  . LEU   B 1 94  ? 37.345 -21.205 16.775 1.00 12.64  ? 100 LEU   C CA  1 
ATOM   1854 C  C   . LEU   B 1 94  ? 37.791 -22.657 16.650 1.00 12.56  ? 100 LEU   C C   1 
ATOM   1855 O  O   . LEU   B 1 94  ? 38.312 -23.249 17.601 1.00 13.70  ? 100 LEU   C O   1 
ATOM   1856 C  CB  . LEU   B 1 94  ? 38.602 -20.351 16.376 1.00 13.53  ? 100 LEU   C CB  1 
ATOM   1857 C  CG  . LEU   B 1 94  ? 38.423 -18.848 16.347 1.00 14.37  ? 100 LEU   C CG  1 
ATOM   1858 C  CD1 . LEU   B 1 94  ? 39.706 -18.197 15.845 1.00 18.51  ? 100 LEU   C CD1 1 
ATOM   1859 C  CD2 . LEU   B 1 94  ? 37.247 -18.412 15.457 1.00 16.91  ? 100 LEU   C CD2 1 
ATOM   1860 N  N   . ALA   B 1 95  ? 37.637 -23.179 15.440 1.00 12.49  ? 101 ALA   C N   1 
ATOM   1861 C  CA  . ALA   B 1 95  ? 38.190 -24.475 15.038 1.00 12.23  ? 101 ALA   C CA  1 
ATOM   1862 C  C   . ALA   B 1 95  ? 38.752 -24.347 13.604 1.00 12.28  ? 101 ALA   C C   1 
ATOM   1863 O  O   . ALA   B 1 95  ? 38.381 -23.413 12.880 1.00 12.05  ? 101 ALA   C O   1 
ATOM   1864 C  CB  . ALA   B 1 95  ? 37.100 -25.589 15.057 1.00 13.55  ? 101 ALA   C CB  1 
ATOM   1865 N  N   . VAL   B 1 96  ? 39.593 -25.290 13.196 1.00 12.90  ? 102 VAL   C N   1 
ATOM   1866 C  CA  . VAL   B 1 96  ? 40.043 -25.356 11.821 1.00 13.58  ? 102 VAL   C CA  1 
ATOM   1867 C  C   . VAL   B 1 96  ? 38.989 -26.108 11.012 1.00 13.64  ? 102 VAL   C C   1 
ATOM   1868 O  O   . VAL   B 1 96  ? 38.683 -27.288 11.298 1.00 15.21  ? 102 VAL   C O   1 
ATOM   1869 C  CB  . VAL   B 1 96  ? 41.409 -26.088 11.799 1.00 14.77  ? 102 VAL   C CB  1 
ATOM   1870 C  CG1 . VAL   B 1 96  ? 41.865 -26.233 10.341 1.00 16.68  ? 102 VAL   C CG1 1 
ATOM   1871 C  CG2 . VAL   B 1 96  ? 42.430 -25.302 12.620 1.00 16.31  ? 102 VAL   C CG2 1 
ATOM   1872 N  N   . GLY   B 1 97  ? 38.383 -25.412 10.071 1.00 14.22  ? 103 GLY   C N   1 
ATOM   1873 C  CA  . GLY   B 1 97  ? 37.313 -26.023 9.299  1.00 14.76  ? 103 GLY   C CA  1 
ATOM   1874 C  C   . GLY   B 1 97  ? 36.658 -25.062 8.364  1.00 14.87  ? 103 GLY   C C   1 
ATOM   1875 O  O   . GLY   B 1 97  ? 36.948 -23.844 8.368  1.00 17.18  ? 103 GLY   C O   1 
ATOM   1876 N  N   . HIS   B 1 98  ? 35.782 -25.610 7.524  1.00 15.48  ? 104 HIS   C N   1 
ATOM   1877 C  CA  . HIS   B 1 98  ? 35.111 -24.808 6.545  1.00 15.25  ? 104 HIS   C CA  1 
ATOM   1878 C  C   . HIS   B 1 98  ? 33.834 -24.109 7.060  1.00 14.65  ? 104 HIS   C C   1 
ATOM   1879 O  O   . HIS   B 1 98  ? 33.012 -24.749 7.747  1.00 14.51  ? 104 HIS   C O   1 
ATOM   1880 C  CB  . HIS   B 1 98  ? 34.786 -25.671 5.335  1.00 17.71  ? 104 HIS   C CB  1 
ATOM   1881 C  CG  . HIS   B 1 98  ? 34.235 -24.862 4.219  1.00 20.26  ? 104 HIS   C CG  1 
ATOM   1882 N  ND1 . HIS   B 1 98  ? 35.028 -23.929 3.530  1.00 23.23  ? 104 HIS   C ND1 1 
ATOM   1883 C  CD2 . HIS   B 1 98  ? 32.970 -24.820 3.739  1.00 22.99  ? 104 HIS   C CD2 1 
ATOM   1884 C  CE1 . HIS   B 1 98  ? 34.203 -23.349 2.661  1.00 25.38  ? 104 HIS   C CE1 1 
ATOM   1885 N  NE2 . HIS   B 1 98  ? 32.961 -23.867 2.740  1.00 25.24  ? 104 HIS   C NE2 1 
ATOM   1886 N  N   . SER   B 1 99  ? 33.633 -22.834 6.696  1.00 14.76  ? 105 SER   C N   1 
ATOM   1887 C  CA  . SER   B 1 99  ? 32.406 -22.093 7.063  1.00 14.82  ? 105 SER   C CA  1 
ATOM   1888 C  C   . SER   B 1 99  ? 32.152 -20.941 6.053  1.00 16.23  ? 105 SER   C C   1 
ATOM   1889 O  O   . SER   B 1 99  ? 33.011 -20.042 5.935  1.00 19.09  ? 105 SER   C O   1 
ATOM   1890 C  CB  . SER   B 1 99  ? 32.611 -21.526 8.464  1.00 16.08  ? 105 SER   C CB  1 
ATOM   1891 O  OG  . SER   B 1 99  ? 31.517 -20.680 8.807  1.00 16.38  ? 105 SER   C OG  1 
ATOM   1892 N  N   . GLU   B 1 100 ? 31.046 -21.064 5.304  1.00 17.06  ? 106 GLU   C N   1 
ATOM   1893 C  CA  . GLU   B 1 100 ? 30.558 -20.066 4.320  1.00 17.31  ? 106 GLU   C CA  1 
ATOM   1894 C  C   . GLU   B 1 100 ? 29.482 -19.269 5.105  1.00 15.16  ? 106 GLU   C C   1 
ATOM   1895 O  O   . GLU   B 1 100 ? 28.905 -19.746 6.107  1.00 14.32  ? 106 GLU   C O   1 
ATOM   1896 C  CB  . GLU   B 1 100 ? 29.790 -20.775 3.130  1.00 19.75  ? 106 GLU   C CB  1 
ATOM   1897 C  CG  . GLU   B 1 100 ? 30.474 -21.809 2.257  1.00 25.46  ? 106 GLU   C CG  1 
ATOM   1898 C  CD  . GLU   B 1 100 ? 31.426 -21.251 1.240  1.00 28.93  ? 106 GLU   C CD  1 
ATOM   1899 O  OE1 . GLU   B 1 100 ? 31.506 -20.006 1.117  1.00 28.40  ? 106 GLU   C OE1 1 
ATOM   1900 O  OE2 . GLU   B 1 100 ? 32.105 -22.055 0.571  1.00 30.29  ? 106 GLU   C OE2 1 
ATOM   1901 N  N   . PRO   B 1 101 ? 29.073 -18.077 4.611  1.00 15.91  ? 107 PRO   C N   1 
ATOM   1902 C  CA  . PRO   B 1 101 ? 27.974 -17.358 5.308  1.00 14.77  ? 107 PRO   C CA  1 
ATOM   1903 C  C   . PRO   B 1 101 ? 26.699 -18.193 5.484  1.00 15.38  ? 107 PRO   C C   1 
ATOM   1904 O  O   . PRO   B 1 101 ? 26.077 -18.124 6.560  1.00 14.82  ? 107 PRO   C O   1 
ATOM   1905 C  CB  . PRO   B 1 101 ? 27.686 -16.143 4.370  1.00 17.29  ? 107 PRO   C CB  1 
ATOM   1906 C  CG  . PRO   B 1 101 ? 28.867 -16.066 3.461  1.00 21.13  ? 107 PRO   C CG  1 
ATOM   1907 C  CD  . PRO   B 1 101 ? 29.671 -17.291 3.498  1.00 18.90  ? 107 PRO   C CD  1 
ATOM   1908 N  N   . GLY   B 1 102 ? 26.332 -19.019 4.497  1.00 14.90  ? 108 GLY   C N   1 
ATOM   1909 C  CA  . GLY   B 1 102 ? 25.112 -19.835 4.582  1.00 15.31  ? 108 GLY   C CA  1 
ATOM   1910 C  C   . GLY   B 1 102 ? 25.223 -20.940 5.642  1.00 14.89  ? 108 GLY   C C   1 
ATOM   1911 O  O   . GLY   B 1 102 ? 24.230 -21.592 5.988  1.00 16.01  ? 108 GLY   C O   1 
ATOM   1912 N  N   . ASP   B 1 103 ? 26.463 -21.220 6.174  1.00 14.08  ? 109 ASP   C N   1 
ATOM   1913 C  CA  . ASP   B 1 103 ? 26.615 -22.233 7.214  1.00 12.78  ? 109 ASP   C CA  1 
ATOM   1914 C  C   . ASP   B 1 103 ? 26.249 -21.726 8.591  1.00 12.91  ? 109 ASP   C C   1 
ATOM   1915 O  O   . ASP   B 1 103 ? 26.138 -22.540 9.523  1.00 12.91  ? 109 ASP   C O   1 
ATOM   1916 C  CB  . ASP   B 1 103 ? 28.091 -22.716 7.246  1.00 13.90  ? 109 ASP   C CB  1 
ATOM   1917 C  CG  . ASP   B 1 103 ? 28.409 -23.526 6.023  1.00 16.04  ? 109 ASP   C CG  1 
ATOM   1918 O  OD1 . ASP   B 1 103 ? 27.546 -24.268 5.576  1.00 15.64  ? 109 ASP   C OD1 1 
ATOM   1919 O  OD2 . ASP   B 1 103 ? 29.528 -23.387 5.482  1.00 16.14  ? 109 ASP   C OD2 1 
ATOM   1920 N  N   . CYS   B 1 104 ? 26.043 -20.413 8.791  1.00 11.86  ? 110 CYS   C N   1 
ATOM   1921 C  CA  . CYS   B 1 104 ? 25.622 -19.872 10.091 1.00 11.56  ? 110 CYS   C CA  1 
ATOM   1922 C  C   . CYS   B 1 104 ? 24.385 -20.576 10.583 1.00 11.92  ? 110 CYS   C C   1 
ATOM   1923 O  O   . CYS   B 1 104 ? 23.450 -20.799 9.803  1.00 13.38  ? 110 CYS   C O   1 
ATOM   1924 C  CB  . CYS   B 1 104 ? 25.405 -18.364 10.018 1.00 11.69  ? 110 CYS   C CB  1 
ATOM   1925 S  SG  . CYS   B 1 104 ? 26.936 -17.388 9.921  1.00 14.04  ? 110 CYS   C SG  1 
ATOM   1926 N  N   . GLY   B 1 105 ? 24.384 -20.906 11.866 1.00 10.53  ? 111 GLY   C N   1 
ATOM   1927 C  CA  . GLY   B 1 105 ? 23.240 -21.597 12.475 1.00 11.51  ? 111 GLY   C CA  1 
ATOM   1928 C  C   . GLY   B 1 105 ? 23.443 -23.097 12.631 1.00 11.62  ? 111 GLY   C C   1 
ATOM   1929 O  O   . GLY   B 1 105 ? 22.664 -23.755 13.347 1.00 12.53  ? 111 GLY   C O   1 
ATOM   1930 N  N   . GLY   B 1 106 ? 24.477 -23.665 11.973 1.00 12.04  ? 112 GLY   C N   1 
ATOM   1931 C  CA  . GLY   B 1 106 ? 24.787 -25.093 12.132 1.00 12.00  ? 112 GLY   C CA  1 
ATOM   1932 C  C   . GLY   B 1 106 ? 25.193 -25.375 13.580 1.00 11.35  ? 112 GLY   C C   1 
ATOM   1933 O  O   . GLY   B 1 106 ? 25.941 -24.601 14.193 1.00 11.40  ? 112 GLY   C O   1 
ATOM   1934 N  N   . ILE   B 1 107 ? 24.726 -26.502 14.090 1.00 11.11  ? 113 ILE   C N   1 
ATOM   1935 C  CA  . ILE   B 1 107 ? 25.014 -26.817 15.502 1.00 11.41  ? 113 ILE   C CA  1 
ATOM   1936 C  C   . ILE   B 1 107 ? 26.371 -27.493 15.719 1.00 11.73  ? 113 ILE   C C   1 
ATOM   1937 O  O   . ILE   B 1 107 ? 26.797 -28.347 14.939 1.00 11.43  ? 113 ILE   C O   1 
ATOM   1938 C  CB  . ILE   B 1 107 ? 23.847 -27.759 16.023 1.00 13.79  ? 113 ILE   C CB  1 
ATOM   1939 C  CG1 . ILE   B 1 107 ? 22.635 -26.792 16.466 1.00 16.72  ? 113 ILE   C CG1 1 
ATOM   1940 C  CG2 . ILE   B 1 107 ? 24.304 -28.644 17.234 1.00 13.94  ? 113 ILE   C CG2 1 
ATOM   1941 C  CD1 . ILE   B 1 107 ? 21.338 -27.530 16.836 1.00 20.45  ? 113 ILE   C CD1 1 
ATOM   1942 N  N   . LEU   B 1 108 ? 27.061 -27.040 16.778 1.00 10.83  ? 114 LEU   C N   1 
ATOM   1943 C  CA  . LEU   B 1 108 ? 28.233 -27.729 17.334 1.00 10.15  ? 114 LEU   C CA  1 
ATOM   1944 C  C   . LEU   B 1 108 ? 27.703 -28.470 18.589 1.00 9.99   ? 114 LEU   C C   1 
ATOM   1945 O  O   . LEU   B 1 108 ? 27.064 -27.866 19.461 1.00 10.76  ? 114 LEU   C O   1 
ATOM   1946 C  CB  . LEU   B 1 108 ? 29.264 -26.675 17.740 1.00 10.22  ? 114 LEU   C CB  1 
ATOM   1947 C  CG  . LEU   B 1 108 ? 30.479 -27.172 18.553 1.00 10.41  ? 114 LEU   C CG  1 
ATOM   1948 C  CD1 . LEU   B 1 108 ? 31.368 -28.125 17.706 1.00 12.64  ? 114 LEU   C CD1 1 
ATOM   1949 C  CD2 . LEU   B 1 108 ? 31.326 -25.986 19.054 1.00 11.25  ? 114 LEU   C CD2 1 
ATOM   1950 N  N   . ARG   B 1 109 ? 27.993 -29.762 18.673 1.00 10.21  ? 115 ARG   C N   1 
ATOM   1951 C  CA  . ARG   B 1 109 ? 27.534 -30.576 19.821 1.00 11.43  ? 115 ARG   C CA  1 
ATOM   1952 C  C   . ARG   B 1 109 ? 28.667 -31.414 20.373 1.00 11.53  ? 115 ARG   C C   1 
ATOM   1953 O  O   . ARG   B 1 109 ? 29.572 -31.835 19.661 1.00 11.95  ? 115 ARG   C O   1 
ATOM   1954 C  CB  . ARG   B 1 109 ? 26.378 -31.498 19.368 1.00 14.87  ? 115 ARG   C CB  1 
ATOM   1955 C  CG  . ARG   B 1 109 ? 26.799 -32.522 18.331 1.00 18.14  ? 115 ARG   C CG  1 
ATOM   1956 C  CD  . ARG   B 1 109 ? 25.643 -33.420 17.884 1.00 23.52  ? 115 ARG   C CD  1 
ATOM   1957 N  NE  . ARG   B 1 109 ? 24.775 -32.723 16.937 1.00 28.61  ? 115 ARG   C NE  1 
ATOM   1958 C  CZ  . ARG   B 1 109 ? 23.483 -32.481 17.133 1.00 38.01  ? 115 ARG   C CZ  1 
ATOM   1959 N  NH1 . ARG   B 1 109 ? 22.908 -32.797 18.290 1.00 40.76  ? 115 ARG   C NH1 1 
ATOM   1960 N  NH2 . ARG   B 1 109 ? 22.772 -31.848 16.206 1.00 39.80  ? 115 ARG   C NH2 1 
ATOM   1961 N  N   . CYS   B 1 110 ? 28.589 -31.667 21.680 1.00 11.93  ? 116 CYS   C N   1 
ATOM   1962 C  CA  . CYS   B 1 110 ? 29.542 -32.560 22.384 1.00 12.69  ? 116 CYS   C CA  1 
ATOM   1963 C  C   . CYS   B 1 110 ? 28.678 -33.655 23.050 1.00 13.92  ? 116 CYS   C C   1 
ATOM   1964 O  O   . CYS   B 1 110 ? 27.460 -33.742 22.860 1.00 13.40  ? 116 CYS   C O   1 
ATOM   1965 C  CB  . CYS   B 1 110 ? 30.345 -31.777 23.425 1.00 11.07  ? 116 CYS   C CB  1 
ATOM   1966 S  SG  . CYS   B 1 110 ? 29.311 -31.093 24.782 1.00 11.89  ? 116 CYS   C SG  1 
ATOM   1967 N  N   . GLN   B 1 111 ? 29.317 -34.503 23.890 1.00 14.76  ? 117 GLN   C N   1 
ATOM   1968 C  CA  . GLN   B 1 111 ? 28.548 -35.526 24.606 1.00 16.38  ? 117 GLN   C CA  1 
ATOM   1969 C  C   . GLN   B 1 111 ? 27.474 -34.959 25.547 1.00 16.35  ? 117 GLN   C C   1 
ATOM   1970 O  O   . GLN   B 1 111 ? 26.509 -35.676 25.881 1.00 17.90  ? 117 GLN   C O   1 
ATOM   1971 C  CB  . GLN   B 1 111 ? 29.493 -36.453 25.418 1.00 17.11  ? 117 GLN   C CB  1 
ATOM   1972 C  CG  . GLN   B 1 111 ? 30.156 -35.755 26.615 1.00 19.80  ? 117 GLN   C CG  1 
ATOM   1973 C  CD  . GLN   B 1 111 ? 31.135 -36.611 27.383 1.00 32.18  ? 117 GLN   C CD  1 
ATOM   1974 O  OE1 . GLN   B 1 111 ? 32.353 -36.543 27.156 1.00 36.34  ? 117 GLN   C OE1 1 
ATOM   1975 N  NE2 . GLN   B 1 111 ? 30.619 -37.377 28.328 1.00 32.36  ? 117 GLN   C NE2 1 
ATOM   1976 N  N   . HIS   B 1 112 ? 27.580 -33.675 25.947 1.00 14.32  ? 118 HIS   C N   1 
ATOM   1977 C  CA  . HIS   B 1 112 ? 26.591 -33.120 26.876 1.00 14.44  ? 118 HIS   C CA  1 
ATOM   1978 C  C   . HIS   B 1 112 ? 25.423 -32.413 26.214 1.00 15.36  ? 118 HIS   C C   1 
ATOM   1979 O  O   . HIS   B 1 112 ? 24.472 -32.016 26.904 1.00 16.13  ? 118 HIS   C O   1 
ATOM   1980 C  CB  . HIS   B 1 112 ? 27.298 -32.152 27.815 1.00 14.99  ? 118 HIS   C CB  1 
ATOM   1981 C  CG  . HIS   B 1 112 ? 28.479 -32.784 28.502 1.00 14.26  ? 118 HIS   C CG  1 
ATOM   1982 N  ND1 . HIS   B 1 112 ? 29.802 -32.489 28.156 1.00 12.22  ? 118 HIS   C ND1 1 
ATOM   1983 C  CD2 . HIS   B 1 112 ? 28.500 -33.603 29.583 1.00 17.01  ? 118 HIS   C CD2 1 
ATOM   1984 C  CE1 . HIS   B 1 112 ? 30.562 -33.245 28.944 1.00 13.79  ? 118 HIS   C CE1 1 
ATOM   1985 N  NE2 . HIS   B 1 112 ? 29.819 -33.877 29.853 1.00 17.06  ? 118 HIS   C NE2 1 
ATOM   1986 N  N   . GLY   B 1 113 ? 25.513 -32.181 24.892 1.00 14.27  ? 119 GLY   C N   1 
ATOM   1987 C  CA  . GLY   B 1 113 ? 24.447 -31.473 24.193 1.00 14.14  ? 119 GLY   C CA  1 
ATOM   1988 C  C   . GLY   B 1 113 ? 24.962 -30.411 23.241 1.00 12.18  ? 119 GLY   C C   1 
ATOM   1989 O  O   . GLY   B 1 113 ? 26.081 -30.503 22.742 1.00 12.68  ? 119 GLY   C O   1 
ATOM   1990 N  N   . VAL   B 1 114 ? 24.113 -29.387 22.975 1.00 12.57  ? 120 VAL   C N   1 
ATOM   1991 C  CA  . VAL   B 1 114 ? 24.467 -28.318 22.029 1.00 12.59  ? 120 VAL   C CA  1 
ATOM   1992 C  C   . VAL   B 1 114 ? 25.403 -27.320 22.700 1.00 11.91  ? 120 VAL   C C   1 
ATOM   1993 O  O   . VAL   B 1 114 ? 25.077 -26.744 23.762 1.00 12.54  ? 120 VAL   C O   1 
ATOM   1994 C  CB  . VAL   B 1 114 ? 23.175 -27.631 21.552 1.00 13.20  ? 120 VAL   C CB  1 
ATOM   1995 C  CG1 . VAL   B 1 114 ? 23.535 -26.426 20.661 1.00 14.67  ? 120 VAL   C CG1 1 
ATOM   1996 C  CG2 . VAL   B 1 114 ? 22.251 -28.613 20.809 1.00 14.82  ? 120 VAL   C CG2 1 
ATOM   1997 N  N   . VAL   B 1 115 ? 26.570 -27.110 22.098 1.00 10.78  ? 121 VAL   C N   1 
ATOM   1998 C  CA  . VAL   B 1 115 ? 27.587 -26.172 22.605 1.00 11.33  ? 121 VAL   C CA  1 
ATOM   1999 C  C   . VAL   B 1 115 ? 27.356 -24.755 22.082 1.00 12.21  ? 121 VAL   C C   1 
ATOM   2000 O  O   . VAL   B 1 115 ? 27.589 -23.756 22.786 1.00 12.26  ? 121 VAL   C O   1 
ATOM   2001 C  CB  . VAL   B 1 115 ? 28.986 -26.715 22.208 1.00 10.86  ? 121 VAL   C CB  1 
ATOM   2002 C  CG1 . VAL   B 1 115 ? 30.074 -25.700 22.551 1.00 12.49  ? 121 VAL   C CG1 1 
ATOM   2003 C  CG2 . VAL   B 1 115 ? 29.237 -28.102 22.831 1.00 12.36  ? 121 VAL   C CG2 1 
ATOM   2004 N  N   . GLY   B 1 116 ? 27.000 -24.675 20.807 1.00 10.83  ? 122 GLY   C N   1 
ATOM   2005 C  CA  . GLY   B 1 116 ? 26.786 -23.373 20.186 1.00 12.16  ? 122 GLY   C CA  1 
ATOM   2006 C  C   . GLY   B 1 116 ? 26.438 -23.521 18.721 1.00 10.80  ? 122 GLY   C C   1 
ATOM   2007 O  O   . GLY   B 1 116 ? 26.128 -24.642 18.279 1.00 11.61  ? 122 GLY   C O   1 
ATOM   2008 N  N   . ILE   B 1 117 ? 26.419 -22.373 17.989 1.00 10.39  ? 123 ILE   C N   1 
ATOM   2009 C  CA  . ILE   B 1 117 ? 26.077 -22.419 16.574 1.00 10.59  ? 123 ILE   C CA  1 
ATOM   2010 C  C   . ILE   B 1 117 ? 27.127 -21.689 15.767 1.00 10.48  ? 123 ILE   C C   1 
ATOM   2011 O  O   . ILE   B 1 117 ? 27.740 -20.702 16.227 1.00 11.30  ? 123 ILE   C O   1 
ATOM   2012 C  CB  . ILE   B 1 117 ? 24.672 -21.773 16.290 1.00 11.31  ? 123 ILE   C CB  1 
ATOM   2013 C  CG1 . ILE   B 1 117 ? 24.554 -20.366 16.916 1.00 12.00  ? 123 ILE   C CG1 1 
ATOM   2014 C  CG2 . ILE   B 1 117 ? 23.564 -22.724 16.724 1.00 12.72  ? 123 ILE   C CG2 1 
ATOM   2015 C  CD1 . ILE   B 1 117 ? 23.191 -19.582 16.498 1.00 13.62  ? 123 ILE   C CD1 1 
ATOM   2016 N  N   . VAL   B 1 118 ? 27.282 -22.087 14.489 1.00 10.75  ? 124 VAL   C N   1 
ATOM   2017 C  CA  . VAL   B 1 118 ? 28.219 -21.407 13.586 1.00 10.97  ? 124 VAL   C CA  1 
ATOM   2018 C  C   . VAL   B 1 118 ? 27.851 -19.929 13.479 1.00 11.53  ? 124 VAL   C C   1 
ATOM   2019 O  O   . VAL   B 1 118 ? 26.669 -19.584 13.249 1.00 10.89  ? 124 VAL   C O   1 
ATOM   2020 C  CB  . VAL   B 1 118 ? 28.218 -22.055 12.181 1.00 10.63  ? 124 VAL   C CB  1 
ATOM   2021 C  CG1 . VAL   B 1 118 ? 29.071 -21.281 11.194 1.00 11.54  ? 124 VAL   C CG1 1 
ATOM   2022 C  CG2 . VAL   B 1 118 ? 28.691 -23.517 12.226 1.00 11.57  ? 124 VAL   C CG2 1 
ATOM   2023 N  N   . SER   B 1 119 ? 28.870 -19.036 13.561 1.00 10.88  ? 125 SER   C N   1 
ATOM   2024 C  CA  . SER   B 1 119 ? 28.677 -17.585 13.447 1.00 11.14  ? 125 SER   C CA  1 
ATOM   2025 C  C   . SER   B 1 119 ? 29.687 -16.925 12.534 1.00 12.29  ? 125 SER   C C   1 
ATOM   2026 O  O   . SER   B 1 119 ? 29.354 -15.839 12.005 1.00 12.82  ? 125 SER   C O   1 
ATOM   2027 C  CB  . SER   B 1 119 ? 28.699 -17.000 14.860 1.00 12.31  ? 125 SER   C CB  1 
ATOM   2028 O  OG  . SER   B 1 119 ? 28.590 -15.570 14.834 1.00 13.08  ? 125 SER   C OG  1 
ATOM   2029 N  N   . THR   B 1 120 ? 30.930 -17.463 12.410 1.00 12.67  ? 126 THR   C N   1 
ATOM   2030 C  CA  . THR   B 1 120 ? 31.956 -16.772 11.590 1.00 12.06  ? 126 THR   C CA  1 
ATOM   2031 C  C   . THR   B 1 120 ? 32.645 -17.787 10.696 1.00 11.53  ? 126 THR   C C   1 
ATOM   2032 O  O   . THR   B 1 120 ? 32.562 -19.012 10.929 1.00 11.50  ? 126 THR   C O   1 
ATOM   2033 C  CB  . THR   B 1 120 ? 33.028 -16.048 12.469 1.00 12.63  ? 126 THR   C CB  1 
ATOM   2034 O  OG1 . THR   B 1 120 ? 33.873 -17.010 13.110 1.00 13.74  ? 126 THR   C OG1 1 
ATOM   2035 C  CG2 . THR   B 1 120 ? 32.418 -15.123 13.477 1.00 14.60  ? 126 THR   C CG2 1 
ATOM   2036 N  N   . GLY   B 1 121 ? 33.352 -17.313 9.698  1.00 12.71  ? 127 GLY   C N   1 
ATOM   2037 C  CA  . GLY   B 1 121 ? 34.118 -18.179 8.791  1.00 14.41  ? 127 GLY   C CA  1 
ATOM   2038 C  C   . GLY   B 1 121 ? 35.144 -17.407 8.009  1.00 18.02  ? 127 GLY   C C   1 
ATOM   2039 O  O   . GLY   B 1 121 ? 35.026 -16.195 7.862  1.00 20.99  ? 127 GLY   C O   1 
ATOM   2040 N  N   . GLY   B 1 122 ? 36.007 -18.103 7.340  1.00 21.15  ? 128 GLY   C N   1 
ATOM   2041 C  CA  . GLY   B 1 122 ? 37.078 -17.474 6.558  1.00 23.90  ? 128 GLY   C CA  1 
ATOM   2042 C  C   . GLY   B 1 122 ? 38.465 -17.868 7.067  1.00 24.06  ? 128 GLY   C C   1 
ATOM   2043 O  O   . GLY   B 1 122 ? 38.666 -18.290 8.210  1.00 24.05  ? 128 GLY   C O   1 
ATOM   2044 N  N   . ASN   B 1 123 ? 39.468 -17.724 6.188  1.00 23.20  ? 129 ASN   C N   1 
ATOM   2045 C  CA  . ASN   B 1 123 ? 40.867 -18.061 6.483  1.00 23.86  ? 129 ASN   C CA  1 
ATOM   2046 C  C   . ASN   B 1 123 ? 41.029 -19.522 6.945  1.00 21.57  ? 129 ASN   C C   1 
ATOM   2047 O  O   . ASN   B 1 123 ? 42.023 -19.813 7.622  1.00 24.16  ? 129 ASN   C O   1 
ATOM   2048 C  CB  . ASN   B 1 123 ? 41.471 -17.097 7.534  1.00 29.41  ? 129 ASN   C CB  1 
ATOM   2049 C  CG  . ASN   B 1 123 ? 42.452 -16.031 7.011  1.00 37.82  ? 129 ASN   C CG  1 
ATOM   2050 O  OD1 . ASN   B 1 123 ? 42.890 -16.043 5.851  1.00 39.74  ? 129 ASN   C OD1 1 
ATOM   2051 N  ND2 . ASN   B 1 123 ? 42.812 -15.061 7.852  1.00 40.64  ? 129 ASN   C ND2 1 
ATOM   2052 N  N   . GLY   B 1 124 ? 40.119 -20.421 6.548  1.00 19.67  ? 130 GLY   C N   1 
ATOM   2053 C  CA  . GLY   B 1 124 ? 40.173 -21.836 6.958  1.00 18.74  ? 130 GLY   C CA  1 
ATOM   2054 C  C   . GLY   B 1 124 ? 39.788 -22.076 8.397  1.00 16.27  ? 130 GLY   C C   1 
ATOM   2055 O  O   . GLY   B 1 124 ? 40.055 -23.170 8.908  1.00 16.67  ? 130 GLY   C O   1 
ATOM   2056 N  N   . LEU   B 1 125 ? 39.125 -21.103 9.029  1.00 15.10  ? 131 LEU   C N   1 
ATOM   2057 C  CA  . LEU   B 1 125 ? 38.654 -21.222 10.400 1.00 14.79  ? 131 LEU   C CA  1 
ATOM   2058 C  C   . LEU   B 1 125 ? 37.116 -21.116 10.425 1.00 14.84  ? 131 LEU   C C   1 
ATOM   2059 O  O   . LEU   B 1 125 ? 36.485 -20.496 9.532  1.00 17.86  ? 131 LEU   C O   1 
ATOM   2060 C  CB  . LEU   B 1 125 ? 39.278 -20.112 11.284 1.00 17.08  ? 131 LEU   C CB  1 
ATOM   2061 C  CG  . LEU   B 1 125 ? 40.831 -20.127 11.387 1.00 19.57  ? 131 LEU   C CG  1 
ATOM   2062 C  CD1 . LEU   B 1 125 ? 41.368 -18.773 11.859 1.00 24.53  ? 131 LEU   C CD1 1 
ATOM   2063 C  CD2 . LEU   B 1 125 ? 41.317 -21.266 12.220 1.00 20.22  ? 131 LEU   C CD2 1 
ATOM   2064 N  N   . VAL   B 1 126 ? 36.525 -21.761 11.390 1.00 12.15  ? 132 VAL   C N   1 
ATOM   2065 C  CA  . VAL   B 1 126 ? 35.070 -21.640 11.641 1.00 11.99  ? 132 VAL   C CA  1 
ATOM   2066 C  C   . VAL   B 1 126 ? 34.921 -21.179 13.103 1.00 11.50  ? 132 VAL   C C   1 
ATOM   2067 O  O   . VAL   B 1 126 ? 35.589 -21.708 14.000 1.00 11.95  ? 132 VAL   C O   1 
ATOM   2068 C  CB  . VAL   B 1 126 ? 34.338 -22.991 11.388 1.00 11.80  ? 132 VAL   C CB  1 
ATOM   2069 C  CG1 . VAL   B 1 126 ? 35.006 -24.175 12.063 1.00 13.71  ? 132 VAL   C CG1 1 
ATOM   2070 C  CG2 . VAL   B 1 126 ? 32.848 -22.902 11.767 1.00 13.05  ? 132 VAL   C CG2 1 
ATOM   2071 N  N   . GLY   B 1 127 ? 34.034 -20.210 13.296 1.00 10.98  ? 133 GLY   C N   1 
ATOM   2072 C  CA  . GLY   B 1 127 ? 33.794 -19.697 14.639 1.00 11.78  ? 133 GLY   C CA  1 
ATOM   2073 C  C   . GLY   B 1 127 ? 32.376 -20.029 15.074 1.00 11.61  ? 133 GLY   C C   1 
ATOM   2074 O  O   . GLY   B 1 127 ? 31.432 -19.881 14.287 1.00 11.64  ? 133 GLY   C O   1 
ATOM   2075 N  N   . PHE   B 1 128 ? 32.254 -20.394 16.344 1.00 10.69  ? 134 PHE   C N   1 
ATOM   2076 C  CA  . PHE   B 1 128 ? 30.968 -20.765 16.969 1.00 10.67  ? 134 PHE   C CA  1 
ATOM   2077 C  C   . PHE   B 1 128 ? 30.625 -19.847 18.107 1.00 11.37  ? 134 PHE   C C   1 
ATOM   2078 O  O   . PHE   B 1 128 ? 31.481 -19.586 18.966 1.00 11.78  ? 134 PHE   C O   1 
ATOM   2079 C  CB  . PHE   B 1 128 ? 31.036 -22.216 17.536 1.00 11.62  ? 134 PHE   C CB  1 
ATOM   2080 C  CG  . PHE   B 1 128 ? 31.556 -23.233 16.529 1.00 11.22  ? 134 PHE   C CG  1 
ATOM   2081 C  CD1 . PHE   B 1 128 ? 30.709 -23.823 15.610 1.00 11.08  ? 134 PHE   C CD1 1 
ATOM   2082 C  CD2 . PHE   B 1 128 ? 32.893 -23.626 16.545 1.00 12.20  ? 134 PHE   C CD2 1 
ATOM   2083 C  CE1 . PHE   B 1 128 ? 31.187 -24.773 14.732 1.00 12.03  ? 134 PHE   C CE1 1 
ATOM   2084 C  CE2 . PHE   B 1 128 ? 33.384 -24.592 15.641 1.00 12.85  ? 134 PHE   C CE2 1 
ATOM   2085 C  CZ  . PHE   B 1 128 ? 32.528 -25.169 14.762 1.00 12.49  ? 134 PHE   C CZ  1 
ATOM   2086 N  N   . ALA   B 1 129 ? 29.381 -19.329 18.096 1.00 10.69  ? 135 ALA   C N   1 
ATOM   2087 C  CA  . ALA   B 1 129 ? 28.862 -18.543 19.236 1.00 10.97  ? 135 ALA   C CA  1 
ATOM   2088 C  C   . ALA   B 1 129 ? 28.473 -19.530 20.373 1.00 12.13  ? 135 ALA   C C   1 
ATOM   2089 O  O   . ALA   B 1 129 ? 27.569 -20.363 20.209 1.00 11.42  ? 135 ALA   C O   1 
ATOM   2090 C  CB  . ALA   B 1 129 ? 27.623 -17.750 18.790 1.00 11.61  ? 135 ALA   C CB  1 
ATOM   2091 N  N   . ASP   B 1 130 ? 29.172 -19.449 21.494 1.00 11.49  ? 136 ASP   C N   1 
ATOM   2092 C  CA  . ASP   B 1 130 ? 28.887 -20.339 22.623 1.00 11.81  ? 136 ASP   C CA  1 
ATOM   2093 C  C   . ASP   B 1 130 ? 27.545 -20.003 23.251 1.00 12.35  ? 136 ASP   C C   1 
ATOM   2094 O  O   . ASP   B 1 130 ? 27.162 -18.819 23.312 1.00 12.46  ? 136 ASP   C O   1 
ATOM   2095 C  CB  . ASP   B 1 130 ? 29.980 -20.099 23.690 1.00 12.58  ? 136 ASP   C CB  1 
ATOM   2096 C  CG  . ASP   B 1 130 ? 29.863 -21.013 24.893 1.00 14.86  ? 136 ASP   C CG  1 
ATOM   2097 O  OD1 . ASP   B 1 130 ? 29.764 -22.237 24.712 1.00 14.58  ? 136 ASP   C OD1 1 
ATOM   2098 O  OD2 . ASP   B 1 130 ? 29.782 -20.483 26.040 1.00 16.85  ? 136 ASP   C OD2 1 
ATOM   2099 N  N   . VAL   B 1 131 ? 26.826 -21.021 23.721 1.00 12.35  ? 137 VAL   C N   1 
ATOM   2100 C  CA  . VAL   B 1 131 ? 25.591 -20.825 24.506 1.00 12.34  ? 137 VAL   C CA  1 
ATOM   2101 C  C   . VAL   B 1 131 ? 25.640 -21.490 25.876 1.00 12.62  ? 137 VAL   C C   1 
ATOM   2102 O  O   . VAL   B 1 131 ? 24.659 -21.436 26.639 1.00 13.10  ? 137 VAL   C O   1 
ATOM   2103 C  CB  . VAL   B 1 131 ? 24.325 -21.294 23.753 1.00 12.51  ? 137 VAL   C CB  1 
ATOM   2104 C  CG1 . VAL   B 1 131 ? 24.139 -20.461 22.451 1.00 12.24  ? 137 VAL   C CG1 1 
ATOM   2105 C  CG2 . VAL   B 1 131 ? 24.371 -22.779 23.433 1.00 12.29  ? 137 VAL   C CG2 1 
ATOM   2106 N  N   . ARG   B 1 132 ? 26.782 -22.122 26.235 1.00 12.42  ? 138 ARG   C N   1 
ATOM   2107 C  CA  . ARG   B 1 132 ? 26.852 -22.914 27.501 1.00 12.89  ? 138 ARG   C CA  1 
ATOM   2108 C  C   . ARG   B 1 132 ? 26.804 -22.101 28.764 1.00 12.74  ? 138 ARG   C C   1 
ATOM   2109 O  O   . ARG   B 1 132 ? 26.471 -22.644 29.830 1.00 13.98  ? 138 ARG   C O   1 
ATOM   2110 C  CB  . ARG   B 1 132 ? 28.115 -23.780 27.472 1.00 12.14  ? 138 ARG   C CB  1 
ATOM   2111 C  CG  . ARG   B 1 132 ? 28.095 -24.831 26.337 1.00 11.93  ? 138 ARG   C CG  1 
ATOM   2112 C  CD  . ARG   B 1 132 ? 29.412 -25.605 26.390 1.00 12.03  ? 138 ARG   C CD  1 
ATOM   2113 N  NE  . ARG   B 1 132 ? 30.512 -24.715 25.998 1.00 12.60  ? 138 ARG   C NE  1 
ATOM   2114 C  CZ  . ARG   B 1 132 ? 31.754 -25.115 25.810 1.00 13.34  ? 138 ARG   C CZ  1 
ATOM   2115 N  NH1 . ARG   B 1 132 ? 32.132 -26.349 26.168 1.00 12.86  ? 138 ARG   C NH1 1 
ATOM   2116 N  NH2 . ARG   B 1 132 ? 32.660 -24.269 25.341 1.00 13.01  ? 138 ARG   C NH2 1 
ATOM   2117 N  N   . ASP   B 1 133 ? 27.056 -20.790 28.679 1.00 12.68  ? 139 ASP   C N   1 
ATOM   2118 C  CA  . ASP   B 1 133 ? 26.982 -19.912 29.854 1.00 14.16  ? 139 ASP   C CA  1 
ATOM   2119 C  C   . ASP   B 1 133 ? 25.557 -19.368 30.046 1.00 14.62  ? 139 ASP   C C   1 
ATOM   2120 O  O   . ASP   B 1 133 ? 25.327 -18.747 31.098 1.00 15.84  ? 139 ASP   C O   1 
ATOM   2121 C  CB  . ASP   B 1 133 ? 27.958 -18.714 29.710 1.00 14.49  ? 139 ASP   C CB  1 
ATOM   2122 C  CG  . ASP   B 1 133 ? 27.598 -17.798 28.556 1.00 16.62  ? 139 ASP   C CG  1 
ATOM   2123 O  OD1 . ASP   B 1 133 ? 27.256 -18.309 27.470 1.00 15.65  ? 139 ASP   C OD1 1 
ATOM   2124 O  OD2 . ASP   B 1 133 ? 27.629 -16.544 28.745 1.00 19.01  ? 139 ASP   C OD2 1 
ATOM   2125 N  N   . LEU   B 1 134 ? 24.615 -19.611 29.100 1.00 13.66  ? 140 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 134 ? 23.261 -19.031 29.186 1.00 13.55  ? 140 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 134 ? 22.381 -19.995 29.950 1.00 13.76  ? 140 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 134 ? 21.565 -20.731 29.398 1.00 13.88  ? 140 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 134 ? 22.729 -18.794 27.770 1.00 13.40  ? 140 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 134 ? 23.598 -17.848 26.893 1.00 14.39  ? 140 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 134 ? 23.015 -17.756 25.444 1.00 15.08  ? 140 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 134 ? 23.718 -16.433 27.514 1.00 15.67  ? 140 LEU   C CD2 1 
ATOM   2133 N  N   . LEU   B 1 135 ? 22.613 -20.056 31.293 1.00 14.14  ? 141 LEU   C N   1 
ATOM   2134 C  CA  . LEU   B 1 135 ? 21.983 -21.098 32.140 1.00 16.04  ? 141 LEU   C CA  1 
ATOM   2135 C  C   . LEU   B 1 135 ? 20.467 -20.971 32.206 1.00 15.31  ? 141 LEU   C C   1 
ATOM   2136 O  O   . LEU   B 1 135 ? 19.757 -21.977 32.343 1.00 16.19  ? 141 LEU   C O   1 
ATOM   2137 C  CB  . LEU   B 1 135 ? 22.571 -21.132 33.581 1.00 15.54  ? 141 LEU   C CB  1 
ATOM   2138 C  CG  . LEU   B 1 135 ? 24.133 -21.121 33.677 1.00 18.38  ? 141 LEU   C CG  1 
ATOM   2139 C  CD1 . LEU   B 1 135 ? 24.641 -21.264 35.149 1.00 19.84  ? 141 LEU   C CD1 1 
ATOM   2140 C  CD2 . LEU   B 1 135 ? 24.807 -22.178 32.820 1.00 17.97  ? 141 LEU   C CD2 1 
ATOM   2141 N  N   . TRP   B 1 136 ? 19.969 -19.749 32.000 1.00 15.00  ? 142 TRP   C N   1 
ATOM   2142 C  CA  . TRP   B 1 136 ? 18.532 -19.467 32.025 1.00 16.42  ? 142 TRP   C CA  1 
ATOM   2143 C  C   . TRP   B 1 136 ? 17.799 -20.179 30.896 1.00 17.15  ? 142 TRP   C C   1 
ATOM   2144 O  O   . TRP   B 1 136 ? 16.576 -20.324 30.977 1.00 18.36  ? 142 TRP   C O   1 
ATOM   2145 C  CB  . TRP   B 1 136 ? 18.284 -17.951 32.025 1.00 16.46  ? 142 TRP   C CB  1 
ATOM   2146 C  CG  . TRP   B 1 136 ? 18.969 -17.228 30.901 1.00 15.85  ? 142 TRP   C CG  1 
ATOM   2147 C  CD1 . TRP   B 1 136 ? 20.142 -16.535 30.971 1.00 16.76  ? 142 TRP   C CD1 1 
ATOM   2148 C  CD2 . TRP   B 1 136 ? 18.445 -17.002 29.567 1.00 15.87  ? 142 TRP   C CD2 1 
ATOM   2149 N  NE1 . TRP   B 1 136 ? 20.434 -15.974 29.737 1.00 17.71  ? 142 TRP   C NE1 1 
ATOM   2150 C  CE2 . TRP   B 1 136 ? 19.385 -16.213 28.875 1.00 17.13  ? 142 TRP   C CE2 1 
ATOM   2151 C  CE3 . TRP   B 1 136 ? 17.280 -17.393 28.916 1.00 16.13  ? 142 TRP   C CE3 1 
ATOM   2152 C  CZ2 . TRP   B 1 136 ? 19.207 -15.848 27.532 1.00 17.17  ? 142 TRP   C CZ2 1 
ATOM   2153 C  CZ3 . TRP   B 1 136 ? 17.067 -16.971 27.616 1.00 17.45  ? 142 TRP   C CZ3 1 
ATOM   2154 C  CH2 . TRP   B 1 136 ? 18.026 -16.221 26.935 1.00 17.69  ? 142 TRP   C CH2 1 
ATOM   2155 N  N   . LEU   B 1 137 ? 18.485 -20.624 29.824 1.00 15.93  ? 143 LEU   C N   1 
ATOM   2156 C  CA  . LEU   B 1 137 ? 17.794 -21.386 28.770 1.00 16.63  ? 143 LEU   C CA  1 
ATOM   2157 C  C   . LEU   B 1 137 ? 17.193 -22.698 29.317 1.00 19.66  ? 143 LEU   C C   1 
ATOM   2158 O  O   . LEU   B 1 137 ? 16.267 -23.248 28.718 1.00 21.44  ? 143 LEU   C O   1 
ATOM   2159 C  CB  . LEU   B 1 137 ? 18.755 -21.736 27.627 1.00 16.00  ? 143 LEU   C CB  1 
ATOM   2160 C  CG  . LEU   B 1 137 ? 19.216 -20.550 26.741 1.00 15.28  ? 143 LEU   C CG  1 
ATOM   2161 C  CD1 . LEU   B 1 137 ? 20.364 -21.004 25.807 1.00 16.37  ? 143 LEU   C CD1 1 
ATOM   2162 C  CD2 . LEU   B 1 137 ? 18.056 -19.997 25.869 1.00 17.71  ? 143 LEU   C CD2 1 
ATOM   2163 N  N   . ASP   B 1 138 ? 17.711 -23.193 30.478 1.00 19.02  ? 144 ASP   C N   1 
ATOM   2164 C  CA  . ASP   B 1 138 ? 17.253 -24.464 31.052 1.00 21.31  ? 144 ASP   C CA  1 
ATOM   2165 C  C   . ASP   B 1 138 ? 16.019 -24.303 31.967 1.00 24.19  ? 144 ASP   C C   1 
ATOM   2166 O  O   . ASP   B 1 138 ? 15.573 -25.313 32.528 1.00 25.13  ? 144 ASP   C O   1 
ATOM   2167 C  CB  . ASP   B 1 138 ? 18.352 -25.112 31.906 1.00 20.25  ? 144 ASP   C CB  1 
ATOM   2168 C  CG  . ASP   B 1 138 ? 19.602 -25.537 31.138 1.00 20.35  ? 144 ASP   C CG  1 
ATOM   2169 O  OD1 . ASP   B 1 138 ? 19.561 -25.559 29.893 1.00 20.94  ? 144 ASP   C OD1 1 
ATOM   2170 O  OD2 . ASP   B 1 138 ? 20.635 -25.820 31.803 1.00 23.30  ? 144 ASP   C OD2 1 
ATOM   2171 N  N   . GLU   B 1 139 ? 15.505 -23.089 32.157 1.00 25.21  ? 145 GLU   C N   1 
ATOM   2172 C  CA  . GLU   B 1 139 ? 14.381 -22.867 33.075 1.00 29.89  ? 145 GLU   C CA  1 
ATOM   2173 C  C   . GLU   B 1 139 ? 13.289 -21.954 32.481 1.00 34.05  ? 145 GLU   C C   1 
ATOM   2174 O  O   . GLU   B 1 139 ? 13.481 -21.366 31.417 1.00 34.10  ? 145 GLU   C O   1 
ATOM   2175 C  CB  . GLU   B 1 139 ? 14.945 -22.279 34.388 1.00 34.60  ? 145 GLU   C CB  1 
ATOM   2176 C  CG  . GLU   B 1 139 ? 15.620 -20.937 34.178 1.00 43.47  ? 145 GLU   C CG  1 
ATOM   2177 C  CD  . GLU   B 1 139 ? 16.644 -20.531 35.224 1.00 52.85  ? 145 GLU   C CD  1 
ATOM   2178 O  OE1 . GLU   B 1 139 ? 16.910 -19.312 35.357 1.00 53.54  ? 145 GLU   C OE1 1 
ATOM   2179 O  OE2 . GLU   B 1 139 ? 17.178 -21.432 35.912 1.00 55.82  ? 145 GLU   C OE2 1 
ATOM   2180 N  N   . GLU   B 1 140 ? 12.194 -21.745 33.252 1.00 37.46  ? 146 GLU   C N   1 
ATOM   2181 C  CA  . GLU   B 1 140 ? 11.022 -20.888 32.977 1.00 40.61  ? 146 GLU   C CA  1 
ATOM   2182 C  C   . GLU   B 1 140 ? 9.926  -21.695 32.302 1.00 42.95  ? 146 GLU   C C   1 
ATOM   2183 O  O   . GLU   B 1 140 ? 9.606  -22.786 32.788 1.00 43.65  ? 146 GLU   C O   1 
ATOM   2184 C  CB  . GLU   B 1 140 ? 11.365 -19.588 32.229 1.00 42.94  ? 146 GLU   C CB  1 
ATOM   2185 C  CG  . GLU   B 1 140 ? 10.186 -18.689 31.909 1.00 49.85  ? 146 GLU   C CG  1 
ATOM   2186 C  CD  . GLU   B 1 140 ? 9.793  -17.722 33.013 1.00 58.51  ? 146 GLU   C CD  1 
ATOM   2187 O  OE1 . GLU   B 1 140 ? 10.420 -16.640 33.105 1.00 60.46  ? 146 GLU   C OE1 1 
ATOM   2188 O  OE2 . GLU   B 1 140 ? 8.852  -18.038 33.777 1.00 59.90  ? 146 GLU   C OE2 1 
HETATM 2189 N  N1  . A1B1E C 2 .   ? 10.720 15.481  17.532 0.75 19.09  ? 201 A1B1E A N1  1 
HETATM 2190 C  C4  . A1B1E C 2 .   ? 11.266 15.849  22.153 0.75 25.26  ? 201 A1B1E A C4  1 
HETATM 2191 C  C5  . A1B1E C 2 .   ? 11.242 16.448  20.740 0.75 23.90  ? 201 A1B1E A C5  1 
HETATM 2192 C  C6  . A1B1E C 2 .   ? 10.155 15.762  19.877 0.75 23.60  ? 201 A1B1E A C6  1 
HETATM 2193 C  C7  . A1B1E C 2 .   ? 10.152 16.271  18.446 0.75 21.80  ? 201 A1B1E A C7  1 
HETATM 2194 C  C8  . A1B1E C 2 .   ? 8.806  15.926  20.584 0.75 25.29  ? 201 A1B1E A C8  1 
HETATM 2195 C  C10 . A1B1E C 2 .   ? 6.765  15.323  24.765 0.75 30.83  ? 201 A1B1E A C10 1 
HETATM 2196 C  C13 . A1B1E C 2 .   ? 6.432  13.045  25.299 0.75 30.77  ? 201 A1B1E A C13 1 
HETATM 2197 O  O2  . A1B1E C 2 .   ? 9.664  17.371  18.168 0.75 22.98  ? 201 A1B1E A O2  1 
HETATM 2198 C  C3  . A1B1E C 2 .   ? 9.891  15.956  22.803 0.75 26.17  ? 201 A1B1E A C3  1 
HETATM 2199 N  N   . A1B1E C 2 .   ? 8.867  15.356  21.935 0.75 26.75  ? 201 A1B1E A N   1 
HETATM 2200 C  C2  . A1B1E C 2 .   ? 8.040  14.362  22.309 0.75 27.45  ? 201 A1B1E A C2  1 
HETATM 2201 O  O1  . A1B1E C 2 .   ? 7.087  14.066  21.624 0.75 27.44  ? 201 A1B1E A O1  1 
HETATM 2202 C  C1  . A1B1E C 2 .   ? 8.268  13.622  23.645 0.75 28.25  ? 201 A1B1E A C1  1 
HETATM 2203 O  O   . A1B1E C 2 .   ? 8.170  12.205  23.569 0.75 28.07  ? 201 A1B1E A O   1 
HETATM 2204 C  C   . A1B1E C 2 .   ? 9.412  11.553  23.223 0.75 26.83  ? 201 A1B1E A C   1 
HETATM 2205 C  C9  . A1B1E C 2 .   ? 7.155  14.004  24.598 0.75 30.14  ? 201 A1B1E A C9  1 
HETATM 2206 N  N2  . A1B1E C 2 .   ? 5.387  13.316  26.097 0.75 31.17  ? 201 A1B1E A N2  1 
HETATM 2207 C  C12 . A1B1E C 2 .   ? 5.030  14.596  26.216 0.75 31.40  ? 201 A1B1E A C12 1 
HETATM 2208 C  C11 . A1B1E C 2 .   ? 5.690  15.630  25.579 0.75 31.44  ? 201 A1B1E A C11 1 
HETATM 2209 ZN ZN  . ZN    D 3 .   ? 11.099 -3.965  5.809  1.00 20.51  2 202 ZN    A ZN  1 
HETATM 2210 S  S   . DMS   E 4 .   ? 19.204 -1.782  24.249 1.00 81.46  ? 203 DMS   A S   1 
HETATM 2211 O  O   . DMS   E 4 .   ? 18.377 -2.152  23.054 1.00 81.32  ? 203 DMS   A O   1 
HETATM 2212 C  C1  . DMS   E 4 .   ? 19.328 -3.249  25.303 1.00 81.40  ? 203 DMS   A C1  1 
HETATM 2213 C  C2  . DMS   E 4 .   ? 20.948 -1.794  23.750 1.00 81.49  ? 203 DMS   A C2  1 
HETATM 2214 S  S   . DMS   F 4 .   ? 19.521 20.436  5.649  1.00 76.97  ? 204 DMS   A S   1 
HETATM 2215 O  O   . DMS   F 4 .   ? 19.768 21.433  6.746  1.00 76.79  ? 204 DMS   A O   1 
HETATM 2216 C  C1  . DMS   F 4 .   ? 20.815 20.650  4.392  1.00 77.00  ? 204 DMS   A C1  1 
HETATM 2217 C  C2  . DMS   F 4 .   ? 18.190 21.122  4.622  1.00 77.06  ? 204 DMS   A C2  1 
HETATM 2218 ZN ZN  . ZN    G 3 .   ? 30.520 -31.152 26.703 1.00 12.78  2 201 ZN    C ZN  1 
HETATM 2219 S  S   . DMS   H 4 .   ? 20.787 -32.284 9.288  1.00 87.97  ? 202 DMS   C S   1 
HETATM 2220 O  O   . DMS   H 4 .   ? 21.992 -32.680 8.497  1.00 88.20  ? 202 DMS   C O   1 
HETATM 2221 C  C1  . DMS   H 4 .   ? 21.251 -32.290 11.026 1.00 87.91  ? 202 DMS   C C1  1 
HETATM 2222 C  C2  . DMS   H 4 .   ? 20.586 -30.488 9.152  1.00 87.87  ? 202 DMS   C C2  1 
HETATM 2223 O  O   . HOH   I 5 .   ? 5.403  18.717  24.259 1.00 47.03  ? 301 HOH   A O   1 
HETATM 2224 O  O   . HOH   I 5 .   ? 35.341 -3.818  7.915  1.00 23.19  ? 302 HOH   A O   1 
HETATM 2225 O  O   . HOH   I 5 .   ? 11.179 8.799   4.293  1.00 22.50  ? 303 HOH   A O   1 
HETATM 2226 O  O   . HOH   I 5 .   ? 13.169 11.418  24.630 1.00 24.65  ? 304 HOH   A O   1 
HETATM 2227 O  O   . HOH   I 5 .   ? 2.977  9.452   8.988  1.00 28.83  ? 305 HOH   A O   1 
HETATM 2228 O  O   . HOH   I 5 .   ? 22.950 13.284  23.774 1.00 46.39  ? 306 HOH   A O   1 
HETATM 2229 O  O   . HOH   I 5 .   ? 6.534  3.473   3.333  1.00 37.81  ? 307 HOH   A O   1 
HETATM 2230 O  O   . HOH   I 5 .   ? 8.662  19.191  19.636 1.00 24.07  ? 308 HOH   A O   1 
HETATM 2231 O  O   . HOH   I 5 .   ? 37.444 14.945  14.075 1.00 54.14  ? 309 HOH   A O   1 
HETATM 2232 O  O   . HOH   I 5 .   ? 13.905 2.890   1.251  1.00 23.26  ? 310 HOH   A O   1 
HETATM 2233 O  O   . HOH   I 5 .   ? 7.323  20.324  17.536 1.00 25.50  ? 311 HOH   A O   1 
HETATM 2234 O  O   . HOH   I 5 .   ? 31.497 -2.527  15.220 1.00 49.58  ? 312 HOH   A O   1 
HETATM 2235 O  O   . HOH   I 5 .   ? 29.351 22.281  19.387 1.00 30.32  ? 313 HOH   A O   1 
HETATM 2236 O  O   . HOH   I 5 .   ? 8.349  24.948  23.655 1.00 36.39  ? 314 HOH   A O   1 
HETATM 2237 O  O   . HOH   I 5 .   ? 0.481  -0.898  19.360 1.00 22.05  ? 315 HOH   A O   1 
HETATM 2238 O  O   . HOH   I 5 .   ? 23.373 21.666  7.217  1.00 25.46  ? 316 HOH   A O   1 
HETATM 2239 O  O   . HOH   I 5 .   ? 27.854 8.027   1.747  1.00 34.20  ? 317 HOH   A O   1 
HETATM 2240 O  O   . HOH   I 5 .   ? 12.768 -5.931  30.375 1.00 41.36  ? 318 HOH   A O   1 
HETATM 2241 O  O   . HOH   I 5 .   ? 0.564  -1.130  9.082  1.00 35.58  ? 319 HOH   A O   1 
HETATM 2242 O  O   . HOH   I 5 .   ? 4.636  -3.561  28.810 1.00 28.72  ? 320 HOH   A O   1 
HETATM 2243 O  O   . HOH   I 5 .   ? 19.294 10.083  19.635 1.00 13.73  ? 321 HOH   A O   1 
HETATM 2244 O  O   . HOH   I 5 .   ? 17.451 1.023   28.166 1.00 26.31  ? 322 HOH   A O   1 
HETATM 2245 O  O   . HOH   I 5 .   ? 30.317 10.509  15.585 1.00 32.52  ? 323 HOH   A O   1 
HETATM 2246 O  O   . HOH   I 5 .   ? 35.282 7.956   9.490  1.00 48.19  ? 324 HOH   A O   1 
HETATM 2247 O  O   . HOH   I 5 .   ? 28.108 3.138   4.937  1.00 33.02  ? 325 HOH   A O   1 
HETATM 2248 O  O   . HOH   I 5 .   ? 33.718 14.219  9.666  1.00 33.32  ? 326 HOH   A O   1 
HETATM 2249 O  O   . HOH   I 5 .   ? 10.753 5.691   3.390  1.00 27.47  ? 327 HOH   A O   1 
HETATM 2250 O  O   . HOH   I 5 .   ? 2.585  -2.849  20.727 1.00 25.37  ? 328 HOH   A O   1 
HETATM 2251 O  O   . HOH   I 5 .   ? -0.067 1.277   15.823 1.00 13.64  ? 329 HOH   A O   1 
HETATM 2252 O  O   . HOH   I 5 .   ? 9.520  22.001  10.110 1.00 48.87  ? 330 HOH   A O   1 
HETATM 2253 O  O   . HOH   I 5 .   ? 21.831 2.412   -0.879 1.00 31.14  ? 331 HOH   A O   1 
HETATM 2254 O  O   . HOH   I 5 .   ? 10.313 10.337  31.319 1.00 24.32  ? 332 HOH   A O   1 
HETATM 2255 O  O   . HOH   I 5 .   ? 24.862 5.138   21.428 1.00 28.93  ? 333 HOH   A O   1 
HETATM 2256 O  O   . HOH   I 5 .   ? 14.017 13.824  23.949 1.00 21.43  ? 334 HOH   A O   1 
HETATM 2257 O  O   . HOH   I 5 .   ? 33.833 -2.369  13.563 1.00 35.90  ? 335 HOH   A O   1 
HETATM 2258 O  O   . HOH   I 5 .   ? 22.604 0.868   17.394 1.00 15.75  ? 336 HOH   A O   1 
HETATM 2259 O  O   . HOH   I 5 .   ? 14.922 11.362  0.085  1.00 32.29  ? 337 HOH   A O   1 
HETATM 2260 O  O   . HOH   I 5 .   ? 23.225 11.788  21.987 1.00 36.84  ? 338 HOH   A O   1 
HETATM 2261 O  O   . HOH   I 5 .   ? 20.905 -4.111  14.144 1.00 16.08  ? 339 HOH   A O   1 
HETATM 2262 O  O   . HOH   I 5 .   ? 11.273 12.691  11.116 1.00 17.42  ? 340 HOH   A O   1 
HETATM 2263 O  O   . HOH   I 5 .   ? 18.356 21.866  9.497  1.00 20.10  ? 341 HOH   A O   1 
HETATM 2264 O  O   . HOH   I 5 .   ? 6.010  17.232  21.714 1.00 37.72  ? 342 HOH   A O   1 
HETATM 2265 O  O   . HOH   I 5 .   ? 16.528 3.890   23.635 1.00 17.16  ? 343 HOH   A O   1 
HETATM 2266 O  O   . HOH   I 5 .   ? 13.666 4.041   23.482 1.00 12.67  ? 344 HOH   A O   1 
HETATM 2267 O  O   . HOH   I 5 .   ? 29.848 11.625  18.529 1.00 27.29  ? 345 HOH   A O   1 
HETATM 2268 O  O   . HOH   I 5 .   ? 5.629  5.447   32.617 1.00 20.89  ? 346 HOH   A O   1 
HETATM 2269 O  O   . HOH   I 5 .   ? 3.746  -8.161  9.893  1.00 53.30  ? 347 HOH   A O   1 
HETATM 2270 O  O   . HOH   I 5 .   ? 21.645 4.988   24.655 1.00 44.69  ? 348 HOH   A O   1 
HETATM 2271 O  O   . HOH   I 5 .   ? 30.517 2.983   14.821 1.00 23.88  ? 349 HOH   A O   1 
HETATM 2272 O  O   . HOH   I 5 .   ? 31.558 20.006  11.738 1.00 23.21  ? 350 HOH   A O   1 
HETATM 2273 O  O   . HOH   I 5 .   ? 29.932 -1.426  8.645  1.00 34.80  ? 351 HOH   A O   1 
HETATM 2274 O  O   . HOH   I 5 .   ? 20.695 -0.967  3.022  1.00 30.57  ? 352 HOH   A O   1 
HETATM 2275 O  O   . HOH   I 5 .   ? 26.836 -1.191  8.821  1.00 24.94  ? 353 HOH   A O   1 
HETATM 2276 O  O   . HOH   I 5 .   ? 16.855 -3.490  27.788 1.00 32.04  ? 354 HOH   A O   1 
HETATM 2277 O  O   . HOH   I 5 .   ? 29.368 11.975  21.282 1.00 33.28  ? 355 HOH   A O   1 
HETATM 2278 O  O   . HOH   I 5 .   ? 28.827 15.788  4.332  1.00 32.33  ? 356 HOH   A O   1 
HETATM 2279 O  O   . HOH   I 5 .   ? 28.885 3.419   12.697 1.00 16.10  ? 357 HOH   A O   1 
HETATM 2280 O  O   . HOH   I 5 .   ? 20.278 18.030  23.973 1.00 42.92  ? 358 HOH   A O   1 
HETATM 2281 O  O   . HOH   I 5 .   ? 36.859 2.463   10.081 1.00 47.20  ? 359 HOH   A O   1 
HETATM 2282 O  O   . HOH   I 5 .   ? 20.737 -2.536  16.861 1.00 15.00  ? 360 HOH   A O   1 
HETATM 2283 O  O   . HOH   I 5 .   ? 33.610 11.103  15.714 1.00 40.75  ? 361 HOH   A O   1 
HETATM 2284 O  O   . HOH   I 5 .   ? 13.201 11.388  9.188  1.00 15.08  ? 362 HOH   A O   1 
HETATM 2285 O  O   . HOH   I 5 .   ? 11.567 -6.969  24.688 1.00 28.49  ? 363 HOH   A O   1 
HETATM 2286 O  O   . HOH   I 5 .   ? 32.252 2.186   5.978  1.00 39.53  ? 364 HOH   A O   1 
HETATM 2287 O  O   . HOH   I 5 .   ? 22.832 -0.605  5.367  1.00 21.85  ? 365 HOH   A O   1 
HETATM 2288 O  O   . HOH   I 5 .   ? 6.514  -6.910  23.656 1.00 27.05  ? 366 HOH   A O   1 
HETATM 2289 O  O   . HOH   I 5 .   ? 9.656  4.040   33.468 1.00 13.95  ? 367 HOH   A O   1 
HETATM 2290 O  O   . HOH   I 5 .   ? 8.378  6.553   33.807 1.00 18.60  ? 368 HOH   A O   1 
HETATM 2291 O  O   . HOH   I 5 .   ? 5.019  8.228   2.325  1.00 32.55  ? 369 HOH   A O   1 
HETATM 2292 O  O   . HOH   I 5 .   ? 11.558 17.907  4.793  1.00 38.50  ? 370 HOH   A O   1 
HETATM 2293 O  O   . HOH   I 5 .   ? 17.509 19.992  16.963 1.00 17.19  ? 371 HOH   A O   1 
HETATM 2294 O  O   . HOH   I 5 .   ? 32.756 16.597  9.246  1.00 32.35  ? 372 HOH   A O   1 
HETATM 2295 O  O   . HOH   I 5 .   ? 3.124  7.337   24.239 1.00 27.23  ? 373 HOH   A O   1 
HETATM 2296 O  O   . HOH   I 5 .   ? 19.433 2.953   19.380 1.00 18.90  ? 374 HOH   A O   1 
HETATM 2297 O  O   . HOH   I 5 .   ? 31.973 8.769   7.664  1.00 23.86  ? 375 HOH   A O   1 
HETATM 2298 O  O   . HOH   I 5 .   ? 15.174 14.535  26.264 1.00 31.56  ? 376 HOH   A O   1 
HETATM 2299 O  O   . HOH   I 5 .   ? 3.984  -4.015  6.023  1.00 28.04  ? 377 HOH   A O   1 
HETATM 2300 O  O   . HOH   I 5 .   ? 30.325 4.589   5.785  1.00 22.88  ? 378 HOH   A O   1 
HETATM 2301 O  O   . HOH   I 5 .   ? 4.373  15.066  21.192 1.00 79.46  ? 379 HOH   A O   1 
HETATM 2302 O  O   . HOH   I 5 .   ? 0.160  5.694   6.015  1.00 27.90  ? 380 HOH   A O   1 
HETATM 2303 O  O   . HOH   I 5 .   ? 36.491 18.110  14.459 1.00 31.56  ? 381 HOH   A O   1 
HETATM 2304 O  O   . HOH   I 5 .   ? 17.170 -5.342  12.173 1.00 36.81  ? 382 HOH   A O   1 
HETATM 2305 O  O   . HOH   I 5 .   ? 1.168  11.795  27.481 1.00 32.57  ? 383 HOH   A O   1 
HETATM 2306 O  O   . HOH   I 5 .   ? 4.152  0.329   23.955 1.00 17.92  ? 384 HOH   A O   1 
HETATM 2307 O  O   . HOH   I 5 .   ? 2.543  16.064  19.442 1.00 34.51  ? 385 HOH   A O   1 
HETATM 2308 O  O   . HOH   I 5 .   ? 14.411 -2.468  17.896 1.00 17.81  ? 386 HOH   A O   1 
HETATM 2309 O  O   . HOH   I 5 .   ? 33.861 18.722  10.811 1.00 26.92  ? 387 HOH   A O   1 
HETATM 2310 O  O   . HOH   I 5 .   ? 17.386 10.712  26.061 1.00 24.85  ? 388 HOH   A O   1 
HETATM 2311 O  O   . HOH   I 5 .   ? 35.337 10.857  12.263 1.00 55.83  ? 389 HOH   A O   1 
HETATM 2312 O  O   . HOH   I 5 .   ? 17.106 6.039   26.781 1.00 26.39  ? 390 HOH   A O   1 
HETATM 2313 O  O   . HOH   I 5 .   ? 8.506  -6.439  9.706  1.00 30.55  ? 391 HOH   A O   1 
HETATM 2314 O  O   . HOH   I 5 .   ? 27.850 17.623  24.186 1.00 24.16  ? 392 HOH   A O   1 
HETATM 2315 O  O   . HOH   I 5 .   ? 27.055 -1.317  15.899 1.00 27.62  ? 393 HOH   A O   1 
HETATM 2316 O  O   . HOH   I 5 .   ? 30.756 15.745  22.877 1.00 27.86  ? 394 HOH   A O   1 
HETATM 2317 O  O   . HOH   I 5 .   ? 16.458 21.249  19.125 1.00 23.85  ? 395 HOH   A O   1 
HETATM 2318 O  O   . HOH   I 5 .   ? 2.044  14.507  16.943 1.00 40.30  ? 396 HOH   A O   1 
HETATM 2319 O  O   . HOH   I 5 .   ? 24.193 -3.358  16.211 1.00 38.89  ? 397 HOH   A O   1 
HETATM 2320 O  O   . HOH   I 5 .   ? 25.172 17.877  4.604  1.00 36.45  ? 398 HOH   A O   1 
HETATM 2321 O  O   . HOH   I 5 .   ? 25.374 19.689  21.704 1.00 28.21  ? 399 HOH   A O   1 
HETATM 2322 O  O   . HOH   I 5 .   ? 22.486 19.539  19.691 1.00 31.62  ? 400 HOH   A O   1 
HETATM 2323 O  O   . HOH   I 5 .   ? 23.144 -6.552  11.896 1.00 31.75  ? 401 HOH   A O   1 
HETATM 2324 O  O   . HOH   I 5 .   ? 18.055 17.663  4.160  1.00 34.11  ? 402 HOH   A O   1 
HETATM 2325 O  O   . HOH   I 5 .   ? 35.852 15.374  11.077 1.00 41.50  ? 403 HOH   A O   1 
HETATM 2326 O  O   . HOH   I 5 .   ? 13.764 25.178  25.950 1.00 40.75  ? 404 HOH   A O   1 
HETATM 2327 O  O   . HOH   I 5 .   ? 5.186  26.727  19.760 1.00 34.57  ? 405 HOH   A O   1 
HETATM 2328 O  O   . HOH   I 5 .   ? 17.413 0.670   20.191 1.00 18.75  ? 406 HOH   A O   1 
HETATM 2329 O  O   . HOH   I 5 .   ? 19.764 13.231  2.129  1.00 32.05  ? 407 HOH   A O   1 
HETATM 2330 O  O   . HOH   I 5 .   ? 15.193 15.176  3.404  1.00 31.93  ? 408 HOH   A O   1 
HETATM 2331 O  O   . HOH   I 5 .   ? 36.248 -0.375  12.603 1.00 35.91  ? 409 HOH   A O   1 
HETATM 2332 O  O   . HOH   I 5 .   ? 19.225 16.988  26.174 1.00 43.56  ? 410 HOH   A O   1 
HETATM 2333 O  O   . HOH   I 5 .   ? 3.647  11.534  18.967 1.00 39.78  ? 411 HOH   A O   1 
HETATM 2334 O  O   . HOH   I 5 .   ? 3.342  -0.323  21.395 1.00 21.55  ? 412 HOH   A O   1 
HETATM 2335 O  O   . HOH   I 5 .   ? 17.681 24.388  10.282 1.00 37.03  ? 413 HOH   A O   1 
HETATM 2336 O  O   . HOH   I 5 .   ? 1.916  22.952  21.213 1.00 34.21  ? 414 HOH   A O   1 
HETATM 2337 O  O   . HOH   I 5 .   ? 3.092  0.570   28.830 1.00 40.36  ? 415 HOH   A O   1 
HETATM 2338 O  O   . HOH   I 5 .   ? 16.794 -3.954  2.848  1.00 25.29  ? 416 HOH   A O   1 
HETATM 2339 O  O   . HOH   I 5 .   ? 33.912 5.222   16.659 1.00 32.88  ? 417 HOH   A O   1 
HETATM 2340 O  O   . HOH   I 5 .   ? 0.448  -1.286  16.652 1.00 18.81  ? 418 HOH   A O   1 
HETATM 2341 O  O   . HOH   I 5 .   ? 19.538 -0.485  33.274 1.00 36.84  ? 419 HOH   A O   1 
HETATM 2342 O  O   . HOH   I 5 .   ? 7.214  13.747  4.702  1.00 23.95  ? 420 HOH   A O   1 
HETATM 2343 O  O   . HOH   I 5 .   ? 23.203 19.128  6.279  1.00 20.54  ? 421 HOH   A O   1 
HETATM 2344 O  O   . HOH   I 5 .   ? 14.211 24.450  17.767 1.00 36.62  ? 422 HOH   A O   1 
HETATM 2345 O  O   . HOH   I 5 .   ? 34.057 7.785   16.643 1.00 35.41  ? 423 HOH   A O   1 
HETATM 2346 O  O   . HOH   I 5 .   ? 15.806 21.430  7.208  1.00 25.30  ? 424 HOH   A O   1 
HETATM 2347 O  O   . HOH   I 5 .   ? 4.013  9.043   27.527 1.00 38.69  ? 425 HOH   A O   1 
HETATM 2348 O  O   . HOH   I 5 .   ? 20.933 9.954   21.900 1.00 17.50  ? 426 HOH   A O   1 
HETATM 2349 O  O   . HOH   I 5 .   ? 22.723 3.433   20.835 1.00 20.47  ? 427 HOH   A O   1 
HETATM 2350 O  O   . HOH   I 5 .   ? 23.340 8.298   21.758 1.00 26.20  ? 428 HOH   A O   1 
HETATM 2351 O  O   . HOH   I 5 .   ? 1.388  7.778   27.058 1.00 43.20  ? 429 HOH   A O   1 
HETATM 2352 O  O   . HOH   I 5 .   ? 17.101 -2.479  19.661 1.00 18.65  ? 430 HOH   A O   1 
HETATM 2353 O  O   . HOH   I 5 .   ? 20.867 -4.741  11.462 1.00 29.37  ? 431 HOH   A O   1 
HETATM 2354 O  O   . HOH   I 5 .   ? 19.636 9.341   -0.906 1.00 26.93  ? 432 HOH   A O   1 
HETATM 2355 O  O   . HOH   I 5 .   ? 9.255  3.605   3.021  1.00 32.04  ? 433 HOH   A O   1 
HETATM 2356 O  O   . HOH   I 5 .   ? -0.785 15.724  11.567 1.00 32.95  ? 434 HOH   A O   1 
HETATM 2357 O  O   . HOH   I 5 .   ? 1.229  4.454   26.433 1.00 29.33  ? 435 HOH   A O   1 
HETATM 2358 O  O   . HOH   I 5 .   ? -1.457 -2.984  15.651 1.00 31.67  ? 436 HOH   A O   1 
HETATM 2359 O  O   . HOH   I 5 .   ? 8.635  21.121  7.484  1.00 56.26  ? 437 HOH   A O   1 
HETATM 2360 O  O   . HOH   I 5 .   ? 22.722 16.817  24.033 1.00 46.32  ? 438 HOH   A O   1 
HETATM 2361 O  O   . HOH   I 5 .   ? 10.400 16.110  30.475 1.00 49.74  ? 439 HOH   A O   1 
HETATM 2362 O  O   . HOH   I 5 .   ? 35.521 4.341   18.681 1.00 52.92  ? 440 HOH   A O   1 
HETATM 2363 O  O   . HOH   I 5 .   ? 31.834 7.107   5.384  1.00 32.01  ? 441 HOH   A O   1 
HETATM 2364 O  O   . HOH   I 5 .   ? 19.121 -3.358  33.815 1.00 42.28  ? 442 HOH   A O   1 
HETATM 2365 O  O   . HOH   I 5 .   ? 30.602 13.035  23.194 1.00 42.43  ? 443 HOH   A O   1 
HETATM 2366 O  O   . HOH   I 5 .   ? 18.478 2.214   22.631 1.00 37.32  ? 444 HOH   A O   1 
HETATM 2367 O  O   . HOH   I 5 .   ? 38.506 0.936   13.416 1.00 52.47  ? 445 HOH   A O   1 
HETATM 2368 O  O   . HOH   I 5 .   ? 16.877 -4.934  34.222 1.00 30.94  ? 446 HOH   A O   1 
HETATM 2369 O  O   . HOH   I 5 .   ? 23.601 6.490   23.355 1.00 43.70  ? 447 HOH   A O   1 
HETATM 2370 O  O   . HOH   I 5 .   ? 8.051  18.223  26.242 1.00 87.18  ? 448 HOH   A O   1 
HETATM 2371 O  O   . HOH   I 5 .   ? 18.545 3.185   26.063 1.00 43.59  ? 449 HOH   A O   1 
HETATM 2372 O  O   . HOH   I 5 .   ? 29.664 0.695   16.545 1.00 32.40  ? 450 HOH   A O   1 
HETATM 2373 O  O   . HOH   I 5 .   ? 10.730 17.212  25.847 1.00 37.06  ? 451 HOH   A O   1 
HETATM 2374 O  O   . HOH   I 5 .   ? 2.580  -0.054  26.254 1.00 33.55  ? 452 HOH   A O   1 
HETATM 2375 O  O   . HOH   I 5 .   ? 6.126  5.460   1.625  1.00 32.44  ? 453 HOH   A O   1 
HETATM 2376 O  O   . HOH   I 5 .   ? 23.781 1.037   19.805 1.00 31.41  ? 454 HOH   A O   1 
HETATM 2377 O  O   . HOH   I 5 .   ? 0.059  0.058   23.241 1.00 31.33  ? 455 HOH   A O   1 
HETATM 2378 O  O   . HOH   I 5 .   ? 2.284  8.448   2.087  1.00 46.99  ? 456 HOH   A O   1 
HETATM 2379 O  O   . HOH   I 5 .   ? 30.297 7.094   17.782 1.00 37.56  ? 457 HOH   A O   1 
HETATM 2380 O  O   . HOH   I 5 .   ? 37.690 -4.513  6.754  1.00 33.97  ? 458 HOH   A O   1 
HETATM 2381 O  O   . HOH   I 5 .   ? 12.484 -4.983  33.071 1.00 27.44  ? 459 HOH   A O   1 
HETATM 2382 O  O   . HOH   I 5 .   ? 21.048 11.476  24.530 1.00 34.50  ? 460 HOH   A O   1 
HETATM 2383 O  O   . HOH   I 5 .   ? 12.021 14.817  25.446 1.00 119.05 ? 461 HOH   A O   1 
HETATM 2384 O  O   . HOH   I 5 .   ? 31.207 4.564   17.066 1.00 26.36  ? 462 HOH   A O   1 
HETATM 2385 O  O   . HOH   I 5 .   ? 26.843 3.153   23.041 1.00 56.27  ? 463 HOH   A O   1 
HETATM 2386 O  O   . HOH   I 5 .   ? 2.409  -5.145  22.472 1.00 34.60  ? 464 HOH   A O   1 
HETATM 2387 O  O   . HOH   I 5 .   ? 21.294 -1.019  18.979 1.00 31.29  ? 465 HOH   A O   1 
HETATM 2388 O  O   . HOH   I 5 .   ? 32.297 11.274  6.488  1.00 35.74  ? 466 HOH   A O   1 
HETATM 2389 O  O   . HOH   I 5 .   ? 29.056 1.544   19.031 1.00 53.21  ? 467 HOH   A O   1 
HETATM 2390 O  O   . HOH   I 5 .   ? 26.672 0.273   19.757 1.00 47.62  ? 468 HOH   A O   1 
HETATM 2391 O  O   . HOH   J 5 .   ? 38.207 -25.971 28.354 1.00 33.21  ? 301 HOH   C O   1 
HETATM 2392 O  O   . HOH   J 5 .   ? 17.381 -33.281 24.141 1.00 42.73  ? 302 HOH   C O   1 
HETATM 2393 O  O   . HOH   J 5 .   ? 38.242 -7.340  7.106  1.00 22.60  ? 303 HOH   C O   1 
HETATM 2394 O  O   . HOH   J 5 .   ? 31.326 -17.820 -0.059 1.00 40.98  ? 304 HOH   C O   1 
HETATM 2395 O  O   . HOH   J 5 .   ? 32.115 -6.611  20.064 1.00 45.43  ? 305 HOH   C O   1 
HETATM 2396 O  O   . HOH   J 5 .   ? 38.744 -18.676 21.495 1.00 24.46  ? 306 HOH   C O   1 
HETATM 2397 O  O   . HOH   J 5 .   ? 14.551 -18.593 31.831 1.00 35.23  ? 307 HOH   C O   1 
HETATM 2398 O  O   . HOH   J 5 .   ? 17.761 -6.044  24.034 1.00 24.43  ? 308 HOH   C O   1 
HETATM 2399 O  O   . HOH   J 5 .   ? 43.286 -7.220  20.759 1.00 54.18  ? 309 HOH   C O   1 
HETATM 2400 O  O   . HOH   J 5 .   ? 24.391 -9.571  26.902 1.00 42.32  ? 310 HOH   C O   1 
HETATM 2401 O  O   . HOH   J 5 .   ? 22.824 -5.937  21.117 1.00 18.86  ? 311 HOH   C O   1 
HETATM 2402 O  O   . HOH   J 5 .   ? 30.671 -18.117 26.854 1.00 17.94  ? 312 HOH   C O   1 
HETATM 2403 O  O   . HOH   J 5 .   ? 14.699 -23.881 12.290 1.00 31.05  ? 313 HOH   C O   1 
HETATM 2404 O  O   . HOH   J 5 .   ? 19.688 -4.121  20.143 1.00 21.14  ? 314 HOH   C O   1 
HETATM 2405 O  O   . HOH   J 5 .   ? 17.807 -27.553 16.465 1.00 17.53  ? 315 HOH   C O   1 
HETATM 2406 O  O   . HOH   J 5 .   ? 30.872 -32.779 0.819  1.00 38.13  ? 316 HOH   C O   1 
HETATM 2407 O  O   . HOH   J 5 .   ? 20.655 -18.722 12.795 1.00 13.89  ? 317 HOH   C O   1 
HETATM 2408 O  O   . HOH   J 5 .   ? 10.196 -17.546 18.290 1.00 27.60  ? 318 HOH   C O   1 
HETATM 2409 O  O   . HOH   J 5 .   ? 14.630 -28.881 25.501 1.00 36.47  ? 319 HOH   C O   1 
HETATM 2410 O  O   . HOH   J 5 .   ? 24.531 -5.864  15.146 1.00 31.60  ? 320 HOH   C O   1 
HETATM 2411 O  O   . HOH   J 5 .   ? 37.272 -31.981 10.946 1.00 25.20  ? 321 HOH   C O   1 
HETATM 2412 O  O   . HOH   J 5 .   ? 24.762 -15.702 7.350  1.00 18.14  ? 322 HOH   C O   1 
HETATM 2413 O  O   . HOH   J 5 .   ? 21.965 -28.600 4.767  1.00 26.52  ? 323 HOH   C O   1 
HETATM 2414 O  O   . HOH   J 5 .   ? 37.121 -18.725 28.151 1.00 28.14  ? 324 HOH   C O   1 
HETATM 2415 O  O   . HOH   J 5 .   ? 36.066 -26.161 34.182 1.00 34.06  ? 325 HOH   C O   1 
HETATM 2416 O  O   . HOH   J 5 .   ? 28.112 -5.104  18.577 1.00 40.60  ? 326 HOH   C O   1 
HETATM 2417 O  O   . HOH   J 5 .   ? 18.566 -8.800  13.742 1.00 27.73  ? 327 HOH   C O   1 
HETATM 2418 O  O   . HOH   J 5 .   ? 36.292 -2.510  11.020 1.00 31.48  ? 328 HOH   C O   1 
HETATM 2419 O  O   . HOH   J 5 .   ? 21.321 -24.955 3.971  1.00 41.38  ? 329 HOH   C O   1 
HETATM 2420 O  O   . HOH   J 5 .   ? 18.636 -32.477 19.841 1.00 40.63  ? 330 HOH   C O   1 
HETATM 2421 O  O   . HOH   J 5 .   ? 40.399 -27.279 15.201 1.00 13.18  ? 331 HOH   C O   1 
HETATM 2422 O  O   . HOH   J 5 .   ? 27.022 -7.500  2.240  1.00 53.50  ? 332 HOH   C O   1 
HETATM 2423 O  O   . HOH   J 5 .   ? 25.969 -25.269 8.758  1.00 13.86  ? 333 HOH   C O   1 
HETATM 2424 O  O   . HOH   J 5 .   ? 16.544 -14.806 8.235  1.00 48.55  ? 334 HOH   C O   1 
HETATM 2425 O  O   . HOH   J 5 .   ? 37.090 -10.533 4.850  1.00 39.80  ? 335 HOH   C O   1 
HETATM 2426 O  O   . HOH   J 5 .   ? 23.862 -8.127  9.476  1.00 24.64  ? 336 HOH   C O   1 
HETATM 2427 O  O   . HOH   J 5 .   ? 35.890 -28.475 2.844  1.00 39.16  ? 337 HOH   C O   1 
HETATM 2428 O  O   . HOH   J 5 .   ? 32.380 -23.694 29.087 1.00 16.05  ? 338 HOH   C O   1 
HETATM 2429 O  O   . HOH   J 5 .   ? 35.054 -32.833 3.331  1.00 38.43  ? 339 HOH   C O   1 
HETATM 2430 O  O   . HOH   J 5 .   ? 40.034 -29.615 11.893 1.00 22.41  ? 340 HOH   C O   1 
HETATM 2431 O  O   . HOH   J 5 .   ? 29.829 -15.254 19.551 1.00 15.76  ? 341 HOH   C O   1 
HETATM 2432 O  O   . HOH   J 5 .   ? 26.489 -5.445  9.991  1.00 22.87  ? 342 HOH   C O   1 
HETATM 2433 O  O   . HOH   J 5 .   ? 13.224 -11.229 28.477 1.00 38.52  ? 343 HOH   C O   1 
HETATM 2434 O  O   . HOH   J 5 .   ? 13.806 -24.371 29.276 1.00 30.37  ? 344 HOH   C O   1 
HETATM 2435 O  O   . HOH   J 5 .   ? 17.480 -24.015 8.575  1.00 37.25  ? 345 HOH   C O   1 
HETATM 2436 O  O   . HOH   J 5 .   ? 30.882 -21.502 28.366 1.00 16.79  ? 346 HOH   C O   1 
HETATM 2437 O  O   . HOH   J 5 .   ? 41.329 -24.977 7.241  1.00 29.77  ? 347 HOH   C O   1 
HETATM 2438 O  O   . HOH   J 5 .   ? 9.819  -8.870  23.916 1.00 28.53  ? 348 HOH   C O   1 
HETATM 2439 O  O   . HOH   J 5 .   ? 6.700  -9.208  22.588 1.00 36.54  ? 349 HOH   C O   1 
HETATM 2440 O  O   . HOH   J 5 .   ? 21.692 -26.172 34.351 1.00 28.01  ? 350 HOH   C O   1 
HETATM 2441 O  O   . HOH   J 5 .   ? 30.992 -23.795 -1.295 1.00 22.85  ? 351 HOH   C O   1 
HETATM 2442 O  O   . HOH   J 5 .   ? 19.110 -27.675 28.138 1.00 18.24  ? 352 HOH   C O   1 
HETATM 2443 O  O   . HOH   J 5 .   ? 36.231 -21.336 6.887  1.00 23.39  ? 353 HOH   C O   1 
HETATM 2444 O  O   . HOH   J 5 .   ? 26.145 -15.179 30.675 1.00 35.40  ? 354 HOH   C O   1 
HETATM 2445 O  O   . HOH   J 5 .   ? 33.457 -32.924 0.887  1.00 43.35  ? 355 HOH   C O   1 
HETATM 2446 O  O   . HOH   J 5 .   ? 20.700 -25.693 13.802 1.00 20.95  ? 356 HOH   C O   1 
HETATM 2447 O  O   . HOH   J 5 .   ? 11.826 -24.276 21.639 1.00 17.48  ? 357 HOH   C O   1 
HETATM 2448 O  O   . HOH   J 5 .   ? 35.089 -13.131 8.713  1.00 19.84  ? 358 HOH   C O   1 
HETATM 2449 O  O   . HOH   J 5 .   ? 9.124  -8.028  21.274 1.00 25.57  ? 359 HOH   C O   1 
HETATM 2450 O  O   . HOH   J 5 .   ? 7.256  -30.468 22.091 1.00 42.23  ? 360 HOH   C O   1 
HETATM 2451 O  O   . HOH   J 5 .   ? 21.917 -21.360 4.407  1.00 52.50  ? 361 HOH   C O   1 
HETATM 2452 O  O   . HOH   J 5 .   ? 26.935 -35.580 20.794 1.00 26.55  ? 362 HOH   C O   1 
HETATM 2453 O  O   . HOH   J 5 .   ? 29.684 -13.055 12.997 1.00 16.23  ? 363 HOH   C O   1 
HETATM 2454 O  O   . HOH   J 5 .   ? 10.589 -16.914 12.392 1.00 32.76  ? 364 HOH   C O   1 
HETATM 2455 O  O   . HOH   J 5 .   ? 31.937 -10.409 13.755 1.00 19.45  ? 365 HOH   C O   1 
HETATM 2456 O  O   . HOH   J 5 .   ? 23.720 -3.395  19.037 1.00 34.16  ? 366 HOH   C O   1 
HETATM 2457 O  O   . HOH   J 5 .   ? 36.481 -16.156 12.398 1.00 32.62  ? 367 HOH   C O   1 
HETATM 2458 O  O   . HOH   J 5 .   ? 29.644 -31.342 32.665 1.00 24.85  ? 368 HOH   C O   1 
HETATM 2459 O  O   . HOH   J 5 .   ? 34.750 -34.938 18.075 1.00 28.62  ? 369 HOH   C O   1 
HETATM 2460 O  O   . HOH   J 5 .   ? 14.674 -18.411 10.457 1.00 36.06  ? 370 HOH   C O   1 
HETATM 2461 O  O   . HOH   J 5 .   ? 34.040 -33.637 24.134 1.00 32.92  ? 371 HOH   C O   1 
HETATM 2462 O  O   . HOH   J 5 .   ? 25.682 -37.861 24.258 1.00 33.91  ? 372 HOH   C O   1 
HETATM 2463 O  O   . HOH   J 5 .   ? 22.833 -8.518  14.030 1.00 16.17  ? 373 HOH   C O   1 
HETATM 2464 O  O   . HOH   J 5 .   ? 10.380 -16.935 14.976 1.00 29.65  ? 374 HOH   C O   1 
HETATM 2465 O  O   . HOH   J 5 .   ? 31.044 -6.023  5.823  1.00 42.24  ? 375 HOH   C O   1 
HETATM 2466 O  O   . HOH   J 5 .   ? 23.418 -33.574 29.049 1.00 28.78  ? 376 HOH   C O   1 
HETATM 2467 O  O   . HOH   J 5 .   ? 13.054 -29.490 19.044 1.00 33.77  ? 377 HOH   C O   1 
HETATM 2468 O  O   . HOH   J 5 .   ? 23.151 -25.359 8.858  1.00 18.79  ? 378 HOH   C O   1 
HETATM 2469 O  O   . HOH   J 5 .   ? 22.195 -23.751 6.157  1.00 32.85  ? 379 HOH   C O   1 
HETATM 2470 O  O   . HOH   J 5 .   ? 32.885 -9.810  11.128 1.00 15.05  ? 380 HOH   C O   1 
HETATM 2471 O  O   . HOH   J 5 .   ? 37.534 -31.469 25.754 1.00 27.35  ? 381 HOH   C O   1 
HETATM 2472 O  O   . HOH   J 5 .   ? 28.876 -36.244 7.845  1.00 21.47  ? 382 HOH   C O   1 
HETATM 2473 O  O   . HOH   J 5 .   ? 22.701 -7.584  25.527 1.00 46.34  ? 383 HOH   C O   1 
HETATM 2474 O  O   . HOH   J 5 .   ? 30.217 -18.148 8.384  1.00 23.85  ? 384 HOH   C O   1 
HETATM 2475 O  O   . HOH   J 5 .   ? 32.051 -34.591 24.819 1.00 30.28  ? 385 HOH   C O   1 
HETATM 2476 O  O   . HOH   J 5 .   ? 28.016 -16.356 22.064 1.00 13.03  ? 386 HOH   C O   1 
HETATM 2477 O  O   . HOH   J 5 .   ? 31.475 -13.373 4.192  1.00 32.73  ? 387 HOH   C O   1 
HETATM 2478 O  O   . HOH   J 5 .   ? 4.179  -10.425 19.578 1.00 29.02  ? 388 HOH   C O   1 
HETATM 2479 O  O   . HOH   J 5 .   ? 22.796 -28.091 12.624 1.00 20.46  ? 389 HOH   C O   1 
HETATM 2480 O  O   . HOH   J 5 .   ? 38.581 -13.473 10.833 1.00 36.19  ? 390 HOH   C O   1 
HETATM 2481 O  O   . HOH   J 5 .   ? 8.730  -13.310 10.752 1.00 23.83  ? 391 HOH   C O   1 
HETATM 2482 O  O   . HOH   J 5 .   ? 3.804  -8.257  14.698 1.00 25.70  ? 392 HOH   C O   1 
HETATM 2483 O  O   . HOH   J 5 .   ? 31.043 -35.690 31.766 1.00 40.03  ? 393 HOH   C O   1 
HETATM 2484 O  O   . HOH   J 5 .   ? 22.442 -13.876 29.849 1.00 34.59  ? 394 HOH   C O   1 
HETATM 2485 O  O   . HOH   J 5 .   ? 37.781 -23.555 4.385  1.00 37.83  ? 395 HOH   C O   1 
HETATM 2486 O  O   . HOH   J 5 .   ? 5.786  -16.939 22.192 1.00 50.56  ? 396 HOH   C O   1 
HETATM 2487 O  O   . HOH   J 5 .   ? 11.366 -22.547 28.652 1.00 27.81  ? 397 HOH   C O   1 
HETATM 2488 O  O   . HOH   J 5 .   ? 43.145 -25.417 23.775 1.00 23.28  ? 398 HOH   C O   1 
HETATM 2489 O  O   . HOH   J 5 .   ? 26.977 -19.132 1.656  1.00 21.76  ? 399 HOH   C O   1 
HETATM 2490 O  O   . HOH   J 5 .   ? 29.984 -15.880 30.337 1.00 33.65  ? 400 HOH   C O   1 
HETATM 2491 O  O   . HOH   J 5 .   ? 35.480 -24.649 24.685 1.00 18.19  ? 401 HOH   C O   1 
HETATM 2492 O  O   . HOH   J 5 .   ? 10.667 -11.958 8.998  1.00 29.05  ? 402 HOH   C O   1 
HETATM 2493 O  O   . HOH   J 5 .   ? 9.944  -24.835 19.743 1.00 22.26  ? 403 HOH   C O   1 
HETATM 2494 O  O   . HOH   J 5 .   ? 10.922 -6.400  13.176 1.00 24.37  ? 404 HOH   C O   1 
HETATM 2495 O  O   . HOH   J 5 .   ? 31.177 -12.158 10.691 1.00 15.20  ? 405 HOH   C O   1 
HETATM 2496 O  O   . HOH   J 5 .   ? 25.907 -31.008 30.842 1.00 17.61  ? 406 HOH   C O   1 
HETATM 2497 O  O   . HOH   J 5 .   ? 26.620 -12.022 27.532 1.00 26.99  ? 407 HOH   C O   1 
HETATM 2498 O  O   . HOH   J 5 .   ? 34.248 -13.492 25.520 1.00 19.46  ? 408 HOH   C O   1 
HETATM 2499 O  O   . HOH   J 5 .   ? 36.876 -29.282 10.110 1.00 20.77  ? 409 HOH   C O   1 
HETATM 2500 O  O   . HOH   J 5 .   ? 29.916 -10.427 27.701 1.00 42.80  ? 410 HOH   C O   1 
HETATM 2501 O  O   . HOH   J 5 .   ? 21.637 -18.914 5.865  1.00 25.50  ? 411 HOH   C O   1 
HETATM 2502 O  O   . HOH   J 5 .   ? 9.683  -18.476 26.626 1.00 30.60  ? 412 HOH   C O   1 
HETATM 2503 O  O   . HOH   J 5 .   ? 26.298 -31.257 14.820 1.00 19.84  ? 413 HOH   C O   1 
HETATM 2504 O  O   . HOH   J 5 .   ? 24.421 -13.825 5.490  1.00 39.05  ? 414 HOH   C O   1 
HETATM 2505 O  O   . HOH   J 5 .   ? 38.815 -13.055 25.747 1.00 28.02  ? 415 HOH   C O   1 
HETATM 2506 O  O   . HOH   J 5 .   ? 5.667  -12.652 23.204 1.00 48.75  ? 416 HOH   C O   1 
HETATM 2507 O  O   . HOH   J 5 .   ? 26.476 -6.062  22.101 1.00 30.73  ? 417 HOH   C O   1 
HETATM 2508 O  O   . HOH   J 5 .   ? 32.893 -30.323 31.671 1.00 20.50  ? 418 HOH   C O   1 
HETATM 2509 O  O   . HOH   J 5 .   ? 41.610 -12.371 18.005 1.00 29.60  ? 419 HOH   C O   1 
HETATM 2510 O  O   . HOH   J 5 .   ? 4.606  -28.044 23.190 1.00 34.85  ? 420 HOH   C O   1 
HETATM 2511 O  O   . HOH   J 5 .   ? 37.693 -20.426 4.808  1.00 34.74  ? 421 HOH   C O   1 
HETATM 2512 O  O   . HOH   J 5 .   ? 35.647 -28.590 7.732  1.00 18.12  ? 422 HOH   C O   1 
HETATM 2513 O  O   . HOH   J 5 .   ? 20.217 -32.238 22.271 1.00 30.28  ? 423 HOH   C O   1 
HETATM 2514 O  O   . HOH   J 5 .   ? 17.141 -25.315 12.695 1.00 25.35  ? 424 HOH   C O   1 
HETATM 2515 O  O   . HOH   J 5 .   ? 35.058 -4.100  17.697 1.00 29.41  ? 425 HOH   C O   1 
HETATM 2516 O  O   . HOH   J 5 .   ? 3.952  -12.806 17.120 1.00 37.30  ? 426 HOH   C O   1 
HETATM 2517 O  O   . HOH   J 5 .   ? 22.966 -33.442 5.355  1.00 34.50  ? 427 HOH   C O   1 
HETATM 2518 O  O   . HOH   J 5 .   ? 38.641 -16.807 3.428  1.00 40.76  ? 428 HOH   C O   1 
HETATM 2519 O  O   . HOH   J 5 .   ? 23.273 -31.018 13.328 1.00 32.85  ? 429 HOH   C O   1 
HETATM 2520 O  O   . HOH   J 5 .   ? 18.529 -8.334  25.529 1.00 19.55  ? 430 HOH   C O   1 
HETATM 2521 O  O   . HOH   J 5 .   ? 39.926 -29.932 14.596 1.00 18.05  ? 431 HOH   C O   1 
HETATM 2522 O  O   . HOH   J 5 .   ? 32.696 -14.339 9.393  1.00 15.74  ? 432 HOH   C O   1 
HETATM 2523 O  O   . HOH   J 5 .   ? 18.757 -19.130 10.790 1.00 18.52  ? 433 HOH   C O   1 
HETATM 2524 O  O   . HOH   J 5 .   ? 33.896 -15.608 27.037 1.00 30.94  ? 434 HOH   C O   1 
HETATM 2525 O  O   . HOH   J 5 .   ? 6.409  -20.065 18.155 1.00 36.06  ? 435 HOH   C O   1 
HETATM 2526 O  O   . HOH   J 5 .   ? 20.329 -23.714 34.817 1.00 30.17  ? 436 HOH   C O   1 
HETATM 2527 O  O   . HOH   J 5 .   ? 38.818 -14.675 13.443 1.00 35.59  ? 437 HOH   C O   1 
HETATM 2528 O  O   . HOH   J 5 .   ? 8.403  -12.862 24.440 1.00 54.50  ? 438 HOH   C O   1 
HETATM 2529 O  O   . HOH   J 5 .   ? 6.431  -22.889 18.250 1.00 34.71  ? 439 HOH   C O   1 
HETATM 2530 O  O   . HOH   J 5 .   ? 15.040 -30.114 18.044 1.00 39.17  ? 440 HOH   C O   1 
HETATM 2531 O  O   . HOH   J 5 .   ? 4.336  -16.096 17.265 1.00 52.95  ? 441 HOH   C O   1 
HETATM 2532 O  O   . HOH   J 5 .   ? 16.385 -20.571 11.509 1.00 25.84  ? 442 HOH   C O   1 
HETATM 2533 O  O   . HOH   J 5 .   ? 9.654  -24.641 29.285 1.00 42.42  ? 443 HOH   C O   1 
HETATM 2534 O  O   . HOH   J 5 .   ? 34.673 -23.213 -0.939 1.00 40.54  ? 444 HOH   C O   1 
HETATM 2535 O  O   . HOH   J 5 .   ? 33.641 -36.206 8.779  1.00 44.78  ? 445 HOH   C O   1 
HETATM 2536 O  O   . HOH   J 5 .   ? 6.617  -17.156 18.413 1.00 43.50  ? 446 HOH   C O   1 
HETATM 2537 O  O   . HOH   J 5 .   ? 35.146 -13.547 6.149  1.00 33.85  ? 447 HOH   C O   1 
HETATM 2538 O  O   . HOH   J 5 .   ? 31.441 -15.698 7.186  1.00 26.98  ? 448 HOH   C O   1 
HETATM 2539 O  O   . HOH   J 5 .   ? 24.225 -16.467 3.190  1.00 39.40  ? 449 HOH   C O   1 
HETATM 2540 O  O   . HOH   J 5 .   ? 37.161 -14.458 9.623  1.00 36.62  ? 450 HOH   C O   1 
HETATM 2541 O  O   . HOH   J 5 .   ? 20.266 -19.457 35.911 1.00 35.18  ? 451 HOH   C O   1 
HETATM 2542 O  O   . HOH   J 5 .   ? 34.471 -30.257 33.854 1.00 37.49  ? 452 HOH   C O   1 
HETATM 2543 O  O   . HOH   J 5 .   ? 33.662 -20.570 -2.097 1.00 39.97  ? 453 HOH   C O   1 
HETATM 2544 O  O   . HOH   J 5 .   ? 23.761 -15.699 31.437 1.00 35.57  ? 454 HOH   C O   1 
HETATM 2545 O  O   . HOH   J 5 .   ? 36.558 -24.483 27.211 1.00 33.17  ? 455 HOH   C O   1 
HETATM 2546 O  O   . HOH   J 5 .   ? 34.113 -31.885 29.540 1.00 25.45  ? 456 HOH   C O   1 
HETATM 2547 O  O   . HOH   J 5 .   ? 26.114 -35.437 7.457  1.00 26.57  ? 457 HOH   C O   1 
HETATM 2548 O  O   . HOH   J 5 .   ? 11.551 -19.407 11.441 1.00 56.35  ? 458 HOH   C O   1 
HETATM 2549 O  O   . HOH   J 5 .   ? 8.867  -19.256 16.834 1.00 38.71  ? 459 HOH   C O   1 
HETATM 2550 O  O   . HOH   J 5 .   ? 10.061 -20.174 28.887 1.00 35.68  ? 460 HOH   C O   1 
HETATM 2551 O  O   . HOH   J 5 .   ? 22.888 -16.582 5.407  1.00 36.40  ? 461 HOH   C O   1 
HETATM 2552 O  O   . HOH   J 5 .   ? 38.703 -8.626  4.836  1.00 46.95  ? 462 HOH   C O   1 
HETATM 2553 O  O   . HOH   J 5 .   ? 6.722  -18.794 26.435 1.00 54.00  ? 463 HOH   C O   1 
HETATM 2554 O  O   . HOH   J 5 .   ? 12.943 -26.716 29.971 1.00 52.80  ? 464 HOH   C O   1 
HETATM 2555 O  O   . HOH   J 5 .   ? 16.321 -27.568 14.116 1.00 31.43  ? 465 HOH   C O   1 
HETATM 2556 O  O   . HOH   J 5 .   ? 10.653 -27.420 18.097 1.00 43.96  ? 466 HOH   C O   1 
HETATM 2557 O  O   . HOH   J 5 .   ? 36.682 -23.413 31.736 1.00 44.91  ? 467 HOH   C O   1 
HETATM 2558 O  O   . HOH   J 5 .   ? 6.126  -12.540 10.808 1.00 38.84  ? 468 HOH   C O   1 
HETATM 2559 O  O   . HOH   J 5 .   ? 22.156 -3.017  20.635 1.00 47.03  ? 469 HOH   C O   1 
HETATM 2560 O  O   . HOH   J 5 .   ? 18.533 -26.159 10.226 1.00 37.95  ? 470 HOH   C O   1 
HETATM 2561 O  O   . HOH   J 5 .   ? 41.439 -15.240 13.781 1.00 41.17  ? 471 HOH   C O   1 
HETATM 2562 O  O   . HOH   J 5 .   ? 31.872 -32.133 33.064 1.00 31.30  ? 472 HOH   C O   1 
HETATM 2563 O  O   . HOH   J 5 .   ? 32.469 -19.338 29.049 1.00 29.40  ? 473 HOH   C O   1 
HETATM 2564 O  O   . HOH   J 5 .   ? 9.985  -21.368 16.269 1.00 34.39  ? 474 HOH   C O   1 
HETATM 2565 O  O   . HOH   J 5 .   ? 18.077 -17.888 8.284  1.00 41.63  ? 475 HOH   C O   1 
HETATM 2566 O  O   . HOH   J 5 .   ? 29.122 -15.961 32.798 1.00 39.32  ? 476 HOH   C O   1 
HETATM 2567 O  O   . HOH   J 5 .   ? 5.603  -10.341 9.360  1.00 56.23  ? 477 HOH   C O   1 
HETATM 2568 O  O   . HOH   J 5 .   ? 16.789 -28.873 28.808 1.00 36.32  ? 478 HOH   C O   1 
HETATM 2569 O  O   . HOH   J 5 .   ? 18.377 -16.387 38.286 1.00 32.45  ? 479 HOH   C O   1 
HETATM 2570 O  O   . HOH   J 5 .   ? 22.696 -11.817 5.930  1.00 39.99  ? 480 HOH   C O   1 
HETATM 2571 O  O   . HOH   J 5 .   ? 35.236 -20.204 29.426 1.00 42.06  ? 481 HOH   C O   1 
HETATM 2572 O  O   . HOH   J 5 .   ? 8.899  -23.530 17.608 1.00 32.84  ? 482 HOH   C O   1 
HETATM 2573 O  O   . HOH   J 5 .   ? 35.128 -23.022 29.016 1.00 26.96  ? 483 HOH   C O   1 
HETATM 2574 O  O   . HOH   J 5 .   ? 39.197 -2.646  10.799 1.00 35.98  ? 484 HOH   C O   1 
HETATM 2575 O  O   . HOH   J 5 .   ? 19.225 -17.604 5.816  1.00 37.93  ? 485 HOH   C O   1 
HETATM 2576 O  O   . HOH   J 5 .   ? 39.447 -11.509 4.634  1.00 51.65  ? 486 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   ? 0.2303 0.2080 0.1994 -0.0097 -0.0039 -0.0133 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2234 0.2023 0.1985 -0.0087 -0.0075 -0.0101 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2122 0.1955 0.1968 -0.0031 -0.0107 -0.0045 7   SER   A C   
4    O O   . SER   A 1   ? 0.2155 0.2015 0.2009 -0.0016 -0.0112 -0.0026 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2654 0.2490 0.2355 -0.0174 -0.0119 -0.0084 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2965 0.2883 0.2665 -0.0201 -0.0169 -0.0026 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1933 0.1767 0.1848 -0.0006 -0.0119 -0.0026 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1760 0.1624 0.1766 0.0036  -0.0133 0.0014  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1689 0.1530 0.1750 0.0070  -0.0114 0.0005  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1847 0.1646 0.1881 0.0077  -0.0089 -0.0026 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1537 0.1402 0.1678 0.0088  -0.0121 0.0034  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1589 0.1441 0.1777 0.0107  -0.0101 0.0024  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1528 0.1391 0.1781 0.0127  -0.0079 0.0033  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1647 0.1523 0.1934 0.0130  -0.0082 0.0057  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1797 0.1666 0.2019 0.0084  -0.0124 0.0041  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1434 0.1289 0.1704 0.0134  -0.0052 0.0015  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1439 0.1298 0.1768 0.0135  -0.0015 0.0008  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1550 0.1416 0.1958 0.0134  -0.0010 0.0019  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1524 0.1393 0.1916 0.0126  -0.0022 0.0014  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1456 0.1319 0.1739 0.0124  0.0014  -0.0020 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1664 0.1538 0.1880 0.0128  0.0004  -0.0020 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1666 0.1525 0.1988 0.0103  0.0065  -0.0042 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1685 0.1594 0.1865 0.0112  0.0018  -0.0023 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1426 0.1296 0.1933 0.0142  0.0014  0.0037  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1535 0.1423 0.2146 0.0145  0.0030  0.0052  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1501 0.1361 0.2160 0.0139  0.0106  0.0014  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1536 0.1371 0.2269 0.0149  0.0150  0.0018  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1648 0.1575 0.2364 0.0160  0.0000  0.0121  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1497 0.1462 0.2147 0.0140  -0.0071 0.0151  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1637 0.1633 0.2280 0.0119  -0.0101 0.0157  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1704 0.1672 0.2290 0.0132  -0.0103 0.0167  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1662 0.1681 0.2223 0.0082  -0.0154 0.0169  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1842 0.1840 0.2349 0.0097  -0.0157 0.0181  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1795 0.1813 0.2283 0.0069  -0.0178 0.0176  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2238 0.2274 0.2633 0.0018  -0.0219 0.0176  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1580 0.1439 0.2195 0.0115  0.0129  -0.0026 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1613 0.1453 0.2247 0.0086  0.0207  -0.0075 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1739 0.1596 0.2433 0.0077  0.0230  -0.0082 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1599 0.1483 0.2244 0.0070  0.0184  -0.0071 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1818 0.1660 0.2318 0.0042  0.0216  -0.0116 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1995 0.1871 0.2412 0.0038  0.0158  -0.0098 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2053 0.1885 0.2551 -0.0013 0.0300  -0.0173 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1835 0.1676 0.2649 0.0078  0.0305  -0.0098 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1783 0.1649 0.2668 0.0070  0.0333  -0.0104 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1731 0.1649 0.2667 0.0099  0.0257  -0.0039 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1751 0.1688 0.2743 0.0133  0.0211  0.0018  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1670 0.1614 0.2555 0.0075  0.0233  -0.0047 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1620 0.1608 0.2517 0.0084  0.0160  0.0003  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1561 0.1529 0.2306 0.0068  0.0099  -0.0002 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1548 0.1531 0.2262 0.0052  0.0061  0.0010  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1773 0.1804 0.2753 0.0070  0.0180  0.0007  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2295 0.2361 0.3471 0.0100  0.0232  0.0038  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2531 0.2660 0.3813 0.0123  0.0188  0.0111  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2059 0.2090 0.3291 0.0095  0.0328  -0.0010 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1406 0.1343 0.2074 0.0075  0.0090  -0.0013 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1511 0.1426 0.2059 0.0071  0.0045  -0.0013 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1418 0.1324 0.1943 0.0091  0.0008  0.0008  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1519 0.1426 0.2085 0.0107  0.0025  0.0013  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1615 0.1518 0.2083 0.0052  0.0071  -0.0042 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1657 0.1578 0.2119 0.0015  0.0103  -0.0061 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1770 0.1694 0.2223 0.0003  0.0081  -0.0046 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1955 0.1887 0.2415 -0.0020 0.0162  -0.0097 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1946 0.1893 0.2392 -0.0037 0.0109  -0.0059 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2062 0.2020 0.2497 -0.0070 0.0193  -0.0116 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2140 0.2108 0.2570 -0.0075 0.0163  -0.0093 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2676 0.2674 0.3084 -0.0129 0.0192  -0.0107 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1372 0.1263 0.1826 0.0086  -0.0032 0.0014  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1339 0.1216 0.1740 0.0092  -0.0060 0.0022  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1438 0.1276 0.1753 0.0097  -0.0053 0.0002  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1512 0.1324 0.1799 0.0087  -0.0054 -0.0004 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1442 0.1340 0.1841 0.0067  -0.0102 0.0045  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1666 0.1544 0.1982 0.0053  -0.0124 0.0040  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1804 0.1723 0.2109 0.0003  -0.0165 0.0063  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1935 0.1804 0.2126 -0.0035 -0.0166 0.0027  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2094 0.1963 0.2220 -0.0058 -0.0176 0.0022  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2167 0.2084 0.2329 -0.0041 -0.0194 0.0058  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2115 0.1927 0.2140 -0.0099 -0.0157 -0.0024 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1395 0.1231 0.1682 0.0112  -0.0043 -0.0004 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1414 0.1231 0.1645 0.0123  -0.0035 -0.0008 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1492 0.1285 0.1680 0.0130  -0.0045 -0.0012 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1531 0.1340 0.1717 0.0131  -0.0054 -0.0010 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1495 0.1346 0.1723 0.0124  -0.0014 -0.0008 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1640 0.1501 0.1836 0.0134  -0.0011 0.0010  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1622 0.1498 0.1881 0.0099  0.0009  -0.0017 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1463 0.1213 0.1620 0.0129  -0.0038 -0.0020 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1516 0.1232 0.1625 0.0124  -0.0032 -0.0038 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1771 0.1487 0.1879 0.0123  -0.0033 -0.0038 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1593 0.1270 0.1697 0.0150  0.0004  -0.0040 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1718 0.1394 0.1859 0.0169  0.0017  -0.0016 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1452 0.1139 0.1524 0.0079  -0.0045 -0.0058 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2245 0.1938 0.2325 0.0078  -0.0049 -0.0054 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1557 0.1305 0.1648 0.0054  -0.0086 -0.0036 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2397 0.2056 0.2406 0.0047  -0.0038 -0.0084 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1163 0.0805 0.1242 0.0067  -0.0031 -0.0065 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2539 0.2293 0.2659 0.0059  -0.0087 -0.0029 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1618 0.1267 0.1688 0.0152  0.0027  -0.0061 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1677 0.1278 0.1768 0.0182  0.0077  -0.0061 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1774 0.1292 0.1862 0.0164  0.0103  -0.0080 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1854 0.1340 0.1885 0.0112  0.0095  -0.0118 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1694 0.1268 0.1745 0.0176  0.0110  -0.0095 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1808 0.1457 0.1857 0.0190  0.0089  -0.0079 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1833 0.1513 0.1838 0.0158  0.0053  -0.0088 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1742 0.1430 0.1848 0.0233  0.0108  -0.0044 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1677 0.1170 0.1829 0.0198  0.0132  -0.0046 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1848 0.1248 0.2003 0.0181  0.0166  -0.0062 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2064 0.1364 0.2162 0.0144  0.0220  -0.0130 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2167 0.1411 0.2210 0.0087  0.0226  -0.0170 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1919 0.1307 0.2169 0.0231  0.0197  0.0000  20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1998 0.1292 0.2261 0.0213  0.0227  -0.0004 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2175 0.1461 0.2550 0.0267  0.0260  0.0076  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.2261 0.1458 0.2661 0.0253  0.0288  0.0086  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2503 0.1557 0.2922 0.0251  0.0368  0.0053  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2558 0.1537 0.2953 0.0249  0.0430  -0.0012 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2686 0.1662 0.3140 0.0241  0.0395  0.0076  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1978 0.1265 0.2078 0.0165  0.0263  -0.0147 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2302 0.1485 0.2342 0.0121  0.0334  -0.0222 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2398 0.1604 0.2312 0.0031  0.0295  -0.0277 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2616 0.1741 0.2451 -0.0036 0.0349  -0.0347 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2431 0.1591 0.2525 0.0170  0.0406  -0.0227 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2362 0.1616 0.2420 0.0170  0.0369  -0.0226 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2248 0.1614 0.2368 0.0225  0.0318  -0.0157 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2465 0.1712 0.2430 0.0118  0.0386  -0.0286 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2293 0.1710 0.2361 0.0208  0.0303  -0.0177 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2464 0.1816 0.2441 0.0146  0.0341  -0.0250 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2366 0.1683 0.2264 0.0024  0.0208  -0.0242 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2283 0.1654 0.2092 -0.0055 0.0156  -0.0261 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2467 0.1877 0.2280 -0.0089 0.0099  -0.0237 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2527 0.2007 0.2297 -0.0148 0.0046  -0.0228 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2211 0.1676 0.2018 -0.0039 0.0110  -0.0232 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2356 0.1794 0.2149 -0.0019 0.0165  -0.0259 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2414 0.1946 0.2199 -0.0011 0.0114  -0.0227 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2638 0.1997 0.2330 -0.0100 0.0229  -0.0338 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2282 0.1661 0.2160 -0.0051 0.0107  -0.0214 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2261 0.1684 0.2153 -0.0081 0.0059  -0.0192 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2494 0.1893 0.2301 -0.0181 0.0059  -0.0233 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2563 0.1859 0.2308 -0.0222 0.0124  -0.0292 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2229 0.1615 0.2192 -0.0034 0.0077  -0.0165 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2298 0.1795 0.2109 -0.0223 -0.0007 -0.0200 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2342 0.1855 0.2073 -0.0334 -0.0022 -0.0225 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2504 0.1975 0.2251 -0.0357 -0.0011 -0.0232 24  THR   A C   
141  O O   . THR   A 18  ? 0.2203 0.1649 0.2030 -0.0284 -0.0001 -0.0207 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2536 0.2205 0.2289 -0.0370 -0.0107 -0.0162 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2448 0.2182 0.2318 -0.0314 -0.0143 -0.0105 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2662 0.2382 0.2409 -0.0347 -0.0127 -0.0141 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2587 0.2060 0.2251 -0.0470 -0.0015 -0.0262 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2594 0.2043 0.2272 -0.0501 -0.0011 -0.0264 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2346 0.1916 0.2142 -0.0450 -0.0077 -0.0187 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2326 0.1857 0.2177 -0.0409 -0.0060 -0.0178 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2726 0.2189 0.2288 -0.0651 -0.0015 -0.0304 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3785 0.3267 0.3370 -0.0694 -0.0032 -0.0290 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.4354 0.3689 0.3936 -0.0684 0.0036  -0.0332 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.4229 0.3866 0.3872 -0.0725 -0.0109 -0.0225 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.4370 0.3768 0.3974 -0.0732 0.0000  -0.0306 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.4554 0.4140 0.4204 -0.0752 -0.0087 -0.0239 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2243 0.1956 0.2088 -0.0445 -0.0142 -0.0129 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2213 0.2028 0.2185 -0.0394 -0.0184 -0.0062 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1993 0.1752 0.2037 -0.0285 -0.0152 -0.0060 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2019 0.1797 0.2134 -0.0258 -0.0151 -0.0040 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2434 0.2399 0.2470 -0.0400 -0.0248 0.0008  26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3342 0.3406 0.3528 -0.0354 -0.0274 0.0073  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3820 0.3941 0.4040 -0.0399 -0.0292 0.0092  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3548 0.3625 0.3829 -0.0265 -0.0265 0.0100  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1960 0.1658 0.1978 -0.0234 -0.0123 -0.0080 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1944 0.1604 0.2017 -0.0150 -0.0095 -0.0073 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1810 0.1386 0.1880 -0.0146 -0.0056 -0.0089 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1804 0.1403 0.1933 -0.0113 -0.0056 -0.0064 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1965 0.1581 0.2009 -0.0107 -0.0069 -0.0089 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2056 0.1749 0.2116 -0.0094 -0.0102 -0.0065 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1922 0.1695 0.2060 -0.0077 -0.0132 -0.0025 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.2011 0.1681 0.2012 -0.0105 -0.0092 -0.0086 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1894 0.1371 0.1894 -0.0187 -0.0018 -0.0130 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1927 0.1309 0.1933 -0.0184 0.0025  -0.0138 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.2021 0.1448 0.2048 -0.0228 -0.0002 -0.0123 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.2025 0.1423 0.2091 -0.0206 0.0015  -0.0103 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.2131 0.1379 0.2062 -0.0227 0.0088  -0.0195 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.2159 0.1340 0.2105 -0.0164 0.0138  -0.0201 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2342 0.1504 0.2236 -0.0176 0.0160  -0.0239 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2260 0.1394 0.2284 -0.0086 0.0174  -0.0162 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2343 0.1448 0.2288 -0.0102 0.0211  -0.0229 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2212 0.1306 0.2242 -0.0045 0.0217  -0.0174 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2404 0.1540 0.2496 -0.0053 0.0172  -0.0108 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2404 0.1467 0.2522 0.0032  0.0257  -0.0126 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2467 0.1579 0.2633 0.0017  0.0203  -0.0058 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2508 0.1583 0.2695 0.0060  0.0246  -0.0063 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1967 0.1482 0.1979 -0.0292 -0.0046 -0.0121 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.2028 0.1605 0.2074 -0.0335 -0.0071 -0.0102 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2068 0.1747 0.2221 -0.0280 -0.0098 -0.0054 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2186 0.1913 0.2385 -0.0301 -0.0107 -0.0037 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2200 0.1850 0.2199 -0.0430 -0.0109 -0.0107 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1910 0.1620 0.2104 -0.0213 -0.0100 -0.0038 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1905 0.1693 0.2194 -0.0166 -0.0106 -0.0007 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1783 0.1524 0.2066 -0.0108 -0.0076 -0.0010 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1791 0.1578 0.2118 -0.0070 -0.0074 0.0000  30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.2026 0.1917 0.2381 -0.0158 -0.0138 0.0024  30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2300 0.2275 0.2684 -0.0221 -0.0175 0.0050  30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2556 0.2592 0.3020 -0.0227 -0.0175 0.0071  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2320 0.2304 0.2631 -0.0280 -0.0204 0.0047  30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1838 0.1493 0.2075 -0.0105 -0.0050 -0.0019 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1691 0.1315 0.1925 -0.0057 -0.0028 -0.0007 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1804 0.1486 0.2078 -0.0045 -0.0022 0.0017  31  LEU   A C   
201  O O   . LEU   A 25  ? 0.2002 0.1699 0.2293 -0.0073 -0.0019 0.0025  31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1820 0.1337 0.2020 -0.0058 0.0004  -0.0008 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1921 0.1418 0.2139 -0.0007 0.0026  0.0025  31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1925 0.1433 0.2130 0.0026  0.0025  0.0012  31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2200 0.1592 0.2423 -0.0001 0.0067  0.0041  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1651 0.1369 0.1932 -0.0015 -0.0018 0.0025  32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1670 0.1444 0.1966 -0.0021 -0.0006 0.0041  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1750 0.1508 0.2025 -0.0006 0.0000  0.0082  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1977 0.1760 0.2252 -0.0029 0.0004  0.0115  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1537 0.1369 0.1856 -0.0013 0.0002  0.0022  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1888 0.1775 0.2195 -0.0040 0.0024  0.0029  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1732 0.1589 0.2108 -0.0021 0.0000  0.0003  32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1734 0.1466 0.1999 0.0031  0.0000  0.0089  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1767 0.1509 0.2041 0.0052  0.0007  0.0143  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1872 0.1557 0.2149 0.0095  0.0018  0.0137  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1717 0.1395 0.1972 0.0101  0.0013  0.0092  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1788 0.1635 0.2052 0.0034  0.0000  0.0161  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1950 0.1847 0.2229 0.0050  -0.0004 0.0227  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2231 0.2174 0.2535 0.0037  -0.0010 0.0306  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1908 0.1831 0.2191 0.0080  -0.0005 0.0233  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2435 0.2444 0.2767 0.0057  -0.0018 0.0368  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2145 0.2143 0.2460 0.0082  -0.0013 0.0319  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1964 0.1866 0.2228 0.0100  -0.0003 0.0182  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2226 0.2284 0.2557 0.0104  -0.0017 0.0350  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2073 0.2024 0.2340 0.0117  -0.0005 0.0205  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2205 0.2231 0.2509 0.0122  -0.0010 0.0286  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1897 0.1543 0.2211 0.0124  0.0039  0.0185  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1911 0.1506 0.2239 0.0166  0.0065  0.0177  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.2069 0.1695 0.2472 0.0205  0.0081  0.0262  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2097 0.1736 0.2543 0.0200  0.0081  0.0328  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.2160 0.1629 0.2467 0.0160  0.0099  0.0122  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2285 0.1674 0.2616 0.0147  0.0126  0.0142  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2552 0.1877 0.2968 0.0192  0.0177  0.0202  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2484 0.1774 0.2942 0.0187  0.0190  0.0251  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2314 0.1619 0.2766 0.0234  0.0211  0.0207  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1845 0.1486 0.2274 0.0243  0.0096  0.0272  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1760 0.1450 0.2286 0.0286  0.0113  0.0367  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1820 0.1449 0.2383 0.0334  0.0162  0.0344  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1889 0.1564 0.2411 0.0335  0.0149  0.0309  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1949 0.1806 0.2468 0.0261  0.0063  0.0426  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2335 0.2287 0.2960 0.0292  0.0064  0.0547  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2720 0.2625 0.3430 0.0351  0.0107  0.0571  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2807 0.2893 0.3432 0.0251  0.0023  0.0620  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1949 0.1465 0.2587 0.0370  0.0226  0.0358  36  SER   A N   
245  C CA  A SER   A 30  ? 0.2105 0.1545 0.2786 0.0412  0.0294  0.0328  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2207 0.1649 0.2882 0.0411  0.0292  0.0325  36  SER   A CA  
247  C C   . SER   A 30  ? 0.2110 0.1672 0.2879 0.0459  0.0290  0.0406  36  SER   A C   
248  O O   . SER   A 30  ? 0.2198 0.1757 0.2949 0.0472  0.0313  0.0358  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2231 0.1518 0.2993 0.0438  0.0380  0.0333  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2657 0.1935 0.3398 0.0432  0.0381  0.0313  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2310 0.1528 0.3145 0.0485  0.0464  0.0317  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3290 0.2596 0.4163 0.0470  0.0389  0.0433  36  SER   A OG  
253  N N   . SER   A 31  ? 0.2047 0.1735 0.2906 0.0474  0.0255  0.0530  37  SER   A N   
254  C CA  . SER   A 31  ? 0.1999 0.1831 0.2949 0.0508  0.0244  0.0618  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1951 0.1883 0.2791 0.0469  0.0192  0.0565  37  SER   A C   
256  O O   . SER   A 31  ? 0.2134 0.2145 0.3025 0.0495  0.0200  0.0597  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2245 0.2222 0.3300 0.0510  0.0204  0.0773  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.2919 0.3013 0.3866 0.0434  0.0123  0.0780  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1750 0.1667 0.2449 0.0409  0.0148  0.0481  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1702 0.1688 0.2301 0.0370  0.0108  0.0426  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1743 0.1617 0.2258 0.0366  0.0130  0.0312  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1676 0.1595 0.2121 0.0339  0.0103  0.0269  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1837 0.1889 0.2355 0.0303  0.0054  0.0420  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.1969 0.2171 0.2536 0.0278  0.0021  0.0532  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1871 0.2132 0.2348 0.0199  -0.0017 0.0512  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1609 0.1911 0.1997 0.0155  -0.0029 0.0444  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1892 0.2285 0.2211 0.0077  -0.0050 0.0437  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.1978 0.2452 0.2296 0.0026  -0.0069 0.0498  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1845 0.2254 0.2096 0.0041  -0.0047 0.0372  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1777 0.1513 0.2291 0.0379  0.0176  0.0262  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1688 0.1333 0.2110 0.0352  0.0188  0.0161  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1647 0.1317 0.1975 0.0300  0.0130  0.0119  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1722 0.1388 0.1984 0.0277  0.0116  0.0066  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1875 0.1526 0.2285 0.0367  0.0215  0.0129  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1956 0.1520 0.2267 0.0328  0.0230  0.0034  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2105 0.1566 0.2386 0.0303  0.0259  -0.0011 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.1952 0.1558 0.2210 0.0313  0.0212  0.0007  39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1611 0.1309 0.1944 0.0280  0.0101  0.0146  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1464 0.1188 0.1735 0.0237  0.0060  0.0111  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1619 0.1281 0.1878 0.0212  0.0059  0.0091  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1733 0.1362 0.2033 0.0221  0.0077  0.0126  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1564 0.1399 0.1842 0.0219  0.0031  0.0152  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1718 0.1632 0.1983 0.0219  0.0022  0.0158  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1860 0.1876 0.2111 0.0176  0.0002  0.0185  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.1819 0.1698 0.2035 0.0211  0.0018  0.0095  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1549 0.1206 0.1765 0.0180  0.0036  0.0046  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1572 0.1198 0.1779 0.0148  0.0027  0.0031  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1554 0.1238 0.1755 0.0125  -0.0003 0.0016  41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1591 0.1301 0.1780 0.0126  -0.0015 0.0000  41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1642 0.1176 0.1813 0.0127  0.0047  -0.0011 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1753 0.1261 0.1912 0.0083  0.0037  -0.0026 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.1932 0.1329 0.2063 0.0060  0.0080  -0.0057 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1734 0.1297 0.1873 0.0047  -0.0003 -0.0046 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1488 0.1196 0.1709 0.0103  -0.0010 0.0023  42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1383 0.1142 0.1626 0.0084  -0.0023 0.0011  42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1475 0.1221 0.1734 0.0057  -0.0032 0.0003  42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1543 0.1264 0.1799 0.0043  -0.0025 0.0011  42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1439 0.1256 0.1696 0.0074  -0.0010 0.0023  42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1653 0.1503 0.1950 0.0056  0.0000  0.0001  42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1598 0.1445 0.1835 0.0089  -0.0005 0.0034  42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1482 0.1254 0.1763 0.0046  -0.0050 -0.0005 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1483 0.1273 0.1794 0.0014  -0.0065 -0.0002 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1580 0.1440 0.1978 0.0017  -0.0061 0.0010  43  SER   A C   
304  O O   . SER   A 37  ? 0.1592 0.1471 0.2021 0.0041  -0.0045 0.0010  43  SER   A O   
305  C CB  . SER   A 37  ? 0.1710 0.1488 0.1983 -0.0016 -0.0090 -0.0007 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1779 0.1595 0.2063 -0.0005 -0.0108 0.0004  43  SER   A OG  
307  N N   . SER   A 38  ? 0.1690 0.1584 0.2137 -0.0008 -0.0067 0.0020  44  SER   A N   
308  C CA  . SER   A 38  ? 0.1758 0.1717 0.2316 0.0000  -0.0050 0.0034  44  SER   A CA  
309  C C   . SER   A 38  ? 0.1936 0.1955 0.2568 0.0002  -0.0081 0.0075  44  SER   A C   
310  O O   . SER   A 38  ? 0.2146 0.2176 0.2733 -0.0028 -0.0124 0.0090  44  SER   A O   
311  C CB  . SER   A 38  ? 0.2038 0.2019 0.2631 -0.0027 -0.0034 0.0031  44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2464 0.2453 0.3035 -0.0062 -0.0072 0.0045  44  SER   A OG  
313  N N   . THR   A 39  ? 0.1915 0.1975 0.2663 0.0032  -0.0055 0.0096  45  THR   A N   
314  C CA  . THR   A 39  ? 0.2060 0.2190 0.2905 0.0040  -0.0085 0.0157  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2233 0.2439 0.3253 0.0052  -0.0058 0.0196  45  THR   A C   
316  O O   . THR   A 39  ? 0.2121 0.2304 0.3187 0.0064  0.0006  0.0160  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2120 0.2226 0.2979 0.0075  -0.0071 0.0164  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2123 0.2198 0.3049 0.0104  0.0000  0.0135  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2283 0.2323 0.2989 0.0069  -0.0088 0.0126  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2323 0.2627 0.3445 0.0045  -0.0101 0.0275  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2429 0.2820 0.3753 0.0066  -0.0073 0.0331  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2415 0.2787 0.3881 0.0126  -0.0010 0.0350  46  THR   A C   
323  O O   . THR   A 40  ? 0.2636 0.2995 0.4225 0.0153  0.0071  0.0332  46  THR   A O   
324  C CB  . THR   A 40  ? 0.2787 0.3315 0.4181 0.0027  -0.0148 0.0423  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3367 0.3926 0.4726 0.0016  -0.0205 0.0475  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.2873 0.3405 0.4132 -0.0041 -0.0189 0.0389  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2392 0.2749 0.3830 0.0140  -0.0038 0.0379  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2490 0.2812 0.4058 0.0193  0.0027  0.0397  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2373 0.2563 0.3820 0.0199  0.0092  0.0294  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2313 0.2455 0.3571 0.0171  0.0060  0.0237  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.2849 0.3227 0.4460 0.0200  -0.0033 0.0490  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2208 0.2344 0.3767 0.0232  0.0187  0.0272  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2343 0.2372 0.3792 0.0221  0.0252  0.0178  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2321 0.2316 0.3708 0.0231  0.0222  0.0196  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2439 0.2468 0.3950 0.0262  0.0205  0.0279  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.2549 0.2524 0.4131 0.0234  0.0381  0.0135  48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3323 0.3322 0.4935 0.0211  0.0426  0.0093  48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4168 0.4103 0.5900 0.0213  0.0570  0.0035  48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4141 0.4086 0.6099 0.0261  0.0633  0.0088  48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4515 0.4383 0.6101 0.0155  0.0631  -0.0071 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.1945 0.1885 0.3147 0.0203  0.0213  0.0127  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.1971 0.1878 0.3095 0.0206  0.0190  0.0131  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.1775 0.1605 0.2931 0.0208  0.0279  0.0089  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.1984 0.1772 0.3180 0.0193  0.0370  0.0031  49  GLY   A O   
345  N N   . CYS   A 44  ? 0.1724 0.1533 0.2837 0.0213  0.0257  0.0108  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.1889 0.1618 0.3031 0.0210  0.0340  0.0074  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.1877 0.1569 0.2839 0.0166  0.0346  0.0002  50  CYS   A C   
348  O O   . CYS   A 44  ? 0.1919 0.1544 0.2886 0.0146  0.0421  -0.0039 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.1936 0.1666 0.3209 0.0249  0.0331  0.0163  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.2293 0.2075 0.3836 0.0302  0.0350  0.0267  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.1729 0.1464 0.2547 0.0149  0.0272  -0.0008 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.1650 0.1375 0.2319 0.0110  0.0273  -0.0060 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.1807 0.1520 0.2424 0.0057  0.0338  -0.0133 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2027 0.1755 0.2676 0.0052  0.0352  -0.0144 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1570 0.1346 0.2130 0.0115  0.0183  -0.0039 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.1720 0.1513 0.2292 0.0144  0.0122  0.0020  51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.1780 0.1549 0.2388 0.0149  0.0139  0.0039  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.1801 0.1631 0.2337 0.0151  0.0062  0.0044  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.1915 0.1609 0.2447 0.0007  0.0377  -0.0180 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2117 0.1823 0.2564 -0.0069 0.0431  -0.0247 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2021 0.1797 0.2327 -0.0103 0.0371  -0.0241 52  THR   A C   
362  O O   . THR   A 46  ? 0.2160 0.1945 0.2433 -0.0084 0.0331  -0.0215 52  THR   A O   
363  C CB  . THR   A 46  ? 0.2701 0.2334 0.3172 -0.0122 0.0545  -0.0313 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3312 0.2923 0.3740 -0.0132 0.0542  -0.0311 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.2825 0.2386 0.3477 -0.0075 0.0618  -0.0308 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.1979 0.1813 0.2212 -0.0150 0.0361  -0.0253 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.1810 0.1729 0.1939 -0.0177 0.0304  -0.0227 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.1895 0.1848 0.1930 -0.0274 0.0349  -0.0269 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.1981 0.1921 0.1989 -0.0354 0.0424  -0.0329 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.1751 0.1731 0.1858 -0.0179 0.0262  -0.0196 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.1884 0.1827 0.2074 -0.0103 0.0228  -0.0166 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.1761 0.1835 0.1797 -0.0191 0.0202  -0.0144 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.1983 0.1907 0.2197 -0.0029 0.0169  -0.0122 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.1675 0.1681 0.1656 -0.0280 0.0309  -0.0240 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.1746 0.1815 0.1627 -0.0383 0.0336  -0.0266 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.1861 0.2050 0.1669 -0.0459 0.0314  -0.0245 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.1847 0.2096 0.1675 -0.0413 0.0248  -0.0178 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.1730 0.1848 0.1588 -0.0359 0.0285  -0.0223 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2127 0.2351 0.1845 -0.0588 0.0374  -0.0302 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2285 0.2646 0.1916 -0.0687 0.0352  -0.0275 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2549 0.3009 0.2072 -0.0806 0.0361  -0.0283 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.2716 0.3158 0.2152 -0.0931 0.0443  -0.0368 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2412 0.2730 0.2026 -0.0753 0.0426  -0.0343 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2351 0.2573 0.2081 -0.0640 0.0423  -0.0338 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2088 0.2379 0.1856 -0.0562 0.0324  -0.0239 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2053 0.2254 0.1921 -0.0473 0.0328  -0.0243 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2166 0.2372 0.2089 -0.0385 0.0258  -0.0175 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.1991 0.2279 0.1895 -0.0366 0.0189  -0.0097 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2371 0.2501 0.2378 -0.0318 0.0263  -0.0184 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2386 0.2955 0.1916 -0.0772 0.0281  -0.0195 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2477 0.3142 0.1928 -0.0860 0.0276  -0.0188 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2522 0.3351 0.2011 -0.0815 0.0176  -0.0060 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.2748 0.3592 0.2326 -0.0710 0.0121  0.0016  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2372 0.2894 0.1850 -0.0815 0.0326  -0.0254 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2338 0.2797 0.1946 -0.0627 0.0258  -0.0186 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.2923 0.3869 0.2352 -0.0894 0.0163  -0.0039 57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3229 0.4339 0.2711 -0.0856 0.0082  0.0083  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3087 0.4147 0.2595 -0.0800 0.0086  0.0068  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3058 0.4270 0.2576 -0.0820 0.0043  0.0142  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.4101 0.5442 0.3489 -0.1021 0.0054  0.0142  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5434 0.6991 0.4903 -0.0992 -0.0034 0.0300  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5653 0.7427 0.5057 -0.1131 -0.0067 0.0367  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.6112 0.7628 0.5715 -0.0837 -0.0066 0.0360  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.2708 0.3569 0.2237 -0.0731 0.0136  -0.0019 58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2401 0.3215 0.1955 -0.0679 0.0137  -0.0026 58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2393 0.3289 0.2043 -0.0570 0.0070  0.0073  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2413 0.3302 0.2142 -0.0481 0.0039  0.0123  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2435 0.3034 0.2020 -0.0610 0.0190  -0.0107 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2630 0.3096 0.2135 -0.0725 0.0299  -0.0233 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2010 0.2980 0.1657 -0.0580 0.0056  0.0099  59  GLN   A N   
411  C CA  A GLN   A 53  ? 0.1888 0.2923 0.1632 -0.0478 0.0014  0.0179  59  GLN   A CA  
412  C CA  B GLN   A 53  ? 0.1948 0.2974 0.1692 -0.0476 0.0014  0.0177  59  GLN   A CA  
413  C C   . GLN   A 53  ? 0.1739 0.2665 0.1484 -0.0430 0.0035  0.0132  59  GLN   A C   
414  O O   . GLN   A 53  ? 0.1750 0.2732 0.1555 -0.0370 0.0015  0.0180  59  GLN   A O   
415  C CB  A GLN   A 53  ? 0.1866 0.3139 0.1642 -0.0522 -0.0032 0.0288  59  GLN   A CB  
416  C CB  B GLN   A 53  ? 0.2080 0.3343 0.1856 -0.0523 -0.0034 0.0289  59  GLN   A CB  
417  C CG  A GLN   A 53  ? 0.1711 0.3117 0.1551 -0.0518 -0.0074 0.0389  59  GLN   A CG  
418  C CG  B GLN   A 53  ? 0.1929 0.3273 0.1705 -0.0565 -0.0056 0.0339  59  GLN   A CG  
419  C CD  A GLN   A 53  ? 0.1872 0.3523 0.1789 -0.0537 -0.0122 0.0525  59  GLN   A CD  
420  C CD  B GLN   A 53  ? 0.2102 0.3322 0.1965 -0.0443 -0.0059 0.0347  59  GLN   A CD  
421  O OE1 A GLN   A 53  ? 0.2176 0.4011 0.2040 -0.0662 -0.0149 0.0578  59  GLN   A OE1 
422  O OE1 B GLN   A 53  ? 0.1836 0.3010 0.1678 -0.0460 -0.0053 0.0329  59  GLN   A OE1 
423  N NE2 A GLN   A 53  ? 0.1637 0.3305 0.1685 -0.0420 -0.0130 0.0587  59  GLN   A NE2 
424  N NE2 B GLN   A 53  ? 0.2160 0.3320 0.2118 -0.0321 -0.0062 0.0368  59  GLN   A NE2 
425  N N   . THR   A 54  ? 0.1631 0.2403 0.1318 -0.0458 0.0083  0.0040  60  THR   A N   
426  C CA  . THR   A 54  ? 0.1762 0.2418 0.1457 -0.0410 0.0102  0.0003  60  THR   A CA  
427  C C   . THR   A 54  ? 0.1733 0.2206 0.1450 -0.0360 0.0133  -0.0052 60  THR   A C   
428  O O   . THR   A 54  ? 0.1986 0.2409 0.1683 -0.0401 0.0164  -0.0091 60  THR   A O   
429  C CB  . THR   A 54  ? 0.2065 0.2736 0.1687 -0.0500 0.0132  -0.0031 60  THR   A CB  
430  O OG1 . THR   A 54  ? 0.2936 0.3531 0.2490 -0.0594 0.0189  -0.0104 60  THR   A OG1 
431  C CG2 . THR   A 54  ? 0.2078 0.2948 0.1682 -0.0562 0.0100  0.0028  60  THR   A CG2 
432  N N   . GLY   A 55  ? 0.1552 0.1943 0.1314 -0.0276 0.0122  -0.0047 61  GLY   A N   
433  C CA  . GLY   A 55  ? 0.1560 0.1805 0.1360 -0.0226 0.0139  -0.0077 61  GLY   A CA  
434  C C   . GLY   A 55  ? 0.1496 0.1686 0.1326 -0.0159 0.0120  -0.0061 61  GLY   A C   
435  O O   . GLY   A 55  ? 0.1541 0.1777 0.1350 -0.0165 0.0110  -0.0046 61  GLY   A O   
436  N N   . VAL   A 56  ? 0.1358 0.1455 0.1236 -0.0104 0.0115  -0.0062 62  VAL   A N   
437  C CA  . VAL   A 56  ? 0.1408 0.1460 0.1304 -0.0059 0.0094  -0.0043 62  VAL   A CA  
438  C C   . VAL   A 56  ? 0.1355 0.1389 0.1287 -0.0002 0.0064  -0.0027 62  VAL   A C   
439  O O   . VAL   A 56  ? 0.1505 0.1509 0.1469 0.0005  0.0071  -0.0036 62  VAL   A O   
440  C CB  . VAL   A 56  ? 0.1635 0.1589 0.1558 -0.0074 0.0124  -0.0053 62  VAL   A CB  
441  C CG1 . VAL   A 56  ? 0.1917 0.1837 0.1865 -0.0036 0.0094  -0.0017 62  VAL   A CG1 
442  C CG2 . VAL   A 56  ? 0.1649 0.1602 0.1529 -0.0140 0.0164  -0.0076 62  VAL   A CG2 
443  N N   . TYR   A 57  ? 0.1395 0.1447 0.1317 0.0029  0.0040  -0.0011 63  TYR   A N   
444  C CA  . TYR   A 57  ? 0.1341 0.1366 0.1284 0.0068  0.0019  -0.0005 63  TYR   A CA  
445  C C   . TYR   A 57  ? 0.1355 0.1344 0.1287 0.0071  -0.0001 0.0008  63  TYR   A C   
446  O O   . TYR   A 57  ? 0.1525 0.1528 0.1425 0.0054  -0.0002 0.0014  63  TYR   A O   
447  C CB  . TYR   A 57  ? 0.1381 0.1454 0.1325 0.0095  0.0018  0.0000  63  TYR   A CB  
448  C CG  . TYR   A 57  ? 0.1350 0.1450 0.1273 0.0106  0.0024  0.0001  63  TYR   A CG  
449  C CD1 . TYR   A 57  ? 0.1431 0.1596 0.1340 0.0090  0.0035  0.0008  63  TYR   A CD1 
450  C CD2 . TYR   A 57  ? 0.1487 0.1549 0.1399 0.0123  0.0025  -0.0011 63  TYR   A CD2 
451  C CE1 . TYR   A 57  ? 0.1643 0.1834 0.1539 0.0099  0.0049  0.0005  63  TYR   A CE1 
452  C CE2 . TYR   A 57  ? 0.1563 0.1641 0.1451 0.0124  0.0045  -0.0023 63  TYR   A CE2 
453  C CZ  . TYR   A 57  ? 0.1728 0.1871 0.1614 0.0117  0.0059  -0.0013 63  TYR   A CZ  
454  O OH  . TYR   A 57  ? 0.1976 0.2140 0.1846 0.0118  0.0088  -0.0027 63  TYR   A OH  
455  N N   . TYR   A 58  ? 0.1340 0.1299 0.1292 0.0085  -0.0020 0.0014  64  TYR   A N   
456  C CA  . TYR   A 58  ? 0.1496 0.1445 0.1426 0.0072  -0.0047 0.0033  64  TYR   A CA  
457  C C   . TYR   A 58  ? 0.1419 0.1381 0.1294 0.0070  -0.0044 0.0010  64  TYR   A C   
458  O O   . TYR   A 58  ? 0.1437 0.1385 0.1319 0.0088  -0.0034 -0.0010 64  TYR   A O   
459  C CB  . TYR   A 58  ? 0.1615 0.1541 0.1600 0.0074  -0.0070 0.0061  64  TYR   A CB  
460  C CG  . TYR   A 58  ? 0.1657 0.1601 0.1619 0.0044  -0.0107 0.0098  64  TYR   A CG  
461  C CD1 . TYR   A 58  ? 0.1693 0.1650 0.1653 0.0022  -0.0118 0.0136  64  TYR   A CD1 
462  C CD2 . TYR   A 58  ? 0.1689 0.1643 0.1622 0.0025  -0.0130 0.0096  64  TYR   A CD2 
463  C CE1 . TYR   A 58  ? 0.1888 0.1882 0.1818 -0.0019 -0.0158 0.0180  64  TYR   A CE1 
464  C CE2 . TYR   A 58  ? 0.1851 0.1843 0.1744 -0.0025 -0.0167 0.0131  64  TYR   A CE2 
465  C CZ  . TYR   A 58  ? 0.1874 0.1892 0.1770 -0.0046 -0.0184 0.0179  64  TYR   A CZ  
466  O OH  . TYR   A 58  ? 0.2105 0.2179 0.1955 -0.0108 -0.0228 0.0226  64  TYR   A OH  
467  N N   . CYS   A 59  ? 0.1394 0.1374 0.1215 0.0042  -0.0046 0.0011  65  CYS   A N   
468  C CA  . CYS   A 59  ? 0.1626 0.1610 0.1387 0.0026  -0.0027 -0.0022 65  CYS   A CA  
469  C C   . CYS   A 59  ? 0.1698 0.1683 0.1403 -0.0029 -0.0059 -0.0009 65  CYS   A C   
470  O O   . CYS   A 59  ? 0.1687 0.1701 0.1357 -0.0067 -0.0080 0.0020  65  CYS   A O   
471  C CB  . CYS   A 59  ? 0.1732 0.1751 0.1467 0.0024  0.0001  -0.0034 65  CYS   A CB  
472  S SG  . CYS   A 59  ? 0.1767 0.1783 0.1434 -0.0002 0.0048  -0.0085 65  CYS   A SG  
473  N N   . SER   A 60  ? 0.1682 0.1645 0.1373 -0.0045 -0.0065 -0.0024 66  SER   A N   
474  C CA  . SER   A 60  ? 0.1819 0.1805 0.1452 -0.0114 -0.0102 -0.0003 66  SER   A CA  
475  C C   . SER   A 60  ? 0.1844 0.1851 0.1370 -0.0181 -0.0084 -0.0033 66  SER   A C   
476  O O   . SER   A 60  ? 0.2001 0.2059 0.1481 -0.0245 -0.0128 0.0012  66  SER   A O   
477  C CB  . SER   A 60  ? 0.2143 0.2107 0.1780 -0.0126 -0.0109 -0.0018 66  SER   A CB  
478  O OG  . SER   A 60  ? 0.2481 0.2394 0.2068 -0.0132 -0.0052 -0.0090 66  SER   A OG  
479  N N   . SER   A 61  ? 0.1710 0.1685 0.1209 -0.0163 -0.0017 -0.0099 67  SER   A N   
480  C CA  . SER   A 61  ? 0.1887 0.1875 0.1286 -0.0227 0.0020  -0.0141 67  SER   A CA  
481  C C   . SER   A 61  ? 0.1816 0.1857 0.1199 -0.0239 0.0002  -0.0105 67  SER   A C   
482  O O   . SER   A 61  ? 0.1854 0.1916 0.1151 -0.0299 0.0028  -0.0134 67  SER   A O   
483  C CB  . SER   A 61  ? 0.1999 0.1931 0.1404 -0.0197 0.0110  -0.0217 67  SER   A CB  
484  O OG  . SER   A 61  ? 0.1874 0.1816 0.1368 -0.0115 0.0133  -0.0205 67  SER   A OG  
485  N N   . ARG   A 62  ? 0.1729 0.1787 0.1192 -0.0192 -0.0037 -0.0045 68  ARG   A N   
486  C CA  . ARG   A 62  ? 0.1814 0.1913 0.1269 -0.0209 -0.0059 -0.0001 68  ARG   A CA  
487  C C   . ARG   A 62  ? 0.1994 0.2110 0.1500 -0.0216 -0.0124 0.0085  68  ARG   A C   
488  O O   . ARG   A 62  ? 0.1954 0.2091 0.1469 -0.0229 -0.0141 0.0133  68  ARG   A O   
489  C CB  . ARG   A 62  ? 0.1815 0.1912 0.1323 -0.0149 -0.0022 -0.0017 68  ARG   A CB  
490  C CG  . ARG   A 62  ? 0.1901 0.2000 0.1388 -0.0136 0.0045  -0.0081 68  ARG   A CG  
491  C CD  . ARG   A 62  ? 0.1972 0.2107 0.1371 -0.0200 0.0064  -0.0098 68  ARG   A CD  
492  N NE  . ARG   A 62  ? 0.2130 0.2268 0.1530 -0.0183 0.0144  -0.0160 68  ARG   A NE  
493  C CZ  . ARG   A 62  ? 0.2017 0.2118 0.1373 -0.0210 0.0201  -0.0223 68  ARG   A CZ  
494  N NH1 . ARG   A 62  ? 0.2238 0.2307 0.1525 -0.0267 0.0178  -0.0235 68  ARG   A NH1 
495  N NH2 . ARG   A 62  ? 0.2252 0.2352 0.1636 -0.0186 0.0287  -0.0274 68  ARG   A NH2 
496  N N   . ARG   A 63  ? 0.1994 0.2095 0.1556 -0.0199 -0.0152 0.0110  69  ARG   A N   
497  C CA  . ARG   A 63  ? 0.2044 0.2155 0.1702 -0.0184 -0.0197 0.0196  69  ARG   A CA  
498  C C   . ARG   A 63  ? 0.2188 0.2267 0.1916 -0.0136 -0.0174 0.0209  69  ARG   A C   
499  O O   . ARG   A 63  ? 0.2358 0.2443 0.2134 -0.0145 -0.0194 0.0278  69  ARG   A O   
500  C CB  . ARG   A 63  ? 0.2373 0.2553 0.2011 -0.0255 -0.0255 0.0282  69  ARG   A CB  
501  C CG  . ARG   A 63  ? 0.2418 0.2639 0.2008 -0.0310 -0.0286 0.0285  69  ARG   A CG  
502  C CD  . ARG   A 63  ? 0.2485 0.2800 0.2099 -0.0373 -0.0358 0.0405  69  ARG   A CD  
503  N NE  . ARG   A 63  ? 0.2803 0.3181 0.2333 -0.0459 -0.0390 0.0403  69  ARG   A NE  
504  C CZ  . ARG   A 63  ? 0.2450 0.2885 0.1831 -0.0568 -0.0400 0.0385  69  ARG   A CZ  
505  N NH1 . ARG   A 63  ? 0.2629 0.3071 0.1937 -0.0598 -0.0382 0.0373  69  ARG   A NH1 
506  N NH2 . ARG   A 63  ? 0.2673 0.3164 0.1972 -0.0659 -0.0424 0.0376  69  ARG   A NH2 
507  N N   . LYS   A 64  ? 0.1897 0.1943 0.1633 -0.0092 -0.0131 0.0148  70  LYS   A N   
508  C CA  . LYS   A 64  ? 0.1979 0.2004 0.1755 -0.0069 -0.0104 0.0147  70  LYS   A CA  
509  C C   . LYS   A 64  ? 0.1877 0.1875 0.1699 -0.0024 -0.0074 0.0108  70  LYS   A C   
510  O O   . LYS   A 64  ? 0.1835 0.1838 0.1641 -0.0005 -0.0063 0.0069  70  LYS   A O   
511  C CB  . LYS   A 64  ? 0.2491 0.2549 0.2191 -0.0092 -0.0082 0.0118  70  LYS   A CB  
512  C CG  . LYS   A 64  ? 0.3834 0.3882 0.3553 -0.0097 -0.0063 0.0130  70  LYS   A CG  
513  C CD  . LYS   A 64  ? 0.4909 0.4998 0.4555 -0.0140 -0.0062 0.0135  70  LYS   A CD  
514  C CE  . LYS   A 64  ? 0.5580 0.5659 0.5237 -0.0154 -0.0041 0.0145  70  LYS   A CE  
515  N NZ  . LYS   A 64  ? 0.5714 0.5726 0.5451 -0.0147 -0.0040 0.0187  70  LYS   A NZ  
516  N N   . HIS   A 65  ? 0.1681 0.1648 0.1556 -0.0016 -0.0053 0.0116  71  HIS   A N   
517  C CA  . HIS   A 65  ? 0.1652 0.1606 0.1552 0.0003  -0.0020 0.0078  71  HIS   A CA  
518  C C   . HIS   A 65  ? 0.1838 0.1828 0.1690 -0.0017 0.0005  0.0053  71  HIS   A C   
519  O O   . HIS   A 65  ? 0.2258 0.2241 0.2096 -0.0046 0.0013  0.0067  71  HIS   A O   
520  C CB  . HIS   A 65  ? 0.1534 0.1429 0.1515 0.0008  0.0003  0.0091  71  HIS   A CB  
521  C CG  . HIS   A 65  ? 0.1741 0.1617 0.1791 0.0032  -0.0019 0.0122  71  HIS   A CG  
522  N ND1 . HIS   A 65  ? 0.2154 0.2018 0.2239 0.0054  -0.0008 0.0097  71  HIS   A ND1 
523  C CD2 . HIS   A 65  ? 0.1532 0.1412 0.1626 0.0031  -0.0052 0.0185  71  HIS   A CD2 
524  C CE1 . HIS   A 65  ? 0.1729 0.1586 0.1883 0.0068  -0.0031 0.0141  71  HIS   A CE1 
525  N NE2 . HIS   A 65  ? 0.2031 0.1905 0.2194 0.0053  -0.0062 0.0198  71  HIS   A NE2 
526  N N   . TYR   A 66  ? 0.1542 0.1580 0.1379 -0.0006 0.0017  0.0025  72  TYR   A N   
527  C CA  . TYR   A 66  ? 0.1723 0.1826 0.1529 -0.0027 0.0035  0.0014  72  TYR   A CA  
528  C C   . TYR   A 66  ? 0.1568 0.1701 0.1388 -0.0044 0.0054  0.0000  72  TYR   A C   
529  O O   . TYR   A 66  ? 0.1547 0.1686 0.1394 -0.0022 0.0051  -0.0004 72  TYR   A O   
530  C CB  . TYR   A 66  ? 0.1716 0.1882 0.1510 -0.0001 0.0036  0.0008  72  TYR   A CB  
531  C CG  . TYR   A 66  ? 0.1829 0.1984 0.1584 -0.0007 0.0029  0.0008  72  TYR   A CG  
532  C CD1 . TYR   A 66  ? 0.2048 0.2229 0.1761 -0.0041 0.0033  0.0014  72  TYR   A CD1 
533  C CD2 . TYR   A 66  ? 0.1884 0.2007 0.1632 0.0009  0.0021  -0.0001 72  TYR   A CD2 
534  C CE1 . TYR   A 66  ? 0.2114 0.2297 0.1777 -0.0060 0.0030  0.0011  72  TYR   A CE1 
535  C CE2 . TYR   A 66  ? 0.2006 0.2128 0.1698 -0.0017 0.0021  -0.0009 72  TYR   A CE2 
536  C CZ  . TYR   A 66  ? 0.2153 0.2308 0.1802 -0.0052 0.0025  -0.0002 72  TYR   A CZ  
537  O OH  . TYR   A 66  ? 0.2415 0.2576 0.1996 -0.0092 0.0026  -0.0011 72  TYR   A OH  
538  N N   . PRO   A 67  ? 0.1571 0.1730 0.1362 -0.0093 0.0074  -0.0007 73  PRO   A N   
539  C CA  . PRO   A 67  ? 0.1489 0.1707 0.1272 -0.0133 0.0091  -0.0020 73  PRO   A CA  
540  C C   . PRO   A 67  ? 0.1668 0.2014 0.1461 -0.0118 0.0076  0.0005  73  PRO   A C   
541  O O   . PRO   A 67  ? 0.1916 0.2315 0.1707 -0.0105 0.0071  0.0021  73  PRO   A O   
542  C CB  . PRO   A 67  ? 0.1774 0.1983 0.1513 -0.0204 0.0121  -0.0038 73  PRO   A CB  
543  C CG  . PRO   A 67  ? 0.1991 0.2179 0.1717 -0.0191 0.0111  -0.0021 73  PRO   A CG  
544  C CD  . PRO   A 67  ? 0.1679 0.1822 0.1438 -0.0127 0.0082  -0.0003 73  PRO   A CD  
545  N N   . VAL   A 68  ? 0.1531 0.1927 0.1344 -0.0121 0.0072  0.0015  74  VAL   A N   
546  C CA  . VAL   A 68  ? 0.1647 0.2175 0.1500 -0.0101 0.0057  0.0061  74  VAL   A CA  
547  C C   . VAL   A 68  ? 0.1435 0.2065 0.1281 -0.0160 0.0053  0.0082  74  VAL   A C   
548  O O   . VAL   A 68  ? 0.1619 0.2204 0.1434 -0.0201 0.0063  0.0053  74  VAL   A O   
549  C CB  . VAL   A 68  ? 0.1849 0.2343 0.1762 -0.0021 0.0049  0.0076  74  VAL   A CB  
550  C CG1 . VAL   A 68  ? 0.2095 0.2529 0.2008 0.0022  0.0056  0.0061  74  VAL   A CG1 
551  C CG2 . VAL   A 68  ? 0.1947 0.2352 0.1862 -0.0013 0.0045  0.0055  74  VAL   A CG2 
552  N N   . SER   A 69  ? 0.1508 0.2295 0.1393 -0.0165 0.0038  0.0142  75  SER   A N   
553  C CA  A SER   A 69  ? 0.1516 0.2445 0.1415 -0.0214 0.0020  0.0193  75  SER   A CA  
554  C CA  B SER   A 69  ? 0.1547 0.2481 0.1447 -0.0214 0.0020  0.0195  75  SER   A CA  
555  C C   . SER   A 69  ? 0.1449 0.2400 0.1449 -0.0129 0.0006  0.0249  75  SER   A C   
556  O O   . SER   A 69  ? 0.1547 0.2486 0.1617 -0.0050 0.0016  0.0269  75  SER   A O   
557  C CB  A SER   A 69  ? 0.1702 0.2815 0.1608 -0.0271 0.0007  0.0248  75  SER   A CB  
558  C CB  B SER   A 69  ? 0.1771 0.2883 0.1687 -0.0258 0.0008  0.0251  75  SER   A CB  
559  O OG  A SER   A 69  ? 0.2143 0.3223 0.1954 -0.0352 0.0027  0.0192  75  SER   A OG  
560  O OG  B SER   A 69  ? 0.2182 0.3469 0.2127 -0.0308 -0.0019 0.0326  75  SER   A OG  
561  N N   . PHE   A 70  ? 0.1471 0.2449 0.1479 -0.0147 -0.0008 0.0273  76  PHE   A N   
562  C CA  . PHE   A 70  ? 0.1514 0.2492 0.1618 -0.0068 -0.0016 0.0326  76  PHE   A CA  
563  C C   . PHE   A 70  ? 0.1446 0.2588 0.1591 -0.0110 -0.0045 0.0416  76  PHE   A C   
564  O O   . PHE   A 70  ? 0.1629 0.2853 0.1695 -0.0215 -0.0059 0.0413  76  PHE   A O   
565  C CB  . PHE   A 70  ? 0.1575 0.2368 0.1657 -0.0024 -0.0003 0.0259  76  PHE   A CB  
566  C CG  . PHE   A 70  ? 0.1563 0.2295 0.1560 -0.0094 0.0001  0.0203  76  PHE   A CG  
567  C CD1 . PHE   A 70  ? 0.1552 0.2185 0.1478 -0.0129 0.0023  0.0129  76  PHE   A CD1 
568  C CD2 . PHE   A 70  ? 0.1523 0.2291 0.1521 -0.0124 -0.0011 0.0227  76  PHE   A CD2 
569  C CE1 . PHE   A 70  ? 0.1631 0.2198 0.1503 -0.0187 0.0045  0.0075  76  PHE   A CE1 
570  C CE2 . PHE   A 70  ? 0.1599 0.2306 0.1525 -0.0189 0.0008  0.0165  76  PHE   A CE2 
571  C CZ  . PHE   A 70  ? 0.1611 0.2217 0.1478 -0.0220 0.0040  0.0088  76  PHE   A CZ  
572  N N   . SER   A 71  ? 0.1426 0.2625 0.1699 -0.0036 -0.0051 0.0502  77  SER   A N   
573  C CA  . SER   A 71  ? 0.1425 0.2797 0.1766 -0.0065 -0.0085 0.0616  77  SER   A CA  
574  C C   . SER   A 71  ? 0.1505 0.2826 0.1790 -0.0104 -0.0098 0.0600  77  SER   A C   
575  O O   . SER   A 71  ? 0.1538 0.2679 0.1768 -0.0079 -0.0076 0.0507  77  SER   A O   
576  C CB  . SER   A 71  ? 0.1655 0.3086 0.2178 0.0039  -0.0074 0.0720  77  SER   A CB  
577  O OG  . SER   A 71  ? 0.1857 0.3110 0.2425 0.0133  -0.0040 0.0681  77  SER   A OG  
578  N N   . LYS   A 72  ? 0.1444 0.2935 0.1745 -0.0171 -0.0135 0.0693  78  LYS   A N   
579  C CA  . LYS   A 72  ? 0.1546 0.3006 0.1797 -0.0215 -0.0145 0.0684  78  LYS   A CA  
580  C C   . LYS   A 72  ? 0.1689 0.3048 0.2053 -0.0101 -0.0135 0.0719  78  LYS   A C   
581  O O   . LYS   A 72  ? 0.1692 0.3079 0.2198 -0.0009 -0.0127 0.0796  78  LYS   A O   
582  C CB  . LYS   A 72  ? 0.1784 0.3480 0.2014 -0.0334 -0.0191 0.0787  78  LYS   A CB  
583  C CG  . LYS   A 72  ? 0.2221 0.3995 0.2308 -0.0472 -0.0190 0.0728  78  LYS   A CG  
584  C CD  . LYS   A 72  ? 0.3122 0.5120 0.3149 -0.0622 -0.0232 0.0809  78  LYS   A CD  
585  C CE  . LYS   A 72  ? 0.3959 0.6002 0.3818 -0.0777 -0.0214 0.0724  78  LYS   A CE  
586  N NZ  . LYS   A 72  ? 0.4545 0.6741 0.4290 -0.0949 -0.0235 0.0749  78  LYS   A NZ  
587  N N   . PRO   A 73  ? 0.1722 0.2962 0.2035 -0.0106 -0.0128 0.0665  79  PRO   A N   
588  C CA  . PRO   A 73  ? 0.1666 0.2803 0.2077 -0.0009 -0.0115 0.0693  79  PRO   A CA  
589  C C   . PRO   A 73  ? 0.1745 0.3027 0.2307 0.0026  -0.0136 0.0852  79  PRO   A C   
590  O O   . PRO   A 73  ? 0.2075 0.3539 0.2633 -0.0056 -0.0179 0.0946  79  PRO   A O   
591  C CB  . PRO   A 73  ? 0.2082 0.3128 0.2398 -0.0058 -0.0114 0.0625  79  PRO   A CB  
592  C CG  . PRO   A 73  ? 0.2590 0.3625 0.2768 -0.0152 -0.0105 0.0528  79  PRO   A CG  
593  C CD  . PRO   A 73  ? 0.1964 0.3155 0.2132 -0.0205 -0.0121 0.0571  79  PRO   A CD  
594  N N   . SER   A 74  ? 0.1665 0.2873 0.2364 0.0140  -0.0102 0.0886  80  SER   A N   
595  C CA  . SER   A 74  ? 0.1718 0.3057 0.2603 0.0193  -0.0107 0.1048  80  SER   A CA  
596  C C   . SER   A 74  ? 0.1635 0.2804 0.2641 0.0309  -0.0049 0.1046  80  SER   A C   
597  O O   . SER   A 74  ? 0.1679 0.2646 0.2617 0.0343  -0.0009 0.0919  80  SER   A O   
598  C CB  . SER   A 74  ? 0.2365 0.3860 0.3340 0.0207  -0.0108 0.1120  80  SER   A CB  
599  O OG  . SER   A 74  ? 0.3652 0.5204 0.4490 0.0124  -0.0128 0.1047  80  SER   A OG  
600  N N   . LEU   A 75  ? 0.1852 0.3112 0.3056 0.0370  -0.0039 0.1199  81  LEU   A N   
601  C CA  . LEU   A 75  ? 0.2111 0.3218 0.3462 0.0480  0.0033  0.1215  81  LEU   A CA  
602  C C   . LEU   A 75  ? 0.2245 0.3344 0.3715 0.0558  0.0096  0.1215  81  LEU   A C   
603  O O   . LEU   A 75  ? 0.2398 0.3688 0.4016 0.0577  0.0085  0.1350  81  LEU   A O   
604  C CB  . LEU   A 75  ? 0.2169 0.3392 0.3686 0.0499  0.0013  0.1397  81  LEU   A CB  
605  C CG  . LEU   A 75  ? 0.2651 0.3710 0.4322 0.0598  0.0088  0.1428  81  LEU   A CG  
606  C CD1 . LEU   A 75  ? 0.2841 0.3678 0.4364 0.0579  0.0105  0.1286  81  LEU   A CD1 
607  C CD2 . LEU   A 75  ? 0.2718 0.3935 0.4576 0.0611  0.0058  0.1641  81  LEU   A CD2 
608  N N   . ILE   A 76  ? 0.2227 0.3125 0.3632 0.0595  0.0159  0.1069  82  ILE   A N   
609  C CA  A ILE   A 76  ? 0.2453 0.3313 0.3922 0.0652  0.0228  0.1027  82  ILE   A CA  
610  C CA  B ILE   A 76  ? 0.2424 0.3291 0.3909 0.0656  0.0229  0.1039  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.2599 0.3255 0.4175 0.0739  0.0337  0.0986  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.2622 0.3099 0.4100 0.0727  0.0355  0.0891  82  ILE   A O   
613  C CB  A ILE   A 76  ? 0.2612 0.3403 0.3865 0.0590  0.0208  0.0870  82  ILE   A CB  
614  C CB  B ILE   A 76  ? 0.2497 0.3333 0.3792 0.0599  0.0209  0.0902  82  ILE   A CB  
615  C CG1 A ILE   A 76  ? 0.2690 0.3657 0.3828 0.0495  0.0119  0.0890  82  ILE   A CG1 
616  C CG1 B ILE   A 76  ? 0.2602 0.3610 0.3777 0.0499  0.0114  0.0927  82  ILE   A CG1 
617  C CG2 A ILE   A 76  ? 0.2704 0.3418 0.3981 0.0635  0.0283  0.0795  82  ILE   A CG2 
618  C CG2 B ILE   A 76  ? 0.2562 0.3387 0.3931 0.0650  0.0279  0.0874  82  ILE   A CG2 
619  C CD1 A ILE   A 76  ? 0.2680 0.3851 0.3900 0.0489  0.0107  0.0973  82  ILE   A CD1 
620  C CD1 B ILE   A 76  ? 0.2607 0.3585 0.3623 0.0447  0.0100  0.0814  82  ILE   A CD1 
621  N N   . PHE   A 77  ? 0.2629 0.3305 0.4393 0.0817  0.0418  0.1041  83  PHE   A N   
622  C CA  . PHE   A 77  ? 0.2677 0.3146 0.4535 0.0889  0.0544  0.0981  83  PHE   A CA  
623  C C   . PHE   A 77  ? 0.2935 0.3246 0.4603 0.0852  0.0584  0.0788  83  PHE   A C   
624  O O   . PHE   A 77  ? 0.3338 0.3732 0.4924 0.0820  0.0556  0.0748  83  PHE   A O   
625  C CB  . PHE   A 77  ? 0.2723 0.3275 0.4861 0.0984  0.0629  0.1106  83  PHE   A CB  
626  C CG  . PHE   A 77  ? 0.3095 0.3417 0.5337 0.1053  0.0780  0.1035  83  PHE   A CG  
627  C CD1 . PHE   A 77  ? 0.3403 0.3598 0.5744 0.1091  0.0828  0.1076  83  PHE   A CD1 
628  C CD2 . PHE   A 77  ? 0.3446 0.3661 0.5658 0.1064  0.0878  0.0909  83  PHE   A CD2 
629  C CE1 . PHE   A 77  ? 0.3750 0.3722 0.6196 0.1148  0.0985  0.1007  83  PHE   A CE1 
630  C CE2 . PHE   A 77  ? 0.3575 0.3571 0.5873 0.1112  0.1032  0.0832  83  PHE   A CE2 
631  C CZ  . PHE   A 77  ? 0.3771 0.3646 0.6193 0.1155  0.1089  0.0882  83  PHE   A CZ  
632  N N   . VAL   A 78  ? 0.2615 0.2710 0.4188 0.0839  0.0633  0.0671  84  VAL   A N   
633  C CA  . VAL   A 78  ? 0.2507 0.2461 0.3902 0.0792  0.0668  0.0502  84  VAL   A CA  
634  C C   . VAL   A 78  ? 0.2630 0.2391 0.4108 0.0833  0.0818  0.0433  84  VAL   A C   
635  O O   . VAL   A 78  ? 0.2671 0.2319 0.4221 0.0858  0.0865  0.0451  84  VAL   A O   
636  C CB  . VAL   A 78  ? 0.2414 0.2299 0.3595 0.0713  0.0586  0.0418  84  VAL   A CB  
637  C CG1 . VAL   A 78  ? 0.2655 0.2414 0.3658 0.0656  0.0613  0.0262  84  VAL   A CG1 
638  C CG2 . VAL   A 78  ? 0.2445 0.2505 0.3554 0.0669  0.0459  0.0479  84  VAL   A CG2 
639  N N   . GLU   A 79  ? 0.2617 0.2330 0.4055 0.0823  0.0891  0.0338  85  GLU   A N   
640  C CA  . GLU   A 79  ? 0.3111 0.2638 0.4607 0.0843  0.1051  0.0248  85  GLU   A CA  
641  C C   . GLU   A 79  ? 0.3421 0.2747 0.4752 0.0775  0.1076  0.0123  85  GLU   A C   
642  O O   . GLU   A 79  ? 0.3371 0.2710 0.4505 0.0700  0.0970  0.0073  85  GLU   A O   
643  C CB  . GLU   A 79  ? 0.3702 0.3243 0.5167 0.0830  0.1117  0.0171  85  GLU   A CB  
644  C CG  . GLU   A 79  ? 0.5176 0.4642 0.6374 0.0724  0.1093  0.0016  85  GLU   A CG  
645  C CD  . GLU   A 79  ? 0.7003 0.6555 0.8133 0.0694  0.1093  -0.0029 85  GLU   A CD  
646  O OE1 . GLU   A 79  ? 0.7408 0.6929 0.8648 0.0728  0.1221  -0.0055 85  GLU   A OE1 
647  O OE2 . GLU   A 79  ? 0.7518 0.7160 0.8487 0.0635  0.0974  -0.0041 85  GLU   A OE2 
648  N N   . ALA   A 80  ? 0.3606 0.2748 0.5031 0.0799  0.1226  0.0074  86  ALA   A N   
649  C CA  . ALA   A 80  ? 0.4171 0.3112 0.5450 0.0725  0.1273  -0.0050 86  ALA   A CA  
650  C C   . ALA   A 80  ? 0.4669 0.3584 0.5687 0.0611  0.1237  -0.0192 86  ALA   A C   
651  O O   . ALA   A 80  ? 0.4928 0.3893 0.5903 0.0593  0.1259  -0.0238 86  ALA   A O   
652  C CB  . ALA   A 80  ? 0.4367 0.3109 0.5783 0.0758  0.1467  -0.0100 86  ALA   A CB  
653  N N   . SER   A 81  ? 0.4695 0.3552 0.5541 0.0531  0.1169  -0.0249 87  SER   A N   
654  C CA  . SER   A 81  ? 0.4678 0.3520 0.5281 0.0413  0.1126  -0.0368 87  SER   A CA  
655  C C   . SER   A 81  ? 0.4733 0.3396 0.5227 0.0328  0.1187  -0.0470 87  SER   A C   
656  O O   . SER   A 81  ? 0.4870 0.3415 0.5479 0.0367  0.1269  -0.0453 87  SER   A O   
657  C CB  . SER   A 81  ? 0.4792 0.3790 0.5294 0.0391  0.0951  -0.0312 87  SER   A CB  
658  O OG  . SER   A 81  ? 0.4732 0.3718 0.5242 0.0396  0.0886  -0.0264 87  SER   A OG  
659  N N   . GLU   A 82  ? 0.4827 0.3484 0.5101 0.0208  0.1138  -0.0563 88  GLU   A N   
660  C CA  . GLU   A 82  ? 0.4798 0.3322 0.4947 0.0108  0.1170  -0.0651 88  GLU   A CA  
661  C C   . GLU   A 82  ? 0.4175 0.2724 0.4360 0.0136  0.1072  -0.0570 88  GLU   A C   
662  O O   . GLU   A 82  ? 0.4200 0.2627 0.4343 0.0084  0.1115  -0.0617 88  GLU   A O   
663  C CB  . GLU   A 82  ? 0.5494 0.4064 0.5406 -0.0032 0.1108  -0.0737 88  GLU   A CB  
664  C CG  . GLU   A 82  ? 0.6697 0.5224 0.6535 -0.0094 0.1215  -0.0837 88  GLU   A CG  
665  C CD  . GLU   A 82  ? 0.8050 0.6708 0.7713 -0.0186 0.1118  -0.0859 88  GLU   A CD  
666  O OE1 . GLU   A 82  ? 0.8488 0.7173 0.8136 -0.0195 0.1170  -0.0893 88  GLU   A OE1 
667  O OE2 . GLU   A 82  ? 0.8241 0.6978 0.7795 -0.0248 0.0991  -0.0833 88  GLU   A OE2 
668  N N   . TYR   A 83  ? 0.3822 0.2525 0.4082 0.0213  0.0951  -0.0452 89  TYR   A N   
669  C CA  . TYR   A 83  ? 0.3447 0.2187 0.3725 0.0227  0.0857  -0.0382 89  TYR   A CA  
670  C C   . TYR   A 83  ? 0.3162 0.1904 0.3633 0.0330  0.0876  -0.0273 89  TYR   A C   
671  O O   . TYR   A 83  ? 0.3107 0.1829 0.3592 0.0329  0.0838  -0.0234 89  TYR   A O   
672  C CB  . TYR   A 83  ? 0.3283 0.2193 0.3488 0.0215  0.0710  -0.0335 89  TYR   A CB  
673  C CG  . TYR   A 83  ? 0.3258 0.2183 0.3282 0.0109  0.0674  -0.0419 89  TYR   A CG  
674  C CD1 . TYR   A 83  ? 0.3679 0.2663 0.3651 0.0091  0.0675  -0.0446 89  TYR   A CD1 
675  C CD2 . TYR   A 83  ? 0.3403 0.2288 0.3312 0.0017  0.0645  -0.0467 89  TYR   A CD2 
676  C CE1 . TYR   A 83  ? 0.3913 0.2926 0.3723 -0.0013 0.0636  -0.0506 89  TYR   A CE1 
677  C CE2 . TYR   A 83  ? 0.3730 0.2659 0.3484 -0.0087 0.0600  -0.0520 89  TYR   A CE2 
678  C CZ  . TYR   A 83  ? 0.4098 0.3083 0.3801 -0.0105 0.0601  -0.0542 89  TYR   A CZ  
679  O OH  . TYR   A 83  ? 0.4557 0.3602 0.4111 -0.0213 0.0550  -0.0578 89  TYR   A OH  
680  N N   . TYR   A 84  ? 0.3200 0.1992 0.3826 0.0419  0.0921  -0.0206 90  TYR   A N   
681  C CA  . TYR   A 84  ? 0.2986 0.1808 0.3816 0.0516  0.0932  -0.0076 90  TYR   A CA  
682  C C   . TYR   A 84  ? 0.3334 0.2101 0.4347 0.0593  0.1069  -0.0053 90  TYR   A C   
683  O O   . TYR   A 84  ? 0.3525 0.2327 0.4513 0.0589  0.1100  -0.0099 90  TYR   A O   
684  C CB  . TYR   A 84  ? 0.2783 0.1819 0.3648 0.0555  0.0798  0.0042  90  TYR   A CB  
685  C CG  . TYR   A 84  ? 0.2451 0.1560 0.3176 0.0496  0.0669  0.0039  90  TYR   A CG  
686  C CD1 . TYR   A 84  ? 0.2444 0.1522 0.3182 0.0488  0.0640  0.0076  90  TYR   A CD1 
687  C CD2 . TYR   A 84  ? 0.2350 0.1558 0.2948 0.0452  0.0585  0.0004  90  TYR   A CD2 
688  C CE1 . TYR   A 84  ? 0.2397 0.1542 0.3022 0.0435  0.0534  0.0071  90  TYR   A CE1 
689  C CE2 . TYR   A 84  ? 0.2306 0.1574 0.2803 0.0405  0.0484  0.0002  90  TYR   A CE2 
690  C CZ  . TYR   A 84  ? 0.2235 0.1469 0.2744 0.0396  0.0462  0.0030  90  TYR   A CZ  
691  O OH  . TYR   A 84  ? 0.2184 0.1477 0.2608 0.0351  0.0374  0.0027  90  TYR   A OH  
692  N N   . PRO   A 85  ? 0.3483 0.2200 0.4696 0.0670  0.1135  0.0041  91  PRO   A N   
693  C CA  . PRO   A 85  ? 0.3536 0.2240 0.4974 0.0764  0.1256  0.0100  91  PRO   A CA  
694  C C   . PRO   A 85  ? 0.3610 0.2555 0.5140 0.0822  0.1161  0.0227  91  PRO   A C   
695  O O   . PRO   A 85  ? 0.3516 0.2614 0.4943 0.0790  0.1011  0.0272  91  PRO   A O   
696  C CB  . PRO   A 85  ? 0.3730 0.2338 0.5364 0.0828  0.1325  0.0196  91  PRO   A CB  
697  C CG  . PRO   A 85  ? 0.3753 0.2441 0.5299 0.0793  0.1183  0.0255  91  PRO   A CG  
698  C CD  . PRO   A 85  ? 0.3473 0.2157 0.4737 0.0681  0.1101  0.0115  91  PRO   A CD  
699  N N   . ALA   A 86  ? 0.3687 0.2675 0.5426 0.0906  0.1249  0.0296  92  ALA   A N   
700  C CA  . ALA   A 86  ? 0.3530 0.2764 0.5374 0.0956  0.1159  0.0432  92  ALA   A CA  
701  C C   . ALA   A 86  ? 0.3347 0.2699 0.5296 0.0988  0.1063  0.0598  92  ALA   A C   
702  O O   . ALA   A 86  ? 0.3506 0.2751 0.5582 0.1026  0.1126  0.0650  92  ALA   A O   
703  C CB  . ALA   A 86  ? 0.3457 0.2711 0.5538 0.1045  0.1285  0.0487  92  ALA   A CB  
704  N N   . ARG   A 87  ? 0.3031 0.2580 0.4887 0.0952  0.0912  0.0659  93  ARG   A N   
705  C CA  . ARG   A 87  ? 0.2870 0.2530 0.4771 0.0950  0.0815  0.0792  93  ARG   A CA  
706  C C   . ARG   A 87  ? 0.2785 0.2687 0.4610 0.0909  0.0675  0.0860  93  ARG   A C   
707  O O   . ARG   A 87  ? 0.2930 0.2892 0.4661 0.0883  0.0654  0.0794  93  ARG   A O   
708  C CB  . ARG   A 87  ? 0.3043 0.2555 0.4764 0.0882  0.0786  0.0694  93  ARG   A CB  
709  C CG  . ARG   A 87  ? 0.3132 0.2695 0.4588 0.0788  0.0673  0.0586  93  ARG   A CG  
710  C CD  . ARG   A 87  ? 0.3108 0.2506 0.4400 0.0725  0.0675  0.0464  93  ARG   A CD  
711  N NE  . ARG   A 87  ? 0.3114 0.2589 0.4221 0.0650  0.0556  0.0424  93  ARG   A NE  
712  C CZ  . ARG   A 87  ? 0.3415 0.2946 0.4380 0.0604  0.0502  0.0350  93  ARG   A CZ  
713  N NH1 . ARG   A 87  ? 0.3292 0.2837 0.4262 0.0619  0.0543  0.0312  93  ARG   A NH1 
714  N NH2 . ARG   A 87  ? 0.2606 0.2183 0.3436 0.0544  0.0412  0.0320  93  ARG   A NH2 
715  N N   . TYR   A 88  ? 0.2784 0.2817 0.4635 0.0891  0.0583  0.0982  94  TYR   A N   
716  C CA  . TYR   A 88  ? 0.2807 0.3054 0.4559 0.0828  0.0457  0.1029  94  TYR   A CA  
717  C C   . TYR   A 88  ? 0.2470 0.2655 0.3982 0.0741  0.0387  0.0913  94  TYR   A C   
718  O O   . TYR   A 88  ? 0.2605 0.2706 0.4089 0.0725  0.0379  0.0911  94  TYR   A O   
719  C CB  . TYR   A 88  ? 0.2836 0.3285 0.4741 0.0838  0.0397  0.1231  94  TYR   A CB  
720  C CG  . TYR   A 88  ? 0.2804 0.3392 0.4951 0.0915  0.0440  0.1371  94  TYR   A CG  
721  C CD1 . TYR   A 88  ? 0.2884 0.3660 0.5016 0.0891  0.0393  0.1396  94  TYR   A CD1 
722  C CD2 . TYR   A 88  ? 0.2921 0.3438 0.5323 0.1014  0.0541  0.1469  94  TYR   A CD2 
723  C CE1 . TYR   A 88  ? 0.2996 0.3913 0.5362 0.0961  0.0433  0.1529  94  TYR   A CE1 
724  C CE2 . TYR   A 88  ? 0.3034 0.3682 0.5687 0.1092  0.0590  0.1603  94  TYR   A CE2 
725  C CZ  . TYR   A 88  ? 0.3159 0.4011 0.5791 0.1066  0.0535  0.1630  94  TYR   A CZ  
726  O OH  . TYR   A 88  ? 0.3450 0.4447 0.6340 0.1143  0.0584  0.1767  94  TYR   A OH  
727  N N   . GLN   A 89  ? 0.2113 0.2336 0.3461 0.0687  0.0341  0.0817  95  GLN   A N   
728  C CA  . GLN   A 89  ? 0.2016 0.2200 0.3157 0.0607  0.0275  0.0717  95  GLN   A CA  
729  C C   . GLN   A 89  ? 0.1884 0.2270 0.2983 0.0547  0.0180  0.0795  95  GLN   A C   
730  O O   . GLN   A 89  ? 0.1953 0.2494 0.3090 0.0541  0.0157  0.0853  95  GLN   A O   
731  C CB  . GLN   A 89  ? 0.2044 0.2134 0.3042 0.0582  0.0291  0.0570  95  GLN   A CB  
732  C CG  . GLN   A 89  ? 0.1967 0.2021 0.2789 0.0511  0.0231  0.0483  95  GLN   A CG  
733  C CD  . GLN   A 89  ? 0.1891 0.1819 0.2593 0.0489  0.0255  0.0350  95  GLN   A CD  
734  O OE1 . GLN   A 89  ? 0.2134 0.1936 0.2850 0.0511  0.0326  0.0294  95  GLN   A OE1 
735  N NE2 . GLN   A 89  ? 0.2030 0.1994 0.2609 0.0436  0.0198  0.0300  95  GLN   A NE2 
736  N N   . SER   A 90  ? 0.1698 0.2089 0.2714 0.0491  0.0130  0.0793  96  SER   A N   
737  C CA  . SER   A 90  ? 0.1570 0.2139 0.2527 0.0415  0.0053  0.0852  96  SER   A CA  
738  C C   . SER   A 90  ? 0.1697 0.2250 0.2472 0.0344  0.0022  0.0728  96  SER   A C   
739  O O   . SER   A 90  ? 0.1807 0.2208 0.2502 0.0353  0.0046  0.0610  96  SER   A O   
740  C CB  . SER   A 90  ? 0.1939 0.2539 0.2918 0.0387  0.0024  0.0928  96  SER   A CB  
741  O OG  . SER   A 90  ? 0.2491 0.2923 0.3370 0.0373  0.0038  0.0817  96  SER   A OG  
742  N N   . HIS   A 91  ? 0.1748 0.2463 0.2465 0.0268  -0.0030 0.0764  97  HIS   A N   
743  C CA  . HIS   A 91  ? 0.1682 0.2391 0.2244 0.0193  -0.0050 0.0661  97  HIS   A CA  
744  C C   . HIS   A 91  ? 0.1534 0.2155 0.2060 0.0226  -0.0022 0.0570  97  HIS   A C   
745  O O   . HIS   A 91  ? 0.1613 0.2144 0.2033 0.0197  -0.0020 0.0464  97  HIS   A O   
746  C CB  . HIS   A 91  ? 0.1841 0.2448 0.2312 0.0154  -0.0054 0.0587  97  HIS   A CB  
747  C CG  . HIS   A 91  ? 0.2085 0.2786 0.2571 0.0105  -0.0083 0.0670  97  HIS   A CG  
748  N ND1 . HIS   A 91  ? 0.2334 0.3152 0.2728 0.0001  -0.0112 0.0671  97  HIS   A ND1 
749  C CD2 . HIS   A 91  ? 0.2266 0.2962 0.2848 0.0142  -0.0082 0.0758  97  HIS   A CD2 
750  C CE1 . HIS   A 91  ? 0.2367 0.3257 0.2792 -0.0030 -0.0134 0.0759  97  HIS   A CE1 
751  N NE2 . HIS   A 91  ? 0.2417 0.3238 0.2961 0.0057  -0.0120 0.0819  97  HIS   A NE2 
752  N N   . LEU   A 92  ? 0.1462 0.2121 0.2079 0.0280  0.0001  0.0613  98  LEU   A N   
753  C CA  . LEU   A 92  ? 0.1545 0.2130 0.2131 0.0307  0.0031  0.0534  98  LEU   A CA  
754  C C   . LEU   A 92  ? 0.1430 0.2157 0.1988 0.0262  0.0008  0.0554  98  LEU   A C   
755  O O   . LEU   A 92  ? 0.1457 0.2351 0.2088 0.0246  -0.0014 0.0660  98  LEU   A O   
756  C CB  . LEU   A 92  ? 0.1718 0.2234 0.2428 0.0396  0.0090  0.0557  98  LEU   A CB  
757  C CG  . LEU   A 92  ? 0.1962 0.2387 0.2634 0.0420  0.0133  0.0466  98  LEU   A CG  
758  C CD1 . LEU   A 92  ? 0.2008 0.2278 0.2556 0.0397  0.0135  0.0352  98  LEU   A CD1 
759  C CD2 . LEU   A 92  ? 0.2232 0.2604 0.3039 0.0498  0.0209  0.0491  98  LEU   A CD2 
760  N N   . MET   A 93  ? 0.1536 0.2203 0.1992 0.0236  0.0012  0.0461  99  MET   A N   
761  C CA  . MET   A 93  ? 0.1450 0.2226 0.1864 0.0187  -0.0003 0.0462  99  MET   A CA  
762  C C   . MET   A 93  ? 0.1581 0.2300 0.2011 0.0235  0.0032  0.0421  99  MET   A C   
763  O O   . MET   A 93  ? 0.1757 0.2327 0.2144 0.0260  0.0054  0.0342  99  MET   A O   
764  C CB  . MET   A 93  ? 0.1557 0.2296 0.1835 0.0106  -0.0020 0.0384  99  MET   A CB  
765  C CG  . MET   A 93  ? 0.1548 0.2341 0.1798 0.0045  -0.0044 0.0411  99  MET   A CG  
766  S SD  . MET   A 93  ? 0.2053 0.2772 0.2166 -0.0044 -0.0036 0.0306  99  MET   A SD  
767  C CE  . MET   A 93  ? 0.2554 0.3065 0.2670 0.0033  -0.0014 0.0226  99  MET   A CE  
768  N N   . LEU   A 94  ? 0.1389 0.2231 0.1877 0.0239  0.0037  0.0474  100 LEU   A N   
769  C CA  . LEU   A 94  ? 0.1517 0.2310 0.2016 0.0278  0.0076  0.0432  100 LEU   A CA  
770  C C   . LEU   A 94  ? 0.1365 0.2206 0.1769 0.0215  0.0059  0.0393  100 LEU   A C   
771  O O   . LEU   A 94  ? 0.1491 0.2459 0.1864 0.0147  0.0025  0.0430  100 LEU   A O   
772  C CB  . LEU   A 94  ? 0.1746 0.2635 0.2411 0.0344  0.0113  0.0520  100 LEU   A CB  
773  C CG  . LEU   A 94  ? 0.2315 0.3144 0.3107 0.0419  0.0153  0.0564  100 LEU   A CG  
774  C CD1 . LEU   A 94  ? 0.2595 0.3508 0.3571 0.0491  0.0210  0.0646  100 LEU   A CD1 
775  C CD2 . LEU   A 94  ? 0.2626 0.3239 0.3353 0.0445  0.0196  0.0455  100 LEU   A CD2 
776  N N   . ALA   A 95  ? 0.1471 0.2214 0.1825 0.0229  0.0086  0.0321  101 ALA   A N   
777  C CA  . ALA   A 95  ? 0.1460 0.2237 0.1737 0.0178  0.0078  0.0288  101 ALA   A CA  
778  C C   . ALA   A 95  ? 0.1357 0.2095 0.1657 0.0219  0.0122  0.0259  101 ALA   A C   
779  O O   . ALA   A 95  ? 0.1447 0.2097 0.1792 0.0275  0.0161  0.0240  101 ALA   A O   
780  C CB  . ALA   A 95  ? 0.1545 0.2205 0.1696 0.0128  0.0059  0.0210  101 ALA   A CB  
781  N N   . VAL   A 96  ? 0.1363 0.2157 0.1619 0.0181  0.0121  0.0248  102 VAL   A N   
782  C CA  . VAL   A 96  ? 0.1454 0.2210 0.1704 0.0201  0.0161  0.0210  102 VAL   A CA  
783  C C   . VAL   A 96  ? 0.1689 0.2300 0.1811 0.0169  0.0150  0.0130  102 VAL   A C   
784  O O   . VAL   A 96  ? 0.1880 0.2480 0.1924 0.0116  0.0117  0.0114  102 VAL   A O   
785  C CB  . VAL   A 96  ? 0.1418 0.2313 0.1683 0.0170  0.0162  0.0243  102 VAL   A CB  
786  C CG1 . VAL   A 96  ? 0.1569 0.2421 0.1807 0.0177  0.0205  0.0194  102 VAL   A CG1 
787  C CG2 . VAL   A 96  ? 0.1314 0.2379 0.1728 0.0202  0.0167  0.0343  102 VAL   A CG2 
788  N N   . GLY   A 97  ? 0.1646 0.2155 0.1759 0.0198  0.0182  0.0086  103 GLY   A N   
789  C CA  . GLY   A 97  ? 0.1775 0.2172 0.1779 0.0163  0.0165  0.0030  103 GLY   A CA  
790  C C   . GLY   A 97  ? 0.1983 0.2290 0.1979 0.0183  0.0206  -0.0013 103 GLY   A C   
791  O O   . GLY   A 97  ? 0.2195 0.2496 0.2271 0.0229  0.0252  -0.0008 103 GLY   A O   
792  N N   . HIS   A 98  ? 0.2130 0.2366 0.2027 0.0139  0.0191  -0.0055 104 HIS   A N   
793  C CA  . HIS   A 98  ? 0.2290 0.2446 0.2149 0.0130  0.0227  -0.0104 104 HIS   A CA  
794  C C   . HIS   A 98  ? 0.2199 0.2279 0.2062 0.0141  0.0211  -0.0112 104 HIS   A C   
795  O O   . HIS   A 98  ? 0.2223 0.2293 0.2066 0.0128  0.0154  -0.0091 104 HIS   A O   
796  C CB  . HIS   A 98  ? 0.2327 0.2467 0.2072 0.0063  0.0210  -0.0131 104 HIS   A CB  
797  C CG  . HIS   A 98  ? 0.2398 0.2475 0.2082 0.0028  0.0254  -0.0187 104 HIS   A CG  
798  N ND1 . HIS   A 98  ? 0.2474 0.2544 0.2180 0.0038  0.0339  -0.0230 104 HIS   A ND1 
799  C CD2 . HIS   A 98  ? 0.2569 0.2589 0.2176 -0.0021 0.0229  -0.0208 104 HIS   A CD2 
800  C CE1 . HIS   A 98  ? 0.2605 0.2602 0.2231 -0.0014 0.0370  -0.0288 104 HIS   A CE1 
801  N NE2 . HIS   A 98  ? 0.2549 0.2524 0.2110 -0.0054 0.0298  -0.0272 104 HIS   A NE2 
802  N N   . SER   A 99  ? 0.2206 0.2227 0.2096 0.0161  0.0267  -0.0143 105 SER   A N   
803  C CA  . SER   A 99  ? 0.2286 0.2233 0.2177 0.0165  0.0259  -0.0155 105 SER   A CA  
804  C C   . SER   A 99  ? 0.2767 0.2636 0.2642 0.0152  0.0338  -0.0215 105 SER   A C   
805  O O   . SER   A 99  ? 0.3081 0.2945 0.3045 0.0199  0.0414  -0.0218 105 SER   A O   
806  C CB  . SER   A 99  ? 0.2289 0.2263 0.2285 0.0223  0.0245  -0.0101 105 SER   A CB  
807  O OG  . SER   A 99  ? 0.2498 0.2398 0.2504 0.0230  0.0247  -0.0112 105 SER   A OG  
808  N N   . GLU   A 100 ? 0.2415 0.2225 0.2187 0.0087  0.0328  -0.0260 106 GLU   A N   
809  C CA  . GLU   A 100 ? 0.2815 0.2539 0.2548 0.0052  0.0413  -0.0334 106 GLU   A CA  
810  C C   . GLU   A 100 ? 0.3122 0.2779 0.2825 0.0027  0.0388  -0.0345 106 GLU   A C   
811  O O   . GLU   A 100 ? 0.3193 0.2876 0.2915 0.0043  0.0309  -0.0296 106 GLU   A O   
812  C CB  . GLU   A 100 ? 0.3097 0.2834 0.2713 -0.0029 0.0442  -0.0387 106 GLU   A CB  
813  C CG  . GLU   A 100 ? 0.2802 0.2582 0.2302 -0.0108 0.0352  -0.0369 106 GLU   A CG  
814  C CD  . GLU   A 100 ? 0.2766 0.2568 0.2138 -0.0204 0.0371  -0.0412 106 GLU   A CD  
815  O OE1 . GLU   A 100 ? 0.3443 0.3199 0.2710 -0.0293 0.0403  -0.0472 106 GLU   A OE1 
816  O OE2 . GLU   A 100 ? 0.2715 0.2586 0.2084 -0.0202 0.0349  -0.0382 106 GLU   A OE2 
817  N N   . PRO   A 101 ? 0.3737 0.3296 0.3416 -0.0002 0.0472  -0.0414 107 PRO   A N   
818  C CA  . PRO   A 101 ? 0.3814 0.3307 0.3454 -0.0039 0.0458  -0.0434 107 PRO   A CA  
819  C C   . PRO   A 101 ? 0.3572 0.3123 0.3095 -0.0124 0.0360  -0.0419 107 PRO   A C   
820  O O   . PRO   A 101 ? 0.3873 0.3466 0.3296 -0.0198 0.0351  -0.0439 107 PRO   A O   
821  C CB  . PRO   A 101 ? 0.4114 0.3490 0.3716 -0.0085 0.0582  -0.0529 107 PRO   A CB  
822  C CG  . PRO   A 101 ? 0.4240 0.3613 0.3953 -0.0011 0.0669  -0.0528 107 PRO   A CG  
823  C CD  . PRO   A 101 ? 0.3883 0.3379 0.3564 -0.0014 0.0595  -0.0485 107 PRO   A CD  
824  N N   . GLY   A 102 ? 0.2777 0.2346 0.2334 -0.0106 0.0288  -0.0370 108 GLY   A N   
825  C CA  . GLY   A 102 ? 0.2739 0.2377 0.2248 -0.0156 0.0189  -0.0325 108 GLY   A CA  
826  C C   . GLY   A 102 ? 0.2304 0.2015 0.1898 -0.0089 0.0120  -0.0247 108 GLY   A C   
827  O O   . GLY   A 102 ? 0.2280 0.2033 0.1882 -0.0104 0.0052  -0.0202 108 GLY   A O   
828  N N   . ASP   A 103 ? 0.2116 0.1846 0.1774 -0.0021 0.0142  -0.0231 109 ASP   A N   
829  C CA  . ASP   A 103 ? 0.1998 0.1788 0.1721 0.0026  0.0090  -0.0170 109 ASP   A CA  
830  C C   . ASP   A 103 ? 0.1875 0.1655 0.1680 0.0078  0.0077  -0.0143 109 ASP   A C   
831  O O   . ASP   A 103 ? 0.1774 0.1596 0.1622 0.0099  0.0037  -0.0103 109 ASP   A O   
832  C CB  . ASP   A 103 ? 0.1921 0.1753 0.1670 0.0059  0.0115  -0.0162 109 ASP   A CB  
833  C CG  . ASP   A 103 ? 0.2009 0.1872 0.1676 0.0003  0.0107  -0.0173 109 ASP   A CG  
834  O OD1 . ASP   A 103 ? 0.1933 0.1816 0.1555 -0.0046 0.0054  -0.0150 109 ASP   A OD1 
835  O OD2 . ASP   A 103 ? 0.1939 0.1814 0.1598 0.0007  0.0156  -0.0196 109 ASP   A OD2 
836  N N   . CYS   A 104 ? 0.1709 0.1430 0.1537 0.0093  0.0116  -0.0166 110 CYS   A N   
837  C CA  . CYS   A 104 ? 0.1770 0.1488 0.1669 0.0132  0.0100  -0.0135 110 CYS   A CA  
838  C C   . CYS   A 104 ? 0.1752 0.1493 0.1643 0.0107  0.0039  -0.0113 110 CYS   A C   
839  O O   . CYS   A 104 ? 0.1784 0.1522 0.1624 0.0055  0.0015  -0.0123 110 CYS   A O   
840  C CB  . CYS   A 104 ? 0.1731 0.1370 0.1648 0.0141  0.0152  -0.0162 110 CYS   A CB  
841  S SG  . CYS   A 104 ? 0.2177 0.1795 0.2178 0.0203  0.0236  -0.0158 110 CYS   A SG  
842  N N   . GLY   A 105 ? 0.1648 0.1422 0.1599 0.0139  0.0017  -0.0078 111 GLY   A N   
843  C CA  . GLY   A 105 ? 0.1609 0.1403 0.1581 0.0124  -0.0025 -0.0056 111 GLY   A CA  
844  C C   . GLY   A 105 ? 0.1539 0.1377 0.1528 0.0125  -0.0046 -0.0032 111 GLY   A C   
845  O O   . GLY   A 105 ? 0.1553 0.1403 0.1588 0.0125  -0.0064 -0.0011 111 GLY   A O   
846  N N   . GLY   A 106 ? 0.1543 0.1399 0.1501 0.0123  -0.0037 -0.0035 112 GLY   A N   
847  C CA  . GLY   A 106 ? 0.1578 0.1464 0.1551 0.0120  -0.0049 -0.0013 112 GLY   A CA  
848  C C   . GLY   A 106 ? 0.1379 0.1281 0.1396 0.0138  -0.0034 -0.0008 112 GLY   A C   
849  O O   . GLY   A 106 ? 0.1371 0.1289 0.1391 0.0154  -0.0016 -0.0013 112 GLY   A O   
850  N N   . ILE   A 107 ? 0.1367 0.1267 0.1420 0.0130  -0.0036 0.0004  113 ILE   A N   
851  C CA  . ILE   A 107 ? 0.1351 0.1261 0.1427 0.0126  -0.0011 -0.0005 113 ILE   A CA  
852  C C   . ILE   A 107 ? 0.1316 0.1261 0.1361 0.0110  0.0007  -0.0011 113 ILE   A C   
853  O O   . ILE   A 107 ? 0.1364 0.1307 0.1393 0.0101  0.0005  -0.0006 113 ILE   A O   
854  C CB  . ILE   A 107 ? 0.1349 0.1229 0.1488 0.0119  0.0000  0.0000  113 ILE   A CB  
855  C CG1 . ILE   A 107 ? 0.1612 0.1481 0.1790 0.0131  -0.0012 0.0005  113 ILE   A CG1 
856  C CG2 . ILE   A 107 ? 0.1551 0.1428 0.1699 0.0095  0.0044  -0.0024 113 ILE   A CG2 
857  C CD1 . ILE   A 107 ? 0.2002 0.1851 0.2271 0.0133  0.0001  0.0022  113 ILE   A CD1 
858  N N   . LEU   A 108 ? 0.1206 0.1195 0.1243 0.0100  0.0020  -0.0014 114 LEU   A N   
859  C CA  . LEU   A 108 ? 0.1289 0.1330 0.1298 0.0065  0.0037  -0.0018 114 LEU   A CA  
860  C C   . LEU   A 108 ? 0.1213 0.1236 0.1228 0.0022  0.0068  -0.0043 114 LEU   A C   
861  O O   . LEU   A 108 ? 0.1320 0.1339 0.1353 0.0018  0.0073  -0.0048 114 LEU   A O   
862  C CB  . LEU   A 108 ? 0.1296 0.1422 0.1301 0.0069  0.0030  0.0009  114 LEU   A CB  
863  C CG  . LEU   A 108 ? 0.1331 0.1548 0.1306 0.0015  0.0040  0.0018  114 LEU   A CG  
864  C CD1 . LEU   A 108 ? 0.1558 0.1791 0.1507 0.0004  0.0044  0.0014  114 LEU   A CD1 
865  C CD2 . LEU   A 108 ? 0.1485 0.1812 0.1485 0.0019  0.0025  0.0072  114 LEU   A CD2 
866  N N   . ARG   A 109 ? 0.1323 0.1325 0.1321 -0.0016 0.0098  -0.0063 115 ARG   A N   
867  C CA  . ARG   A 109 ? 0.1503 0.1467 0.1507 -0.0066 0.0151  -0.0102 115 ARG   A CA  
868  C C   . ARG   A 109 ? 0.1540 0.1539 0.1482 -0.0138 0.0182  -0.0127 115 ARG   A C   
869  O O   . ARG   A 109 ? 0.1516 0.1546 0.1430 -0.0141 0.0167  -0.0112 115 ARG   A O   
870  C CB  . ARG   A 109 ? 0.1659 0.1525 0.1738 -0.0039 0.0176  -0.0107 115 ARG   A CB  
871  C CG  . ARG   A 109 ? 0.1662 0.1494 0.1747 -0.0033 0.0177  -0.0091 115 ARG   A CG  
872  C CD  . ARG   A 109 ? 0.1797 0.1547 0.1987 -0.0002 0.0198  -0.0071 115 ARG   A CD  
873  N NE  . ARG   A 109 ? 0.1881 0.1650 0.2111 0.0049  0.0141  -0.0026 115 ARG   A NE  
874  C CZ  . ARG   A 109 ? 0.1899 0.1648 0.2212 0.0075  0.0143  -0.0009 115 ARG   A CZ  
875  N NH1 . ARG   A 109 ? 0.1983 0.1693 0.2348 0.0061  0.0204  -0.0042 115 ARG   A NH1 
876  N NH2 . ARG   A 109 ? 0.1944 0.1721 0.2279 0.0106  0.0087  0.0034  115 ARG   A NH2 
877  N N   . CYS   A 110 ? 0.1804 0.1796 0.1720 -0.0208 0.0234  -0.0170 116 CYS   A N   
878  C CA  . CYS   A 110 ? 0.2235 0.2255 0.2077 -0.0303 0.0277  -0.0207 116 CYS   A CA  
879  C C   . CYS   A 110 ? 0.2569 0.2466 0.2437 -0.0341 0.0366  -0.0271 116 CYS   A C   
880  O O   . CYS   A 110 ? 0.2435 0.2241 0.2395 -0.0284 0.0387  -0.0271 116 CYS   A O   
881  C CB  . CYS   A 110 ? 0.2077 0.2229 0.1846 -0.0377 0.0261  -0.0199 116 CYS   A CB  
882  S SG  . CYS   A 110 ? 0.2058 0.2199 0.1823 -0.0422 0.0298  -0.0235 116 CYS   A SG  
883  N N   . GLN   A 111 ? 0.2912 0.2809 0.2702 -0.0450 0.0429  -0.0326 117 GLN   A N   
884  C CA  . GLN   A 111 ? 0.3231 0.2998 0.3049 -0.0497 0.0537  -0.0399 117 GLN   A CA  
885  C C   . GLN   A 111 ? 0.3295 0.3025 0.3155 -0.0500 0.0582  -0.0433 117 GLN   A C   
886  O O   . GLN   A 111 ? 0.3742 0.3346 0.3684 -0.0491 0.0669  -0.0475 117 GLN   A O   
887  C CB  . GLN   A 111 ? 0.3823 0.3594 0.3530 -0.0634 0.0607  -0.0466 117 GLN   A CB  
888  C CG  . GLN   A 111 ? 0.4399 0.4304 0.3986 -0.0749 0.0599  -0.0489 117 GLN   A CG  
889  C CD  . GLN   A 111 ? 0.5348 0.5280 0.4807 -0.0905 0.0662  -0.0553 117 GLN   A CD  
890  O OE1 . GLN   A 111 ? 0.5574 0.5639 0.4958 -0.0951 0.0603  -0.0514 117 GLN   A OE1 
891  N NE2 . GLN   A 111 ? 0.5353 0.5166 0.4785 -0.0997 0.0787  -0.0654 117 GLN   A NE2 
892  N N   . HIS   A 112 ? 0.2704 0.2542 0.2523 -0.0505 0.0525  -0.0408 118 HIS   A N   
893  C CA  . HIS   A 112 ? 0.2584 0.2406 0.2426 -0.0521 0.0563  -0.0439 118 HIS   A CA  
894  C C   . HIS   A 112 ? 0.2626 0.2414 0.2589 -0.0400 0.0520  -0.0391 118 HIS   A C   
895  O O   . HIS   A 112 ? 0.2927 0.2690 0.2931 -0.0401 0.0556  -0.0414 118 HIS   A O   
896  C CB  . HIS   A 112 ? 0.2454 0.2424 0.2184 -0.0608 0.0524  -0.0430 118 HIS   A CB  
897  C CG  . HIS   A 112 ? 0.2960 0.2991 0.2561 -0.0746 0.0559  -0.0471 118 HIS   A CG  
898  N ND1 . HIS   A 112 ? 0.2924 0.3098 0.2461 -0.0770 0.0482  -0.0410 118 HIS   A ND1 
899  C CD2 . HIS   A 112 ? 0.3417 0.3398 0.2944 -0.0876 0.0668  -0.0568 118 HIS   A CD2 
900  C CE1 . HIS   A 112 ? 0.3442 0.3650 0.2866 -0.0913 0.0537  -0.0466 118 HIS   A CE1 
901  N NE2 . HIS   A 112 ? 0.3663 0.3753 0.3068 -0.0987 0.0652  -0.0567 118 HIS   A NE2 
902  N N   . GLY   A 113 ? 0.2331 0.2134 0.2338 -0.0306 0.0439  -0.0321 119 GLY   A N   
903  C CA  . GLY   A 113 ? 0.2089 0.1874 0.2190 -0.0211 0.0393  -0.0275 119 GLY   A CA  
904  C C   . GLY   A 113 ? 0.1806 0.1668 0.1882 -0.0156 0.0294  -0.0210 119 GLY   A C   
905  O O   . GLY   A 113 ? 0.1725 0.1640 0.1744 -0.0168 0.0263  -0.0192 119 GLY   A O   
906  N N   . VAL   A 114 ? 0.1641 0.1508 0.1766 -0.0099 0.0253  -0.0179 120 VAL   A N   
907  C CA  . VAL   A 114 ? 0.1612 0.1531 0.1721 -0.0048 0.0176  -0.0127 120 VAL   A CA  
908  C C   . VAL   A 114 ? 0.1489 0.1500 0.1533 -0.0080 0.0151  -0.0111 120 VAL   A C   
909  O O   . VAL   A 114 ? 0.1479 0.1517 0.1508 -0.0121 0.0169  -0.0123 120 VAL   A O   
910  C CB  . VAL   A 114 ? 0.1540 0.1428 0.1717 0.0009  0.0148  -0.0104 120 VAL   A CB  
911  C CG1 . VAL   A 114 ? 0.1688 0.1610 0.1839 0.0048  0.0088  -0.0066 120 VAL   A CG1 
912  C CG2 . VAL   A 114 ? 0.1682 0.1508 0.1940 0.0042  0.0159  -0.0092 120 VAL   A CG2 
913  N N   . VAL   A 115 ? 0.1395 0.1462 0.1410 -0.0065 0.0115  -0.0077 121 VAL   A N   
914  C CA  . VAL   A 115 ? 0.1483 0.1655 0.1466 -0.0087 0.0089  -0.0038 121 VAL   A CA  
915  C C   . VAL   A 115 ? 0.1492 0.1669 0.1516 -0.0023 0.0051  0.0007  121 VAL   A C   
916  O O   . VAL   A 115 ? 0.1562 0.1800 0.1592 -0.0032 0.0036  0.0045  121 VAL   A O   
917  C CB  . VAL   A 115 ? 0.1579 0.1819 0.1526 -0.0110 0.0082  -0.0022 121 VAL   A CB  
918  C CG1 . VAL   A 115 ? 0.1851 0.2222 0.1799 -0.0117 0.0048  0.0046  121 VAL   A CG1 
919  C CG2 . VAL   A 115 ? 0.1823 0.2056 0.1716 -0.0193 0.0128  -0.0071 121 VAL   A CG2 
920  N N   . GLY   A 116 ? 0.1414 0.1527 0.1466 0.0037  0.0038  0.0007  122 GLY   A N   
921  C CA  . GLY   A 116 ? 0.1447 0.1545 0.1530 0.0090  0.0017  0.0035  122 GLY   A CA  
922  C C   . GLY   A 116 ? 0.1312 0.1343 0.1399 0.0128  0.0010  0.0020  122 GLY   A C   
923  O O   . GLY   A 116 ? 0.1367 0.1364 0.1446 0.0118  0.0014  -0.0002 122 GLY   A O   
924  N N   . ILE   A 117 ? 0.1298 0.1307 0.1401 0.0165  0.0006  0.0033  123 ILE   A N   
925  C CA  . ILE   A 117 ? 0.1286 0.1238 0.1373 0.0181  0.0003  0.0012  123 ILE   A CA  
926  C C   . ILE   A 117 ? 0.1393 0.1354 0.1483 0.0207  0.0021  0.0022  123 ILE   A C   
927  O O   . ILE   A 117 ? 0.1482 0.1474 0.1615 0.0229  0.0035  0.0054  123 ILE   A O   
928  C CB  . ILE   A 117 ? 0.1446 0.1335 0.1538 0.0183  -0.0005 -0.0002 123 ILE   A CB  
929  C CG1 . ILE   A 117 ? 0.1623 0.1501 0.1742 0.0198  0.0005  0.0013  123 ILE   A CG1 
930  C CG2 . ILE   A 117 ? 0.1588 0.1469 0.1694 0.0162  -0.0019 -0.0008 123 ILE   A CG2 
931  C CD1 . ILE   A 117 ? 0.1866 0.1678 0.1980 0.0190  0.0001  -0.0006 123 ILE   A CD1 
932  N N   . VAL   A 118 ? 0.1419 0.1354 0.1476 0.0204  0.0026  -0.0001 124 VAL   A N   
933  C CA  . VAL   A 118 ? 0.1466 0.1399 0.1529 0.0226  0.0060  -0.0004 124 VAL   A CA  
934  C C   . VAL   A 118 ? 0.1504 0.1378 0.1599 0.0248  0.0089  -0.0010 124 VAL   A C   
935  O O   . VAL   A 118 ? 0.1572 0.1384 0.1638 0.0229  0.0080  -0.0036 124 VAL   A O   
936  C CB  . VAL   A 118 ? 0.1596 0.1504 0.1598 0.0202  0.0063  -0.0038 124 VAL   A CB  
937  C CG1 . VAL   A 118 ? 0.1601 0.1493 0.1609 0.0219  0.0115  -0.0057 124 VAL   A CG1 
938  C CG2 . VAL   A 118 ? 0.1662 0.1621 0.1641 0.0182  0.0041  -0.0028 124 VAL   A CG2 
939  N N   . SER   A 119 ? 0.1496 0.1387 0.1658 0.0287  0.0128  0.0019  125 SER   A N   
940  C CA  . SER   A 119 ? 0.1663 0.1486 0.1877 0.0315  0.0171  0.0021  125 SER   A CA  
941  C C   . SER   A 119 ? 0.1949 0.1747 0.2214 0.0348  0.0242  0.0014  125 SER   A C   
942  O O   . SER   A 119 ? 0.2207 0.1905 0.2487 0.0355  0.0299  -0.0018 125 SER   A O   
943  C CB  . SER   A 119 ? 0.1723 0.1593 0.2007 0.0335  0.0153  0.0086  125 SER   A CB  
944  O OG  . SER   A 119 ? 0.1934 0.1739 0.2288 0.0367  0.0198  0.0104  125 SER   A OG  
945  N N   . THR   A 120 ? 0.1867 0.1745 0.2159 0.0363  0.0250  0.0036  126 THR   A N   
946  C CA  . THR   A 120 ? 0.2036 0.1897 0.2401 0.0400  0.0330  0.0032  126 THR   A CA  
947  C C   . THR   A 120 ? 0.2142 0.2047 0.2449 0.0376  0.0332  0.0001  126 THR   A C   
948  O O   . THR   A 120 ? 0.2094 0.2060 0.2335 0.0343  0.0270  0.0005  126 THR   A O   
949  C CB  . THR   A 120 ? 0.2272 0.2215 0.2800 0.0464  0.0353  0.0131  126 THR   A CB  
950  O OG1 . THR   A 120 ? 0.2343 0.2436 0.2885 0.0458  0.0301  0.0191  126 THR   A OG1 
951  C CG2 . THR   A 120 ? 0.2274 0.2189 0.2861 0.0483  0.0343  0.0179  126 THR   A CG2 
952  N N   . GLY   A 121 ? 0.2320 0.2191 0.2660 0.0392  0.0414  -0.0032 127 GLY   A N   
953  C CA  . GLY   A 121 ? 0.2667 0.2583 0.2952 0.0365  0.0422  -0.0062 127 GLY   A CA  
954  C C   . GLY   A 121 ? 0.2947 0.2853 0.3321 0.0401  0.0525  -0.0075 127 GLY   A C   
955  O O   . GLY   A 121 ? 0.3277 0.3156 0.3783 0.0458  0.0589  -0.0044 127 GLY   A O   
956  N N   . GLY   A 122 ? 0.2822 0.2760 0.3132 0.0366  0.0540  -0.0114 128 GLY   A N   
957  C CA  . GLY   A 122 ? 0.2788 0.2721 0.3167 0.0388  0.0645  -0.0142 128 GLY   A CA  
958  C C   . GLY   A 122 ? 0.2865 0.2950 0.3350 0.0429  0.0638  -0.0066 128 GLY   A C   
959  O O   . GLY   A 122 ? 0.2832 0.3026 0.3381 0.0455  0.0567  0.0023  128 GLY   A O   
960  N N   . ASN   A 123 ? 0.2829 0.2928 0.3338 0.0428  0.0717  -0.0101 129 ASN   A N   
961  C CA  . ASN   A 123 ? 0.2938 0.3191 0.3580 0.0472  0.0728  -0.0024 129 ASN   A CA  
962  C C   . ASN   A 123 ? 0.2550 0.2935 0.3122 0.0435  0.0616  0.0026  129 ASN   A C   
963  O O   . ASN   A 123 ? 0.2309 0.2846 0.2995 0.0466  0.0601  0.0112  129 ASN   A O   
964  C CB  . ASN   A 123 ? 0.3263 0.3566 0.4137 0.0568  0.0771  0.0077  129 ASN   A CB  
965  C CG  . ASN   A 123 ? 0.4026 0.4193 0.5007 0.0613  0.0912  0.0031  129 ASN   A CG  
966  O OD1 . ASN   A 123 ? 0.4429 0.4498 0.5335 0.0575  0.1000  -0.0076 129 ASN   A OD1 
967  N ND2 . ASN   A 123 ? 0.3878 0.4039 0.5043 0.0690  0.0948  0.0113  129 ASN   A ND2 
968  N N   . GLY   A 124 ? 0.2343 0.2678 0.2737 0.0365  0.0545  -0.0025 130 GLY   A N   
969  C CA  . GLY   A 124 ? 0.2190 0.2621 0.2517 0.0325  0.0453  0.0012  130 GLY   A CA  
970  C C   . GLY   A 124 ? 0.1724 0.2209 0.2092 0.0340  0.0382  0.0082  130 GLY   A C   
971  O O   . GLY   A 124 ? 0.2028 0.2597 0.2354 0.0303  0.0321  0.0112  130 GLY   A O   
972  N N   . LEU   A 125 ? 0.1643 0.2065 0.2068 0.0378  0.0391  0.0096  131 LEU   A N   
973  C CA  . LEU   A 125 ? 0.1654 0.2118 0.2101 0.0380  0.0325  0.0156  131 LEU   A CA  
974  C C   . LEU   A 125 ? 0.1900 0.2233 0.2248 0.0356  0.0296  0.0102  131 LEU   A C   
975  O O   . LEU   A 125 ? 0.2192 0.2404 0.2495 0.0353  0.0338  0.0035  131 LEU   A O   
976  C CB  . LEU   A 125 ? 0.1678 0.2201 0.2300 0.0447  0.0359  0.0241  131 LEU   A CB  
977  C CG  . LEU   A 125 ? 0.1682 0.2370 0.2441 0.0478  0.0383  0.0323  131 LEU   A CG  
978  C CD1 . LEU   A 125 ? 0.1850 0.2561 0.2815 0.0561  0.0447  0.0403  131 LEU   A CD1 
979  C CD2 . LEU   A 125 ? 0.1678 0.2531 0.2403 0.0423  0.0297  0.0388  131 LEU   A CD2 
980  N N   . VAL   A 126 ? 0.1605 0.1965 0.1913 0.0329  0.0229  0.0126  132 VAL   A N   
981  C CA  . VAL   A 126 ? 0.1705 0.1962 0.1947 0.0311  0.0201  0.0090  132 VAL   A CA  
982  C C   . VAL   A 126 ? 0.1619 0.1932 0.1925 0.0324  0.0171  0.0154  132 VAL   A C   
983  O O   . VAL   A 126 ? 0.1581 0.2012 0.1906 0.0304  0.0140  0.0206  132 VAL   A O   
984  C CB  . VAL   A 126 ? 0.1678 0.1901 0.1799 0.0255  0.0156  0.0046  132 VAL   A CB  
985  C CG1 . VAL   A 126 ? 0.1730 0.2050 0.1835 0.0221  0.0121  0.0077  132 VAL   A CG1 
986  C CG2 . VAL   A 126 ? 0.1707 0.1842 0.1785 0.0241  0.0127  0.0022  132 VAL   A CG2 
987  N N   . GLY   A 127 ? 0.1556 0.1788 0.1882 0.0345  0.0179  0.0149  133 GLY   A N   
988  C CA  . GLY   A 127 ? 0.1524 0.1804 0.1899 0.0349  0.0150  0.0209  133 GLY   A CA  
989  C C   . GLY   A 127 ? 0.1556 0.1760 0.1848 0.0314  0.0114  0.0165  133 GLY   A C   
990  O O   . GLY   A 127 ? 0.1809 0.1904 0.2047 0.0309  0.0124  0.0105  133 GLY   A O   
991  N N   . PHE   A 128 ? 0.1409 0.1682 0.1694 0.0283  0.0076  0.0199  134 PHE   A N   
992  C CA  . PHE   A 128 ? 0.1468 0.1684 0.1690 0.0247  0.0050  0.0162  134 PHE   A CA  
993  C C   . PHE   A 128 ? 0.1512 0.1752 0.1775 0.0248  0.0039  0.0207  134 PHE   A C   
994  O O   . PHE   A 128 ? 0.1527 0.1882 0.1837 0.0238  0.0028  0.0277  134 PHE   A O   
995  C CB  . PHE   A 128 ? 0.1530 0.1794 0.1687 0.0190  0.0027  0.0144  134 PHE   A CB  
996  C CG  . PHE   A 128 ? 0.1486 0.1744 0.1605 0.0182  0.0034  0.0113  134 PHE   A CG  
997  C CD1 . PHE   A 128 ? 0.1480 0.1645 0.1553 0.0181  0.0034  0.0063  134 PHE   A CD1 
998  C CD2 . PHE   A 128 ? 0.1570 0.1930 0.1699 0.0169  0.0036  0.0145  134 PHE   A CD2 
999  C CE1 . PHE   A 128 ? 0.1558 0.1725 0.1594 0.0167  0.0037  0.0045  134 PHE   A CE1 
1000 C CE2 . PHE   A 128 ? 0.1624 0.1979 0.1714 0.0157  0.0043  0.0118  134 PHE   A CE2 
1001 C CZ  . PHE   A 128 ? 0.1580 0.1834 0.1621 0.0156  0.0044  0.0068  134 PHE   A CZ  
1002 N N   . ALA   A 129 ? 0.1458 0.1603 0.1707 0.0252  0.0040  0.0175  135 ALA   A N   
1003 C CA  . ALA   A 129 ? 0.1508 0.1668 0.1782 0.0242  0.0027  0.0211  135 ALA   A CA  
1004 C C   . ALA   A 129 ? 0.1456 0.1667 0.1672 0.0179  0.0004  0.0195  135 ALA   A C   
1005 O O   . ALA   A 129 ? 0.1460 0.1607 0.1628 0.0160  0.0004  0.0135  135 ALA   A O   
1006 C CB  . ALA   A 129 ? 0.1499 0.1541 0.1772 0.0261  0.0040  0.0175  135 ALA   A CB  
1007 N N   . ASP   A 130 ? 0.1378 0.1705 0.1603 0.0141  -0.0011 0.0251  136 ASP   A N   
1008 C CA  . ASP   A 130 ? 0.1551 0.1921 0.1709 0.0064  -0.0017 0.0224  136 ASP   A CA  
1009 C C   . ASP   A 130 ? 0.1531 0.1839 0.1677 0.0049  -0.0014 0.0196  136 ASP   A C   
1010 O O   . ASP   A 130 ? 0.1665 0.1949 0.1855 0.0081  -0.0019 0.0230  136 ASP   A O   
1011 C CB  . ASP   A 130 ? 0.1766 0.2299 0.1929 0.0010  -0.0037 0.0301  136 ASP   A CB  
1012 C CG  . ASP   A 130 ? 0.2359 0.2946 0.2437 -0.0091 -0.0033 0.0268  136 ASP   A CG  
1013 O OD1 . ASP   A 130 ? 0.2054 0.2595 0.2074 -0.0123 -0.0010 0.0196  136 ASP   A OD1 
1014 O OD2 . ASP   A 130 ? 0.2908 0.3571 0.2975 -0.0144 -0.0045 0.0309  136 ASP   A OD2 
1015 N N   . VAL   A 131 ? 0.1462 0.1737 0.1558 0.0003  0.0003  0.0133  137 VAL   A N   
1016 C CA  . VAL   A 131 ? 0.1557 0.1791 0.1647 -0.0021 0.0014  0.0104  137 VAL   A CA  
1017 C C   . VAL   A 131 ? 0.1564 0.1859 0.1598 -0.0114 0.0037  0.0080  137 VAL   A C   
1018 O O   . VAL   A 131 ? 0.1495 0.1763 0.1523 -0.0143 0.0056  0.0050  137 VAL   A O   
1019 C CB  . VAL   A 131 ? 0.1461 0.1580 0.1570 0.0015  0.0027  0.0048  137 VAL   A CB  
1020 C CG1 . VAL   A 131 ? 0.1570 0.1628 0.1713 0.0083  0.0009  0.0064  137 VAL   A CG1 
1021 C CG2 . VAL   A 131 ? 0.1609 0.1697 0.1702 -0.0002 0.0052  -0.0001 137 VAL   A CG2 
1022 N N   . ARG   A 132 ? 0.1584 0.1966 0.1571 -0.0171 0.0039  0.0090  138 ARG   A N   
1023 C CA  . ARG   A 132 ? 0.1594 0.2025 0.1507 -0.0280 0.0074  0.0047  138 ARG   A CA  
1024 C C   . ARG   A 132 ? 0.1780 0.2300 0.1662 -0.0349 0.0065  0.0083  138 ARG   A C   
1025 O O   . ARG   A 132 ? 0.1864 0.2395 0.1680 -0.0444 0.0109  0.0027  138 ARG   A O   
1026 C CB  . ARG   A 132 ? 0.1703 0.2215 0.1562 -0.0338 0.0077  0.0049  138 ARG   A CB  
1027 C CG  . ARG   A 132 ? 0.1649 0.2059 0.1524 -0.0289 0.0099  -0.0002 138 ARG   A CG  
1028 C CD  . ARG   A 132 ? 0.1708 0.2205 0.1525 -0.0356 0.0101  0.0003  138 ARG   A CD  
1029 N NE  . ARG   A 132 ? 0.1743 0.2358 0.1595 -0.0321 0.0045  0.0097  138 ARG   A NE  
1030 C CZ  . ARG   A 132 ? 0.1900 0.2614 0.1732 -0.0354 0.0031  0.0128  138 ARG   A CZ  
1031 N NH1 . ARG   A 132 ? 0.1982 0.2703 0.1734 -0.0444 0.0066  0.0071  138 ARG   A NH1 
1032 N NH2 . ARG   A 132 ? 0.2041 0.2855 0.1939 -0.0303 -0.0012 0.0220  138 ARG   A NH2 
1033 N N   . ASP   A 133 ? 0.1658 0.2238 0.1589 -0.0309 0.0017  0.0175  139 ASP   A N   
1034 C CA  . ASP   A 133 ? 0.1777 0.2449 0.1684 -0.0376 0.0002  0.0226  139 ASP   A CA  
1035 C C   . ASP   A 133 ? 0.1836 0.2409 0.1768 -0.0348 0.0019  0.0190  139 ASP   A C   
1036 O O   . ASP   A 133 ? 0.1964 0.2599 0.1868 -0.0412 0.0015  0.0218  139 ASP   A O   
1037 C CB  . ASP   A 133 ? 0.1910 0.2699 0.1883 -0.0343 -0.0055 0.0360  139 ASP   A CB  
1038 C CG  . ASP   A 133 ? 0.2260 0.2942 0.2338 -0.0213 -0.0066 0.0390  139 ASP   A CG  
1039 O OD1 . ASP   A 133 ? 0.2210 0.2778 0.2307 -0.0145 -0.0048 0.0329  139 ASP   A OD1 
1040 O OD2 . ASP   A 133 ? 0.2501 0.3212 0.2642 -0.0186 -0.0088 0.0474  139 ASP   A OD2 
1041 N N   . LEU   A 134 ? 0.1625 0.2059 0.1607 -0.0265 0.0036  0.0136  140 LEU   A N   
1042 C CA  . LEU   A 134 ? 0.1602 0.1953 0.1617 -0.0236 0.0048  0.0111  140 LEU   A CA  
1043 C C   . LEU   A 134 ? 0.1642 0.1957 0.1623 -0.0298 0.0107  0.0021  140 LEU   A C   
1044 O O   . LEU   A 134 ? 0.1647 0.1868 0.1666 -0.0258 0.0138  -0.0039 140 LEU   A O   
1045 C CB  . LEU   A 134 ? 0.1609 0.1850 0.1691 -0.0132 0.0035  0.0104  140 LEU   A CB  
1046 C CG  . LEU   A 134 ? 0.1733 0.1984 0.1857 -0.0067 -0.0001 0.0176  140 LEU   A CG  
1047 C CD1 . LEU   A 134 ? 0.1826 0.1964 0.1989 0.0010  0.0000  0.0145  140 LEU   A CD1 
1048 C CD2 . LEU   A 134 ? 0.2009 0.2306 0.2162 -0.0071 -0.0022 0.0255  140 LEU   A CD2 
1049 N N   . LEU   A 135 ? 0.1641 0.2039 0.1555 -0.0402 0.0127  0.0016  141 LEU   A N   
1050 C CA  . LEU   A 135 ? 0.1762 0.2128 0.1638 -0.0479 0.0205  -0.0081 141 LEU   A CA  
1051 C C   . LEU   A 135 ? 0.1883 0.2157 0.1825 -0.0439 0.0240  -0.0125 141 LEU   A C   
1052 O O   . LEU   A 135 ? 0.1991 0.2194 0.1963 -0.0447 0.0312  -0.0205 141 LEU   A O   
1053 C CB  . LEU   A 135 ? 0.1977 0.2462 0.1743 -0.0624 0.0226  -0.0083 141 LEU   A CB  
1054 C CG  . LEU   A 135 ? 0.2116 0.2735 0.1816 -0.0681 0.0180  -0.0015 141 LEU   A CG  
1055 C CD1 . LEU   A 135 ? 0.2360 0.3107 0.1933 -0.0855 0.0209  -0.0031 141 LEU   A CD1 
1056 C CD2 . LEU   A 135 ? 0.2339 0.2920 0.2039 -0.0656 0.0194  -0.0051 141 LEU   A CD2 
1057 N N   . TRP   A 136 ? 0.1734 0.2005 0.1717 -0.0389 0.0193  -0.0069 142 TRP   A N   
1058 C CA  . TRP   A 136 ? 0.1762 0.1966 0.1811 -0.0354 0.0214  -0.0098 142 TRP   A CA  
1059 C C   . TRP   A 136 ? 0.1780 0.1891 0.1917 -0.0269 0.0226  -0.0129 142 TRP   A C   
1060 O O   . TRP   A 136 ? 0.1913 0.1982 0.2119 -0.0251 0.0257  -0.0159 142 TRP   A O   
1061 C CB  . TRP   A 136 ? 0.1783 0.2005 0.1846 -0.0331 0.0161  -0.0029 142 TRP   A CB  
1062 C CG  . TRP   A 136 ? 0.1658 0.1863 0.1746 -0.0254 0.0100  0.0038  142 TRP   A CG  
1063 C CD1 . TRP   A 136 ? 0.1793 0.2068 0.1858 -0.0261 0.0059  0.0117  142 TRP   A CD1 
1064 C CD2 . TRP   A 136 ? 0.1764 0.1882 0.1914 -0.0165 0.0079  0.0038  142 TRP   A CD2 
1065 N NE1 . TRP   A 136 ? 0.1980 0.2200 0.2096 -0.0173 0.0027  0.0154  142 TRP   A NE1 
1066 C CE2 . TRP   A 136 ? 0.1793 0.1915 0.1947 -0.0122 0.0039  0.0101  142 TRP   A CE2 
1067 C CE3 . TRP   A 136 ? 0.1858 0.1906 0.2064 -0.0126 0.0093  -0.0005 142 TRP   A CE3 
1068 C CZ2 . TRP   A 136 ? 0.1970 0.2014 0.2164 -0.0050 0.0021  0.0104  142 TRP   A CZ2 
1069 C CZ3 . TRP   A 136 ? 0.2144 0.2134 0.2383 -0.0062 0.0061  0.0011  142 TRP   A CZ3 
1070 C CH2 . TRP   A 136 ? 0.2055 0.2036 0.2278 -0.0029 0.0030  0.0056  142 TRP   A CH2 
1071 N N   . LEU   A 137 ? 0.1682 0.1770 0.1825 -0.0217 0.0197  -0.0113 143 LEU   A N   
1072 C CA  . LEU   A 137 ? 0.1890 0.1906 0.2113 -0.0150 0.0205  -0.0132 143 LEU   A CA  
1073 C C   . LEU   A 137 ? 0.2215 0.2195 0.2486 -0.0177 0.0287  -0.0197 143 LEU   A C   
1074 O O   . LEU   A 137 ? 0.2336 0.2268 0.2706 -0.0124 0.0300  -0.0199 143 LEU   A O   
1075 C CB  . LEU   A 137 ? 0.1834 0.1842 0.2039 -0.0111 0.0170  -0.0110 143 LEU   A CB  
1076 C CG  . LEU   A 137 ? 0.1843 0.1857 0.2038 -0.0063 0.0106  -0.0053 143 LEU   A CG  
1077 C CD1 . LEU   A 137 ? 0.2042 0.2061 0.2213 -0.0038 0.0087  -0.0038 143 LEU   A CD1 
1078 C CD2 . LEU   A 137 ? 0.1985 0.1944 0.2239 -0.0011 0.0083  -0.0045 143 LEU   A CD2 
1079 N N   . ASP   A 138 ? 0.2461 0.2468 0.2669 -0.0264 0.0348  -0.0245 144 ASP   A N   
1080 C CA  . ASP   A 138 ? 0.2755 0.2708 0.3010 -0.0298 0.0451  -0.0319 144 ASP   A CA  
1081 C C   . ASP   A 138 ? 0.3232 0.3176 0.3546 -0.0322 0.0513  -0.0356 144 ASP   A C   
1082 O O   . ASP   A 138 ? 0.3514 0.3406 0.3887 -0.0347 0.0615  -0.0421 144 ASP   A O   
1083 C CB  . ASP   A 138 ? 0.2874 0.2854 0.3015 -0.0404 0.0504  -0.0372 144 ASP   A CB  
1084 C CG  . ASP   A 138 ? 0.3349 0.3346 0.3434 -0.0398 0.0463  -0.0348 144 ASP   A CG  
1085 O OD1 . ASP   A 138 ? 0.3472 0.3436 0.3616 -0.0306 0.0410  -0.0304 144 ASP   A OD1 
1086 O OD2 . ASP   A 138 ? 0.4248 0.4301 0.4223 -0.0494 0.0481  -0.0371 144 ASP   A OD2 
1087 N N   . GLU   A 139 ? 0.3296 0.3284 0.3602 -0.0317 0.0464  -0.0318 145 GLU   A N   
1088 C CA  . GLU   A 139 ? 0.3634 0.3624 0.3990 -0.0348 0.0523  -0.0353 145 GLU   A CA  
1089 C C   . GLU   A 139 ? 0.3659 0.3651 0.4104 -0.0277 0.0467  -0.0300 145 GLU   A C   
1090 O O   . GLU   A 139 ? 0.3736 0.3729 0.4177 -0.0218 0.0381  -0.0240 145 GLU   A O   
1091 C CB  . GLU   A 139 ? 0.4225 0.4283 0.4450 -0.0462 0.0539  -0.0373 145 GLU   A CB  
1092 C CG  . GLU   A 139 ? 0.5263 0.5390 0.5407 -0.0460 0.0433  -0.0291 145 GLU   A CG  
1093 C CD  . GLU   A 139 ? 0.6241 0.6462 0.6246 -0.0574 0.0427  -0.0282 145 GLU   A CD  
1094 O OE1 . GLU   A 139 ? 0.6088 0.6371 0.6053 -0.0582 0.0358  -0.0208 145 GLU   A OE1 
1095 O OE2 . GLU   A 139 ? 0.6736 0.6970 0.6674 -0.0661 0.0494  -0.0345 145 GLU   A OE2 
1096 N N   . SER   B 1   ? 0.2190 0.2254 0.2328 0.0096  -0.0121 0.0395  7   SER   C N   
1097 C CA  . SER   B 1   ? 0.2094 0.2187 0.2315 0.0080  -0.0130 0.0395  7   SER   C CA  
1098 C C   . SER   B 1   ? 0.2044 0.2120 0.2259 0.0063  -0.0129 0.0361  7   SER   C C   
1099 O O   . SER   B 1   ? 0.2240 0.2282 0.2382 0.0062  -0.0132 0.0339  7   SER   C O   
1100 C CB  . SER   B 1   ? 0.2524 0.2641 0.2755 0.0074  -0.0174 0.0415  7   SER   C CB  
1101 O OG  . SER   B 1   ? 0.3039 0.3132 0.3192 0.0062  -0.0209 0.0395  7   SER   C OG  
1102 N N   . GLY   B 2   ? 0.2030 0.2126 0.2318 0.0054  -0.0119 0.0358  8   GLY   C N   
1103 C CA  . GLY   B 2   ? 0.1883 0.1960 0.2166 0.0040  -0.0114 0.0334  8   GLY   C CA  
1104 C C   . GLY   B 2   ? 0.1739 0.1831 0.2090 0.0042  -0.0083 0.0331  8   GLY   C C   
1105 O O   . GLY   B 2   ? 0.1863 0.1968 0.2252 0.0055  -0.0062 0.0336  8   GLY   C O   
1106 N N   . ALA   B 3   ? 0.1619 0.1704 0.1983 0.0029  -0.0078 0.0322  9   ALA   C N   
1107 C CA  . ALA   B 3   ? 0.1624 0.1716 0.2037 0.0034  -0.0044 0.0318  9   ALA   C CA  
1108 C C   . ALA   B 3   ? 0.1537 0.1595 0.1907 0.0030  -0.0030 0.0300  9   ALA   C C   
1109 O O   . ALA   B 3   ? 0.1744 0.1778 0.2067 0.0019  -0.0047 0.0294  9   ALA   C O   
1110 C CB  . ALA   B 3   ? 0.1980 0.2109 0.2484 0.0026  -0.0044 0.0341  9   ALA   C CB  
1111 N N   . ILE   B 4   ? 0.1495 0.1548 0.1877 0.0041  0.0003  0.0291  10  ILE   C N   
1112 C CA  . ILE   B 4   ? 0.1687 0.1708 0.2031 0.0042  0.0023  0.0282  10  ILE   C CA  
1113 C C   . ILE   B 4   ? 0.1597 0.1637 0.2012 0.0034  0.0048  0.0299  10  ILE   C C   
1114 O O   . ILE   B 4   ? 0.1640 0.1706 0.2115 0.0041  0.0063  0.0305  10  ILE   C O   
1115 C CB  . ILE   B 4   ? 0.1583 0.1584 0.1878 0.0065  0.0043  0.0259  10  ILE   C CB  
1116 C CG1 . ILE   B 4   ? 0.1748 0.1745 0.2003 0.0075  0.0022  0.0243  10  ILE   C CG1 
1117 C CG2 . ILE   B 4   ? 0.1806 0.1769 0.2044 0.0070  0.0062  0.0255  10  ILE   C CG2 
1118 C CD1 . ILE   B 4   ? 0.1752 0.1741 0.1985 0.0096  0.0034  0.0218  10  ILE   C CD1 
1119 N N   . TYR   B 5   ? 0.1600 0.1623 0.2017 0.0020  0.0056  0.0308  11  TYR   C N   
1120 C CA  . TYR   B 5   ? 0.1699 0.1738 0.2192 0.0012  0.0085  0.0326  11  TYR   C CA  
1121 C C   . TYR   B 5   ? 0.1693 0.1692 0.2137 0.0023  0.0129  0.0324  11  TYR   C C   
1122 O O   . TYR   B 5   ? 0.1935 0.1900 0.2340 0.0014  0.0127  0.0326  11  TYR   C O   
1123 C CB  . TYR   B 5   ? 0.1789 0.1849 0.2350 -0.0018 0.0058  0.0343  11  TYR   C CB  
1124 C CG  . TYR   B 5   ? 0.1751 0.1856 0.2360 -0.0025 0.0015  0.0351  11  TYR   C CG  
1125 C CD1 . TYR   B 5   ? 0.1677 0.1828 0.2378 -0.0020 0.0023  0.0369  11  TYR   C CD1 
1126 C CD2 . TYR   B 5   ? 0.1882 0.1978 0.2435 -0.0030 -0.0029 0.0341  11  TYR   C CD2 
1127 C CE1 . TYR   B 5   ? 0.1860 0.2049 0.2597 -0.0021 -0.0016 0.0380  11  TYR   C CE1 
1128 C CE2 . TYR   B 5   ? 0.2063 0.2193 0.2641 -0.0030 -0.0066 0.0351  11  TYR   C CE2 
1129 C CZ  . TYR   B 5   ? 0.1998 0.2174 0.2668 -0.0025 -0.0060 0.0372  11  TYR   C CZ  
1130 O OH  . TYR   B 5   ? 0.2209 0.2416 0.2896 -0.0021 -0.0096 0.0387  11  TYR   C OH  
1131 N N   . VAL   B 6   ? 0.1818 0.1811 0.2250 0.0046  0.0167  0.0318  12  VAL   C N   
1132 C CA  . VAL   B 6   ? 0.1958 0.1907 0.2323 0.0064  0.0210  0.0317  12  VAL   C CA  
1133 C C   . VAL   B 6   ? 0.1946 0.1907 0.2372 0.0072  0.0262  0.0332  12  VAL   C C   
1134 O O   . VAL   B 6   ? 0.1814 0.1803 0.2285 0.0081  0.0269  0.0325  12  VAL   C O   
1135 C CB  . VAL   B 6   ? 0.2139 0.2060 0.2399 0.0093  0.0202  0.0287  12  VAL   C CB  
1136 C CG1 . VAL   B 6   ? 0.2196 0.2144 0.2481 0.0105  0.0194  0.0266  12  VAL   C CG1 
1137 C CG2 . VAL   B 6   ? 0.2377 0.2252 0.2557 0.0117  0.0244  0.0288  12  VAL   C CG2 
1138 N N   . GLY   B 7   ? 0.2122 0.2063 0.2560 0.0068  0.0305  0.0354  13  GLY   C N   
1139 C CA  . GLY   B 7   ? 0.2159 0.2112 0.2662 0.0077  0.0362  0.0372  13  GLY   C CA  
1140 C C   . GLY   B 7   ? 0.2099 0.2115 0.2741 0.0059  0.0349  0.0384  13  GLY   C C   
1141 O O   . GLY   B 7   ? 0.2233 0.2280 0.2940 0.0030  0.0304  0.0394  13  GLY   C O   
1142 N N   . ASN   B 8   ? 0.2085 0.2117 0.2763 0.0078  0.0378  0.0380  14  ASN   C N   
1143 C CA  . ASN   B 8   ? 0.2068 0.2160 0.2875 0.0067  0.0363  0.0393  14  ASN   C CA  
1144 C C   . ASN   B 8   ? 0.1965 0.2068 0.2750 0.0077  0.0325  0.0370  14  ASN   C C   
1145 O O   . ASN   B 8   ? 0.1965 0.2098 0.2828 0.0085  0.0334  0.0374  14  ASN   C O   
1146 C CB  . ASN   B 8   ? 0.2346 0.2457 0.3249 0.0078  0.0427  0.0414  14  ASN   C CB  
1147 C CG  . ASN   B 8   ? 0.3180 0.3299 0.4159 0.0057  0.0456  0.0446  14  ASN   C CG  
1148 O OD1 . ASN   B 8   ? 0.3480 0.3651 0.4586 0.0031  0.0431  0.0468  14  ASN   C OD1 
1149 N ND2 . ASN   B 8   ? 0.3426 0.3494 0.4326 0.0069  0.0507  0.0450  14  ASN   C ND2 
1150 N N   . TYR   B 9   ? 0.1659 0.1740 0.2353 0.0075  0.0282  0.0350  15  TYR   C N   
1151 C CA  . TYR   B 9   ? 0.1639 0.1728 0.2313 0.0083  0.0248  0.0329  15  TYR   C CA  
1152 C C   . TYR   B 9   ? 0.1592 0.1698 0.2262 0.0063  0.0190  0.0334  15  TYR   C C   
1153 O O   . TYR   B 9   ? 0.1703 0.1790 0.2327 0.0049  0.0172  0.0336  15  TYR   C O   
1154 C CB  . TYR   B 9   ? 0.1731 0.1775 0.2290 0.0106  0.0257  0.0293  15  TYR   C CB  
1155 C CG  . TYR   B 9   ? 0.1887 0.1905 0.2423 0.0132  0.0311  0.0279  15  TYR   C CG  
1156 C CD1 . TYR   B 9   ? 0.2121 0.2157 0.2731 0.0142  0.0338  0.0277  15  TYR   C CD1 
1157 C CD2 . TYR   B 9   ? 0.2241 0.2213 0.2675 0.0148  0.0338  0.0269  15  TYR   C CD2 
1158 C CE1 . TYR   B 9   ? 0.2501 0.2507 0.3081 0.0168  0.0392  0.0261  15  TYR   C CE1 
1159 C CE2 . TYR   B 9   ? 0.2594 0.2537 0.2988 0.0175  0.0389  0.0254  15  TYR   C CE2 
1160 C CZ  . TYR   B 9   ? 0.2911 0.2870 0.3375 0.0185  0.0415  0.0247  15  TYR   C CZ  
1161 O OH  . TYR   B 9   ? 0.3633 0.3559 0.4054 0.0214  0.0468  0.0229  15  TYR   C OH  
1162 N N   . ARG   B 10  ? 0.1426 0.1559 0.2135 0.0064  0.0163  0.0336  16  ARG   C N   
1163 C CA  . ARG   B 10  ? 0.1374 0.1517 0.2062 0.0052  0.0112  0.0339  16  ARG   C CA  
1164 C C   . ARG   B 10  ? 0.1383 0.1512 0.2029 0.0069  0.0109  0.0317  16  ARG   C C   
1165 O O   . ARG   B 10  ? 0.1453 0.1592 0.2148 0.0082  0.0127  0.0315  16  ARG   C O   
1166 C CB  . ARG   B 10  ? 0.1487 0.1679 0.2269 0.0041  0.0085  0.0370  16  ARG   C CB  
1167 C CG  . ARG   B 10  ? 0.1603 0.1805 0.2360 0.0038  0.0039  0.0376  16  ARG   C CG  
1168 C CD  . ARG   B 10  ? 0.1619 0.1868 0.2461 0.0030  0.0009  0.0408  16  ARG   C CD  
1169 N NE  . ARG   B 10  ? 0.1669 0.1932 0.2514 0.0042  -0.0014 0.0423  16  ARG   C NE  
1170 C CZ  . ARG   B 10  ? 0.1922 0.2183 0.2711 0.0039  -0.0055 0.0429  16  ARG   C CZ  
1171 N NH1 . ARG   B 10  ? 0.2144 0.2384 0.2863 0.0023  -0.0081 0.0414  16  ARG   C NH1 
1172 N NH2 . ARG   B 10  ? 0.1937 0.2209 0.2733 0.0054  -0.0064 0.0449  16  ARG   C NH2 
1173 N N   . VAL   B 11  ? 0.1360 0.1464 0.1922 0.0069  0.0087  0.0299  17  VAL   C N   
1174 C CA  . VAL   B 11  ? 0.1300 0.1394 0.1832 0.0083  0.0082  0.0277  17  VAL   C CA  
1175 C C   . VAL   B 11  ? 0.1419 0.1527 0.1953 0.0076  0.0051  0.0292  17  VAL   C C   
1176 O O   . VAL   B 11  ? 0.1457 0.1556 0.1942 0.0066  0.0026  0.0296  17  VAL   C O   
1177 C CB  . VAL   B 11  ? 0.1459 0.1517 0.1902 0.0092  0.0084  0.0247  17  VAL   C CB  
1178 C CG1 . VAL   B 11  ? 0.1693 0.1746 0.2128 0.0105  0.0079  0.0222  17  VAL   C CG1 
1179 C CG2 . VAL   B 11  ? 0.1729 0.1765 0.2144 0.0101  0.0115  0.0238  17  VAL   C CG2 
1180 N N   . VAL   B 12  ? 0.1289 0.1413 0.1872 0.0083  0.0053  0.0300  18  VAL   C N   
1181 C CA  A VAL   B 12  ? 0.1325 0.1460 0.1905 0.0082  0.0029  0.0319  18  VAL   C CA  
1182 C CA  B VAL   B 12  ? 0.1504 0.1639 0.2083 0.0081  0.0029  0.0320  18  VAL   C CA  
1183 C C   . VAL   B 12  ? 0.1376 0.1505 0.1970 0.0094  0.0042  0.0309  18  VAL   C C   
1184 O O   . VAL   B 12  ? 0.1408 0.1530 0.2034 0.0101  0.0064  0.0287  18  VAL   C O   
1185 C CB  A VAL   B 12  ? 0.1256 0.1423 0.1900 0.0079  0.0017  0.0358  18  VAL   C CB  
1186 C CB  B VAL   B 12  ? 0.1850 0.2019 0.2500 0.0078  0.0020  0.0357  18  VAL   C CB  
1187 C CG1 A VAL   B 12  ? 0.1415 0.1593 0.2049 0.0063  -0.0007 0.0369  18  VAL   C CG1 
1188 C CG1 B VAL   B 12  ? 0.1912 0.2091 0.2550 0.0081  -0.0005 0.0384  18  VAL   C CG1 
1189 C CG2 A VAL   B 12  ? 0.0888 0.1072 0.1625 0.0089  0.0046  0.0367  18  VAL   C CG2 
1190 C CG2 B VAL   B 12  ? 0.2193 0.2373 0.2850 0.0063  0.0007  0.0365  18  VAL   C CG2 
1191 N N   . ASN   B 13  ? 0.1279 0.1409 0.1854 0.0096  0.0029  0.0324  19  ASN   C N   
1192 C CA  . ASN   B 13  ? 0.1214 0.1341 0.1824 0.0105  0.0046  0.0322  19  ASN   C CA  
1193 C C   . ASN   B 13  ? 0.1380 0.1523 0.2080 0.0111  0.0063  0.0344  19  ASN   C C   
1194 O O   . ASN   B 13  ? 0.1327 0.1489 0.2049 0.0111  0.0053  0.0379  19  ASN   C O   
1195 C CB  . ASN   B 13  ? 0.1283 0.1407 0.1858 0.0109  0.0037  0.0345  19  ASN   C CB  
1196 C CG  . ASN   B 13  ? 0.1399 0.1505 0.1892 0.0107  0.0024  0.0325  19  ASN   C CG  
1197 O OD1 . ASN   B 13  ? 0.1497 0.1597 0.1930 0.0100  0.0002  0.0330  19  ASN   C OD1 
1198 N ND2 . ASN   B 13  ? 0.1387 0.1484 0.1884 0.0112  0.0036  0.0299  19  ASN   C ND2 
1199 N N   . ARG   B 14  ? 0.1295 0.1430 0.2051 0.0117  0.0088  0.0323  20  ARG   C N   
1200 C CA  . ARG   B 14  ? 0.1286 0.1429 0.2133 0.0124  0.0110  0.0342  20  ARG   C CA  
1201 C C   . ARG   B 14  ? 0.1409 0.1565 0.2281 0.0131  0.0106  0.0394  20  ARG   C C   
1202 O O   . ARG   B 14  ? 0.1333 0.1506 0.2256 0.0138  0.0108  0.0427  20  ARG   C O   
1203 C CB  . ARG   B 14  ? 0.1229 0.1354 0.2128 0.0128  0.0134  0.0306  20  ARG   C CB  
1204 C CG  . ARG   B 14  ? 0.1262 0.1387 0.2255 0.0137  0.0162  0.0317  20  ARG   C CG  
1205 C CD  . ARG   B 14  ? 0.1379 0.1480 0.2422 0.0138  0.0182  0.0275  20  ARG   C CD  
1206 N NE  . ARG   B 14  ? 0.1396 0.1486 0.2528 0.0147  0.0213  0.0274  20  ARG   C NE  
1207 C CZ  . ARG   B 14  ? 0.1339 0.1427 0.2555 0.0154  0.0233  0.0309  20  ARG   C CZ  
1208 N NH1 . ARG   B 14  ? 0.1504 0.1603 0.2719 0.0154  0.0226  0.0354  20  ARG   C NH1 
1209 N NH2 . ARG   B 14  ? 0.1361 0.1432 0.2659 0.0162  0.0262  0.0300  20  ARG   C NH2 
1210 N N   . HIS   B 15  ? 0.1341 0.1489 0.2175 0.0133  0.0103  0.0404  21  HIS   C N   
1211 C CA  . HIS   B 15  ? 0.1395 0.1549 0.2240 0.0144  0.0105  0.0456  21  HIS   C CA  
1212 C C   . HIS   B 15  ? 0.1553 0.1725 0.2345 0.0145  0.0070  0.0489  21  HIS   C C   
1213 O O   . HIS   B 15  ? 0.1699 0.1878 0.2497 0.0159  0.0067  0.0535  21  HIS   C O   
1214 C CB  . HIS   B 15  ? 0.1411 0.1548 0.2236 0.0148  0.0121  0.0460  21  HIS   C CB  
1215 C CG  . HIS   B 15  ? 0.1408 0.1539 0.2132 0.0144  0.0101  0.0449  21  HIS   C CG  
1216 N ND1 . HIS   B 15  ? 0.1532 0.1654 0.2223 0.0135  0.0095  0.0402  21  HIS   C ND1 
1217 C CD2 . HIS   B 15  ? 0.1532 0.1660 0.2180 0.0152  0.0087  0.0480  21  HIS   C CD2 
1218 C CE1 . HIS   B 15  ? 0.1596 0.1711 0.2201 0.0136  0.0080  0.0407  21  HIS   C CE1 
1219 N NE2 . HIS   B 15  ? 0.1609 0.1724 0.2180 0.0145  0.0074  0.0450  21  HIS   C NE2 
1220 N N   . LEU   B 16  ? 0.1452 0.1631 0.2195 0.0132  0.0044  0.0467  22  LEU   C N   
1221 C CA  . LEU   B 16  ? 0.1585 0.1782 0.2289 0.0129  0.0006  0.0490  22  LEU   C CA  
1222 C C   . LEU   B 16  ? 0.1628 0.1852 0.2400 0.0123  -0.0001 0.0492  22  LEU   C C   
1223 O O   . LEU   B 16  ? 0.1684 0.1927 0.2440 0.0115  -0.0036 0.0504  22  LEU   C O   
1224 C CB  . LEU   B 16  ? 0.1635 0.1816 0.2240 0.0117  -0.0018 0.0466  22  LEU   C CB  
1225 C CG  . LEU   B 16  ? 0.1695 0.1851 0.2233 0.0126  -0.0010 0.0468  22  LEU   C CG  
1226 C CD1 . LEU   B 16  ? 0.1825 0.1961 0.2268 0.0116  -0.0031 0.0440  22  LEU   C CD1 
1227 C CD2 . LEU   B 16  ? 0.1700 0.1860 0.2223 0.0144  -0.0014 0.0516  22  LEU   C CD2 
1228 N N   . ALA   B 17  ? 0.1574 0.1796 0.2418 0.0125  0.0032  0.0476  23  ALA   C N   
1229 C CA  . ALA   B 17  ? 0.1577 0.1822 0.2487 0.0122  0.0036  0.0478  23  ALA   C CA  
1230 C C   . ALA   B 17  ? 0.1683 0.1964 0.2657 0.0132  0.0017  0.0526  23  ALA   C C   
1231 O O   . ALA   B 17  ? 0.1714 0.1995 0.2710 0.0148  0.0021  0.0559  23  ALA   C O   
1232 C CB  . ALA   B 17  ? 0.1706 0.1935 0.2672 0.0128  0.0080  0.0450  23  ALA   C CB  
1233 N N   . THR   B 18  ? 0.1599 0.1909 0.2606 0.0122  -0.0002 0.0533  24  THR   C N   
1234 C CA  . THR   B 18  ? 0.1745 0.2098 0.2822 0.0131  -0.0029 0.0578  24  THR   C CA  
1235 C C   . THR   B 18  ? 0.1544 0.1915 0.2743 0.0145  0.0009  0.0590  24  THR   C C   
1236 O O   . THR   B 18  ? 0.1711 0.2059 0.2930 0.0145  0.0054  0.0559  24  THR   C O   
1237 C CB  . THR   B 18  ? 0.1871 0.2254 0.2939 0.0112  -0.0074 0.0577  24  THR   C CB  
1238 O OG1 . THR   B 18  ? 0.1917 0.2303 0.3031 0.0099  -0.0046 0.0553  24  THR   C OG1 
1239 C CG2 . THR   B 18  ? 0.2036 0.2395 0.2983 0.0098  -0.0110 0.0559  24  THR   C CG2 
1240 N N   . HIS   B 19  ? 0.1694 0.2107 0.2975 0.0159  -0.0012 0.0636  25  HIS   C N   
1241 C CA  . HIS   B 19  ? 0.1780 0.2213 0.3186 0.0173  0.0025  0.0650  25  HIS   C CA  
1242 C C   . HIS   B 19  ? 0.1447 0.1891 0.2887 0.0157  0.0044  0.0621  25  HIS   C C   
1243 O O   . HIS   B 19  ? 0.1585 0.2010 0.3068 0.0164  0.0097  0.0601  25  HIS   C O   
1244 C CB  . HIS   B 19  ? 0.1916 0.2401 0.3410 0.0191  -0.0009 0.0706  25  HIS   C CB  
1245 C CG  . HIS   B 19  ? 0.2037 0.2553 0.3672 0.0204  0.0024  0.0721  25  HIS   C CG  
1246 N ND1 . HIS   B 19  ? 0.2322 0.2813 0.4020 0.0226  0.0079  0.0724  25  HIS   C ND1 
1247 C CD2 . HIS   B 19  ? 0.2200 0.2761 0.3919 0.0195  0.0017  0.0725  25  HIS   C CD2 
1248 C CE1 . HIS   B 19  ? 0.2297 0.2823 0.4116 0.0235  0.0099  0.0738  25  HIS   C CE1 
1249 N NE2 . HIS   B 19  ? 0.2273 0.2844 0.4112 0.0217  0.0066  0.0739  25  HIS   C NE2 
1250 N N   . ASN   B 20  ? 0.1575 0.2039 0.2983 0.0134  0.0006  0.0615  26  ASN   C N   
1251 C CA  . ASN   B 20  ? 0.1712 0.2182 0.3154 0.0119  0.0031  0.0592  26  ASN   C CA  
1252 C C   . ASN   B 20  ? 0.1615 0.2028 0.2980 0.0116  0.0079  0.0546  26  ASN   C C   
1253 O O   . ASN   B 20  ? 0.1475 0.1881 0.2879 0.0120  0.0128  0.0531  26  ASN   C O   
1254 C CB  . ASN   B 20  ? 0.1848 0.2343 0.3273 0.0093  -0.0018 0.0592  26  ASN   C CB  
1255 C CG  . ASN   B 20  ? 0.2578 0.3083 0.4062 0.0078  0.0015  0.0579  26  ASN   C CG  
1256 O OD1 . ASN   B 20  ? 0.2998 0.3543 0.4609 0.0085  0.0036  0.0601  26  ASN   C OD1 
1257 N ND2 . ASN   B 20  ? 0.2875 0.3341 0.4274 0.0061  0.0028  0.0546  26  ASN   C ND2 
1258 N N   . ASP   B 21  ? 0.1535 0.1909 0.2788 0.0113  0.0067  0.0523  27  ASP   C N   
1259 C CA  . ASP   B 21  ? 0.1488 0.1813 0.2673 0.0113  0.0105  0.0480  27  ASP   C CA  
1260 C C   . ASP   B 21  ? 0.1388 0.1696 0.2629 0.0134  0.0156  0.0469  27  ASP   C C   
1261 O O   . ASP   B 21  ? 0.1556 0.1841 0.2790 0.0138  0.0196  0.0440  27  ASP   C O   
1262 C CB  . ASP   B 21  ? 0.1452 0.1745 0.2531 0.0109  0.0084  0.0461  27  ASP   C CB  
1263 C CG  . ASP   B 21  ? 0.1592 0.1883 0.2592 0.0090  0.0045  0.0455  27  ASP   C CG  
1264 O OD1 . ASP   B 21  ? 0.1729 0.2022 0.2728 0.0076  0.0049  0.0445  27  ASP   C OD1 
1265 O OD2 . ASP   B 21  ? 0.1580 0.1865 0.2521 0.0088  0.0013  0.0462  27  ASP   C OD2 
1266 N N   . TRP   B 22  ? 0.1406 0.1721 0.2699 0.0149  0.0155  0.0494  28  TRP   C N   
1267 C CA  . TRP   B 22  ? 0.1518 0.1812 0.2874 0.0168  0.0202  0.0483  28  TRP   C CA  
1268 C C   . TRP   B 22  ? 0.1468 0.1784 0.2923 0.0179  0.0238  0.0494  28  TRP   C C   
1269 O O   . TRP   B 22  ? 0.1547 0.1832 0.3018 0.0191  0.0287  0.0464  28  TRP   C O   
1270 C CB  . TRP   B 22  ? 0.1539 0.1834 0.2937 0.0182  0.0195  0.0514  28  TRP   C CB  
1271 C CG  . TRP   B 22  ? 0.1518 0.1776 0.2837 0.0177  0.0188  0.0491  28  TRP   C CG  
1272 C CD1 . TRP   B 22  ? 0.1663 0.1925 0.2918 0.0170  0.0152  0.0509  28  TRP   C CD1 
1273 C CD2 . TRP   B 22  ? 0.1439 0.1653 0.2743 0.0179  0.0220  0.0445  28  TRP   C CD2 
1274 N NE1 . TRP   B 22  ? 0.1704 0.1930 0.2917 0.0168  0.0163  0.0482  28  TRP   C NE1 
1275 C CE2 . TRP   B 22  ? 0.1672 0.1870 0.2917 0.0171  0.0201  0.0441  28  TRP   C CE2 
1276 C CE3 . TRP   B 22  ? 0.1738 0.1923 0.3077 0.0187  0.0262  0.0407  28  TRP   C CE3 
1277 C CZ2 . TRP   B 22  ? 0.1545 0.1706 0.2784 0.0171  0.0220  0.0402  28  TRP   C CZ2 
1278 C CZ3 . TRP   B 22  ? 0.1813 0.1956 0.3127 0.0185  0.0275  0.0362  28  TRP   C CZ3 
1279 C CH2 . TRP   B 22  ? 0.1701 0.1837 0.2975 0.0176  0.0253  0.0362  28  TRP   C CH2 
1280 N N   . ALA   B 23  ? 0.1511 0.1878 0.3027 0.0174  0.0214  0.0532  29  ALA   C N   
1281 C CA  . ALA   B 23  ? 0.1558 0.1954 0.3183 0.0184  0.0248  0.0547  29  ALA   C CA  
1282 C C   . ALA   B 23  ? 0.1778 0.2158 0.3366 0.0174  0.0283  0.0516  29  ALA   C C   
1283 O O   . ALA   B 23  ? 0.1810 0.2200 0.3474 0.0185  0.0328  0.0520  29  ALA   C O   
1284 C CB  . ALA   B 23  ? 0.1593 0.2055 0.3306 0.0181  0.0204  0.0598  29  ALA   C CB  
1285 N N   . ASN   B 24  ? 0.1725 0.2075 0.3193 0.0156  0.0265  0.0486  30  ASN   C N   
1286 C CA  . ASN   B 24  ? 0.1636 0.1962 0.3049 0.0149  0.0298  0.0459  30  ASN   C CA  
1287 C C   . ASN   B 24  ? 0.1630 0.1896 0.2914 0.0152  0.0308  0.0410  30  ASN   C C   
1288 O O   . ASN   B 24  ? 0.1547 0.1790 0.2740 0.0141  0.0303  0.0391  30  ASN   C O   
1289 C CB  . ASN   B 24  ? 0.1746 0.2101 0.3152 0.0123  0.0259  0.0477  30  ASN   C CB  
1290 C CG  . ASN   B 24  ? 0.1880 0.2298 0.3426 0.0120  0.0251  0.0519  30  ASN   C CG  
1291 O OD1 . ASN   B 24  ? 0.2093 0.2523 0.3714 0.0126  0.0301  0.0526  30  ASN   C OD1 
1292 N ND2 . ASN   B 24  ? 0.1849 0.2308 0.3436 0.0114  0.0192  0.0549  30  ASN   C ND2 
1293 N N   . LEU   B 25  ? 0.1654 0.1895 0.2936 0.0167  0.0318  0.0391  31  LEU   C N   
1294 C CA  . LEU   B 25  ? 0.1638 0.1830 0.2815 0.0168  0.0315  0.0345  31  LEU   C CA  
1295 C C   . LEU   B 25  ? 0.1843 0.1993 0.2945 0.0178  0.0355  0.0303  31  LEU   C C   
1296 O O   . LEU   B 25  ? 0.1894 0.2033 0.3036 0.0195  0.0404  0.0298  31  LEU   C O   
1297 C CB  . LEU   B 25  ? 0.1727 0.1904 0.2948 0.0181  0.0322  0.0337  31  LEU   C CB  
1298 C CG  . LEU   B 25  ? 0.1656 0.1791 0.2795 0.0180  0.0312  0.0289  31  LEU   C CG  
1299 C CD1 . LEU   B 25  ? 0.1734 0.1877 0.2805 0.0162  0.0263  0.0295  31  LEU   C CD1 
1300 C CD2 . LEU   B 25  ? 0.1918 0.2035 0.3123 0.0191  0.0329  0.0278  31  LEU   C CD2 
1301 N N   . VAL   B 26  ? 0.1755 0.1877 0.2745 0.0171  0.0334  0.0275  32  VAL   C N   
1302 C CA  . VAL   B 26  ? 0.1881 0.1957 0.2778 0.0185  0.0364  0.0233  32  VAL   C CA  
1303 C C   . VAL   B 26  ? 0.1993 0.2035 0.2839 0.0192  0.0349  0.0184  32  VAL   C C   
1304 O O   . VAL   B 26  ? 0.2193 0.2199 0.3013 0.0211  0.0380  0.0145  32  VAL   C O   
1305 C CB  . VAL   B 26  ? 0.1936 0.2005 0.2743 0.0174  0.0350  0.0237  32  VAL   C CB  
1306 C CG1 . VAL   B 26  ? 0.2227 0.2244 0.2917 0.0193  0.0374  0.0195  32  VAL   C CG1 
1307 C CG2 . VAL   B 26  ? 0.1834 0.1934 0.2704 0.0164  0.0367  0.0281  32  VAL   C CG2 
1308 N N   . TRP   B 27  ? 0.1703 0.1755 0.2533 0.0178  0.0303  0.0184  33  TRP   C N   
1309 C CA  . TRP   B 27  ? 0.1777 0.1801 0.2570 0.0183  0.0287  0.0138  33  TRP   C CA  
1310 C C   . TRP   B 27  ? 0.1684 0.1732 0.2510 0.0167  0.0249  0.0158  33  TRP   C C   
1311 O O   . TRP   B 27  ? 0.1627 0.1700 0.2441 0.0154  0.0225  0.0194  33  TRP   C O   
1312 C CB  . TRP   B 27  ? 0.1953 0.1946 0.2621 0.0189  0.0277  0.0100  33  TRP   C CB  
1313 C CG  . TRP   B 27  ? 0.2052 0.2028 0.2680 0.0190  0.0245  0.0055  33  TRP   C CG  
1314 C CD1 . TRP   B 27  ? 0.2331 0.2278 0.2956 0.0202  0.0250  0.0002  33  TRP   C CD1 
1315 C CD2 . TRP   B 27  ? 0.1894 0.1883 0.2492 0.0178  0.0202  0.0057  33  TRP   C CD2 
1316 N NE1 . TRP   B 27  ? 0.2467 0.2413 0.3065 0.0197  0.0209  -0.0029 33  TRP   C NE1 
1317 C CE2 . TRP   B 27  ? 0.2112 0.2083 0.2693 0.0183  0.0183  0.0006  33  TRP   C CE2 
1318 C CE3 . TRP   B 27  ? 0.1868 0.1881 0.2452 0.0164  0.0179  0.0095  33  TRP   C CE3 
1319 C CZ2 . TRP   B 27  ? 0.2089 0.2070 0.2648 0.0176  0.0144  -0.0004 33  TRP   C CZ2 
1320 C CZ3 . TRP   B 27  ? 0.2026 0.2040 0.2571 0.0159  0.0145  0.0082  33  TRP   C CZ3 
1321 C CH2 . TRP   B 27  ? 0.2050 0.2053 0.2594 0.0165  0.0129  0.0037  33  TRP   C CH2 
1322 N N   . GLU   B 28  ? 0.1624 0.1661 0.2488 0.0168  0.0244  0.0135  34  GLU   C N   
1323 C CA  . GLU   B 28  ? 0.1703 0.1758 0.2593 0.0156  0.0216  0.0154  34  GLU   C CA  
1324 C C   . GLU   B 28  ? 0.1750 0.1782 0.2647 0.0157  0.0208  0.0108  34  GLU   C C   
1325 O O   . GLU   B 28  ? 0.1705 0.1710 0.2626 0.0166  0.0227  0.0068  34  GLU   C O   
1326 C CB  . GLU   B 28  ? 0.1686 0.1767 0.2669 0.0155  0.0223  0.0207  34  GLU   C CB  
1327 C CG  . GLU   B 28  ? 0.1786 0.1855 0.2861 0.0167  0.0258  0.0205  34  GLU   C CG  
1328 C CD  . GLU   B 28  ? 0.2053 0.2099 0.3182 0.0167  0.0265  0.0180  34  GLU   C CD  
1329 O OE1 . GLU   B 28  ? 0.2266 0.2287 0.3449 0.0178  0.0295  0.0155  34  GLU   C OE1 
1330 O OE2 . GLU   B 28  ? 0.1894 0.1944 0.3022 0.0158  0.0244  0.0186  34  GLU   C OE2 
1331 N N   . ASP   B 29  ? 0.1563 0.1606 0.2447 0.0147  0.0181  0.0112  35  ASP   C N   
1332 C CA  . ASP   B 29  ? 0.1542 0.1571 0.2453 0.0144  0.0171  0.0071  35  ASP   C CA  
1333 C C   . ASP   B 29  ? 0.1613 0.1661 0.2565 0.0135  0.0161  0.0105  35  ASP   C C   
1334 O O   . ASP   B 29  ? 0.1539 0.1601 0.2433 0.0130  0.0140  0.0119  35  ASP   C O   
1335 C CB  . ASP   B 29  ? 0.1675 0.1691 0.2496 0.0149  0.0146  0.0020  35  ASP   C CB  
1336 C CG  . ASP   B 29  ? 0.2246 0.2252 0.3096 0.0147  0.0128  -0.0031 35  ASP   C CG  
1337 O OD1 . ASP   B 29  ? 0.2192 0.2211 0.3116 0.0136  0.0126  -0.0017 35  ASP   C OD1 
1338 O OD2 . ASP   B 29  ? 0.2704 0.2692 0.3498 0.0156  0.0112  -0.0083 35  ASP   C OD2 
1339 N N   . SER   B 30  ? 0.1460 0.1506 0.2513 0.0133  0.0181  0.0119  36  SER   C N   
1340 C CA  A SER   B 30  ? 0.1477 0.1536 0.2570 0.0127  0.0182  0.0156  36  SER   C CA  
1341 C CA  B SER   B 30  ? 0.1526 0.1585 0.2615 0.0127  0.0181  0.0156  36  SER   C CA  
1342 C C   . SER   B 30  ? 0.1565 0.1628 0.2643 0.0120  0.0161  0.0124  36  SER   C C   
1343 O O   . SER   B 30  ? 0.1529 0.1606 0.2583 0.0118  0.0155  0.0156  36  SER   C O   
1344 C CB  A SER   B 30  ? 0.1622 0.1670 0.2829 0.0129  0.0213  0.0176  36  SER   C CB  
1345 C CB  B SER   B 30  ? 0.1794 0.1846 0.2993 0.0129  0.0212  0.0184  36  SER   C CB  
1346 O OG  A SER   B 30  ? 0.1614 0.1668 0.2865 0.0124  0.0221  0.0204  36  SER   C OG  
1347 O OG  B SER   B 30  ? 0.2006 0.2033 0.3271 0.0127  0.0223  0.0132  36  SER   C OG  
1348 N N   . SER   B 31  ? 0.1562 0.1611 0.2650 0.0118  0.0149  0.0061  37  SER   C N   
1349 C CA  . SER   B 31  ? 0.1689 0.1748 0.2778 0.0113  0.0126  0.0031  37  SER   C CA  
1350 C C   . SER   B 31  ? 0.1561 0.1634 0.2542 0.0117  0.0099  0.0039  37  SER   C C   
1351 O O   . SER   B 31  ? 0.1673 0.1760 0.2658 0.0114  0.0086  0.0037  37  SER   C O   
1352 C CB  . SER   B 31  ? 0.2039 0.2083 0.3155 0.0111  0.0108  -0.0041 37  SER   C CB  
1353 O OG  . SER   B 31  ? 0.2639 0.2672 0.3651 0.0122  0.0086  -0.0077 37  SER   C OG  
1354 N N   . ARG   B 32  ? 0.1448 0.1516 0.2340 0.0123  0.0096  0.0052  38  ARG   C N   
1355 C CA  . ARG   B 32  ? 0.1462 0.1536 0.2254 0.0127  0.0075  0.0062  38  ARG   C CA  
1356 C C   . ARG   B 32  ? 0.1374 0.1458 0.2142 0.0124  0.0083  0.0120  38  ARG   C C   
1357 O O   . ARG   B 32  ? 0.1315 0.1401 0.2007 0.0125  0.0067  0.0130  38  ARG   C O   
1358 C CB  . ARG   B 32  ? 0.1748 0.1805 0.2457 0.0136  0.0067  0.0038  38  ARG   C CB  
1359 C CG  . ARG   B 32  ? 0.1819 0.1862 0.2518 0.0144  0.0051  -0.0024 38  ARG   C CG  
1360 C CD  . ARG   B 32  ? 0.1559 0.1581 0.2164 0.0158  0.0051  -0.0043 38  ARG   C CD  
1361 N NE  . ARG   B 32  ? 0.1598 0.1620 0.2107 0.0163  0.0034  -0.0027 38  ARG   C NE  
1362 C CZ  . ARG   B 32  ? 0.1673 0.1675 0.2086 0.0179  0.0024  -0.0049 38  ARG   C CZ  
1363 N NH1 . ARG   B 32  ? 0.1759 0.1739 0.2145 0.0192  0.0025  -0.0091 38  ARG   C NH1 
1364 N NH2 . ARG   B 32  ? 0.1667 0.1667 0.2007 0.0184  0.0011  -0.0030 38  ARG   C NH2 
1365 N N   . ASP   B 33  ? 0.1301 0.1390 0.2129 0.0121  0.0105  0.0158  39  ASP   C N   
1366 C CA  . ASP   B 33  ? 0.1302 0.1401 0.2102 0.0120  0.0106  0.0211  39  ASP   C CA  
1367 C C   . ASP   B 33  ? 0.1228 0.1326 0.1960 0.0120  0.0094  0.0215  39  ASP   C C   
1368 O O   . ASP   B 33  ? 0.1247 0.1351 0.1925 0.0116  0.0080  0.0240  39  ASP   C O   
1369 C CB  . ASP   B 33  ? 0.1191 0.1295 0.1960 0.0120  0.0100  0.0233  39  ASP   C CB  
1370 C CG  . ASP   B 33  ? 0.1411 0.1521 0.2148 0.0121  0.0098  0.0285  39  ASP   C CG  
1371 O OD1 . ASP   B 33  ? 0.1463 0.1580 0.2246 0.0124  0.0109  0.0316  39  ASP   C OD1 
1372 O OD2 . ASP   B 33  ? 0.1355 0.1463 0.2021 0.0122  0.0084  0.0295  39  ASP   C OD2 
1373 N N   . LEU   B 34  ? 0.1186 0.1275 0.1920 0.0123  0.0102  0.0190  40  LEU   C N   
1374 C CA  . LEU   B 34  ? 0.1272 0.1360 0.1953 0.0122  0.0099  0.0197  40  LEU   C CA  
1375 C C   . LEU   B 34  ? 0.1275 0.1369 0.2014 0.0125  0.0122  0.0212  40  LEU   C C   
1376 O O   . LEU   B 34  ? 0.1368 0.1454 0.2168 0.0132  0.0143  0.0195  40  LEU   C O   
1377 C CB  . LEU   B 34  ? 0.1388 0.1456 0.2000 0.0128  0.0093  0.0154  40  LEU   C CB  
1378 C CG  . LEU   B 34  ? 0.1453 0.1516 0.1995 0.0128  0.0068  0.0143  40  LEU   C CG  
1379 C CD1 . LEU   B 34  ? 0.1646 0.1687 0.2116 0.0139  0.0063  0.0106  40  LEU   C CD1 
1380 C CD2 . LEU   B 34  ? 0.1543 0.1611 0.2044 0.0119  0.0057  0.0180  40  LEU   C CD2 
1381 N N   . LEU   B 35  ? 0.1228 0.1335 0.1953 0.0120  0.0120  0.0240  41  LEU   C N   
1382 C CA  . LEU   B 35  ? 0.1376 0.1492 0.2159 0.0125  0.0143  0.0255  41  LEU   C CA  
1383 C C   . LEU   B 35  ? 0.1308 0.1427 0.2047 0.0118  0.0141  0.0263  41  LEU   C C   
1384 O O   . LEU   B 35  ? 0.1452 0.1575 0.2143 0.0107  0.0115  0.0275  41  LEU   C O   
1385 C CB  . LEU   B 35  ? 0.1278 0.1422 0.2139 0.0124  0.0140  0.0301  41  LEU   C CB  
1386 C CG  . LEU   B 35  ? 0.1311 0.1472 0.2251 0.0131  0.0163  0.0323  41  LEU   C CG  
1387 C CD1 . LEU   B 35  ? 0.1480 0.1654 0.2510 0.0140  0.0173  0.0352  41  LEU   C CD1 
1388 C CD2 . LEU   B 35  ? 0.1460 0.1648 0.2395 0.0120  0.0146  0.0351  41  LEU   C CD2 
1389 N N   . VAL   B 36  ? 0.1412 0.1523 0.2165 0.0126  0.0172  0.0252  42  VAL   C N   
1390 C CA  . VAL   B 36  ? 0.1379 0.1490 0.2108 0.0121  0.0183  0.0263  42  VAL   C CA  
1391 C C   . VAL   B 36  ? 0.1341 0.1478 0.2165 0.0123  0.0208  0.0291  42  VAL   C C   
1392 O O   . VAL   B 36  ? 0.1566 0.1698 0.2440 0.0138  0.0239  0.0281  42  VAL   C O   
1393 C CB  . VAL   B 36  ? 0.1473 0.1545 0.2118 0.0134  0.0203  0.0226  42  VAL   C CB  
1394 C CG1 . VAL   B 36  ? 0.1748 0.1817 0.2374 0.0130  0.0225  0.0243  42  VAL   C CG1 
1395 C CG2 . VAL   B 36  ? 0.1607 0.1659 0.2167 0.0133  0.0172  0.0200  42  VAL   C CG2 
1396 N N   . SER   B 37  ? 0.1382 0.1546 0.2236 0.0109  0.0196  0.0324  43  SER   C N   
1397 C CA  . SER   B 37  ? 0.1366 0.1563 0.2323 0.0110  0.0216  0.0354  43  SER   C CA  
1398 C C   . SER   B 37  ? 0.1548 0.1743 0.2498 0.0102  0.0237  0.0360  43  SER   C C   
1399 O O   . SER   B 37  ? 0.1641 0.1810 0.2507 0.0093  0.0228  0.0348  43  SER   C O   
1400 C CB  . SER   B 37  ? 0.1446 0.1688 0.2475 0.0101  0.0177  0.0392  43  SER   C CB  
1401 O OG  . SER   B 37  ? 0.1605 0.1853 0.2585 0.0081  0.0133  0.0399  43  SER   C OG  
1402 N N   . SER   B 38  ? 0.1608 0.1826 0.2651 0.0107  0.0273  0.0380  44  SER   C N   
1403 C CA  . SER   B 38  ? 0.1739 0.1958 0.2797 0.0099  0.0303  0.0392  44  SER   C CA  
1404 C C   . SER   B 38  ? 0.1924 0.2188 0.3056 0.0072  0.0263  0.0425  44  SER   C C   
1405 O O   . SER   B 38  ? 0.2065 0.2372 0.3270 0.0067  0.0225  0.0446  44  SER   C O   
1406 C CB  . SER   B 38  ? 0.2127 0.2346 0.3250 0.0119  0.0369  0.0396  44  SER   C CB  
1407 O OG  . SER   B 38  ? 0.2537 0.2806 0.3791 0.0121  0.0364  0.0424  44  SER   C OG  
1408 N N   . THR   B 39  ? 0.1910 0.2163 0.3024 0.0055  0.0270  0.0430  45  THR   C N   
1409 C CA  . THR   B 39  ? 0.1982 0.2272 0.3165 0.0026  0.0230  0.0453  45  THR   C CA  
1410 C C   . THR   B 39  ? 0.2300 0.2610 0.3585 0.0018  0.0277  0.0475  45  THR   C C   
1411 O O   . THR   B 39  ? 0.2239 0.2513 0.3490 0.0034  0.0341  0.0470  45  THR   C O   
1412 C CB  . THR   B 39  ? 0.2122 0.2378 0.3200 0.0008  0.0192  0.0436  45  THR   C CB  
1413 O OG1 . THR   B 39  ? 0.2322 0.2527 0.3327 0.0013  0.0239  0.0425  45  THR   C OG1 
1414 C CG2 . THR   B 39  ? 0.2241 0.2475 0.3217 0.0017  0.0154  0.0414  45  THR   C CG2 
1415 N N   . THR   B 40  ? 0.2569 0.2932 0.3972 -0.0006 0.0244  0.0500  46  THR   C N   
1416 C CA  . THR   B 40  ? 0.2737 0.3121 0.4255 -0.0018 0.0287  0.0523  46  THR   C CA  
1417 C C   . THR   B 40  ? 0.2803 0.3145 0.4259 -0.0040 0.0293  0.0516  46  THR   C C   
1418 O O   . THR   B 40  ? 0.3016 0.3330 0.4478 -0.0036 0.0361  0.0525  46  THR   C O   
1419 C CB  . THR   B 40  ? 0.3186 0.3650 0.4873 -0.0033 0.0248  0.0552  46  THR   C CB  
1420 O OG1 . THR   B 40  ? 0.3724 0.4202 0.5384 -0.0057 0.0162  0.0544  46  THR   C OG1 
1421 C CG2 . THR   B 40  ? 0.3062 0.3562 0.4812 -0.0006 0.0253  0.0564  46  THR   C CG2 
1422 N N   . ALA   B 41  ? 0.2622 0.2950 0.4011 -0.0061 0.0228  0.0501  47  ALA   C N   
1423 C CA  . ALA   B 41  ? 0.2628 0.2910 0.3958 -0.0081 0.0232  0.0493  47  ALA   C CA  
1424 C C   . ALA   B 41  ? 0.2455 0.2663 0.3612 -0.0059 0.0256  0.0469  47  ALA   C C   
1425 O O   . ALA   B 41  ? 0.2430 0.2629 0.3505 -0.0038 0.0238  0.0451  47  ALA   C O   
1426 C CB  . ALA   B 41  ? 0.2841 0.3138 0.4184 -0.0113 0.0150  0.0484  47  ALA   C CB  
1427 N N   . GLN   B 42  ? 0.2509 0.2667 0.3615 -0.0063 0.0294  0.0471  48  GLN   C N   
1428 C CA  . GLN   B 42  ? 0.2701 0.2792 0.3647 -0.0041 0.0310  0.0452  48  GLN   C CA  
1429 C C   . GLN   B 42  ? 0.2667 0.2738 0.3534 -0.0054 0.0244  0.0430  48  GLN   C C   
1430 O O   . GLN   B 42  ? 0.2839 0.2922 0.3758 -0.0086 0.0203  0.0432  48  GLN   C O   
1431 C CB  . GLN   B 42  ? 0.3438 0.3480 0.4357 -0.0036 0.0377  0.0469  48  GLN   C CB  
1432 C CG  . GLN   B 42  ? 0.4664 0.4710 0.5618 -0.0010 0.0454  0.0486  48  GLN   C CG  
1433 C CD  . GLN   B 42  ? 0.6139 0.6127 0.7041 0.0000  0.0523  0.0505  48  GLN   C CD  
1434 O OE1 . GLN   B 42  ? 0.6575 0.6566 0.7572 -0.0024 0.0550  0.0533  48  GLN   C OE1 
1435 N NE2 . GLN   B 42  ? 0.6565 0.6499 0.7318 0.0037  0.0552  0.0492  48  GLN   C NE2 
1436 N N   . GLY   B 43  ? 0.2292 0.2335 0.3038 -0.0030 0.0232  0.0407  49  GLY   C N   
1437 C CA  . GLY   B 43  ? 0.2290 0.2309 0.2949 -0.0035 0.0180  0.0385  49  GLY   C CA  
1438 C C   . GLY   B 43  ? 0.2359 0.2313 0.2921 -0.0028 0.0202  0.0381  49  GLY   C C   
1439 O O   . GLY   B 43  ? 0.2692 0.2617 0.3231 -0.0012 0.0258  0.0394  49  GLY   C O   
1440 N N   . CYS   B 44  ? 0.2263 0.2191 0.2762 -0.0036 0.0162  0.0366  50  CYS   C N   
1441 C CA  . CYS   B 44  ? 0.2428 0.2294 0.2845 -0.0030 0.0178  0.0365  50  CYS   C CA  
1442 C C   . CYS   B 44  ? 0.2422 0.2257 0.2721 -0.0005 0.0160  0.0343  50  CYS   C C   
1443 O O   . CYS   B 44  ? 0.2781 0.2564 0.3011 0.0003  0.0170  0.0343  50  CYS   C O   
1444 C CB  . CYS   B 44  ? 0.2561 0.2414 0.3027 -0.0066 0.0155  0.0368  50  CYS   C CB  
1445 S SG  . CYS   B 44  ? 0.3547 0.3439 0.4176 -0.0099 0.0177  0.0395  50  CYS   C SG  
1446 N N   . ASP   B 45  ? 0.2054 0.1918 0.2333 0.0009  0.0135  0.0325  51  ASP   C N   
1447 C CA  . ASP   B 45  ? 0.2094 0.1936 0.2277 0.0033  0.0117  0.0304  51  ASP   C CA  
1448 C C   . ASP   B 45  ? 0.2129 0.1947 0.2248 0.0065  0.0154  0.0302  51  ASP   C C   
1449 O O   . ASP   B 45  ? 0.2355 0.2184 0.2503 0.0073  0.0189  0.0311  51  ASP   C O   
1450 C CB  . ASP   B 45  ? 0.2024 0.1907 0.2223 0.0036  0.0084  0.0288  51  ASP   C CB  
1451 C CG  . ASP   B 45  ? 0.2440 0.2342 0.2672 0.0012  0.0043  0.0288  51  ASP   C CG  
1452 O OD1 . ASP   B 45  ? 0.2601 0.2473 0.2810 -0.0002 0.0029  0.0286  51  ASP   C OD1 
1453 O OD2 . ASP   B 45  ? 0.2183 0.2126 0.2460 0.0009  0.0025  0.0289  51  ASP   C OD2 
1454 N N   . THR   B 46  ? 0.1900 0.1680 0.1929 0.0086  0.0147  0.0292  52  THR   C N   
1455 C CA  . THR   B 46  ? 0.2014 0.1769 0.1964 0.0122  0.0168  0.0286  52  THR   C CA  
1456 C C   . THR   B 46  ? 0.1950 0.1726 0.1870 0.0139  0.0134  0.0255  52  THR   C C   
1457 O O   . THR   B 46  ? 0.2041 0.1821 0.1955 0.0134  0.0100  0.0245  52  THR   C O   
1458 C CB  . THR   B 46  ? 0.2408 0.2105 0.2281 0.0136  0.0180  0.0299  52  THR   C CB  
1459 O OG1 . THR   B 46  ? 0.2718 0.2391 0.2629 0.0117  0.0218  0.0329  52  THR   C OG1 
1460 C CG2 . THR   B 46  ? 0.2632 0.2304 0.2404 0.0179  0.0191  0.0291  52  THR   C CG2 
1461 N N   . ILE   B 47  ? 0.1973 0.1762 0.1877 0.0160  0.0144  0.0239  53  ILE   C N   
1462 C CA  . ILE   B 47  ? 0.1857 0.1665 0.1744 0.0176  0.0112  0.0208  53  ILE   C CA  
1463 C C   . ILE   B 47  ? 0.1859 0.1635 0.1651 0.0207  0.0100  0.0196  53  ILE   C C   
1464 O O   . ILE   B 47  ? 0.2080 0.1821 0.1804 0.0228  0.0125  0.0206  53  ILE   C O   
1465 C CB  . ILE   B 47  ? 0.1931 0.1762 0.1846 0.0184  0.0125  0.0189  53  ILE   C CB  
1466 C CG1 . ILE   B 47  ? 0.2007 0.1870 0.2019 0.0160  0.0142  0.0205  53  ILE   C CG1 
1467 C CG2 . ILE   B 47  ? 0.2051 0.1902 0.1965 0.0196  0.0091  0.0154  53  ILE   C CG2 
1468 C CD1 . ILE   B 47  ? 0.2316 0.2211 0.2394 0.0134  0.0109  0.0211  53  ILE   C CD1 
1469 N N   . ALA   B 48  ? 0.1729 0.1516 0.1515 0.0212  0.0064  0.0180  54  ALA   C N   
1470 C CA  . ALA   B 48  ? 0.1744 0.1508 0.1451 0.0244  0.0045  0.0168  54  ALA   C CA  
1471 C C   . ALA   B 48  ? 0.1788 0.1560 0.1459 0.0270  0.0039  0.0140  54  ALA   C C   
1472 O O   . ALA   B 48  ? 0.1796 0.1599 0.1521 0.0262  0.0033  0.0117  54  ALA   C O   
1473 C CB  . ALA   B 48  ? 0.1709 0.1494 0.1443 0.0242  0.0009  0.0155  54  ALA   C CB  
1474 N N   . ARG   B 49  ? 0.1903 0.1640 0.1478 0.0304  0.0039  0.0140  55  ARG   C N   
1475 C CA  . ARG   B 49  ? 0.1888 0.1625 0.1405 0.0335  0.0025  0.0108  55  ARG   C CA  
1476 C C   . ARG   B 49  ? 0.2002 0.1732 0.1459 0.0365  -0.0017 0.0098  55  ARG   C C   
1477 O O   . ARG   B 49  ? 0.2152 0.1840 0.1522 0.0391  -0.0009 0.0123  55  ARG   C O   
1478 C CB  . ARG   B 49  ? 0.2046 0.1743 0.1489 0.0352  0.0070  0.0123  55  ARG   C CB  
1479 C CG  . ARG   B 49  ? 0.1872 0.1580 0.1392 0.0321  0.0114  0.0138  55  ARG   C CG  
1480 C CD  . ARG   B 49  ? 0.2031 0.1781 0.1631 0.0306  0.0102  0.0104  55  ARG   C CD  
1481 N NE  . ARG   B 49  ? 0.2003 0.1763 0.1676 0.0282  0.0144  0.0124  55  ARG   C NE  
1482 C CZ  . ARG   B 49  ? 0.1981 0.1778 0.1749 0.0261  0.0140  0.0112  55  ARG   C CZ  
1483 N NH1 . ARG   B 49  ? 0.1893 0.1717 0.1694 0.0260  0.0102  0.0077  55  ARG   C NH1 
1484 N NH2 . ARG   B 49  ? 0.2001 0.1811 0.1841 0.0241  0.0176  0.0135  55  ARG   C NH2 
1485 N N   . CYS   B 50  ? 0.1850 0.1622 0.1367 0.0362  -0.0060 0.0068  56  CYS   C N   
1486 C CA  . CYS   B 50  ? 0.1913 0.1691 0.1410 0.0385  -0.0102 0.0061  56  CYS   C CA  
1487 C C   . CYS   B 50  ? 0.1781 0.1613 0.1368 0.0376  -0.0142 0.0023  56  CYS   C C   
1488 O O   . CYS   B 50  ? 0.1870 0.1728 0.1530 0.0351  -0.0135 0.0005  56  CYS   C O   
1489 C CB  . CYS   B 50  ? 0.1855 0.1614 0.1366 0.0373  -0.0086 0.0099  56  CYS   C CB  
1490 S SG  . CYS   B 50  ? 0.1797 0.1593 0.1431 0.0327  -0.0079 0.0100  56  CYS   C SG  
1491 N N   . ASP   B 51  ? 0.1939 0.1787 0.1528 0.0398  -0.0182 0.0013  57  ASP   C N   
1492 C CA  . ASP   B 51  ? 0.2038 0.1940 0.1729 0.0390  -0.0218 -0.0017 57  ASP   C CA  
1493 C C   . ASP   B 51  ? 0.2090 0.2000 0.1829 0.0385  -0.0216 0.0006  57  ASP   C C   
1494 O O   . ASP   B 51  ? 0.2089 0.2037 0.1890 0.0394  -0.0248 -0.0012 57  ASP   C O   
1495 C CB  . ASP   B 51  ? 0.2449 0.2372 0.2121 0.0421  -0.0272 -0.0059 57  ASP   C CB  
1496 C CG  . ASP   B 51  ? 0.2910 0.2816 0.2501 0.0462  -0.0301 -0.0047 57  ASP   C CG  
1497 O OD1 . ASP   B 51  ? 0.2772 0.2642 0.2316 0.0468  -0.0274 -0.0004 57  ASP   C OD1 
1498 O OD2 . ASP   B 51  ? 0.3661 0.3592 0.3245 0.0488  -0.0355 -0.0081 57  ASP   C OD2 
1499 N N   . CYS   B 52  ? 0.1905 0.1782 0.1621 0.0370  -0.0178 0.0044  58  CYS   C N   
1500 C CA  . CYS   B 52  ? 0.1873 0.1751 0.1630 0.0365  -0.0171 0.0062  58  CYS   C CA  
1501 C C   . CYS   B 52  ? 0.1698 0.1626 0.1565 0.0345  -0.0177 0.0045  58  CYS   C C   
1502 O O   . CYS   B 52  ? 0.1676 0.1626 0.1593 0.0322  -0.0169 0.0032  58  CYS   C O   
1503 C CB  . CYS   B 52  ? 0.1942 0.1777 0.1669 0.0343  -0.0131 0.0096  58  CYS   C CB  
1504 S SG  . CYS   B 52  ? 0.1963 0.1731 0.1578 0.0366  -0.0115 0.0127  58  CYS   C SG  
1505 N N   . GLN   B 53  ? 0.1674 0.1615 0.1578 0.0356  -0.0185 0.0048  59  GLN   C N   
1506 C CA  . GLN   B 53  ? 0.1756 0.1736 0.1761 0.0340  -0.0178 0.0042  59  GLN   C CA  
1507 C C   . GLN   B 53  ? 0.1664 0.1619 0.1661 0.0337  -0.0150 0.0067  59  GLN   C C   
1508 O O   . GLN   B 53  ? 0.1664 0.1644 0.1731 0.0333  -0.0140 0.0067  59  GLN   C O   
1509 C CB  . GLN   B 53  ? 0.1742 0.1772 0.1823 0.0359  -0.0214 0.0014  59  GLN   C CB  
1510 C CG  . GLN   B 53  ? 0.2201 0.2259 0.2312 0.0354  -0.0240 -0.0020 59  GLN   C CG  
1511 C CD  . GLN   B 53  ? 0.2303 0.2417 0.2512 0.0366  -0.0279 -0.0051 59  GLN   C CD  
1512 O OE1 . GLN   B 53  ? 0.2632 0.2758 0.2816 0.0391  -0.0325 -0.0077 59  GLN   C OE1 
1513 N NE2 . GLN   B 53  ? 0.1977 0.2126 0.2301 0.0350  -0.0260 -0.0050 59  GLN   C NE2 
1514 N N   . THR   B 54  ? 0.1636 0.1539 0.1551 0.0337  -0.0135 0.0089  60  THR   C N   
1515 C CA  . THR   B 54  ? 0.1717 0.1587 0.1617 0.0329  -0.0108 0.0108  60  THR   C CA  
1516 C C   . THR   B 54  ? 0.1749 0.1579 0.1597 0.0303  -0.0087 0.0124  60  THR   C C   
1517 O O   . THR   B 54  ? 0.1825 0.1637 0.1629 0.0303  -0.0089 0.0129  60  THR   C O   
1518 C CB  . THR   B 54  ? 0.2143 0.1984 0.2011 0.0358  -0.0110 0.0117  60  THR   C CB  
1519 O OG1 . THR   B 54  ? 0.2654 0.2453 0.2446 0.0371  -0.0115 0.0129  60  THR   C OG1 
1520 C CG2 . THR   B 54  ? 0.2163 0.2049 0.2094 0.0386  -0.0133 0.0103  60  THR   C CG2 
1521 N N   . GLY   B 55  ? 0.1611 0.1431 0.1469 0.0281  -0.0068 0.0131  61  GLY   C N   
1522 C CA  . GLY   B 55  ? 0.1707 0.1497 0.1532 0.0254  -0.0055 0.0144  61  GLY   C CA  
1523 C C   . GLY   B 55  ? 0.1524 0.1301 0.1350 0.0237  -0.0042 0.0148  61  GLY   C C   
1524 O O   . GLY   B 55  ? 0.1715 0.1490 0.1548 0.0251  -0.0036 0.0145  61  GLY   C O   
1525 N N   . VAL   B 56  ? 0.1495 0.1262 0.1313 0.0209  -0.0038 0.0156  62  VAL   C N   
1526 C CA  . VAL   B 56  ? 0.1544 0.1295 0.1347 0.0194  -0.0032 0.0159  62  VAL   C CA  
1527 C C   . VAL   B 56  ? 0.1495 0.1280 0.1334 0.0171  -0.0035 0.0166  62  VAL   C C   
1528 O O   . VAL   B 56  ? 0.1588 0.1381 0.1441 0.0158  -0.0039 0.0171  62  VAL   C O   
1529 C CB  . VAL   B 56  ? 0.1635 0.1327 0.1384 0.0183  -0.0032 0.0161  62  VAL   C CB  
1530 C CG1 . VAL   B 56  ? 0.1913 0.1586 0.1639 0.0164  -0.0034 0.0158  62  VAL   C CG1 
1531 C CG2 . VAL   B 56  ? 0.1776 0.1427 0.1490 0.0209  -0.0025 0.0157  62  VAL   C CG2 
1532 N N   . TYR   B 57  ? 0.1552 0.1352 0.1401 0.0168  -0.0030 0.0169  63  TYR   C N   
1533 C CA  . TYR   B 57  ? 0.1358 0.1188 0.1240 0.0149  -0.0034 0.0180  63  TYR   C CA  
1534 C C   . TYR   B 57  ? 0.1465 0.1273 0.1304 0.0137  -0.0040 0.0186  63  TYR   C C   
1535 O O   . TYR   B 57  ? 0.1649 0.1428 0.1441 0.0148  -0.0033 0.0180  63  TYR   C O   
1536 C CB  . TYR   B 57  ? 0.1460 0.1337 0.1406 0.0157  -0.0024 0.0184  63  TYR   C CB  
1537 C CG  . TYR   B 57  ? 0.1507 0.1389 0.1455 0.0168  -0.0007 0.0191  63  TYR   C CG  
1538 C CD1 . TYR   B 57  ? 0.1556 0.1429 0.1499 0.0189  0.0006  0.0182  63  TYR   C CD1 
1539 C CD2 . TYR   B 57  ? 0.1464 0.1359 0.1421 0.0160  -0.0002 0.0209  63  TYR   C CD2 
1540 C CE1 . TYR   B 57  ? 0.1620 0.1496 0.1567 0.0201  0.0030  0.0191  63  TYR   C CE1 
1541 C CE2 . TYR   B 57  ? 0.1576 0.1471 0.1527 0.0174  0.0021  0.0220  63  TYR   C CE2 
1542 C CZ  . TYR   B 57  ? 0.1671 0.1556 0.1618 0.0194  0.0039  0.0211  63  TYR   C CZ  
1543 O OH  . TYR   B 57  ? 0.1923 0.1807 0.1869 0.0210  0.0071  0.0224  63  TYR   C OH  
1544 N N   . TYR   B 58  ? 0.1482 0.1308 0.1340 0.0118  -0.0052 0.0198  64  TYR   C N   
1545 C CA  . TYR   B 58  ? 0.1567 0.1380 0.1386 0.0107  -0.0067 0.0203  64  TYR   C CA  
1546 C C   . TYR   B 58  ? 0.1551 0.1392 0.1382 0.0117  -0.0057 0.0220  64  TYR   C C   
1547 O O   . TYR   B 58  ? 0.1522 0.1403 0.1416 0.0116  -0.0052 0.0235  64  TYR   C O   
1548 C CB  . TYR   B 58  ? 0.1732 0.1550 0.1568 0.0081  -0.0091 0.0208  64  TYR   C CB  
1549 C CG  . TYR   B 58  ? 0.1881 0.1685 0.1670 0.0071  -0.0116 0.0209  64  TYR   C CG  
1550 C CD1 . TYR   B 58  ? 0.1926 0.1678 0.1639 0.0072  -0.0124 0.0189  64  TYR   C CD1 
1551 C CD2 . TYR   B 58  ? 0.1918 0.1757 0.1736 0.0063  -0.0134 0.0227  64  TYR   C CD2 
1552 C CE1 . TYR   B 58  ? 0.2139 0.1874 0.1795 0.0067  -0.0150 0.0184  64  TYR   C CE1 
1553 C CE2 . TYR   B 58  ? 0.1995 0.1822 0.1760 0.0058  -0.0164 0.0227  64  TYR   C CE2 
1554 C CZ  . TYR   B 58  ? 0.2112 0.1886 0.1793 0.0058  -0.0174 0.0203  64  TYR   C CZ  
1555 O OH  . TYR   B 58  ? 0.2478 0.2235 0.2092 0.0056  -0.0207 0.0197  64  TYR   C OH  
1556 N N   . CYS   B 59  ? 0.1510 0.1324 0.1278 0.0129  -0.0051 0.0219  65  CYS   C N   
1557 C CA  . CYS   B 59  ? 0.1716 0.1544 0.1475 0.0143  -0.0035 0.0239  65  CYS   C CA  
1558 C C   . CYS   B 59  ? 0.1809 0.1620 0.1499 0.0136  -0.0063 0.0246  65  CYS   C C   
1559 O O   . CYS   B 59  ? 0.1901 0.1667 0.1504 0.0141  -0.0068 0.0230  65  CYS   C O   
1560 C CB  . CYS   B 59  ? 0.1680 0.1490 0.1414 0.0168  -0.0001 0.0234  65  CYS   C CB  
1561 S SG  . CYS   B 59  ? 0.1948 0.1765 0.1664 0.0189  0.0031  0.0265  65  CYS   C SG  
1562 N N   . SER   B 60  ? 0.1935 0.1780 0.1662 0.0125  -0.0082 0.0267  66  SER   C N   
1563 C CA  A SER   B 60  ? 0.2117 0.1952 0.1787 0.0118  -0.0118 0.0272  66  SER   C CA  
1564 C CA  B SER   B 60  ? 0.2052 0.1888 0.1723 0.0119  -0.0118 0.0273  66  SER   C CA  
1565 C C   . SER   B 60  ? 0.2140 0.1949 0.1717 0.0143  -0.0106 0.0283  66  SER   C C   
1566 O O   . SER   B 60  ? 0.2333 0.2108 0.1820 0.0141  -0.0136 0.0268  66  SER   C O   
1567 C CB  A SER   B 60  ? 0.2348 0.2230 0.2088 0.0105  -0.0142 0.0295  66  SER   C CB  
1568 C CB  B SER   B 60  ? 0.2065 0.1949 0.1807 0.0108  -0.0138 0.0298  66  SER   C CB  
1569 O OG  A SER   B 60  ? 0.2642 0.2555 0.2432 0.0121  -0.0113 0.0326  66  SER   C OG  
1570 O OG  B SER   B 60  ? 0.2079 0.1956 0.1766 0.0102  -0.0181 0.0302  66  SER   C OG  
1571 N N   . SER   B 61  ? 0.1917 0.1737 0.1512 0.0165  -0.0061 0.0305  67  SER   C N   
1572 C CA  . SER   B 61  ? 0.2045 0.1837 0.1550 0.0193  -0.0038 0.0321  67  SER   C CA  
1573 C C   . SER   B 61  ? 0.2351 0.2088 0.1767 0.0205  -0.0022 0.0291  67  SER   C C   
1574 O O   . SER   B 61  ? 0.2555 0.2260 0.1877 0.0229  -0.0002 0.0299  67  SER   C O   
1575 C CB  . SER   B 61  ? 0.2077 0.1896 0.1646 0.0211  0.0011  0.0356  67  SER   C CB  
1576 O OG  . SER   B 61  ? 0.2150 0.1975 0.1785 0.0214  0.0047  0.0341  67  SER   C OG  
1577 N N   . ARG   B 62  ? 0.2170 0.1891 0.1604 0.0192  -0.0029 0.0258  68  ARG   C N   
1578 C CA  . ARG   B 62  ? 0.2241 0.1905 0.1592 0.0202  -0.0018 0.0227  68  ARG   C CA  
1579 C C   . ARG   B 62  ? 0.2314 0.1946 0.1630 0.0177  -0.0065 0.0192  68  ARG   C C   
1580 O O   . ARG   B 62  ? 0.2486 0.2064 0.1740 0.0183  -0.0060 0.0163  68  ARG   C O   
1581 C CB  . ARG   B 62  ? 0.2202 0.1870 0.1613 0.0215  0.0024  0.0221  68  ARG   C CB  
1582 C CG  . ARG   B 62  ? 0.2677 0.2376 0.2138 0.0238  0.0074  0.0251  68  ARG   C CG  
1583 C CD  . ARG   B 62  ? 0.2637 0.2292 0.1997 0.0267  0.0109  0.0257  68  ARG   C CD  
1584 N NE  . ARG   B 62  ? 0.3077 0.2758 0.2489 0.0290  0.0166  0.0290  68  ARG   C NE  
1585 C CZ  . ARG   B 62  ? 0.3527 0.3229 0.2944 0.0297  0.0179  0.0328  68  ARG   C CZ  
1586 N NH1 . ARG   B 62  ? 0.3665 0.3365 0.3027 0.0287  0.0137  0.0338  68  ARG   C NH1 
1587 N NH2 . ARG   B 62  ? 0.3735 0.3454 0.3208 0.0317  0.0237  0.0358  68  ARG   C NH2 
1588 N N   . ARG   B 63  ? 0.2294 0.1958 0.1668 0.0149  -0.0106 0.0196  69  ARG   C N   
1589 C CA  . ARG   B 63  ? 0.2410 0.2052 0.1786 0.0120  -0.0147 0.0167  69  ARG   C CA  
1590 C C   . ARG   B 63  ? 0.2552 0.2160 0.1941 0.0121  -0.0124 0.0145  69  ARG   C C   
1591 O O   . ARG   B 63  ? 0.2815 0.2370 0.2153 0.0113  -0.0137 0.0115  69  ARG   C O   
1592 C CB  . ARG   B 63  ? 0.2578 0.2176 0.1852 0.0114  -0.0188 0.0144  69  ARG   C CB  
1593 C CG  . ARG   B 63  ? 0.3030 0.2660 0.2285 0.0114  -0.0223 0.0165  69  ARG   C CG  
1594 C CD  . ARG   B 63  ? 0.3531 0.3215 0.2889 0.0085  -0.0259 0.0178  69  ARG   C CD  
1595 N NE  . ARG   B 63  ? 0.3836 0.3540 0.3163 0.0082  -0.0309 0.0188  69  ARG   C NE  
1596 C CZ  . ARG   B 63  ? 0.4105 0.3855 0.3459 0.0096  -0.0308 0.0229  69  ARG   C CZ  
1597 N NH1 . ARG   B 63  ? 0.3899 0.3677 0.3309 0.0113  -0.0257 0.0259  69  ARG   C NH1 
1598 N NH2 . ARG   B 63  ? 0.4056 0.3824 0.3382 0.0095  -0.0361 0.0238  69  ARG   C NH2 
1599 N N   . LYS   B 64  ? 0.2218 0.1858 0.1678 0.0133  -0.0089 0.0160  70  LYS   C N   
1600 C CA  . LYS   B 64  ? 0.2357 0.1968 0.1825 0.0141  -0.0067 0.0144  70  LYS   C CA  
1601 C C   . LYS   B 64  ? 0.2172 0.1825 0.1733 0.0138  -0.0059 0.0156  70  LYS   C C   
1602 O O   . LYS   B 64  ? 0.2114 0.1819 0.1733 0.0139  -0.0052 0.0176  70  LYS   C O   
1603 C CB  . LYS   B 64  ? 0.2903 0.2498 0.2335 0.0175  -0.0026 0.0144  70  LYS   C CB  
1604 C CG  . LYS   B 64  ? 0.4374 0.3900 0.3702 0.0188  -0.0019 0.0119  70  LYS   C CG  
1605 C CD  . LYS   B 64  ? 0.5162 0.4669 0.4496 0.0218  0.0025  0.0114  70  LYS   C CD  
1606 C CE  . LYS   B 64  ? 0.6126 0.5568 0.5356 0.0239  0.0046  0.0094  70  LYS   C CE  
1607 N NZ  . LYS   B 64  ? 0.6752 0.6191 0.5907 0.0244  0.0043  0.0102  70  LYS   C NZ  
1608 N N   . HIS   B 65  ? 0.2053 0.1680 0.1622 0.0135  -0.0057 0.0143  71  HIS   C N   
1609 C CA  . HIS   B 65  ? 0.2002 0.1657 0.1636 0.0140  -0.0047 0.0150  71  HIS   C CA  
1610 C C   . HIS   B 65  ? 0.2212 0.1860 0.1844 0.0171  -0.0020 0.0146  71  HIS   C C   
1611 O O   . HIS   B 65  ? 0.2560 0.2156 0.2142 0.0182  -0.0012 0.0132  71  HIS   C O   
1612 C CB  . HIS   B 65  ? 0.2081 0.1711 0.1724 0.0122  -0.0060 0.0145  71  HIS   C CB  
1613 C CG  . HIS   B 65  ? 0.1902 0.1549 0.1571 0.0091  -0.0084 0.0151  71  HIS   C CG  
1614 N ND1 . HIS   B 65  ? 0.2263 0.1953 0.1997 0.0081  -0.0085 0.0167  71  HIS   C ND1 
1615 C CD2 . HIS   B 65  ? 0.1939 0.1564 0.1579 0.0070  -0.0109 0.0142  71  HIS   C CD2 
1616 C CE1 . HIS   B 65  ? 0.1962 0.1658 0.1714 0.0054  -0.0108 0.0170  71  HIS   C CE1 
1617 N NE2 . HIS   B 65  ? 0.2267 0.1927 0.1967 0.0045  -0.0127 0.0154  71  HIS   C NE2 
1618 N N   . TYR   B 66  ? 0.1829 0.1525 0.1522 0.0184  -0.0008 0.0156  72  TYR   C N   
1619 C CA  . TYR   B 66  ? 0.1779 0.1477 0.1488 0.0213  0.0015  0.0152  72  TYR   C CA  
1620 C C   . TYR   B 66  ? 0.1734 0.1453 0.1490 0.0222  0.0007  0.0150  72  TYR   C C   
1621 O O   . TYR   B 66  ? 0.1709 0.1467 0.1512 0.0213  -0.0004 0.0155  72  TYR   C O   
1622 C CB  . TYR   B 66  ? 0.1891 0.1634 0.1648 0.0224  0.0035  0.0164  72  TYR   C CB  
1623 C CG  . TYR   B 66  ? 0.1957 0.1679 0.1657 0.0227  0.0051  0.0171  72  TYR   C CG  
1624 C CD1 . TYR   B 66  ? 0.2270 0.1954 0.1921 0.0249  0.0077  0.0163  72  TYR   C CD1 
1625 C CD2 . TYR   B 66  ? 0.2076 0.1817 0.1774 0.0212  0.0044  0.0186  72  TYR   C CD2 
1626 C CE1 . TYR   B 66  ? 0.2477 0.2138 0.2064 0.0257  0.0096  0.0169  72  TYR   C CE1 
1627 C CE2 . TYR   B 66  ? 0.2218 0.1939 0.1853 0.0220  0.0058  0.0195  72  TYR   C CE2 
1628 C CZ  . TYR   B 66  ? 0.2450 0.2129 0.2024 0.0242  0.0085  0.0186  72  TYR   C CZ  
1629 O OH  . TYR   B 66  ? 0.2598 0.2252 0.2096 0.0253  0.0100  0.0194  72  TYR   C OH  
1630 N N   . PRO   B 67  ? 0.1804 0.1497 0.1546 0.0245  0.0014  0.0143  73  PRO   C N   
1631 C CA  . PRO   B 67  ? 0.1701 0.1416 0.1482 0.0261  0.0003  0.0143  73  PRO   C CA  
1632 C C   . PRO   B 67  ? 0.1813 0.1588 0.1672 0.0276  0.0009  0.0142  73  PRO   C C   
1633 O O   . PRO   B 67  ? 0.2089 0.1869 0.1965 0.0289  0.0031  0.0142  73  PRO   C O   
1634 C CB  . PRO   B 67  ? 0.2078 0.1743 0.1820 0.0284  0.0010  0.0139  73  PRO   C CB  
1635 C CG  . PRO   B 67  ? 0.2446 0.2075 0.2150 0.0286  0.0031  0.0133  73  PRO   C CG  
1636 C CD  . PRO   B 67  ? 0.1999 0.1636 0.1685 0.0259  0.0030  0.0135  73  PRO   C CD  
1637 N N   . VAL   B 68  ? 0.1568 0.1384 0.1474 0.0274  -0.0009 0.0139  74  VAL   C N   
1638 C CA  . VAL   B 68  ? 0.1632 0.1505 0.1625 0.0283  -0.0008 0.0134  74  VAL   C CA  
1639 C C   . VAL   B 68  ? 0.1585 0.1485 0.1609 0.0296  -0.0036 0.0121  74  VAL   C C   
1640 O O   . VAL   B 68  ? 0.1625 0.1508 0.1605 0.0293  -0.0053 0.0120  74  VAL   C O   
1641 C CB  . VAL   B 68  ? 0.1763 0.1668 0.1797 0.0260  -0.0002 0.0139  74  VAL   C CB  
1642 C CG1 . VAL   B 68  ? 0.2072 0.1961 0.2084 0.0254  0.0027  0.0154  74  VAL   C CG1 
1643 C CG2 . VAL   B 68  ? 0.1850 0.1749 0.1858 0.0238  -0.0018 0.0141  74  VAL   C CG2 
1644 N N   . SER   B 69  ? 0.1602 0.1548 0.1707 0.0312  -0.0041 0.0111  75  SER   C N   
1645 C CA  . SER   B 69  ? 0.1557 0.1544 0.1713 0.0321  -0.0073 0.0093  75  SER   C CA  
1646 C C   . SER   B 69  ? 0.1509 0.1534 0.1731 0.0298  -0.0071 0.0085  75  SER   C C   
1647 O O   . SER   B 69  ? 0.1524 0.1560 0.1791 0.0286  -0.0043 0.0096  75  SER   C O   
1648 C CB  . SER   B 69  ? 0.1766 0.1788 0.1992 0.0349  -0.0084 0.0083  75  SER   C CB  
1649 O OG  . SER   B 69  ? 0.2453 0.2438 0.2622 0.0373  -0.0084 0.0092  75  SER   C OG  
1650 N N   . PHE   B 70  ? 0.1461 0.1498 0.1684 0.0292  -0.0097 0.0069  76  PHE   C N   
1651 C CA  . PHE   B 70  ? 0.1433 0.1498 0.1718 0.0271  -0.0093 0.0060  76  PHE   C CA  
1652 C C   . PHE   B 70  ? 0.1413 0.1511 0.1746 0.0278  -0.0129 0.0026  76  PHE   C C   
1653 O O   . PHE   B 70  ? 0.1455 0.1545 0.1737 0.0298  -0.0159 0.0014  76  PHE   C O   
1654 C CB  . PHE   B 70  ? 0.1518 0.1554 0.1748 0.0248  -0.0077 0.0076  76  PHE   C CB  
1655 C CG  . PHE   B 70  ? 0.1375 0.1378 0.1516 0.0252  -0.0091 0.0075  76  PHE   C CG  
1656 C CD1 . PHE   B 70  ? 0.1544 0.1505 0.1606 0.0257  -0.0084 0.0093  76  PHE   C CD1 
1657 C CD2 . PHE   B 70  ? 0.1501 0.1512 0.1639 0.0252  -0.0107 0.0057  76  PHE   C CD2 
1658 C CE1 . PHE   B 70  ? 0.1581 0.1509 0.1571 0.0260  -0.0090 0.0097  76  PHE   C CE1 
1659 C CE2 . PHE   B 70  ? 0.1458 0.1436 0.1513 0.0258  -0.0111 0.0061  76  PHE   C CE2 
1660 C CZ  . PHE   B 70  ? 0.1574 0.1511 0.1558 0.0263  -0.0102 0.0082  76  PHE   C CZ  
1661 N N   . SER   B 71  ? 0.1290 0.1421 0.1716 0.0263  -0.0126 0.0013  77  SER   C N   
1662 C CA  . SER   B 71  ? 0.1353 0.1518 0.1842 0.0268  -0.0163 -0.0027 77  SER   C CA  
1663 C C   . SER   B 71  ? 0.1543 0.1688 0.1969 0.0264  -0.0180 -0.0046 77  SER   C C   
1664 O O   . SER   B 71  ? 0.1717 0.1826 0.2064 0.0257  -0.0160 -0.0025 77  SER   C O   
1665 C CB  . SER   B 71  ? 0.1427 0.1631 0.2054 0.0252  -0.0148 -0.0035 77  SER   C CB  
1666 O OG  . SER   B 71  ? 0.1726 0.1918 0.2370 0.0228  -0.0116 -0.0020 77  SER   C OG  
1667 N N   . LYS   B 72  ? 0.1698 0.1864 0.2156 0.0271  -0.0218 -0.0087 78  LYS   C N   
1668 C CA  . LYS   B 72  ? 0.1691 0.1835 0.2081 0.0273  -0.0233 -0.0110 78  LYS   C CA  
1669 C C   . LYS   B 72  ? 0.1679 0.1823 0.2130 0.0246  -0.0204 -0.0113 78  LYS   C C   
1670 O O   . LYS   B 72  ? 0.1866 0.2038 0.2432 0.0230  -0.0192 -0.0115 78  LYS   C O   
1671 C CB  . LYS   B 72  ? 0.2239 0.2408 0.2650 0.0291  -0.0289 -0.0160 78  LYS   C CB  
1672 C CG  . LYS   B 72  ? 0.2606 0.2778 0.2960 0.0323  -0.0322 -0.0156 78  LYS   C CG  
1673 C CD  . LYS   B 72  ? 0.3819 0.4025 0.4208 0.0343  -0.0387 -0.0207 78  LYS   C CD  
1674 C CE  . LYS   B 72  ? 0.5040 0.5240 0.5347 0.0381  -0.0420 -0.0197 78  LYS   C CE  
1675 N NZ  . LYS   B 72  ? 0.5799 0.5940 0.5951 0.0394  -0.0396 -0.0165 78  LYS   C NZ  
1676 N N   . PRO   B 73  ? 0.1648 0.1761 0.2032 0.0241  -0.0189 -0.0110 79  PRO   C N   
1677 C CA  . PRO   B 73  ? 0.1722 0.1834 0.2170 0.0218  -0.0160 -0.0110 79  PRO   C CA  
1678 C C   . PRO   B 73  ? 0.1728 0.1865 0.2280 0.0210  -0.0180 -0.0155 79  PRO   C C   
1679 O O   . PRO   B 73  ? 0.2001 0.2139 0.2531 0.0224  -0.0220 -0.0201 79  PRO   C O   
1680 C CB  . PRO   B 73  ? 0.2049 0.2125 0.2404 0.0222  -0.0149 -0.0110 79  PRO   C CB  
1681 C CG  . PRO   B 73  ? 0.2297 0.2351 0.2539 0.0241  -0.0156 -0.0091 79  PRO   C CG  
1682 C CD  . PRO   B 73  ? 0.1864 0.1939 0.2117 0.0258  -0.0193 -0.0104 79  PRO   C CD  
1683 N N   . SER   B 74  ? 0.1549 0.1704 0.2216 0.0190  -0.0154 -0.0142 80  SER   C N   
1684 C CA  . SER   B 74  ? 0.1642 0.1823 0.2434 0.0180  -0.0170 -0.0184 80  SER   C CA  
1685 C C   . SER   B 74  ? 0.1635 0.1813 0.2523 0.0157  -0.0126 -0.0163 80  SER   C C   
1686 O O   . SER   B 74  ? 0.1502 0.1665 0.2359 0.0151  -0.0089 -0.0115 80  SER   C O   
1687 C CB  . SER   B 74  ? 0.2009 0.2229 0.2879 0.0184  -0.0191 -0.0189 80  SER   C CB  
1688 O OG  . SER   B 74  ? 0.2713 0.2936 0.3496 0.0209  -0.0229 -0.0198 80  SER   C OG  
1689 N N   . LEU   B 75  ? 0.1683 0.1877 0.2694 0.0144  -0.0135 -0.0199 81  LEU   C N   
1690 C CA  . LEU   B 75  ? 0.1784 0.1975 0.2908 0.0124  -0.0094 -0.0183 81  LEU   C CA  
1691 C C   . LEU   B 75  ? 0.1896 0.2117 0.3119 0.0117  -0.0071 -0.0150 81  LEU   C C   
1692 O O   . LEU   B 75  ? 0.2143 0.2397 0.3456 0.0115  -0.0096 -0.0181 81  LEU   C O   
1693 C CB  . LEU   B 75  ? 0.2017 0.2202 0.3224 0.0114  -0.0114 -0.0245 81  LEU   C CB  
1694 C CG  . LEU   B 75  ? 0.2351 0.2524 0.3677 0.0094  -0.0072 -0.0233 81  LEU   C CG  
1695 C CD1 . LEU   B 75  ? 0.2272 0.2411 0.3527 0.0097  -0.0035 -0.0198 81  LEU   C CD1 
1696 C CD2 . LEU   B 75  ? 0.2620 0.2789 0.4045 0.0082  -0.0100 -0.0306 81  LEU   C CD2 
1697 N N   . ILE   B 76  ? 0.1907 0.2120 0.3108 0.0116  -0.0026 -0.0088 82  ILE   C N   
1698 C CA  . ILE   B 76  ? 0.2050 0.2282 0.3306 0.0116  0.0005  -0.0047 82  ILE   C CA  
1699 C C   . ILE   B 76  ? 0.2045 0.2268 0.3389 0.0103  0.0058  -0.0007 82  ILE   C C   
1700 O O   . ILE   B 76  ? 0.1864 0.2060 0.3157 0.0102  0.0077  0.0018  82  ILE   C O   
1701 C CB  . ILE   B 76  ? 0.2407 0.2628 0.3530 0.0132  0.0011  -0.0007 82  ILE   C CB  
1702 C CG1 . ILE   B 76  ? 0.2705 0.2931 0.3739 0.0148  -0.0037 -0.0039 82  ILE   C CG1 
1703 C CG2 . ILE   B 76  ? 0.2624 0.2855 0.3781 0.0135  0.0053  0.0041  82  ILE   C CG2 
1704 C CD1 . ILE   B 76  ? 0.2879 0.3142 0.3988 0.0156  -0.0059 -0.0061 82  ILE   C CD1 
1705 N N   . PHE   B 77  ? 0.2054 0.2298 0.3525 0.0097  0.0087  0.0006  83  PHE   C N   
1706 C CA  . PHE   B 77  ? 0.2037 0.2267 0.3583 0.0089  0.0145  0.0055  83  PHE   C CA  
1707 C C   . PHE   B 77  ? 0.2096 0.2314 0.3537 0.0104  0.0178  0.0118  83  PHE   C C   
1708 O O   . PHE   B 77  ? 0.2430 0.2663 0.3844 0.0115  0.0181  0.0128  83  PHE   C O   
1709 C CB  . PHE   B 77  ? 0.2081 0.2335 0.3806 0.0077  0.0171  0.0049  83  PHE   C CB  
1710 C CG  . PHE   B 77  ? 0.2163 0.2395 0.3975 0.0068  0.0231  0.0095  83  PHE   C CG  
1711 C CD1 . PHE   B 77  ? 0.2245 0.2452 0.4099 0.0056  0.0231  0.0078  83  PHE   C CD1 
1712 C CD2 . PHE   B 77  ? 0.2325 0.2553 0.4153 0.0077  0.0291  0.0161  83  PHE   C CD2 
1713 C CE1 . PHE   B 77  ? 0.2439 0.2622 0.4368 0.0052  0.0288  0.0126  83  PHE   C CE1 
1714 C CE2 . PHE   B 77  ? 0.2383 0.2586 0.4276 0.0074  0.0348  0.0210  83  PHE   C CE2 
1715 C CZ  . PHE   B 77  ? 0.2428 0.2609 0.4378 0.0061  0.0346  0.0194  83  PHE   C CZ  
1716 N N   . VAL   B 78  ? 0.1671 0.1862 0.3058 0.0106  0.0204  0.0161  84  VAL   C N   
1717 C CA  . VAL   B 78  ? 0.1737 0.1912 0.3011 0.0121  0.0226  0.0216  84  VAL   C CA  
1718 C C   . VAL   B 78  ? 0.1728 0.1890 0.3065 0.0123  0.0286  0.0274  84  VAL   C C   
1719 O O   . VAL   B 78  ? 0.1729 0.1880 0.3137 0.0115  0.0301  0.0282  84  VAL   C O   
1720 C CB  . VAL   B 78  ? 0.1831 0.1986 0.2984 0.0123  0.0199  0.0219  84  VAL   C CB  
1721 C CG1 . VAL   B 78  ? 0.1961 0.2101 0.3000 0.0136  0.0213  0.0270  84  VAL   C CG1 
1722 C CG2 . VAL   B 78  ? 0.2005 0.2167 0.3100 0.0122  0.0148  0.0165  84  VAL   C CG2 
1723 N N   . GLU   B 79  ? 0.1613 0.1772 0.2919 0.0138  0.0322  0.0317  85  GLU   C N   
1724 C CA  . GLU   B 79  ? 0.1740 0.1882 0.3082 0.0146  0.0382  0.0380  85  GLU   C CA  
1725 C C   . GLU   B 79  ? 0.1683 0.1799 0.2932 0.0154  0.0381  0.0420  85  GLU   C C   
1726 O O   . GLU   B 79  ? 0.1644 0.1756 0.2790 0.0154  0.0337  0.0403  85  GLU   C O   
1727 C CB  . GLU   B 79  ? 0.2192 0.2332 0.3496 0.0164  0.0423  0.0415  85  GLU   C CB  
1728 C CG  . GLU   B 79  ? 0.2948 0.3118 0.4379 0.0158  0.0437  0.0387  85  GLU   C CG  
1729 C CD  . GLU   B 79  ? 0.3988 0.4169 0.5608 0.0141  0.0468  0.0384  85  GLU   C CD  
1730 O OE1 . GLU   B 79  ? 0.4473 0.4630 0.6126 0.0144  0.0516  0.0435  85  GLU   C OE1 
1731 O OE2 . GLU   B 79  ? 0.4238 0.4450 0.5972 0.0124  0.0440  0.0330  85  GLU   C OE2 
1732 N N   . ALA   B 80  ? 0.1704 0.1802 0.3001 0.0161  0.0429  0.0474  86  ALA   C N   
1733 C CA  . ALA   B 80  ? 0.1845 0.1922 0.3069 0.0172  0.0428  0.0517  86  ALA   C CA  
1734 C C   . ALA   B 80  ? 0.2057 0.2125 0.3110 0.0188  0.0406  0.0537  86  ALA   C C   
1735 O O   . ALA   B 80  ? 0.2376 0.2442 0.3371 0.0199  0.0420  0.0544  86  ALA   C O   
1736 C CB  . ALA   B 80  ? 0.2011 0.2067 0.3306 0.0184  0.0492  0.0581  86  ALA   C CB  
1737 N N   . SER   B 81  ? 0.1890 0.1955 0.2873 0.0189  0.0368  0.0540  87  SER   C N   
1738 C CA  . SER   B 81  ? 0.2107 0.2165 0.2939 0.0201  0.0341  0.0557  87  SER   C CA  
1739 C C   . SER   B 81  ? 0.2266 0.2312 0.3066 0.0216  0.0343  0.0612  87  SER   C C   
1740 O O   . SER   B 81  ? 0.2227 0.2269 0.3125 0.0217  0.0371  0.0638  87  SER   C O   
1741 C CB  . SER   B 81  ? 0.2039 0.2110 0.2818 0.0187  0.0284  0.0504  87  SER   C CB  
1742 O OG  . SER   B 81  ? 0.2013 0.2091 0.2838 0.0177  0.0264  0.0496  87  SER   C OG  
1743 N N   . GLU   B 82  ? 0.2492 0.2531 0.3161 0.0227  0.0311  0.0628  88  GLU   C N   
1744 C CA  . GLU   B 82  ? 0.2625 0.2660 0.3266 0.0242  0.0303  0.0680  88  GLU   C CA  
1745 C C   . GLU   B 82  ? 0.2551 0.2605 0.3272 0.0229  0.0277  0.0665  88  GLU   C C   
1746 O O   . GLU   B 82  ? 0.2758 0.2811 0.3508 0.0242  0.0284  0.0710  88  GLU   C O   
1747 C CB  . GLU   B 82  ? 0.3324 0.3350 0.3809 0.0257  0.0269  0.0698  88  GLU   C CB  
1748 C CG  . GLU   B 82  ? 0.4417 0.4457 0.4842 0.0240  0.0208  0.0653  88  GLU   C CG  
1749 C CD  . GLU   B 82  ? 0.5271 0.5299 0.5556 0.0254  0.0172  0.0674  88  GLU   C CD  
1750 O OE1 . GLU   B 82  ? 0.5425 0.5427 0.5624 0.0276  0.0196  0.0700  88  GLU   C OE1 
1751 O OE2 . GLU   B 82  ? 0.5406 0.5452 0.5671 0.0245  0.0120  0.0663  88  GLU   C OE2 
1752 N N   . TYR   B 83  ? 0.2191 0.2260 0.2958 0.0206  0.0256  0.0606  89  TYR   C N   
1753 C CA  . TYR   B 83  ? 0.2115 0.2198 0.2944 0.0196  0.0236  0.0590  89  TYR   C CA  
1754 C C   . TYR   B 83  ? 0.2178 0.2262 0.3131 0.0181  0.0256  0.0550  89  TYR   C C   
1755 O O   . TYR   B 83  ? 0.2299 0.2389 0.3309 0.0177  0.0249  0.0542  89  TYR   C O   
1756 C CB  . TYR   B 83  ? 0.2007 0.2105 0.2757 0.0185  0.0184  0.0558  89  TYR   C CB  
1757 C CG  . TYR   B 83  ? 0.1967 0.2061 0.2659 0.0174  0.0171  0.0511  89  TYR   C CG  
1758 C CD1 . TYR   B 83  ? 0.1976 0.2059 0.2564 0.0181  0.0163  0.0520  89  TYR   C CD1 
1759 C CD2 . TYR   B 83  ? 0.1835 0.1935 0.2573 0.0158  0.0166  0.0457  89  TYR   C CD2 
1760 C CE1 . TYR   B 83  ? 0.1858 0.1936 0.2400 0.0174  0.0154  0.0480  89  TYR   C CE1 
1761 C CE2 . TYR   B 83  ? 0.1858 0.1956 0.2547 0.0152  0.0153  0.0419  89  TYR   C CE2 
1762 C CZ  . TYR   B 83  ? 0.1743 0.1830 0.2339 0.0160  0.0148  0.0431  89  TYR   C CZ  
1763 O OH  . TYR   B 83  ? 0.1895 0.1977 0.2448 0.0157  0.0139  0.0397  89  TYR   C OH  
1764 N N   . TYR   B 84  ? 0.1851 0.1929 0.2856 0.0174  0.0281  0.0525  90  TYR   C N   
1765 C CA  . TYR   B 84  ? 0.1733 0.1810 0.2865 0.0160  0.0299  0.0487  90  TYR   C CA  
1766 C C   . TYR   B 84  ? 0.1699 0.1767 0.2911 0.0161  0.0345  0.0503  90  TYR   C C   
1767 O O   . TYR   B 84  ? 0.1704 0.1772 0.2863 0.0169  0.0357  0.0521  90  TYR   C O   
1768 C CB  . TYR   B 84  ? 0.1647 0.1736 0.2768 0.0144  0.0265  0.0414  90  TYR   C CB  
1769 C CG  . TYR   B 84  ? 0.1534 0.1629 0.2605 0.0140  0.0229  0.0390  90  TYR   C CG  
1770 C CD1 . TYR   B 84  ? 0.1521 0.1611 0.2653 0.0140  0.0235  0.0389  90  TYR   C CD1 
1771 C CD2 . TYR   B 84  ? 0.1488 0.1590 0.2459 0.0137  0.0195  0.0368  90  TYR   C CD2 
1772 C CE1 . TYR   B 84  ? 0.1531 0.1627 0.2623 0.0137  0.0210  0.0368  90  TYR   C CE1 
1773 C CE2 . TYR   B 84  ? 0.1456 0.1563 0.2388 0.0133  0.0169  0.0348  90  TYR   C CE2 
1774 C CZ  . TYR   B 84  ? 0.1502 0.1607 0.2497 0.0133  0.0178  0.0347  90  TYR   C CZ  
1775 O OH  . TYR   B 84  ? 0.1492 0.1602 0.2455 0.0131  0.0160  0.0330  90  TYR   C OH  
1776 N N   . PRO   B 85  ? 0.1736 0.1795 0.3083 0.0152  0.0373  0.0491  91  PRO   C N   
1777 C CA  . PRO   B 85  ? 0.1664 0.1718 0.3109 0.0147  0.0415  0.0495  91  PRO   C CA  
1778 C C   . PRO   B 85  ? 0.1712 0.1788 0.3165 0.0132  0.0389  0.0432  91  PRO   C C   
1779 O O   . PRO   B 85  ? 0.1669 0.1758 0.3058 0.0126  0.0340  0.0383  91  PRO   C O   
1780 C CB  . PRO   B 85  ? 0.1720 0.1756 0.3309 0.0138  0.0441  0.0490  91  PRO   C CB  
1781 C CG  . PRO   B 85  ? 0.1801 0.1842 0.3370 0.0130  0.0398  0.0438  91  PRO   C CG  
1782 C CD  . PRO   B 85  ? 0.1747 0.1799 0.3169 0.0144  0.0365  0.0463  91  PRO   C CD  
1783 N N   . ALA   B 86  ? 0.1560 0.1641 0.3108 0.0126  0.0422  0.0430  92  ALA   C N   
1784 C CA  . ALA   B 86  ? 0.1746 0.1852 0.3332 0.0113  0.0396  0.0369  92  ALA   C CA  
1785 C C   . ALA   B 86  ? 0.1824 0.1932 0.3482 0.0094  0.0360  0.0301  92  ALA   C C   
1786 O O   . ALA   B 86  ? 0.2001 0.2090 0.3756 0.0087  0.0382  0.0305  92  ALA   C O   
1787 C CB  . ALA   B 86  ? 0.1736 0.1849 0.3442 0.0110  0.0444  0.0387  92  ALA   C CB  
1788 N N   . ARG   B 87  ? 0.1786 0.1911 0.3381 0.0090  0.0307  0.0244  93  ARG   C N   
1789 C CA  . ARG   B 87  ? 0.1813 0.1935 0.3440 0.0078  0.0271  0.0180  93  ARG   C CA  
1790 C C   . ARG   B 87  ? 0.1724 0.1867 0.3280 0.0078  0.0216  0.0123  93  ARG   C C   
1791 O O   . ARG   B 87  ? 0.1677 0.1833 0.3143 0.0088  0.0206  0.0138  93  ARG   C O   
1792 C CB  . ARG   B 87  ? 0.1844 0.1943 0.3407 0.0085  0.0268  0.0195  93  ARG   C CB  
1793 C CG  . ARG   B 87  ? 0.1701 0.1806 0.3104 0.0097  0.0242  0.0212  93  ARG   C CG  
1794 C CD  . ARG   B 87  ? 0.1799 0.1889 0.3158 0.0103  0.0240  0.0228  93  ARG   C CD  
1795 N NE  . ARG   B 87  ? 0.1759 0.1857 0.2985 0.0109  0.0207  0.0226  93  ARG   C NE  
1796 C CZ  . ARG   B 87  ? 0.1868 0.1960 0.3044 0.0111  0.0189  0.0209  93  ARG   C CZ  
1797 N NH1 . ARG   B 87  ? 0.1829 0.1906 0.3069 0.0110  0.0202  0.0196  93  ARG   C NH1 
1798 N NH2 . ARG   B 87  ? 0.1963 0.2061 0.3029 0.0115  0.0162  0.0208  93  ARG   C NH2 
1799 N N   . TYR   B 88  ? 0.1898 0.2038 0.3480 0.0070  0.0182  0.0058  94  TYR   C N   
1800 C CA  . TYR   B 88  ? 0.2090 0.2243 0.3585 0.0074  0.0128  0.0007  94  TYR   C CA  
1801 C C   . TYR   B 88  ? 0.1921 0.2056 0.3272 0.0086  0.0117  0.0022  94  TYR   C C   
1802 O O   . TYR   B 88  ? 0.2016 0.2130 0.3371 0.0086  0.0134  0.0031  94  TYR   C O   
1803 C CB  . TYR   B 88  ? 0.2371 0.2520 0.3938 0.0064  0.0096  -0.0068 94  TYR   C CB  
1804 C CG  . TYR   B 88  ? 0.2615 0.2792 0.4318 0.0051  0.0088  -0.0097 94  TYR   C CG  
1805 C CD1 . TYR   B 88  ? 0.2702 0.2912 0.4383 0.0057  0.0053  -0.0118 94  TYR   C CD1 
1806 C CD2 . TYR   B 88  ? 0.2734 0.2904 0.4597 0.0034  0.0121  -0.0097 94  TYR   C CD2 
1807 C CE1 . TYR   B 88  ? 0.2833 0.3076 0.4655 0.0046  0.0046  -0.0142 94  TYR   C CE1 
1808 C CE2 . TYR   B 88  ? 0.2843 0.3042 0.4848 0.0020  0.0116  -0.0122 94  TYR   C CE2 
1809 C CZ  . TYR   B 88  ? 0.2974 0.3213 0.4962 0.0026  0.0078  -0.0144 94  TYR   C CZ  
1810 O OH  . TYR   B 88  ? 0.3287 0.3561 0.5434 0.0012  0.0072  -0.0169 94  TYR   C OH  
1811 N N   . GLN   B 89  ? 0.1703 0.1848 0.2941 0.0097  0.0092  0.0024  95  GLN   C N   
1812 C CA  . GLN   B 89  ? 0.1585 0.1715 0.2696 0.0106  0.0079  0.0032  95  GLN   C CA  
1813 C C   . GLN   B 89  ? 0.1410 0.1542 0.2457 0.0112  0.0035  -0.0023 95  GLN   C C   
1814 O O   . GLN   B 89  ? 0.1527 0.1678 0.2580 0.0116  0.0012  -0.0043 95  GLN   C O   
1815 C CB  . GLN   B 89  ? 0.1659 0.1791 0.2691 0.0112  0.0092  0.0088  95  GLN   C CB  
1816 C CG  . GLN   B 89  ? 0.1814 0.1933 0.2734 0.0118  0.0079  0.0098  95  GLN   C CG  
1817 C CD  . GLN   B 89  ? 0.1706 0.1821 0.2568 0.0120  0.0094  0.0154  95  GLN   C CD  
1818 O OE1 . GLN   B 89  ? 0.1759 0.1875 0.2663 0.0120  0.0121  0.0195  95  GLN   C OE1 
1819 N NE2 . GLN   B 89  ? 0.1590 0.1700 0.2353 0.0124  0.0075  0.0157  95  GLN   C NE2 
1820 N N   . SER   B 90  ? 0.1353 0.1465 0.2337 0.0117  0.0024  -0.0046 96  SER   C N   
1821 C CA  . SER   B 90  ? 0.1454 0.1561 0.2362 0.0128  -0.0014 -0.0094 96  SER   C CA  
1822 C C   . SER   B 90  ? 0.1362 0.1463 0.2142 0.0140  -0.0021 -0.0068 96  SER   C C   
1823 O O   . SER   B 90  ? 0.1432 0.1528 0.2180 0.0137  0.0002  -0.0020 96  SER   C O   
1824 C CB  . SER   B 90  ? 0.1701 0.1784 0.2612 0.0130  -0.0017 -0.0140 96  SER   C CB  
1825 O OG  . SER   B 90  ? 0.1755 0.1819 0.2623 0.0132  0.0013  -0.0106 96  SER   C OG  
1826 N N   . HIS   B 91  ? 0.1447 0.1545 0.2154 0.0154  -0.0056 -0.0102 97  HIS   C N   
1827 C CA  . HIS   B 91  ? 0.1480 0.1565 0.2066 0.0167  -0.0064 -0.0084 97  HIS   C CA  
1828 C C   . HIS   B 91  ? 0.1418 0.1513 0.1993 0.0163  -0.0051 -0.0035 97  HIS   C C   
1829 O O   . HIS   B 91  ? 0.1556 0.1634 0.2056 0.0164  -0.0040 -0.0004 97  HIS   C O   
1830 C CB  . HIS   B 91  ? 0.1652 0.1709 0.2171 0.0170  -0.0044 -0.0075 97  HIS   C CB  
1831 C CG  . HIS   B 91  ? 0.1786 0.1826 0.2293 0.0179  -0.0052 -0.0125 97  HIS   C CG  
1832 N ND1 . HIS   B 91  ? 0.2065 0.2085 0.2469 0.0200  -0.0073 -0.0153 97  HIS   C ND1 
1833 C CD2 . HIS   B 91  ? 0.1824 0.1859 0.2409 0.0172  -0.0042 -0.0154 97  HIS   C CD2 
1834 C CE1 . HIS   B 91  ? 0.2145 0.2149 0.2555 0.0206  -0.0076 -0.0199 97  HIS   C CE1 
1835 N NE2 . HIS   B 91  ? 0.2134 0.2144 0.2654 0.0188  -0.0057 -0.0203 97  HIS   C NE2 
1836 N N   . LEU   B 92  ? 0.1345 0.1462 0.1991 0.0159  -0.0051 -0.0030 98  LEU   C N   
1837 C CA  . LEU   B 92  ? 0.1359 0.1481 0.1994 0.0157  -0.0035 0.0012  98  LEU   C CA  
1838 C C   . LEU   B 92  ? 0.1331 0.1463 0.1938 0.0171  -0.0058 0.0001  98  LEU   C C   
1839 O O   . LEU   B 92  ? 0.1379 0.1530 0.2030 0.0178  -0.0085 -0.0036 98  LEU   C O   
1840 C CB  . LEU   B 92  ? 0.1500 0.1639 0.2246 0.0146  -0.0006 0.0032  98  LEU   C CB  
1841 C CG  . LEU   B 92  ? 0.1606 0.1744 0.2331 0.0146  0.0018  0.0080  98  LEU   C CG  
1842 C CD1 . LEU   B 92  ? 0.1693 0.1810 0.2344 0.0142  0.0030  0.0116  98  LEU   C CD1 
1843 C CD2 . LEU   B 92  ? 0.1724 0.1877 0.2558 0.0140  0.0050  0.0099  98  LEU   C CD2 
1844 N N   . MET   B 93  ? 0.1340 0.1458 0.1873 0.0177  -0.0051 0.0032  99  MET   C N   
1845 C CA  . MET   B 93  ? 0.1273 0.1393 0.1773 0.0193  -0.0068 0.0028  99  MET   C CA  
1846 C C   . MET   B 93  ? 0.1376 0.1498 0.1895 0.0191  -0.0039 0.0061  99  MET   C C   
1847 O O   . MET   B 93  ? 0.1466 0.1571 0.1950 0.0182  -0.0017 0.0092  99  MET   C O   
1848 C CB  . MET   B 93  ? 0.1532 0.1621 0.1914 0.0203  -0.0079 0.0033  99  MET   C CB  
1849 C CG  . MET   B 93  ? 0.1740 0.1820 0.2087 0.0209  -0.0100 0.0004  99  MET   C CG  
1850 S SD  . MET   B 93  ? 0.1798 0.1836 0.2015 0.0219  -0.0100 0.0021  99  MET   C SD  
1851 C CE  . MET   B 93  ? 0.1839 0.1863 0.2054 0.0194  -0.0065 0.0059  99  MET   C CE  
1852 N N   . LEU   B 94  ? 0.1259 0.1402 0.1827 0.0202  -0.0040 0.0056  100 LEU   C N   
1853 C CA  . LEU   B 94  ? 0.1361 0.1501 0.1939 0.0204  -0.0006 0.0088  100 LEU   C CA  
1854 C C   . LEU   B 94  ? 0.1381 0.1504 0.1888 0.0223  -0.0011 0.0093  100 LEU   C C   
1855 O O   . LEU   B 94  ? 0.1527 0.1656 0.2023 0.0238  -0.0042 0.0070  100 LEU   C O   
1856 C CB  . LEU   B 94  ? 0.1418 0.1595 0.2128 0.0204  0.0012  0.0085  100 LEU   C CB  
1857 C CG  . LEU   B 94  ? 0.1487 0.1680 0.2292 0.0186  0.0026  0.0082  100 LEU   C CG  
1858 C CD1 . LEU   B 94  ? 0.1957 0.2182 0.2896 0.0186  0.0050  0.0084  100 LEU   C CD1 
1859 C CD2 . LEU   B 94  ? 0.1832 0.1999 0.2594 0.0175  0.0056  0.0119  100 LEU   C CD2 
1860 N N   . ALA   B 95  ? 0.1395 0.1494 0.1856 0.0225  0.0018  0.0122  101 ALA   C N   
1861 C CA  . ALA   B 95  ? 0.1387 0.1466 0.1794 0.0243  0.0024  0.0128  101 ALA   C CA  
1862 C C   . ALA   B 95  ? 0.1387 0.1464 0.1815 0.0248  0.0069  0.0153  101 ALA   C C   
1863 O O   . ALA   B 95  ? 0.1349 0.1429 0.1802 0.0236  0.0093  0.0173  101 ALA   C O   
1864 C CB  . ALA   B 95  ? 0.1611 0.1642 0.1894 0.0241  0.0014  0.0134  101 ALA   C CB  
1865 N N   . VAL   B 96  ? 0.1475 0.1541 0.1886 0.0269  0.0083  0.0155  102 VAL   C N   
1866 C CA  . VAL   B 96  ? 0.1568 0.1620 0.1972 0.0278  0.0131  0.0180  102 VAL   C CA  
1867 C C   . VAL   B 96  ? 0.1638 0.1636 0.1909 0.0274  0.0136  0.0193  102 VAL   C C   
1868 O O   . VAL   B 96  ? 0.1875 0.1838 0.2066 0.0280  0.0117  0.0182  102 VAL   C O   
1869 C CB  . VAL   B 96  ? 0.1701 0.1764 0.2148 0.0304  0.0146  0.0173  102 VAL   C CB  
1870 C CG1 . VAL   B 96  ? 0.1956 0.1997 0.2382 0.0318  0.0203  0.0199  102 VAL   C CG1 
1871 C CG2 . VAL   B 96  ? 0.1827 0.1951 0.2420 0.0305  0.0132  0.0157  102 VAL   C CG2 
1872 N N   . GLY   B 97  ? 0.1722 0.1711 0.1971 0.0265  0.0157  0.0216  103 GLY   C N   
1873 C CA  . GLY   B 97  ? 0.1846 0.1788 0.1973 0.0259  0.0152  0.0226  103 GLY   C CA  
1874 C C   . GLY   B 97  ? 0.1864 0.1805 0.1979 0.0251  0.0168  0.0254  103 GLY   C C   
1875 O O   . GLY   B 97  ? 0.2116 0.2091 0.2321 0.0247  0.0187  0.0268  103 GLY   C O   
1876 N N   . HIS   B 98  ? 0.1991 0.1893 0.1996 0.0248  0.0161  0.0262  104 HIS   C N   
1877 C CA  . HIS   B 98  ? 0.1973 0.1871 0.1949 0.0245  0.0172  0.0291  104 HIS   C CA  
1878 C C   . HIS   B 98  ? 0.1883 0.1801 0.1882 0.0222  0.0137  0.0296  104 HIS   C C   
1879 O O   . HIS   B 98  ? 0.1877 0.1787 0.1847 0.0207  0.0099  0.0276  104 HIS   C O   
1880 C CB  . HIS   B 98  ? 0.2346 0.2193 0.2190 0.0256  0.0175  0.0295  104 HIS   C CB  
1881 C CG  . HIS   B 98  ? 0.2685 0.2527 0.2487 0.0260  0.0187  0.0329  104 HIS   C CG  
1882 N ND1 . HIS   B 98  ? 0.3044 0.2897 0.2885 0.0278  0.0238  0.0361  104 HIS   C ND1 
1883 C CD2 . HIS   B 98  ? 0.3058 0.2888 0.2792 0.0249  0.0152  0.0337  104 HIS   C CD2 
1884 C CE1 . HIS   B 98  ? 0.3339 0.3182 0.3123 0.0280  0.0234  0.0391  104 HIS   C CE1 
1885 N NE2 . HIS   B 98  ? 0.3347 0.3178 0.3065 0.0264  0.0179  0.0376  104 HIS   C NE2 
1886 N N   . SER   B 99  ? 0.1873 0.1813 0.1923 0.0220  0.0153  0.0324  105 SER   C N   
1887 C CA  . SER   B 99  ? 0.1865 0.1823 0.1941 0.0202  0.0126  0.0333  105 SER   C CA  
1888 C C   . SER   B 99  ? 0.2039 0.2003 0.2127 0.0210  0.0150  0.0376  105 SER   C C   
1889 O O   . SER   B 99  ? 0.2369 0.2348 0.2535 0.0218  0.0189  0.0393  105 SER   C O   
1890 C CB  . SER   B 99  ? 0.1979 0.1970 0.2161 0.0191  0.0118  0.0312  105 SER   C CB  
1891 O OG  . SER   B 99  ? 0.1999 0.2008 0.2218 0.0177  0.0102  0.0322  105 SER   C OG  
1892 N N   . GLU   B 100 ? 0.2175 0.2124 0.2184 0.0209  0.0126  0.0393  106 GLU   C N   
1893 C CA  . GLU   B 100 ? 0.2208 0.2159 0.2209 0.0219  0.0138  0.0438  106 GLU   C CA  
1894 C C   . GLU   B 100 ? 0.1899 0.1882 0.1978 0.0201  0.0111  0.0441  106 GLU   C C   
1895 O O   . GLU   B 100 ? 0.1783 0.1776 0.1881 0.0182  0.0079  0.0411  106 GLU   C O   
1896 C CB  . GLU   B 100 ? 0.2574 0.2493 0.2436 0.0228  0.0111  0.0449  106 GLU   C CB  
1897 C CG  . GLU   B 100 ? 0.3350 0.3227 0.3098 0.0245  0.0125  0.0438  106 GLU   C CG  
1898 C CD  . GLU   B 100 ? 0.3803 0.3663 0.3526 0.0275  0.0183  0.0474  106 GLU   C CD  
1899 O OE1 . GLU   B 100 ? 0.3704 0.3585 0.3500 0.0281  0.0211  0.0512  106 GLU   C OE1 
1900 O OE2 . GLU   B 100 ? 0.4017 0.3840 0.3652 0.0292  0.0205  0.0465  106 GLU   C OE2 
1901 N N   . PRO   B 101 ? 0.1978 0.1973 0.2096 0.0208  0.0125  0.0482  107 PRO   C N   
1902 C CA  . PRO   B 101 ? 0.1800 0.1822 0.1990 0.0194  0.0101  0.0486  107 PRO   C CA  
1903 C C   . PRO   B 101 ? 0.1893 0.1919 0.2033 0.0180  0.0048  0.0470  107 PRO   C C   
1904 O O   . PRO   B 101 ? 0.1795 0.1840 0.1996 0.0163  0.0031  0.0450  107 PRO   C O   
1905 C CB  . PRO   B 101 ? 0.2111 0.2136 0.2321 0.0211  0.0122  0.0541  107 PRO   C CB  
1906 C CG  . PRO   B 101 ? 0.2619 0.2620 0.2792 0.0232  0.0169  0.0563  107 PRO   C CG  
1907 C CD  . PRO   B 101 ? 0.2363 0.2345 0.2471 0.0232  0.0170  0.0528  107 PRO   C CD  
1908 N N   . GLY   B 102 ? 0.1876 0.1881 0.1906 0.0186  0.0022  0.0475  108 GLY   C N   
1909 C CA  . GLY   B 102 ? 0.1939 0.1947 0.1931 0.0169  -0.0031 0.0459  108 GLY   C CA  
1910 C C   . GLY   B 102 ? 0.1887 0.1887 0.1882 0.0150  -0.0043 0.0413  108 GLY   C C   
1911 O O   . GLY   B 102 ? 0.2029 0.2035 0.2021 0.0132  -0.0079 0.0398  108 GLY   C O   
1912 N N   . ASP   B 103 ? 0.1787 0.1774 0.1790 0.0154  -0.0011 0.0391  109 ASP   C N   
1913 C CA  . ASP   B 103 ? 0.1626 0.1603 0.1629 0.0141  -0.0021 0.0353  109 ASP   C CA  
1914 C C   . ASP   B 103 ? 0.1603 0.1607 0.1697 0.0128  -0.0020 0.0341  109 ASP   C C   
1915 O O   . ASP   B 103 ? 0.1606 0.1602 0.1695 0.0118  -0.0031 0.0314  109 ASP   C O   
1916 C CB  . ASP   B 103 ? 0.1782 0.1739 0.1762 0.0154  0.0009  0.0336  109 ASP   C CB  
1917 C CG  . ASP   B 103 ? 0.2101 0.2020 0.1975 0.0167  0.0009  0.0338  109 ASP   C CG  
1918 O OD1 . ASP   B 103 ? 0.2078 0.1979 0.1886 0.0158  -0.0025 0.0331  109 ASP   C OD1 
1919 O OD2 . ASP   B 103 ? 0.2122 0.2029 0.1981 0.0186  0.0045  0.0345  109 ASP   C OD2 
1920 N N   . CYS   B 104 ? 0.1434 0.1465 0.1607 0.0130  -0.0006 0.0361  110 CYS   C N   
1921 C CA  . CYS   B 104 ? 0.1363 0.1415 0.1615 0.0120  -0.0003 0.0347  110 CYS   C CA  
1922 C C   . CYS   B 104 ? 0.1410 0.1465 0.1652 0.0105  -0.0031 0.0339  110 CYS   C C   
1923 O O   . CYS   B 104 ? 0.1602 0.1661 0.1820 0.0099  -0.0056 0.0357  110 CYS   C O   
1924 C CB  . CYS   B 104 ? 0.1344 0.1419 0.1680 0.0126  0.0015  0.0372  110 CYS   C CB  
1925 S SG  . CYS   B 104 ? 0.1622 0.1697 0.2014 0.0139  0.0057  0.0375  110 CYS   C SG  
1926 N N   . GLY   B 105 ? 0.1229 0.1282 0.1490 0.0098  -0.0028 0.0313  111 GLY   C N   
1927 C CA  . GLY   B 105 ? 0.1354 0.1407 0.1613 0.0083  -0.0044 0.0307  111 GLY   C CA  
1928 C C   . GLY   B 105 ? 0.1402 0.1424 0.1591 0.0077  -0.0057 0.0287  111 GLY   C C   
1929 O O   . GLY   B 105 ? 0.1518 0.1533 0.1709 0.0065  -0.0063 0.0279  111 GLY   C O   
1930 N N   . GLY   B 106 ? 0.1482 0.1481 0.1611 0.0086  -0.0056 0.0279  112 GLY   C N   
1931 C CA  . GLY   B 106 ? 0.1512 0.1474 0.1576 0.0084  -0.0064 0.0259  112 GLY   C CA  
1932 C C   . GLY   B 106 ? 0.1427 0.1383 0.1503 0.0088  -0.0051 0.0240  112 GLY   C C   
1933 O O   . GLY   B 106 ? 0.1416 0.1387 0.1527 0.0100  -0.0036 0.0233  112 GLY   C O   
1934 N N   . ILE   B 107 ? 0.1416 0.1346 0.1460 0.0080  -0.0058 0.0232  113 ILE   C N   
1935 C CA  . ILE   B 107 ? 0.1459 0.1378 0.1501 0.0088  -0.0046 0.0218  113 ILE   C CA  
1936 C C   . ILE   B 107 ? 0.1521 0.1416 0.1518 0.0107  -0.0042 0.0202  113 ILE   C C   
1937 O O   . ILE   B 107 ? 0.1507 0.1376 0.1459 0.0109  -0.0047 0.0200  113 ILE   C O   
1938 C CB  . ILE   B 107 ? 0.1769 0.1667 0.1803 0.0072  -0.0048 0.0223  113 ILE   C CB  
1939 C CG1 . ILE   B 107 ? 0.2106 0.2038 0.2209 0.0061  -0.0040 0.0237  113 ILE   C CG1 
1940 C CG2 . ILE   B 107 ? 0.1813 0.1678 0.1806 0.0084  -0.0035 0.0212  113 ILE   C CG2 
1941 C CD1 . ILE   B 107 ? 0.2575 0.2497 0.2696 0.0042  -0.0038 0.0247  113 ILE   C CD1 
1942 N N   . LEU   B 108 ? 0.1399 0.1306 0.1412 0.0123  -0.0035 0.0190  114 LEU   C N   
1943 C CA  . LEU   B 108 ? 0.1329 0.1218 0.1308 0.0143  -0.0036 0.0175  114 LEU   C CA  
1944 C C   . LEU   B 108 ? 0.1329 0.1193 0.1274 0.0147  -0.0033 0.0174  114 LEU   C C   
1945 O O   . LEU   B 108 ? 0.1416 0.1292 0.1380 0.0145  -0.0027 0.0174  114 LEU   C O   
1946 C CB  . LEU   B 108 ? 0.1311 0.1233 0.1337 0.0158  -0.0035 0.0161  114 LEU   C CB  
1947 C CG  . LEU   B 108 ? 0.1344 0.1260 0.1352 0.0182  -0.0044 0.0143  114 LEU   C CG  
1948 C CD1 . LEU   B 108 ? 0.1641 0.1539 0.1623 0.0193  -0.0042 0.0146  114 LEU   C CD1 
1949 C CD2 . LEU   B 108 ? 0.1416 0.1372 0.1488 0.0192  -0.0049 0.0124  114 LEU   C CD2 
1950 N N   . ARG   B 109 ? 0.1387 0.1212 0.1280 0.0155  -0.0034 0.0175  115 ARG   C N   
1951 C CA  . ARG   B 109 ? 0.1566 0.1358 0.1419 0.0161  -0.0026 0.0180  115 ARG   C CA  
1952 C C   . ARG   B 109 ? 0.1602 0.1370 0.1410 0.0189  -0.0031 0.0174  115 ARG   C C   
1953 O O   . ARG   B 109 ? 0.1659 0.1420 0.1460 0.0198  -0.0037 0.0168  115 ARG   C O   
1954 C CB  . ARG   B 109 ? 0.2016 0.1775 0.1858 0.0137  -0.0020 0.0195  115 ARG   C CB  
1955 C CG  . ARG   B 109 ? 0.2452 0.2177 0.2264 0.0134  -0.0027 0.0192  115 ARG   C CG  
1956 C CD  . ARG   B 109 ? 0.3145 0.2837 0.2955 0.0107  -0.0027 0.0199  115 ARG   C CD  
1957 N NE  . ARG   B 109 ? 0.3765 0.3489 0.3617 0.0082  -0.0039 0.0202  115 ARG   C NE  
1958 C CZ  . ARG   B 109 ? 0.4936 0.4674 0.4832 0.0059  -0.0038 0.0213  115 ARG   C CZ  
1959 N NH1 . ARG   B 109 ? 0.5287 0.5010 0.5191 0.0059  -0.0016 0.0225  115 ARG   C NH1 
1960 N NH2 . ARG   B 109 ? 0.5139 0.4909 0.5075 0.0040  -0.0055 0.0216  115 ARG   C NH2 
1961 N N   . CYS   B 110 ? 0.1669 0.1421 0.1442 0.0207  -0.0026 0.0177  116 CYS   C N   
1962 C CA  . CYS   B 110 ? 0.1792 0.1516 0.1514 0.0239  -0.0032 0.0177  116 CYS   C CA  
1963 C C   . CYS   B 110 ? 0.1982 0.1652 0.1654 0.0239  -0.0012 0.0199  116 CYS   C C   
1964 O O   . CYS   B 110 ? 0.1915 0.1574 0.1602 0.0212  0.0006  0.0212  116 CYS   C O   
1965 C CB  . CYS   B 110 ? 0.1577 0.1332 0.1297 0.0266  -0.0050 0.0159  116 CYS   C CB  
1966 S SG  . CYS   B 110 ? 0.1691 0.1444 0.1383 0.0268  -0.0036 0.0161  116 CYS   C SG  
1967 N N   . GLN   B 111 ? 0.2119 0.1756 0.1735 0.0271  -0.0013 0.0207  117 GLN   C N   
1968 C CA  . GLN   B 111 ? 0.2358 0.1939 0.1925 0.0275  0.0013  0.0234  117 GLN   C CA  
1969 C C   . GLN   B 111 ? 0.2357 0.1942 0.1915 0.0270  0.0036  0.0245  117 GLN   C C   
1970 O O   . GLN   B 111 ? 0.2571 0.2115 0.2115 0.0260  0.0067  0.0270  117 GLN   C O   
1971 C CB  . GLN   B 111 ? 0.2485 0.2030 0.1988 0.0317  0.0008  0.0245  117 GLN   C CB  
1972 C CG  . GLN   B 111 ? 0.2829 0.2402 0.2294 0.0353  -0.0012 0.0235  117 GLN   C CG  
1973 C CD  . GLN   B 111 ? 0.4427 0.3972 0.3830 0.0399  -0.0026 0.0247  117 GLN   C CD  
1974 O OE1 . GLN   B 111 ? 0.4937 0.4510 0.4360 0.0419  -0.0058 0.0230  117 GLN   C OE1 
1975 N NE2 . GLN   B 111 ? 0.4491 0.3983 0.3823 0.0418  -0.0001 0.0278  117 GLN   C NE2 
1976 N N   . HIS   B 112 ? 0.2079 0.1710 0.1652 0.0274  0.0024  0.0225  118 HIS   C N   
1977 C CA  . HIS   B 112 ? 0.2099 0.1729 0.1658 0.0274  0.0050  0.0233  118 HIS   C CA  
1978 C C   . HIS   B 112 ? 0.2182 0.1839 0.1816 0.0236  0.0066  0.0234  118 HIS   C C   
1979 O O   . HIS   B 112 ? 0.2280 0.1935 0.1915 0.0234  0.0094  0.0244  118 HIS   C O   
1980 C CB  . HIS   B 112 ? 0.2171 0.1827 0.1697 0.0304  0.0029  0.0208  118 HIS   C CB  
1981 C CG  . HIS   B 112 ? 0.2108 0.1746 0.1565 0.0344  0.0005  0.0206  118 HIS   C CG  
1982 N ND1 . HIS   B 112 ? 0.1829 0.1502 0.1311 0.0357  -0.0037 0.0180  118 HIS   C ND1 
1983 C CD2 . HIS   B 112 ? 0.2502 0.2093 0.1868 0.0378  0.0017  0.0228  118 HIS   C CD2 
1984 C CE1 . HIS   B 112 ? 0.2060 0.1708 0.1472 0.0396  -0.0052 0.0188  118 HIS   C CE1 
1985 N NE2 . HIS   B 112 ? 0.2517 0.2115 0.1851 0.0411  -0.0022 0.0216  118 HIS   C NE2 
1986 N N   . GLY   B 113 ? 0.2014 0.1698 0.1710 0.0210  0.0047  0.0225  119 GLY   C N   
1987 C CA  . GLY   B 113 ? 0.1963 0.1678 0.1732 0.0177  0.0055  0.0228  119 GLY   C CA  
1988 C C   . GLY   B 113 ? 0.1681 0.1444 0.1501 0.0168  0.0030  0.0208  119 GLY   C C   
1989 O O   . GLY   B 113 ? 0.1746 0.1514 0.1557 0.0178  0.0008  0.0194  119 GLY   C O   
1990 N N   . VAL   B 114 ? 0.1700 0.1497 0.1581 0.0149  0.0037  0.0209  120 VAL   C N   
1991 C CA  . VAL   B 114 ? 0.1670 0.1509 0.1605 0.0140  0.0018  0.0197  120 VAL   C CA  
1992 C C   . VAL   B 114 ? 0.1577 0.1437 0.1511 0.0162  0.0010  0.0173  120 VAL   C C   
1993 O O   . VAL   B 114 ? 0.1660 0.1520 0.1586 0.0173  0.0024  0.0165  120 VAL   C O   
1994 C CB  . VAL   B 114 ? 0.1715 0.1581 0.1718 0.0116  0.0028  0.0211  120 VAL   C CB  
1995 C CG1 . VAL   B 114 ? 0.1870 0.1776 0.1926 0.0111  0.0014  0.0203  120 VAL   C CG1 
1996 C CG2 . VAL   B 114 ? 0.1921 0.1771 0.1937 0.0091  0.0027  0.0230  120 VAL   C CG2 
1997 N N   . VAL   B 115 ? 0.1425 0.1300 0.1370 0.0169  -0.0010 0.0159  121 VAL   C N   
1998 C CA  . VAL   B 115 ? 0.1481 0.1380 0.1443 0.0186  -0.0023 0.0132  121 VAL   C CA  
1999 C C   . VAL   B 115 ? 0.1554 0.1490 0.1595 0.0172  -0.0020 0.0127  121 VAL   C C   
2000 O O   . VAL   B 115 ? 0.1548 0.1498 0.1613 0.0180  -0.0021 0.0105  121 VAL   C O   
2001 C CB  . VAL   B 115 ? 0.1425 0.1325 0.1376 0.0200  -0.0043 0.0123  121 VAL   C CB  
2002 C CG1 . VAL   B 115 ? 0.1605 0.1538 0.1600 0.0212  -0.0060 0.0095  121 VAL   C CG1 
2003 C CG2 . VAL   B 115 ? 0.1653 0.1514 0.1529 0.0218  -0.0046 0.0130  121 VAL   C CG2 
2004 N N   . GLY   B 116 ? 0.1364 0.1310 0.1439 0.0153  -0.0017 0.0146  122 GLY   C N   
2005 C CA  . GLY   B 116 ? 0.1499 0.1476 0.1647 0.0143  -0.0012 0.0149  122 GLY   C CA  
2006 C C   . GLY   B 116 ? 0.1319 0.1302 0.1483 0.0127  -0.0013 0.0175  122 GLY   C C   
2007 O O   . GLY   B 116 ? 0.1443 0.1405 0.1562 0.0121  -0.0018 0.0186  122 GLY   C O   
2008 N N   . ILE   B 117 ? 0.1238 0.1247 0.1464 0.0122  -0.0008 0.0183  123 ILE   C N   
2009 C CA  . ILE   B 117 ? 0.1260 0.1274 0.1490 0.0112  -0.0011 0.0209  123 ILE   C CA  
2010 C C   . ILE   B 117 ? 0.1231 0.1259 0.1493 0.0119  -0.0005 0.0212  123 ILE   C C   
2011 O O   . ILE   B 117 ? 0.1311 0.1355 0.1629 0.0125  0.0004  0.0199  123 ILE   C O   
2012 C CB  . ILE   B 117 ? 0.1332 0.1363 0.1605 0.0099  -0.0008 0.0232  123 ILE   C CB  
2013 C CG1 . ILE   B 117 ? 0.1389 0.1440 0.1733 0.0104  0.0008  0.0226  123 ILE   C CG1 
2014 C CG2 . ILE   B 117 ? 0.1523 0.1541 0.1769 0.0088  -0.0012 0.0236  123 ILE   C CG2 
2015 C CD1 . ILE   B 117 ? 0.1567 0.1639 0.1970 0.0095  0.0014  0.0254  123 ILE   C CD1 
2016 N N   . VAL   B 118 ? 0.1278 0.1298 0.1508 0.0118  -0.0007 0.0231  124 VAL   C N   
2017 C CA  . VAL   B 118 ? 0.1293 0.1323 0.1551 0.0127  0.0008  0.0242  124 VAL   C CA  
2018 C C   . VAL   B 118 ? 0.1330 0.1384 0.1667 0.0124  0.0021  0.0257  124 VAL   C C   
2019 O O   . VAL   B 118 ? 0.1243 0.1304 0.1590 0.0117  0.0016  0.0276  124 VAL   C O   
2020 C CB  . VAL   B 118 ? 0.1277 0.1290 0.1473 0.0129  0.0006  0.0262  124 VAL   C CB  
2021 C CG1 . VAL   B 118 ? 0.1381 0.1402 0.1602 0.0140  0.0030  0.0281  124 VAL   C CG1 
2022 C CG2 . VAL   B 118 ? 0.1430 0.1413 0.1553 0.0133  -0.0003 0.0244  124 VAL   C CG2 
2023 N N   . SER   B 119 ? 0.1222 0.1289 0.1623 0.0131  0.0040  0.0251  125 SER   C N   
2024 C CA  . SER   B 119 ? 0.1221 0.1304 0.1706 0.0130  0.0058  0.0265  125 SER   C CA  
2025 C C   . SER   B 119 ? 0.1351 0.1438 0.1879 0.0138  0.0084  0.0284  125 SER   C C   
2026 O O   . SER   B 119 ? 0.1399 0.1492 0.1980 0.0138  0.0103  0.0312  125 SER   C O   
2027 C CB  . SER   B 119 ? 0.1349 0.1439 0.1887 0.0127  0.0055  0.0230  125 SER   C CB  
2028 O OG  . SER   B 119 ? 0.1414 0.1514 0.2042 0.0125  0.0074  0.0238  125 SER   C OG  
2029 N N   . THR   B 120 ? 0.1403 0.1488 0.1923 0.0145  0.0090  0.0271  126 THR   C N   
2030 C CA  . THR   B 120 ? 0.1304 0.1395 0.1882 0.0153  0.0124  0.0290  126 THR   C CA  
2031 C C   . THR   B 120 ? 0.1266 0.1342 0.1773 0.0165  0.0134  0.0301  126 THR   C C   
2032 O O   . THR   B 120 ? 0.1293 0.1356 0.1722 0.0166  0.0112  0.0284  126 THR   C O   
2033 C CB  . THR   B 120 ? 0.1333 0.1444 0.2020 0.0149  0.0132  0.0259  126 THR   C CB  
2034 O OG1 . THR   B 120 ? 0.1480 0.1595 0.2145 0.0154  0.0113  0.0225  126 THR   C OG1 
2035 C CG2 . THR   B 120 ? 0.1561 0.1678 0.2308 0.0139  0.0121  0.0237  126 THR   C CG2 
2036 N N   . GLY   B 121 ? 0.1407 0.1481 0.1940 0.0175  0.0171  0.0330  127 GLY   C N   
2037 C CA  . GLY   B 121 ? 0.1649 0.1706 0.2119 0.0191  0.0191  0.0341  127 GLY   C CA  
2038 C C   . GLY   B 121 ? 0.2081 0.2144 0.2621 0.0202  0.0242  0.0369  127 GLY   C C   
2039 O O   . GLY   B 121 ? 0.2429 0.2501 0.3046 0.0198  0.0264  0.0392  127 GLY   C O   
2040 N N   . GLY   B 122 ? 0.2494 0.2545 0.2996 0.0218  0.0268  0.0375  128 GLY   C N   
2041 C CA  . GLY   B 122 ? 0.2819 0.2874 0.3388 0.0231  0.0326  0.0405  128 GLY   C CA  
2042 C C   . GLY   B 122 ? 0.2805 0.2882 0.3455 0.0235  0.0339  0.0377  128 GLY   C C   
2043 O O   . GLY   B 122 ? 0.2785 0.2883 0.3470 0.0226  0.0299  0.0335  128 GLY   C O   
2044 N N   . ASN   B 123 ? 0.2685 0.2759 0.3370 0.0252  0.0397  0.0405  129 ASN   C N   
2045 C CA  . ASN   B 123 ? 0.2729 0.2829 0.3507 0.0260  0.0417  0.0387  129 ASN   C CA  
2046 C C   . ASN   B 123 ? 0.2468 0.2561 0.3167 0.0268  0.0381  0.0351  129 ASN   C C   
2047 O O   . ASN   B 123 ? 0.2756 0.2880 0.3543 0.0271  0.0374  0.0325  129 ASN   C O   
2048 C CB  . ASN   B 123 ? 0.3357 0.3504 0.4313 0.0240  0.0406  0.0361  129 ASN   C CB  
2049 C CG  . ASN   B 123 ? 0.4367 0.4533 0.5471 0.0241  0.0469  0.0390  129 ASN   C CG  
2050 O OD1 . ASN   B 123 ? 0.4623 0.4770 0.5706 0.0260  0.0532  0.0434  129 ASN   C OD1 
2051 N ND2 . ASN   B 123 ? 0.4660 0.4861 0.5919 0.0220  0.0456  0.0368  129 ASN   C ND2 
2052 N N   . GLY   B 124 ? 0.2293 0.2346 0.2836 0.0274  0.0359  0.0352  130 GLY   C N   
2053 C CA  . GLY   B 124 ? 0.2206 0.2243 0.2671 0.0281  0.0328  0.0321  130 GLY   C CA  
2054 C C   . GLY   B 124 ? 0.1879 0.1936 0.2368 0.0265  0.0267  0.0282  130 GLY   C C   
2055 O O   . GLY   B 124 ? 0.1944 0.1993 0.2396 0.0273  0.0244  0.0258  130 GLY   C O   
2056 N N   . LEU   B 125 ? 0.1706 0.1783 0.2247 0.0244  0.0244  0.0278  131 LEU   C N   
2057 C CA  . LEU   B 125 ? 0.1659 0.1750 0.2211 0.0230  0.0191  0.0243  131 LEU   C CA  
2058 C C   . LEU   B 125 ? 0.1700 0.1769 0.2171 0.0216  0.0166  0.0250  131 LEU   C C   
2059 O O   . LEU   B 125 ? 0.2093 0.2151 0.2543 0.0212  0.0186  0.0281  131 LEU   C O   
2060 C CB  . LEU   B 125 ? 0.1886 0.2021 0.2583 0.0220  0.0184  0.0223  131 LEU   C CB  
2061 C CG  . LEU   B 125 ? 0.2153 0.2322 0.2962 0.0231  0.0201  0.0212  131 LEU   C CG  
2062 C CD1 . LEU   B 125 ? 0.2716 0.2924 0.3682 0.0217  0.0206  0.0201  131 LEU   C CD1 
2063 C CD2 . LEU   B 125 ? 0.2242 0.2417 0.3024 0.0244  0.0165  0.0182  131 LEU   C CD2 
2064 N N   . VAL   B 126 ? 0.1375 0.1438 0.1801 0.0209  0.0126  0.0224  132 VAL   C N   
2065 C CA  . VAL   B 126 ? 0.1378 0.1428 0.1751 0.0194  0.0101  0.0228  132 VAL   C CA  
2066 C C   . VAL   B 126 ? 0.1290 0.1362 0.1719 0.0185  0.0073  0.0197  132 VAL   C C   
2067 O O   . VAL   B 126 ? 0.1341 0.1421 0.1779 0.0192  0.0054  0.0170  132 VAL   C O   
2068 C CB  . VAL   B 126 ? 0.1406 0.1418 0.1659 0.0195  0.0083  0.0227  132 VAL   C CB  
2069 C CG1 . VAL   B 126 ? 0.1660 0.1662 0.1886 0.0206  0.0069  0.0202  132 VAL   C CG1 
2070 C CG2 . VAL   B 126 ? 0.1578 0.1584 0.1798 0.0177  0.0058  0.0229  132 VAL   C CG2 
2071 N N   . GLY   B 127 ? 0.1211 0.1291 0.1670 0.0172  0.0071  0.0204  133 GLY   C N   
2072 C CA  . GLY   B 127 ? 0.1294 0.1387 0.1795 0.0165  0.0049  0.0174  133 GLY   C CA  
2073 C C   . GLY   B 127 ? 0.1301 0.1377 0.1735 0.0156  0.0032  0.0176  133 GLY   C C   
2074 O O   . GLY   B 127 ? 0.1315 0.1383 0.1725 0.0149  0.0040  0.0204  133 GLY   C O   
2075 N N   . PHE   B 128 ? 0.1192 0.1265 0.1606 0.0158  0.0009  0.0147  134 PHE   C N   
2076 C CA  . PHE   B 128 ? 0.1213 0.1270 0.1571 0.0152  -0.0001 0.0147  134 PHE   C CA  
2077 C C   . PHE   B 128 ? 0.1285 0.1351 0.1684 0.0150  -0.0006 0.0124  134 PHE   C C   
2078 O O   . PHE   B 128 ? 0.1324 0.1400 0.1750 0.0158  -0.0018 0.0091  134 PHE   C O   
2079 C CB  . PHE   B 128 ? 0.1368 0.1402 0.1644 0.0161  -0.0018 0.0137  134 PHE   C CB  
2080 C CG  . PHE   B 128 ? 0.1337 0.1355 0.1569 0.0166  -0.0014 0.0152  134 PHE   C CG  
2081 C CD1 . PHE   B 128 ? 0.1344 0.1341 0.1524 0.0157  -0.0010 0.0174  134 PHE   C CD1 
2082 C CD2 . PHE   B 128 ? 0.1456 0.1480 0.1700 0.0182  -0.0016 0.0139  134 PHE   C CD2 
2083 C CE1 . PHE   B 128 ? 0.1488 0.1463 0.1619 0.0163  -0.0007 0.0181  134 PHE   C CE1 
2084 C CE2 . PHE   B 128 ? 0.1559 0.1564 0.1760 0.0190  -0.0007 0.0151  134 PHE   C CE2 
2085 C CZ  . PHE   B 128 ? 0.1543 0.1520 0.1682 0.0181  -0.0002 0.0170  134 PHE   C CZ  
2086 N N   . ALA   B 129 ? 0.1197 0.1261 0.1604 0.0140  0.0004  0.0138  135 ALA   C N   
2087 C CA  . ALA   B 129 ? 0.1224 0.1288 0.1656 0.0140  0.0005  0.0116  135 ALA   C CA  
2088 C C   . ALA   B 129 ? 0.1406 0.1449 0.1756 0.0149  -0.0006 0.0100  135 ALA   C C   
2089 O O   . ALA   B 129 ? 0.1337 0.1366 0.1638 0.0144  -0.0003 0.0122  135 ALA   C O   
2090 C CB  . ALA   B 129 ? 0.1290 0.1359 0.1761 0.0130  0.0024  0.0142  135 ALA   C CB  
2091 N N   . ASP   B 130 ? 0.1329 0.1370 0.1667 0.0162  -0.0021 0.0064  136 ASP   C N   
2092 C CA  . ASP   B 130 ? 0.1407 0.1424 0.1658 0.0175  -0.0029 0.0052  136 ASP   C CA  
2093 C C   . ASP   B 130 ? 0.1485 0.1488 0.1722 0.0173  -0.0008 0.0057  136 ASP   C C   
2094 O O   . ASP   B 130 ? 0.1475 0.1487 0.1772 0.0167  0.0005  0.0049  136 ASP   C O   
2095 C CB  . ASP   B 130 ? 0.1505 0.1526 0.1750 0.0193  -0.0055 0.0008  136 ASP   C CB  
2096 C CG  . ASP   B 130 ? 0.1837 0.1830 0.1980 0.0214  -0.0066 -0.0002 136 ASP   C CG  
2097 O OD1 . ASP   B 130 ? 0.1826 0.1802 0.1910 0.0218  -0.0065 0.0022  136 ASP   C OD1 
2098 O OD2 . ASP   B 130 ? 0.2101 0.2084 0.2218 0.0226  -0.0072 -0.0034 136 ASP   C OD2 
2099 N N   . VAL   B 131 ? 0.1516 0.1495 0.1682 0.0177  0.0000  0.0072  137 VAL   C N   
2100 C CA  . VAL   B 131 ? 0.1525 0.1489 0.1673 0.0179  0.0026  0.0076  137 VAL   C CA  
2101 C C   . VAL   B 131 ? 0.1603 0.1535 0.1657 0.0202  0.0027  0.0061  137 VAL   C C   
2102 O O   . VAL   B 131 ? 0.1679 0.1593 0.1706 0.0208  0.0056  0.0066  137 VAL   C O   
2103 C CB  . VAL   B 131 ? 0.1540 0.1506 0.1708 0.0160  0.0046  0.0117  137 VAL   C CB  
2104 C CG1 . VAL   B 131 ? 0.1467 0.1463 0.1720 0.0143  0.0044  0.0134  137 VAL   C CG1 
2105 C CG2 . VAL   B 131 ? 0.1537 0.1484 0.1648 0.0157  0.0037  0.0137  137 VAL   C CG2 
2106 N N   . ARG   B 132 ? 0.1597 0.1522 0.1599 0.0218  -0.0001 0.0045  138 ARG   C N   
2107 C CA  . ARG   B 132 ? 0.1703 0.1594 0.1600 0.0245  -0.0002 0.0038  138 ARG   C CA  
2108 C C   . ARG   B 132 ? 0.1701 0.1579 0.1560 0.0265  0.0000  0.0003  138 ARG   C C   
2109 O O   . ARG   B 132 ? 0.1901 0.1745 0.1666 0.0288  0.0013  0.0005  138 ARG   C O   
2110 C CB  . ARG   B 132 ? 0.1621 0.1511 0.1480 0.0260  -0.0037 0.0032  138 ARG   C CB  
2111 C CG  . ARG   B 132 ? 0.1591 0.1479 0.1463 0.0245  -0.0034 0.0067  138 ARG   C CG  
2112 C CD  . ARG   B 132 ? 0.1614 0.1501 0.1455 0.0264  -0.0065 0.0058  138 ARG   C CD  
2113 N NE  . ARG   B 132 ? 0.1649 0.1576 0.1563 0.0262  -0.0091 0.0030  138 ARG   C NE  
2114 C CZ  . ARG   B 132 ? 0.1735 0.1676 0.1660 0.0275  -0.0119 0.0021  138 ARG   C CZ  
2115 N NH1 . ARG   B 132 ? 0.1705 0.1621 0.1560 0.0297  -0.0128 0.0033  138 ARG   C NH1 
2116 N NH2 . ARG   B 132 ? 0.1651 0.1630 0.1661 0.0269  -0.0135 -0.0001 138 ARG   C NH2 
2117 N N   . ASP   B 133 ? 0.1664 0.1564 0.1592 0.0258  -0.0008 -0.0029 139 ASP   C N   
2118 C CA  . ASP   B 133 ? 0.1867 0.1751 0.1761 0.0277  -0.0006 -0.0070 139 ASP   C CA  
2119 C C   . ASP   B 133 ? 0.1925 0.1794 0.1834 0.0271  0.0045  -0.0056 139 ASP   C C   
2120 O O   . ASP   B 133 ? 0.2103 0.1948 0.1967 0.0290  0.0056  -0.0088 139 ASP   C O   
2121 C CB  . ASP   B 133 ? 0.1875 0.1784 0.1848 0.0270  -0.0038 -0.0116 139 ASP   C CB  
2122 C CG  . ASP   B 133 ? 0.2095 0.2030 0.2191 0.0241  -0.0019 -0.0101 139 ASP   C CG  
2123 O OD1 . ASP   B 133 ? 0.1955 0.1905 0.2087 0.0224  -0.0006 -0.0057 139 ASP   C OD1 
2124 O OD2 . ASP   B 133 ? 0.2376 0.2315 0.2533 0.0237  -0.0016 -0.0134 139 ASP   C OD2 
2125 N N   . LEU   B 134 ? 0.1779 0.1661 0.1748 0.0248  0.0073  -0.0011 140 LEU   C N   
2126 C CA  . LEU   B 134 ? 0.1755 0.1633 0.1762 0.0243  0.0120  0.0005  140 LEU   C CA  
2127 C C   . LEU   B 134 ? 0.1818 0.1665 0.1746 0.0256  0.0155  0.0031  140 LEU   C C   
2128 O O   . LEU   B 134 ? 0.1823 0.1675 0.1776 0.0241  0.0176  0.0074  140 LEU   C O   
2129 C CB  . LEU   B 134 ? 0.1687 0.1600 0.1803 0.0213  0.0125  0.0040  140 LEU   C CB  
2130 C CG  . LEU   B 134 ? 0.1775 0.1717 0.1975 0.0200  0.0098  0.0024  140 LEU   C CG  
2131 C CD1 . LEU   B 134 ? 0.1824 0.1796 0.2110 0.0176  0.0103  0.0067  140 LEU   C CD1 
2132 C CD2 . LEU   B 134 ? 0.1926 0.1862 0.2164 0.0209  0.0105  -0.0018 140 LEU   C CD2 
2133 N N   . LEU   B 135 ? 0.1915 0.1724 0.1735 0.0288  0.0161  0.0004  141 LEU   C N   
2134 C CA  . LEU   B 135 ? 0.2200 0.1971 0.1923 0.0307  0.0196  0.0032  141 LEU   C CA  
2135 C C   . LEU   B 135 ? 0.2094 0.1860 0.1861 0.0300  0.0258  0.0064  141 LEU   C C   
2136 O O   . LEU   B 135 ? 0.2220 0.1968 0.1962 0.0300  0.0291  0.0105  141 LEU   C O   
2137 C CB  . LEU   B 135 ? 0.2196 0.1925 0.1782 0.0348  0.0188  -0.0004 141 LEU   C CB  
2138 C CG  . LEU   B 135 ? 0.2565 0.2304 0.2114 0.0360  0.0119  -0.0044 141 LEU   C CG  
2139 C CD1 . LEU   B 135 ? 0.2814 0.2511 0.2213 0.0404  0.0106  -0.0076 141 LEU   C CD1 
2140 C CD2 . LEU   B 135 ? 0.2501 0.2258 0.2070 0.0346  0.0087  -0.0016 141 LEU   C CD2 
2141 N N   . TRP   B 136 ? 0.2022 0.1807 0.1872 0.0292  0.0275  0.0049  142 TRP   C N   
2142 C CA  . TRP   B 136 ? 0.2179 0.1967 0.2092 0.0287  0.0334  0.0078  142 TRP   C CA  
2143 C C   . TRP   B 136 ? 0.2229 0.2050 0.2235 0.0254  0.0337  0.0129  142 TRP   C C   
2144 O O   . TRP   B 136 ? 0.2365 0.2190 0.2420 0.0250  0.0385  0.0162  142 TRP   C O   
2145 C CB  . TRP   B 136 ? 0.2156 0.1955 0.2141 0.0288  0.0346  0.0049  142 TRP   C CB  
2146 C CG  . TRP   B 136 ? 0.2035 0.1873 0.2114 0.0265  0.0300  0.0036  142 TRP   C CG  
2147 C CD1 . TRP   B 136 ? 0.2155 0.1991 0.2222 0.0269  0.0259  -0.0011 142 TRP   C CD1 
2148 C CD2 . TRP   B 136 ? 0.1981 0.1864 0.2186 0.0236  0.0295  0.0071  142 TRP   C CD2 
2149 N NE1 . TRP   B 136 ? 0.2225 0.2100 0.2403 0.0244  0.0233  -0.0002 142 TRP   C NE1 
2150 C CE2 . TRP   B 136 ? 0.2118 0.2020 0.2373 0.0225  0.0255  0.0048  142 TRP   C CE2 
2151 C CE3 . TRP   B 136 ? 0.1980 0.1888 0.2261 0.0218  0.0319  0.0120  142 TRP   C CE3 
2152 C CZ2 . TRP   B 136 ? 0.2074 0.2015 0.2436 0.0202  0.0241  0.0076  142 TRP   C CZ2 
2153 C CZ3 . TRP   B 136 ? 0.2097 0.2048 0.2486 0.0195  0.0298  0.0143  142 TRP   C CZ3 
2154 C CH2 . TRP   B 136 ? 0.2112 0.2076 0.2532 0.0189  0.0262  0.0123  142 TRP   C CH2 
2155 N N   . LEU   B 137 ? 0.2057 0.1903 0.2093 0.0232  0.0288  0.0137  143 LEU   C N   
2156 C CA  . LEU   B 137 ? 0.2113 0.1985 0.2222 0.0203  0.0286  0.0180  143 LEU   C CA  
2157 C C   . LEU   B 137 ? 0.2524 0.2365 0.2582 0.0206  0.0319  0.0211  143 LEU   C C   
2158 O O   . LEU   B 137 ? 0.2718 0.2577 0.2849 0.0183  0.0332  0.0246  143 LEU   C O   
2159 C CB  . LEU   B 137 ? 0.2022 0.1914 0.2144 0.0185  0.0231  0.0178  143 LEU   C CB  
2160 C CG  . LEU   B 137 ? 0.1894 0.1821 0.2091 0.0175  0.0203  0.0161  143 LEU   C CG  
2161 C CD1 . LEU   B 137 ? 0.2033 0.1970 0.2218 0.0165  0.0155  0.0157  143 LEU   C CD1 
2162 C CD2 . LEU   B 137 ? 0.2150 0.2114 0.2463 0.0155  0.0216  0.0191  143 LEU   C CD2 
2163 N N   . ASP   B 138 ? 0.2498 0.2294 0.2434 0.0236  0.0331  0.0199  144 ASP   C N   
2164 C CA  . ASP   B 138 ? 0.2820 0.2579 0.2699 0.0243  0.0365  0.0233  144 ASP   C CA  
2165 C C   . ASP   B 138 ? 0.3189 0.2928 0.3073 0.0256  0.0439  0.0254  144 ASP   C C   
2166 O O   . ASP   B 138 ? 0.3335 0.3039 0.3175 0.0264  0.0478  0.0286  144 ASP   C O   
2167 C CB  . ASP   B 138 ? 0.2747 0.2462 0.2484 0.0274  0.0348  0.0218  144 ASP   C CB  
2168 C CG  . ASP   B 138 ? 0.2760 0.2486 0.2484 0.0266  0.0284  0.0203  144 ASP   C CG  
2169 O OD1 . ASP   B 138 ? 0.2793 0.2554 0.2608 0.0234  0.0258  0.0211  144 ASP   C OD1 
2170 O OD2 . ASP   B 138 ? 0.3177 0.2878 0.2800 0.0294  0.0259  0.0184  144 ASP   C OD2 
2171 N N   . GLU   B 139 ? 0.3296 0.3053 0.3231 0.0262  0.0462  0.0238  145 GLU   C N   
2172 C CA  . GLU   B 139 ? 0.3893 0.3631 0.3831 0.0280  0.0538  0.0255  145 GLU   C CA  
2173 C C   . GLU   B 139 ? 0.4355 0.4139 0.4443 0.0261  0.0562  0.0266  145 GLU   C C   
2174 O O   . GLU   B 139 ? 0.4317 0.4146 0.4494 0.0238  0.0516  0.0257  145 GLU   C O   
2175 C CB  . GLU   B 139 ? 0.4553 0.4243 0.4352 0.0324  0.0555  0.0216  145 GLU   C CB  
2176 C CG  . GLU   B 139 ? 0.5663 0.5372 0.5482 0.0327  0.0515  0.0164  145 GLU   C CG  
2177 C CD  . GLU   B 139 ? 0.6912 0.6579 0.6589 0.0364  0.0494  0.0112  145 GLU   C CD  
2178 O OE1 . GLU   B 139 ? 0.6993 0.6664 0.6686 0.0371  0.0482  0.0067  145 GLU   C OE1 
2179 O OE2 . GLU   B 139 ? 0.7342 0.6972 0.6893 0.0386  0.0487  0.0116  145 GLU   C OE2 
2180 N N   . GLU   B 140 ? 0.4784 0.4555 0.4894 0.0277  0.0637  0.0285  146 GLU   C N   
2181 C CA  . GLU   B 140 ? 0.5123 0.4933 0.5373 0.0269  0.0676  0.0299  146 GLU   C CA  
2182 C C   . GLU   B 140 ? 0.5364 0.5212 0.5745 0.0237  0.0693  0.0351  146 GLU   C C   
2183 O O   . GLU   B 140 ? 0.5474 0.5293 0.5819 0.0237  0.0729  0.0381  146 GLU   C O   
2184 C CB  . GLU   B 140 ? 0.5382 0.5229 0.5703 0.0261  0.0633  0.0268  146 GLU   C CB  
2185 C CG  . GLU   B 140 ? 0.6194 0.6082 0.6664 0.0256  0.0669  0.0286  146 GLU   C CG  
2186 C CD  . GLU   B 140 ? 0.7312 0.7167 0.7753 0.0293  0.0736  0.0265  146 GLU   C CD  
2187 O OE1 . GLU   B 140 ? 0.7572 0.7415 0.7987 0.0307  0.0717  0.0221  146 GLU   C OE1 
2188 O OE2 . GLU   B 140 ? 0.7491 0.7329 0.7938 0.0308  0.0810  0.0291  146 GLU   C OE2 
2189 N N1  . A1B1E C .   ? 0.2384 0.1990 0.2880 0.0440  0.0383  0.0072  201 A1B1E A N1  
2190 C C4  . A1B1E C .   ? 0.3371 0.2681 0.3546 0.0271  0.0551  -0.0250 201 A1B1E A C4  
2191 C C5  . A1B1E C .   ? 0.3147 0.2473 0.3459 0.0343  0.0541  -0.0163 201 A1B1E A C5  
2192 C C6  . A1B1E C .   ? 0.3028 0.2496 0.3442 0.0407  0.0502  -0.0068 201 A1B1E A C6  
2193 C C7  . A1B1E C .   ? 0.2743 0.2258 0.3280 0.0460  0.0478  0.0032  201 A1B1E A C7  
2194 C C8  . A1B1E C .   ? 0.3217 0.2689 0.3701 0.0441  0.0587  -0.0078 201 A1B1E A C8  
2195 C C10 . A1B1E C .   ? 0.4015 0.3394 0.4303 0.0325  0.0805  -0.0331 201 A1B1E A C10 
2196 C C13 . A1B1E C .   ? 0.3995 0.3560 0.4135 0.0267  0.0668  -0.0313 201 A1B1E A C13 
2197 O O2  . A1B1E C .   ? 0.2864 0.2333 0.3533 0.0513  0.0550  0.0074  201 A1B1E A O2  
2198 C C3  . A1B1E C .   ? 0.3467 0.2777 0.3698 0.0301  0.0636  -0.0268 201 A1B1E A C3  
2199 N N   . A1B1E C .   ? 0.3459 0.2899 0.3805 0.0374  0.0600  -0.0173 201 A1B1E A N   
2200 C C2  . A1B1E C .   ? 0.3523 0.3058 0.3848 0.0371  0.0579  -0.0167 201 A1B1E A C2  
2201 O O1  . A1B1E C .   ? 0.3452 0.3091 0.3884 0.0427  0.0566  -0.0090 201 A1B1E A O1  
2202 C C1  . A1B1E C .   ? 0.3684 0.3203 0.3848 0.0288  0.0571  -0.0251 201 A1B1E A C1  
2203 O O   . A1B1E C .   ? 0.3643 0.3274 0.3750 0.0270  0.0480  -0.0220 201 A1B1E A O   
2204 C C   . A1B1E C .   ? 0.3506 0.3152 0.3535 0.0231  0.0386  -0.0209 201 A1B1E A C   
2205 C C9  . A1B1E C .   ? 0.3923 0.3411 0.4116 0.0293  0.0680  -0.0300 201 A1B1E A C9  
2206 N N2  . A1B1E C .   ? 0.4041 0.3591 0.4212 0.0271  0.0767  -0.0354 201 A1B1E A N2  
2207 C C12 . A1B1E C .   ? 0.4071 0.3517 0.4341 0.0305  0.0892  -0.0386 201 A1B1E A C12 
2208 C C11 . A1B1E C .   ? 0.4086 0.3439 0.4420 0.0334  0.0917  -0.0375 201 A1B1E A C11 
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